1
Table S1
GenBank accession numbers and references of organisms and proteins
presented in main text and figures
Figure
Organisms Name
Organism
Accession
Number
Reference(s)
Fig 2
Pseudomonas putida
AB238971
Keil
et al
. 1985; Keil
et al
. 1987a; Keil
et
al
. 1987b; Osborne
et
al.
1988; Assinder
et
al.
1992; Assinder
et
al.
1993; Gallegos
et
al
. 1997; Sentchilo
et
al.
2000; Tsuda and
Genka 2001; Yano
et
al.
2007; Miyakoshi
et al.
2012
Fig 2
Treponema primitia
str. ZAS
-‐
2
CP001843
Rosenthal
et al.
2011
Fig
2
Treponema primitia
str. ZAS
-‐
1
CP001843
Ballor
et al.
2011
Fig 2
Novosphingobium aromaticivorans
AF079317
Romine
et al
. 1999
Fig 2
Novosphingobium
sp.
FR856862
D'Argenio
et al
. 2011
Fig 2
Methylocella silvestris
CP001280
Chen
et al
. 2010
Fig 2
Sphingobium japonicum
AP010803
Nagata
et al.
2010
Fig 2
Azoarcus
sp.
AM406670
Krause
et al.
2006
Fig 2
Thauera
sp.
CP001281
NA
Fig 2
Dechloromonas aromatica
CP000089
NA
Fig 2
Azotobacter vinelandii
CP001157
Setubal
et al.
2009
Fig 2
Methylibium
petroleiphilum
CP000555
Kane
et al
. 2007
Catechol 2,3
-‐
dioxygenase
Accession
Number
Fig 3
Novosphingobium aromaticivorans
NP_049202
Romine
et al
.1999
Fig 3
Sphingomonas agrestis
AAB03075
Yrjala
et al.
1994
Fig 3
Rhizobium
sp.
ABF82226
NA
Fig 3
Beijerinckia
sp.
B57264
Kim and Zylstra
1995
Fig 3
Sphingomonas
sp.
AAM14600
NA
Fig 3
Sphingomonas
sp.
ADK27485
NA
Fig 3
Novosphingobium
pentaromativorans
ZP_09195387
NA
Fig 3
Novosphingobium
sp.
YP_004534265
D'Argenio
et al
. 2011
Fig 3
Sphingomonas
sp.
AAD11448
NA
Fig 3
Sphingomonas
sp.
AAD11452
NA
Fig 3
Treponema primitia
str. ZAS
-‐
1
ZP_09718346
Ballor
et al.
2011
Fig 3
Treponema primitia
str. ZAS
-‐
2
YP_004531633
Rosenthal
et al.
2011
Fig 3
lake sediment
Fig 3
activated sludge
BAH89314
Suenaga
et al
. 2007;
Suenaga
et al
. 2009
Fig 3
activated sludge
BAH90343
Suenaga
et al
. 2007;
Suenaga
et al
. 2009
2
Fig 3
Methylocella silvestris
YP_002361794
Chen
et al
. 2010
Fig 3
Sphingobium japonicum
YP_003544642
Nagata
et al.
2010
Fig 3
Pseudomonas
putida
BAB62050
NA
Fig 3
Thauera
sp.
YP_002890083
NA
Fig 3
Dechloromonas aromatica
YP_287003
NA
Fig 3
Azotobacter vinelandii
YP_002800217
Setubal
et al.
2009
Fig 3
Pseudomonas putida
YP_709322
Keil
et al
. 1985; Keil
et al
. 1987a; Keil
et
al
. 1987b; Osborne
et
al.
1988; Assinder
et
al.
1992; Assinder
et
al.
1993; Gallegos
et
al
. 1997; Sentchilo
et
al.
2000; Tsuda and
Genka 2001; Yano
et
al.
2007; Miyakoshi
et al.
2012
Fig 3
Alcaligenes xylosoxydans
Fig 3
Marinobacter algicola
ZP_01893284
NA
Fig 3
whale fall rib bone
Fig 3
Marinobacterium stanieri
ZP_09507225
NA
Fig 3
Marinobacterium stanieri
ZP_09506167
NA
Fig 3
marine gamma proteobacterium
HTCC2207
ZP_01224201
NA
Fig 3
sludge
Fig 3
Novosphingobium nitrogenifigens
ZP_08210144
NA
Fig 3
Cupriavidus necator
Fig 3
Methyloversatilis universalis
ZP_08506618
NA
Fig 3
Methylibium petroleiphilum
YP_001021468
Kane
et al
. 2007
3
Table S2
Treponema primitia
str.
ZAS
-‐
1 and ZAS
-‐
2
meta
-‐
cleavage pathway genes and pfam features
Present in
Protein Size
(a.a.)
in
Gene Annotation
str.
ZAS
-‐
1
str.
ZAS
-‐
2
str.
ZAS
-‐
1
str.
ZAS
-‐
2
Pfam(s) Represented
(PF#, family, domain)
ferredoxin
-‐
like peptide
+
+
98
94
PF00111, Fer2, [2Fe
-‐
2S] cluster binding
catechol 2,3
-‐
dioxygenase
+
+
308
308
PF00903, Glyoxalase, glyoxalase/ bleomycin
resistance protein/ dioxygenase
PF00903, Glyoxalase, glyoxalase/ bleomycin
resistance protein/ dioxygenase
2
-‐
hydroxymuconic
semialdehyde hydrolase
+
+
274
274
PF00561, Abhydrolase 1,
a
/
b
hydrolase fold
2
-‐
oxopent
-‐
4
-‐
enoate
hydratase
+
+
260
260
PF01557, FAA hydrolase,
fumarylacetoacetate hydrolase
4
-‐
hydroxy
-‐
2
-‐
oxopentanoate aldolase
+
+
340
335
PF00682, HMGL
-‐
like, HMGL
-‐
like
PF07836, DmpG comm., DmpG
-‐
like
communication
acetaldehyde
dehydrogenase
+
+
291
288
PF01118, Semialdehyde dh, semialdehyde
dehydrogenase NAD binding
PF09290, Acetdehyd dimer, prokaryotic
acetaldehyde dehydrogenase dimerisation
2
-‐
hydroxymuconic
semialdehyde
dehydrogenase
-‐
-‐
PF00171 Aldedh, aldehyde dehydrogenase
family
4
-‐
oxalocrotonate
tautomerase
-‐
-‐
PF01361 Tautomerase, tautomerase enzyme
4
-‐
oxalocrotonate
decarboxylase
-‐
-‐
PF01557 FAA hydrolase, fumarylacetoacetate
hydrolase
4
-‐
oxalocrotonate carboxy
-‐
lyase
-‐
-‐
PF01557 FAA hydrolase, fumarylacetoacetate
hydrolase
4
Table S3
Gene
expression patterns of
Treponema primitia
str. ZAS
-‐
2 in pure
culture or co
-‐
culture with
T.
azotonutricium
str. ZAS
-‐
9
Cohort
Expression Range
Pure
Culture
Co
-‐
Culture
(reads/kb)
No. genes
%
No. genes
%
1
a
0
344
9
395
10
2
1
-‐
9
503
13
556
14
3
b
10
-‐
99
1642
43
1548
40
4
c
100
-‐
999
1248
32
1234
32
5
> 1000
110
3
117
3
Analysis complements Table S4.
Analysis based on expression dataset from Rosenthal
et al
. 2011.
a
In addition to having 0 reads/kb, all genes in Cohort 1 have 0 expression.
b
Cohort includes
meta
-‐
cleavage
pathway 2
-‐
hydroxymuconic semialdehyde hydrolase, 2
-‐
oxopent
-‐
4
-‐
enoate hydratase, 4
-‐
hyd
roxy
-‐
2
-‐
oxopentanoate aldolase, acetaldehyde dehydrogeanse, and the
associated ferredoxin
-‐
like peptide.
c
Cohort includes
meta
-‐
cleavage
pathway catechol 2,3
-‐
dioxygenase.
5
Table S4
Expression of
Treponema primiti
a
str. ZAS
-‐
2 genes
Gene
Pure
Culture Expression
Co
-‐
Culture Expression
(normalized reads/kb)
(normalized reads/kb)
Meta
-‐
cleavage
pathway
Ferredoxin
-‐
like peptide
a
53
13
catechol 2,3
-‐
dioxygenase
b
219
170
2
-‐
hydoxymuconic semialdehyde hydrolase
a
43
60
2
-‐
oxopent
-‐
4
-‐
enoate hydratase
a
60
43
4
-‐
hydroxy
-‐
2
-‐
oxopentanoate aldolase
a
61
36
acetaldehyde dehydrogenase
a
59
62
House
-‐
keeping
ATP
-‐
dependent Clp protease ATP
-‐
binding subunit
ClpX
314
345
Metallo
-‐
beta
-‐
lactamase family protein, RNA
-‐
specific
140
144
RNA polymerase sigma factor RpoD
72
77
RNA polymerase sigma factor RpoD
183
135
RNA polymerase sigma factor RpoD
188
162
RNA polymerase sigma factor RpoD
94
92
RNA polymerase sigma factor RpoD
30
94
Acetogenesis
Formate dehydrogenase chain D
62
2
Formate dehydrogenase chain D
399
21
Formate dehydrogenase; cysteine
-‐
containing variant
601
33
Formate dehydrogenase; selenocysteine
-‐
containing
variant
168
331
Carbon monoxide dehydrogenase CooS subunit
2698
2524
Formate
-‐
tetrahydrofolate ligase (FTHFS)
1463
1600
Glycolysis
Hexokinase
168
190
Glucose
-‐
6
-‐
phosphate isomerase
169
170
6
-‐
phosphofructokinase
121
139
Fructose
-‐
bisphosphate aldolase class II
703
947
Triosephosphate isomerase
344
418
NAD
-‐
dependent glyceraldehyde
-‐
3
-‐
phosphate
dehydrogenase
134
173
NAD
-‐
dependent glyceraldehyde
-‐
3
-‐
phosphate
dehydrogenase
152
167
2,3
-‐
bisphosphoglycerate
-‐
independent
phosphoglycerate mutase
440
393
Enolase
851
967
Pyruvate kinase
89
93
Misc.
acetate kinase
914
1085
Fe
-‐
S cluster containing hydrogenase
components 2
552
39
Periplasmic [Fe] hydrogenas large subunit
495
31
Expression data from Rosenthal
et al
. 2011.
6
Normalized gene expression values are number of reads mapped to a particular gene divided by size
of that gene.
a
Belong
to Cohort 3 (Table S3).
b
Belongs to Cohort 4 (Table S3).
7
!
!
!
!
!
!
"
"
"
"
"
"
"
"
!
!
!
!
!
!
!
!
!
!
"
"
"
"
!
"
!
"
!
!
!
!
!
!
!
!
!
"
"
"
"
"
!
!
"
!
!
!
"
"
"
"
!
!
!
!
!
!
"
"
!
!
!
!
ferredoxin-like peptide
catechol 2,3-dioxygenase
2-hydroxymuconic
semialdehyde hydrolase
2-oxopent-4-enoate hydratase
4-hydroxy-2-oxopentanoate
aldolase
acetaldehyde dehydrogenase
str. ZAS-1
str. ZAS-2
str. ZAS-1
str. ZAS-1
str. ZAS-1
str. ZAS-1
str. ZAS-1
str. ZAS-2
str. ZAS-2
str. ZAS-2
str. ZAS-2
str. ZAS-2
8
Fig. S1
PFAM domains and conserved functional residues and sequence motifs in
Treponema primitia
str. ZAS
-‐
1 and ZAS
-‐
2
meta
-‐
cleavage pathway proteins.
The
primary structure span
s
of
meta
-‐
pathway proteins are
represented by black lines,
and PFAM domains within the
meta
-‐
pathway proteins are represented by grey
rectangles. Symbols rep
resenting conserved functional residues are centered over
the location of the functional residues. Active site residues are represent
ed by black
inverted triangles
, metal
-‐
binding residues are repre
sented by white diamonds
,
residues contributing to protein
structure are represent
ed by light grey squares
,
and substrate
-‐
binding residues are represente
d by grey circles
. Conserved
sequence motifs are r
epresented by white bars
.
9
Fig.
S2
Phylogenetic position of
Treponema primitia
str.
ZAS
-‐
1 and ZAS
-‐
2
2
-‐
hydroxymuconic se
mialdehyde hydrolase (PF00561, s
tep 2).
Bayesian protein
phylogenetic analysis (2540 trees from 1,016,000 generations; PSRF = 1.000;
average standard deviation of split frequencies = 0.011955) is
based on 222
unambiguously aligned amino acid positions of a 274 amino acid
-‐
long protein.
Bayes
ian posterior probabilities
(when greater than 50) are reported above the
nodes. Phylip PROTPARS maximum parsimony support after analysis of 1000
bootstraps (
when greater than 50%) is reported below nodes. Shaded circles
indicate nodes supported by both maximum parsimony and Fitch distance matrix
methods. Open circles indicate nodes supported by one of those methods. Scale bar
indicates distance depicted as
0.1 amino acid changes per alignment position.
10
Fig.
S3
Phylogenetic position of
Treponema primitia
str.
ZAS
-‐
1 and ZAS
-‐
2 2
-‐
oxopent
-‐
4
-‐
enoate hydratase
(PF01557, s
tep 3).
Bayesian protein phylogenetic analysis (313
trees from 125,000 generations; PSRF = 1.000; average standard deviation of split
frequencies = 0.009239) is based on 243 unambiguously aligned amino acid
positions of a 260 amino acid
-‐
long protein.
Bayes
ian pos
terior probabilities
(when
greater than 50) are reported above the nodes. Phylip PROTPARS maximum
parsimony support after analysis of 1000 bootstraps (when greater than 50%) is
reported below nodes. Shaded circles indicate nodes supported by both maximum
parsimony and Fitch distance matrix methods. Open circles indicate nodes
supported by one of those methods. Scale bar indicates distance depicted as 0.1
amino acid changes per alignment position.
11
Fig. S
4
Phylogenetic position of
Treponema
primitia
str. ZAS
-‐
1 and ZAS
-‐
2
ferredoxin
-‐
like
peptide
(PF00111, Step 1’).
Bayesian protein phylogenetic analysis
(183 trees from 73,000 generations; PSRF = 1.001; average standard deviation of
split frequencies = 0.011280) is based on 85 unambiguously ali
gned amino acid
positions of a 98 amino acid
-‐
long protein.
Bayes
ian posterior probabilities
(when
greater than 50) are reported above the nodes. Phylip PROTPARS maximum
parsimony support after analysis of 1000 bootstraps (when greater than 50%) is
report
ed below nodes. Shaded circles indicate nodes supported by both maximum
parsimony and Fitch distance matrix methods. Open circles indicate nodes
supported by one of those methods. Scale bar indicates distance depicted as 0.1
amino acid changes per align
ment position.
12
Fig. S
5
Phylogenetic position of
Treponema primitia
str. ZAS
-‐
1 and ZAS
-‐
2 4
-‐
hydroxy
-‐
2
-‐
oxopentanoate aldolase (PF00682 and PF07836, Step 4).
Bayesian
protein phylogenetic analysis (375 trees from 150,000 generations; PSRF = 1.000;
average standard deviation of split frequencies = 0.002661) is based on 331
unambiguously aligned amino acid positions of a 340 amino acid
-‐
long protein.
Bayes
ian posterior probabilities
(when greater than 50) are reported above the
nodes. Phylip
PROTPARS maximum parsimony support after analysis of 1000
bootstraps (when greater than 50%) is reported below nodes. Shaded circles
indicate nodes supported by both maximum parsimony and Fitch distance matrix
methods. Open circles indicate nodes suppor
ted by one of those methods. Scale bar
indicates distance depicted as 0.1 amino acid changes per alignment position.
13
Fig. S
6
Phylogenetic position of
Treponema primitia
str. ZAS
-‐
1 and ZAS
-‐
2
acetaldehyde dehydrogenase (PF01118 and PF09290, Step 5)
.
Bayesian protein
phylogenetic analysis (279 trees from 111,500 generations; PSRF = 1.004; average
standard deviation of split frequencies = 0.018287) is based on 259 unambiguously
aligned amino acid positions of a 291 amino acid
-‐
long protein.
Bayes
ian
posterior
probabilities
(when greater than 50) are reported above the nodes. Phylip
PROTPARS maximum parsimony support after analysis of 1000 bootstraps (when
greater than 50%) is reported below nodes. Shaded circles indicate nodes
14
supported by both maxi
mum parsimony and Fitch distance matrix methods. Open
circles indicate nodes supported by one of those methods. Scale bar indicates
distance depicted as 0.1 amino acid changes per alignment position.
15
Fig. S
7
Phylogenetic position of
Treponema primitia
str. ZAS
-‐
1 and ZAS
-‐
2 N
-‐
terminal
Domain (PF00903).
Bayesian protein phylogenetic analysis (220 trees from 88,000
generations; PSRF = 0.999; average standard deviation of split frequencies =
0.014790) is b
ased on 56 unambiguously aligned amino acid positions of a 64 amino
acid
-‐
long domain.
Bayes
ian posterior probabilities
(when greater than 50) are
reported above the nodes. Phylip PROTPARS maximum parsimony support after
analysis of 1000 bootstraps (when
greater than 50%) is reported below nodes.
Shaded circles indicate nodes supported by both maximum parsimony and Fitch
distance matrix methods. Open circles indicate nodes supported by one of those
16
methods. Scale bar indicates distance depicted as 0.1 a
mino acid changes per
alignment position.
17
Fig. S
8
Phylogenetic position of
Treponema primitia
str. ZAS
-‐
1 and ZAS
-‐
2 N
-‐
terminal
Domain (PF00903) with extra
-‐
domain region.
Bayesian protein phylogenetic
analysis (600 trees from 240,000 generations; PSRF = 1.000; average standard
deviation of split frequencies = 0.010855) is based on 67 unambiguously aligned
amino acid positions of a 68 amino acid
-‐
long region.
Bayes
ian poster
ior
probabilities
(when greater than 50) are reported above the nodes. Phylip
PROTPARS maximum parsimony support after analysis of 1000 bootstraps (when
greater than 50%) is reported below nodes. Shaded circles indicate nodes
supported by both maximum pa
rsimony and Fitch distance matrix methods. Open
18
circles indicate nodes supported by one of those methods. Scale bar indicates
distance depicted as 0.1 amino acid changes per alignment position.
19
Fig. S
9
Phylogenetic position of
Treponema primitia
str. ZAS
-‐
1 and ZAS
-‐
2 N
-‐
terminal
Domain (PF00903) with intra
-‐
domain region.
Bayesian protein phylogenetic
analysis (375 trees from 150,000 generations; PSRF = 1.000; average standard
deviation of split frequenc
ies = 0.010443) is based on 88 unambiguously aligned
amino acid positions of a 139 amino acid
-‐
long region.
Bayes
ian posterior
probabilities
(when greater than 50) are reported above the nodes. Phylip
PROTPARS maximum parsimony support after analysis of 1
000 bootstraps (when
greater than 50%) is reported below nodes. Shaded circles indicate nodes
supported by both maximum parsimony and Fitch distance matrix methods. Open
20
circles indicate nodes supported by one of those methods. Scale bar indicates
dista
nce depicted as 0.1 amino acid changes per alignment position.
21
Fig. S
10
Phylogenetic position of
Treponema primitia
str. ZAS
-‐
1 and ZAS
-‐
2 C
-‐
terminal Domain (PF00903).
Bayesian protein phylogenetic analysis (350 trees
from 140,000 generations; PSRF = 1.000; average standard deviation of split
frequencies = 0.014588) is based on 115 unambiguously aligned amino acid
positions of a 116 amino acid
-‐
long domain.
Bayes
ian post
erior probabilities
(when
greater than 50) are reported above the nodes. Phylip PROTPARS maximum
parsimony support after analysis of 1000 bootstraps (when greater than 50%) is
reported below nodes. Shaded circles indicate nodes supported by both maximum
parsimony and Fitch distance matrix methods. Open circles indicate nodes
supported by one of those methods. Scale bar indicates distance depicted as 0.1
amino acid changes per alignment position.
22
Fig. S
11
Phylogenetic position of
Treponema primitia
s
tr. ZAS
-‐
1 and ZAS
-‐
2 C
-‐
terminal Domain (PF00903) with extra
-‐
domain region.
Bayesian protein
phylogenetic analysis (450 trees from 180,000 generations; PSRF = 1.000; average
standard deviation of split frequencies = 0.010860) is based on 155 unambiguously
a
ligned amino acid positions of a 158 amino acid
-‐
long region.
Bayes
ian posterior
probabilities
(when greater than 50) are reported above the nodes. Phylip
PROTPARS maximum parsimony support after analysis of 1000 bootstraps (when
greater than 50%) is repo
rted below nodes. Shaded circles indicate nodes
supported by both maximum parsimony and Fitch distance matrix methods. Open
circles indicate nodes supported by one of those methods. Scale bar indicates
distance depicted as 0.1 amino acid changes per ali
gnment position.
23
Fig. S1
2
Phylogenetic position of
Treponema primitia
str. ZAS
-‐
1 and ZAS
-‐
2 C
-‐
terminal Domain (PF00903) with intra
-‐
domain region.
Bayesian protein
phylogenetic analysis (500 trees from 200,000 generations; PSRF = 1.000; average
standard deviation of split frequencies = 0.010844) is based on 140 unambiguously
aligned amino acid positions of a 141 amino acid
-‐
long region.
Bayes
ian post
erior
probabilities
(when greater than 50) are reported above the nodes. Phylip
PROTPARS maximum parsimony support after analysis of 1000 bootstraps (when
greater than 50%) is reported below nodes. Shaded circles indicate nodes
supported by both maximum
parsimony and Fitch distance matrix methods. Open
circles indicate nodes supported by one of those methods. Scale bar indicates
distance depicted as 0.1 amino acid changes per alignment position.
24
Fig. S1
3
Phylogenetic position of
Treponema primitia
s
tr. ZAS
-‐
1 and ZAS
-‐
2 4
-‐
hydroxy
-‐
2
-‐
oxopentanoate aldolase HMGL
-‐
like domain (PF00682).
Bayesian protein
phylogenetic analysis (313 trees from 125,000 generations; PSRF = 1.000; average
standard deviation of split frequencies = 0.009037) is based on 243 unambi
guously
aligned amino acid positions of a 232 amino acid
-‐
long domain.
Bayes
ian posterior
probabilities
(when greater than 50) are reported above the nodes. Phylip
PROTPARS maximum parsimony support after analysis of 1000 bootstraps (when
greater than 50%
) is reported below nodes. Shaded circles indicate nodes
supported by both maximum parsimony and Fitch distance matrix methods. Open
circles indicate nodes supported by one of those methods. Scale bar indicates
distance depicted as 0.1 amino acid change
s per alignment position.
25
Fig. S14
Phylogenetic position of
Treponema primitia
str. ZAS
-‐
1 and ZAS
-‐
2 4
-‐
hydroxy
-‐
2
-‐
oxopentanoate aldolase DmpG
-‐
like communication domain (PF07836).
Bayesian protein phylogenetic analysis (480 trees from 192,000
generations; PSRF
= 1.000; average standard deviation of split frequencies = 0.016899) is based on 65
unambiguously aligned amino acid positions of a 66
amino acid
-‐
long domain.
Bayes
ian posterior probabilities
(when greater than 50) are reported above the
nodes. Phylip PROTPARS maximum parsimony support after analysis of 1000
bootstraps (when greater than 50%) is reported below nodes. Shaded circles
indicate nodes supported by both maximum parsimony and Fitch
distance matrix
methods. Open circles indicate nodes supported by one of those methods. Scale bar
indicates distance depicted as 0.1 amino acid changes per alignment position.
26
Fig. S1
5
Phylogenetic position of
Treponema primitia
str. ZAS
-‐
1 and
ZAS
-‐
2
acetaldehyde dehydrogenase, NAD binding domain (PF01118).
Bayesian protein
phylogenetic analysis (123 trees from 205,000 generations; PSRF = 1.000; average
standard deviation of split frequencies = 0.010781) is based on 110 unambiguously
aligned ami
no acid positions of a 110 amino acid
-‐
long domain.
Bayes
ian posterior
probabilities
(when greater than 50) are reported above the nodes. Phylip
PROTPARS maximum parsimony support after analysis of 1000 bootstraps (when
greater than 50%) is reported below
nodes. Shaded circles indicate nodes
supported by both maximum parsimony and Fitch distance matrix methods. Open
circles indicate nodes supported by one of those methods. Scale bar indicates
distance depicted as 0.1 amino acid changes per alignment pos
ition.
27
Fig. S1
6
Phylogenetic position of
Treponema primitia
str. ZAS
-‐
1 and ZAS
-‐
2
acetaldehyde dehydrogenase dimerisation domain (PF09290).
Bayesian protein
phylogenetic analysis (145 trees from 58,000 generations; PSRF = 0.999; average
standard
deviation of split frequencies = 0.013476) is based on 135 unambiguously
aligned amino acid positions of a 137 amino acid
-‐
long domain.
Bayes
ian posterior
probabilities
(when greater than 50) are reported above the nodes. Phylip
PROTPARS maximum parsimony
support after analysis of 1000 bootstraps (when
greater than 50%) is reported below nodes. Shaded circles indicate nodes
supported by both maximum parsimony and Fitch distance matrix methods. Open
circles indicate nodes supported by one of those methods
. Scale bar indicates
distance depicted as 0.1 amino acid changes per alignment position.