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Conserved domains on  [gi|1776941518|dbj|BBF43151|]
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phage shock protein E precursor [Lachnospiraceae bacterium KM106-2]

Protein Classification

rhodanese-like domain-containing protein( domain architecture ID 10068911)

rhodanese-like domain-containing protein may have sulfurtransferase activity if an active site cysteine is present

CATH:  3.40.250.10
PubMed:  12151332|17454295
SCOP:  4000452

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 38-125 3.87e-33

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


:

Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 111.62  E-value: 3.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  38 ELQEMINQEsDLVVLDVRTESEYLSGHIPNAILLPYDQISEQAEASLPDKDAKIIVYCHSGRRSAIATKELTALGYTNIY 117
Cdd:cd00158     1 ELKELLDDE-DAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVY 79


                  ....*....
gi 1776941518 118 NF-GAISNW 125
Cdd:cd00158    80 NLeGGMLAW 88
YehR super family cl44134
Uncharacterized lipoprotein YehR, DUF1307 family [Function unknown];
4-37 1.98e-03

Uncharacterized lipoprotein YehR, DUF1307 family [Function unknown];


The actual alignment was detected with superfamily member NF041193:

Pssm-ID: 479601  Cd Length: 190  Bit Score: 36.20  E-value: 1.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1776941518   4 KTKLLLIIVSLTILTGCGFNNESKESNHETPTTS 37
Cdd:NF041193    2 KKILILLGALLLLLTGCGQKKESKASSKSTTKSS 35
 
Name Accession Description Interval E-value
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 38-125 3.87e-33

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 111.62  E-value: 3.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  38 ELQEMINQEsDLVVLDVRTESEYLSGHIPNAILLPYDQISEQAEASLPDKDAKIIVYCHSGRRSAIATKELTALGYTNIY 117
Cdd:cd00158     1 ELKELLDDE-DAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVY 79


                  ....*....
gi 1776941518 118 NF-GAISNW 125
Cdd:cd00158    80 NLeGGMLAW 88
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 35-128 1.74e-32

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 110.44  E-value: 1.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  35 TTSELQEMINQEsDLVVLDVRTESEYLSGHIPNAILLPYDQISEQAEAsLPdKDAKIIVYCHSGRRSAIATKELTALGYT 114
Cdd:COG0607     7 SPAELAELLESE-DAVLLDVREPEEFAAGHIPGAINIPLGELAERLDE-LP-KDKPIVVYCASGGRSAQAAALLRRAGYT 83

                          90
                  ....*....|....*
gi 1776941518 115 NIYNF-GAISNWTSE 128
Cdd:COG0607    84 NVYNLaGGIEAWKAA 98
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 45-128 8.90e-23

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 85.59  E-value: 8.90e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518   45 QESDLVVLDVRTESEYLSGHIPNAILLPYDQISEQA------------EASLPDKDAKIIVYCHSGRRSAIATKELTALG 112
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRgeldilefeellKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90
                   ....*....|....*..
gi 1776941518  113 YTNIYNF-GAISNWTSE 128
Cdd:smart00450  81 FKNVYLLdGGYKEWSAA 97
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 45-125 6.69e-22

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 82.92  E-value: 6.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  45 QESDLVVLDVRTESEYLSGHIPNAILLPYDQISEQAEASLP--------DKDAKIIVYCHSGRRSAIATKELTALGYTNI 116
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLEllekllelLKDKPIVVYCNSGNRAAAAAALLKALGYKNV 81

                          90
                  ....*....|
gi 1776941518 117 YNF-GAISNW 125
Cdd:pfam00581  82 YVLdGGFEAW 91
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
35-128 4.68e-19

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 81.21  E-value: 4.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  35 TTSELQEMinQESDLVVLDVRTESEYLSGHIPNAILLPYDQISEQAEASLPDKDAKIIVYCHSGRRSAIATKELTALGYT 114
Cdd:PRK08762    6 SPAEARAR--AAQGAVLIDVREAHERASGQAEGALRIPRGFLELRIETHLPDRDREIVLICASGTRSAHAAATLRELGYT 83

                          90
                  ....*....|....*
gi 1776941518 115 NIYNF-GAISNWTSE 128
Cdd:PRK08762   84 RVASVaGGFSAWKDA 98
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 47-114 2.85e-05

tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a selenophosphate-dependent tRNA 2-selenouridine synthase, essential for modification of some tRNAs to replace a sulfur atom with selenium. This enzyme works with SelD, the selenium donor protein, which also acts in selenocysteine incorporation. Although the members of this protein family show a fairly deep split, sequences from both sides of the split are supported by co-occurence with, and often proximity to, the selD gene. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274463 [Multi-domain]  Cd Length: 311  Bit Score: 41.81  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  47 SDLVVLDVRTESEYLSGHIPNAILLP-------------YDQ-----------------ISEQAEASLPDKDAK--IIVY 94
Cdd:TIGR03167   1 AFDPLIDVRSPAEFAEGHLPGAINLPllndeeraevgtlYKQvgpfaaiklglalvspnLAAHVEQWRAFADGPpqPLLY 80

                          90       100
                  ....*....|....*....|.
gi 1776941518  95 C-HSGRRSAIATKELTALGYT 114
Cdd:TIGR03167  81 CwRGGMRSGSLAWLLAQIGFR 101
lipo_SP0191 NF041193
SP0191 family lipoprotein;
4-37 1.98e-03

SP0191 family lipoprotein;


Pssm-ID: 469097  Cd Length: 190  Bit Score: 36.20  E-value: 1.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1776941518   4 KTKLLLIIVSLTILTGCGFNNESKESNHETPTTS 37
Cdd:NF041193    2 KKILILLGALLLLLTGCGQKKESKASSKSTTKSS 35
 
Name Accession Description Interval E-value
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 38-125 3.87e-33

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 111.62  E-value: 3.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  38 ELQEMINQEsDLVVLDVRTESEYLSGHIPNAILLPYDQISEQAEASLPDKDAKIIVYCHSGRRSAIATKELTALGYTNIY 117
Cdd:cd00158     1 ELKELLDDE-DAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVY 79


                  ....*....
gi 1776941518 118 NF-GAISNW 125
Cdd:cd00158    80 NLeGGMLAW 88
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 35-128 1.74e-32

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 110.44  E-value: 1.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  35 TTSELQEMINQEsDLVVLDVRTESEYLSGHIPNAILLPYDQISEQAEAsLPdKDAKIIVYCHSGRRSAIATKELTALGYT 114
Cdd:COG0607     7 SPAELAELLESE-DAVLLDVREPEEFAAGHIPGAINIPLGELAERLDE-LP-KDKPIVVYCASGGRSAQAAALLRRAGYT 83

                          90
                  ....*....|....*
gi 1776941518 115 NIYNF-GAISNWTSE 128
Cdd:COG0607    84 NVYNLaGGIEAWKAA 98
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 45-128 8.90e-23

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 85.59  E-value: 8.90e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518   45 QESDLVVLDVRTESEYLSGHIPNAILLPYDQISEQA------------EASLPDKDAKIIVYCHSGRRSAIATKELTALG 112
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRgeldilefeellKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90
                   ....*....|....*..
gi 1776941518  113 YTNIYNF-GAISNWTSE 128
Cdd:smart00450  81 FKNVYLLdGGYKEWSAA 97
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 45-125 6.69e-22

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 82.92  E-value: 6.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  45 QESDLVVLDVRTESEYLSGHIPNAILLPYDQISEQAEASLP--------DKDAKIIVYCHSGRRSAIATKELTALGYTNI 116
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLEllekllelLKDKPIVVYCNSGNRAAAAAALLKALGYKNV 81

                          90
                  ....*....|
gi 1776941518 117 YNF-GAISNW 125
Cdd:pfam00581  82 YVLdGGFEAW 91
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
35-128 4.68e-19

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 81.21  E-value: 4.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  35 TTSELQEMinQESDLVVLDVRTESEYLSGHIPNAILLPYDQISEQAEASLPDKDAKIIVYCHSGRRSAIATKELTALGYT 114
Cdd:PRK08762    6 SPAEARAR--AAQGAVLIDVREAHERASGQAEGALRIPRGFLELRIETHLPDRDREIVLICASGTRSAHAAATLRELGYT 83

                          90
                  ....*....|....*
gi 1776941518 115 NIYNF-GAISNWTSE 128
Cdd:PRK08762   84 RVASVaGGFSAWKDA 98
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 35-125 1.66e-18

Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein 67B2 of Drosophila melanogaster and other similar proteins, many of which are uncharacterized.


Pssm-ID: 238777 [Multi-domain]  Cd Length: 106  Bit Score: 74.61  E-value: 1.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  35 TTSELQEMINQESDLVVLDVRTESEYLSGHIPNAILLPYD------QISEQAEASL-----PDKDAKIIVYCHSGRRSAI 103
Cdd:cd01519     2 SFEEVKNLPNPHPNKVLIDVREPEELKTGKIPGAINIPLSslpdalALSEEEFEKKygfpkPSKDKELIFYCKAGVRSKA 81

                          90       100
                  ....*....|....*....|...
gi 1776941518 104 ATKELTALGYTNIYNF-GAISNW 125
Cdd:cd01519    82 AAELARSLGYENVGNYpGSWLDW 104
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 35-127 8.56e-16

3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 70.97  E-value: 8.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  35 TTSELQEMINQEsDLVVLDVRTESEYL---------SGHIPNAILLPY-------------DQISEQAEASLPDKDAKII 92
Cdd:COG2897   141 DADEVLAALGDP-DAVLVDARSPERYRgevepidprAGHIPGAVNLPWtdlldedgtfksaEELRALFAALGIDPDKPVI 219

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1776941518  93 VYCHSGRRSAIATKELTALGYTNIYNF-GAISNWTS 127
Cdd:COG2897   220 TYCGSGVRAAHTWLALELLGYPNVRLYdGSWSEWGS 255
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 35-128 1.30e-15

Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes uncharacterized putative rhodanese-related domains.


Pssm-ID: 238786 [Multi-domain]  Cd Length: 101  Bit Score: 67.03  E-value: 1.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  35 TTSELQEMINQESD-LVVLDVRTESEYLSGHIPNAILLPYDQISEQAEaSLP--DKDAKIIVYCHSGRRSAIATKELTAL 111
Cdd:cd01528     3 SVAELAEWLADEREePVLIDVREPEELEIAFLPGFLHLPMSEIPERSK-ELDsdNPDKDIVVLCHHGGRSMQVAQWLLRQ 81

                          90
                  ....*....|....*...
gi 1776941518 112 GYTNIYNF-GAISNWTSE 128
Cdd:cd01528    82 GFENVYNLqGGIDAWSLE 99
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 38-125 3.59e-14

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.


Pssm-ID: 238782 [Multi-domain]  Cd Length: 90  Bit Score: 63.05  E-value: 3.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  38 ELQEMINQEsdLVVLDVRTESEYLSGHIPNAILLPYDQISEQAeASLPdKDAKIIVYCHSGRRSAIATKELTALGYtNIY 117
Cdd:cd01524     5 ELDNYRADG--VTLIDVRTPQEFEKGHIKGAINIPLDELRDRL-NELP-KDKEIIVYCAVGLRGYIAARILTQNGF-KVK 79


                  ....*....
gi 1776941518 118 NF-GAISNW 125
Cdd:cd01524    80 NLdGGYKTY 88
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 35-117 4.14e-14

GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine.


Pssm-ID: 238721 [Multi-domain]  Cd Length: 96  Bit Score: 63.05  E-value: 4.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  35 TTSELQEMINQESDLVVLDVRTESEY--LSGHIPNAILL---PYDQISEQAeaslpDKDAKIIVYCHSGRRSAIATKELT 109
Cdd:cd01444     3 SVDELAELLAAGEAPVLLDVRDPASYaaLPDHIPGAIHLdedSLDDWLGDL-----DRDRPVVVYCYHGNSSAQLAQALR 77


                  ....*...
gi 1776941518 110 ALGYTNIY 117
Cdd:cd01444    78 EAGFTDVR 85
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 52-123 5.03e-13

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 60.63  E-value: 5.03e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776941518  52 LDVRTESEYLSGHIPNAILLPYDQISEQAEASLPDKDAKIIVYCHSGRRSAIATKELTALGYTNIYNFGAIS 123
Cdd:PRK10287   24 IDVRVPEQYQQEHVQGAINIPLKEVKERIATAVPDKNDTVKLYCNAGRQSGQAKEILSEMGYTHAENAGGLK 95
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 35-127 1.10e-12

Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the second repeat. Only the second repeat contains the catalytically active Cys residue.


Pssm-ID: 238726 [Multi-domain]  Cd Length: 118  Bit Score: 59.95  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  35 TTSELQEMINQEsDLVVLDVRTESEYL-----------SGHIPNAILLPY-------------DQISEQAEASLPDKDAK 90
Cdd:cd01449     2 TAEEVLANLDSG-DVQLVDARSPERFRgevpeprpglrSGHIPGAVNIPWtslldedgtfkspEELRALFAALGITPDKP 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1776941518  91 IIVYCHSGRRSAIATKELTALGYTNIYN-FGAISNWTS 127
Cdd:cd01449    81 VIVYCGSGVTACVLLLALELLGYKNVRLyDGSWSEWGS 118
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 40-127 2.45e-12

Member of the Rhodanese Homology Domain superfamily. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. Only the second and most of the fourth repeats contain the putative catalytic Cys residue. This CD aligns the 1st , 2nd, 3rd, and 4th repeats.


Pssm-ID: 238787 [Multi-domain]  Cd Length: 96  Bit Score: 58.84  E-value: 2.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  40 QEMINQESDLVVLDVRTESEYLSGHIPNAILLPYDQI----SEQAEASLPDKDAKIIVYCHSGRRSAIATKELTALGYTN 115
Cdd:cd01529     4 DWLGEHEPGTALLDVRAEDEYAAGHLPGKRSIPGAALvlrsQELQALEAPGRATRYVLTCDGSLLARFAAQELLALGGKP 83

                          90
                  ....*....|...
gi 1776941518 116 IYNF-GAISNWTS 127
Cdd:cd01529    84 VALLdGGTSAWVA 96
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 47-125 2.51e-12

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 62.20  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  47 SDLVVLDVRTESEYLSGHIPNAILLPYDQISEQAEASLPDKDAKIIVYCHSGRRSAIATKELTALGYTNIYNF-GAISNW 125
Cdd:PRK05597  273 DGVTLIDVREPSEFAAYSIPGAHNVPLSAIREGANPPSVSAGDEVVVYCAAGVRSAQAVAILERAGYTGMSSLdGGIEGW 352
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
 25-115 5.66e-12

Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 2nd repeat which does contain the putative catalytic Cys residue.


Pssm-ID: 238791 [Multi-domain]  Cd Length: 109  Bit Score: 57.86  E-value: 5.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  25 ESKESNHETP--TTSELQEMINQESDLVVLDVRTESEYLSGHIPNAILLPYDQISEQAEASLPDKDAKIIVYCHSGRRSA 102
Cdd:cd01533     1 ELVEAVRHTPsvSADELAALQARGAPLVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGELAPDPRTPIVVNCAGRTRSI 80

                          90
                  ....*....|...
gi 1776941518 103 IATKELTALGYTN 115
Cdd:cd01533    81 IGAQSLINAGLPN 93
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 33-129 5.96e-12

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 61.26  E-value: 5.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  33 TPTTSELQEMINQESDLVVLDVRTESEYLSGHIPNAILLPYDQI-SEQAEASLPdKDAKIIVYCHSGRRSAIATKELTAL 111
Cdd:PRK07878  288 TITPRELKEWLDSGKKIALIDVREPVEWDIVHIPGAQLIPKSEIlSGEALAKLP-QDRTIVLYCKTGVRSAEALAALKKA 366

                          90
                  ....*....|....*....
gi 1776941518 112 GYTNIYNF-GAISNWTSEL 129
Cdd:PRK07878  367 GFSDAVHLqGGVVAWAKQV 385
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 35-118 5.40e-11

Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative rhodanese-related sulfurtransferases of several uncharacterized proteins.


Pssm-ID: 238780 [Multi-domain]  Cd Length: 117  Bit Score: 55.80  E-value: 5.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  35 TTSELQEMINQESDLVVLDVRTESE-YLSGHIPNAILLPY-------------DQISEQAeaslpDKDAKIIVYCHSGRR 100
Cdd:cd01522     2 TPAEAWALLQADPQAVLVDVRTEAEwKFVGGVPDAVHVAWqvypdmeinpnflAELEEKV-----GKDRPVLLLCRSGNR 76

                          90
                  ....*....|....*...
gi 1776941518 101 SAIATKELTALGYTNIYN 118
Cdd:cd01522    77 SIAAAEAAAQAGFTNVYN 94
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 48-128 1.24e-10

Member of the Rhodanese Homology Domain superfamily. This CD includes the putative rhodanese-like protein, Psp2, of Yersinia pestis biovar Medievalis and other similar uncharacterized proteins.


Pssm-ID: 238779 [Multi-domain]  Cd Length: 110  Bit Score: 54.67  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  48 DLVVLDVRTESEYLSGHIPNAILLPYDQISEQAEASLPdKDAKIIVY-----CHSGRRSAIAtkeLTALGYTNIYNFGAI 122
Cdd:cd01521    25 DFVLVDVRSAEAYARGHVPGAINLPHREICENATAKLD-KEKLFVVYcdgpgCNGATKAALK---LAELGFPVKEMIGGL 100


                  ....*.
gi 1776941518 123 SNWTSE 128
Cdd:cd01521   101 DWWKRE 106
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
35-129 3.24e-10

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 56.28  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  35 TTSELQEMIN-QESDLVVLDVRTESEYLSGHIPNAILLPYDQIsEQAEASLPDKDA----KIIVYCHSGRRSAIATKELT 109
Cdd:PRK07411  285 TVTELKALLDsGADDFVLIDVRNPNEYEIARIPGSVLVPLPDI-ENGPGVEKVKELlnghRLIAHCKMGGRSAKALGILK 363

                          90       100
                  ....*....|....*....|
gi 1776941518 110 ALGYTNIYNFGAISNWTSEL 129
Cdd:PRK07411  364 EAGIEGTNVKGGITAWSREV 383
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 45-125 2.44e-09

Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as a polysulfide binding and transferase domain in anaerobic gram-negative bacteria, functioning in oxidative phosphorylation with polysulfide-sulfur as a terminal electron acceptor. The active site contains the same conserved cysteine that is the catalytic residue in other Rhodanese Homology Domain proteins.


Pssm-ID: 238724 [Multi-domain]  Cd Length: 103  Bit Score: 50.89  E-value: 2.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  45 QESDLVVLDVRTESEY-LSGHIPNAILLPYDQISEQAEASLP------DKDAKIIVYCHSGRRSAIATKELTALGYTNIY 117
Cdd:cd01447    11 GSPGVLLVDVRDPRELeRTGMIPGAFHAPRGMLEFWADPDSPyhkpafAEDKPFVFYCASGWRSALAGKTLQDMGLKPVY 90


                  ....*....
gi 1776941518 118 NF-GAISNW 125
Cdd:cd01447    91 NIeGGFKDW 99
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 33-125 1.63e-08

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, and similar uncharacterized putative rhodanese-related sulfurtransferases.


Pssm-ID: 238785 [Multi-domain]  Cd Length: 99  Bit Score: 48.64  E-value: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  33 TPTTSELQEMINQESDLVvlDVRTESEYLSGHIPNAILLPYDQIsEQAEASLPDKDAkIIVYCHSGRRSAIATKELTALG 112
Cdd:cd01527     3 TISPNDACELLAQGAVLV--DIREPDEYLRERIPGARLVPLSQL-ESEGLPLVGANA-IIFHCRSGMRTQQNAERLAAIS 78

                          90
                  ....*....|....
gi 1776941518 113 YTNIYNF-GAISNW 125
Cdd:cd01527    79 AGEAYVLeGGLDAW 92
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 46-113 1.64e-08

Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 3rd repeat which does not contain the putative catalytic Cys residue.


Pssm-ID: 238792 [Multi-domain]  Cd Length: 95  Bit Score: 48.62  E-value: 1.64e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776941518  46 ESDLVVLDVRTESEYLSGHIPNAILLPYDQISEQAEASLPDKDAKIIVYCHSGRRSAIATKELTALGY 113
Cdd:cd01534    14 DRTVYRFDVRTPEEYEAGHLPGFRHTPGGQLVQETDHFAPVRGARIVLADDDGVRADMTASWLAQMGW 81
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 35-114 2.45e-08

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 48.84  E-value: 2.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  35 TTSELQEMINQESDLVVLDVRTESEYLSGHIPNAILLP--------YDQISEQAEASLPDKDAKIIVYCHSGRRSAIATK 106
Cdd:cd01526    11 SVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPlsellskaAELKSLQELPLDNDKDSPIYVVCRRGNDSQTAVR 90


                  ....*...
gi 1776941518 107 ELTALGYT 114
Cdd:cd01526    91 KLKELGLE 98
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 38-125 7.46e-08

Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with rhodanese-like domains found N-terminal of the metallo-beta-lactamase domain.


Pssm-ID: 238781 [Multi-domain]  Cd Length: 100  Bit Score: 47.10  E-value: 7.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  38 ELQEMINQESDLVVLDVRTESEYLSGHIPNAILLPYD------QISEQAEASLPDKDAKIIVYCHSGRRSAIATKELTAL 111
Cdd:cd01523     5 DLYARLLAGQPLFILDVRNESDYERWKIDGENNTPYFdpyfdfLEIEEDILDQLPDDQEVTVICAKEGSSQFVAELLAER 84

                          90
                  ....*....|....
gi 1776941518 112 GYTNIYNFGAISNW 125
Cdd:cd01523    85 GYDVDYLAGGMKAW 98
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 37-125 1.14e-07

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, Bacillus subtilis YbfQ, and similar uncharacterized proteins.


Pssm-ID: 238776 [Multi-domain]  Cd Length: 101  Bit Score: 46.42  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  37 SELQEMInQESDLVVLDVRTESEYLSGHIPNAILLPYDQISEQ---AEASLPD-KDAKIIVYCHSGRRSAIATKELTALG 112
Cdd:cd01518     7 AEWNELL-EDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFpfwLDENLDLlKGKKVLMYCTGGIRCEKASAYLKERG 85

                          90
                  ....*....|....
gi 1776941518 113 YTNIYNF-GAISNW 125
Cdd:cd01518    86 FKNVYQLkGGILKY 99
PLN02160 PLN02160
thiosulfate sulfurtransferase
 52-121 2.61e-07

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 46.62  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  52 LDVRTESEYLSGH--------IPNAILLPYDQISEQ----AEASLPDKDAKIIVYCHSGRRSAIATKELTALGYTNIYNF 119
Cdd:PLN02160   33 LDVRTQDEFRRGHceaakivnIPYMLNTPQGRVKNQefleQVSSLLNPADDILVGCQSGARSLKATTELVAAGYKKVRNK 112


                  ..
gi 1776941518 120 GA 121
Cdd:PLN02160  113 GG 114
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 35-77 6.94e-07

Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the 1st repeat, which does not contain the catalytically active Cys residue. The role of the 1st repeat is uncertain, but it is believed to be involved in protein interaction.


Pssm-ID: 238725 [Multi-domain]  Cd Length: 122  Bit Score: 44.92  E-value: 6.94e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1776941518  35 TTSELQEMINQEsDLVVLDVRTES-------EYLSGHIPNAILLPYDQIS 77
Cdd:cd01448     3 SPDWLAEHLDDP-DVRILDARWYLpdrdgrkEYLEGHIPGAVFFDLDEDL 51
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
38-117 3.27e-06

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 44.84  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  38 ELQEMINQEsDLVVLDVRTESEYLSGHIPNAILLPYDQISEQ---AEASL-PDKDAKIIVYCHSGRRSAIATKELTALGY 113
Cdd:PRK00142  118 EVNELLDDP-DVVFIDMRNDYEYEIGHFENAIEPDIETFREFppwVEENLdPLKDKKVVMYCTGGIRCEKASAWMKHEGF 196


                  ....
gi 1776941518 114 TNIY 117
Cdd:PRK00142  197 KEVY 200
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 39-89 3.82e-06

3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 44.40  E-value: 3.82e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  39 LQEMINQEsDLVVLDVRT-----ESEYLSGHIPNAILLPYDQ-ISEQAEAS---LPDKDA 89
Cdd:COG2897     1 LAAHLDDP-DVVILDVRWdlpdgRAAYEAGHIPGAVFLDLDTdLSDPRSPGrhpLPSPEA 59
SelU COG2603
tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal ...
 34-113 1.18e-05

tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal structure and biogenesis]; tRNA 2-selenouridine synthase SelU, contains rhodanese domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442015 [Multi-domain]  Cd Length: 341  Bit Score: 43.22  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  34 PTTSELQEMINQESDLVVLDVRTESEYLSGHIPNAILLP-------------YDQISEQA-----------------EAS 83
Cdd:COG2603     2 SKRITLDDFLELLDDDPLIDVRSPVEFAEGHIPGAINLPllddeeraevgtcYKQQGPFAaiklghalvsgklaahrEEA 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1776941518  84 LPDKDA--KIIVYC-HSGRRSAIATKELTALGY 113
Cdd:COG2603    82 WAFAPKhpRPLVYCwRGGLRSGSVAQWLREAGI 114
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 47-113 2.75e-05

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 42.12  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  47 SDLVVLDVRTESEYLSGHIPNAILLP-------------YDQIS--------------------EQAEASLPDKDAKIIV 93
Cdd:PRK11784   14 NDTPLIDVRSPIEFAEGHIPGAINLPllndeeraevgtcYKQQGqfaaialghalvagniaahrEEAWADFPRANPRGLL 93

                          90       100
                  ....*....|....*....|.
gi 1776941518  94 YC-HSGRRSAIATKELTALGY 113
Cdd:PRK11784   94 YCwRGGLRSGSVQQWLKEAGI 114
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 47-114 2.85e-05

tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a selenophosphate-dependent tRNA 2-selenouridine synthase, essential for modification of some tRNAs to replace a sulfur atom with selenium. This enzyme works with SelD, the selenium donor protein, which also acts in selenocysteine incorporation. Although the members of this protein family show a fairly deep split, sequences from both sides of the split are supported by co-occurence with, and often proximity to, the selD gene. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274463 [Multi-domain]  Cd Length: 311  Bit Score: 41.81  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  47 SDLVVLDVRTESEYLSGHIPNAILLP-------------YDQ-----------------ISEQAEASLPDKDAK--IIVY 94
Cdd:TIGR03167   1 AFDPLIDVRSPAEFAEGHLPGAINLPllndeeraevgtlYKQvgpfaaiklglalvspnLAAHVEQWRAFADGPpqPLLY 80

                          90       100
                  ....*....|....*....|.
gi 1776941518  95 C-HSGRRSAIATKELTALGYT 114
Cdd:TIGR03167  81 CwRGGMRSGSLAWLLAQIGFR 101
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
40-117 5.52e-05

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 39.62  E-value: 5.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776941518  40 QEMINQEsDLVVLDVRTESEYLSGHIPNAILLPYDQISE-QAEAslpDKDAKIIVYCHSGRRSAIATKELTALGYTNIY 117
Cdd:PRK00162   13 HQKLQEG-GAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAfMRQA---DFDTPVMVMCYHGNSSQGAAQYLLQQGFDVVY 87
RHOD_YbbB cd01520
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ...
 34-114 1.93e-04

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP /GTP binding proteins including E. coli YbbB.


Pssm-ID: 238778 [Multi-domain]  Cd Length: 128  Bit Score: 38.43  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  34 PTTSELQEMINQESDLVvlDVRTESEYLSGHIPNAILLP-------------YDQ--------------------ISEQA 80
Cdd:cd01520     1 ITAEDLLALRKADGPLI--DVRSPKEFFEGHLPGAINLPllddeeralvgtlYKQqgreaaielglelvsgklkrILNEA 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1776941518  81 EASLPDKDAKIIVYC-HSGRRSAIATKELTALGYT 114
Cdd:cd01520    79 WEARLERDPKLLIYCaRGGMRSQSLAWLLESLGID 113
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 38-111 7.14e-04

Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included in this CD are eukaryotic arsenate resistance proteins such as Saccharomyces cerevisiae Acr2p and similar proteins. Cdc25 phosphatases activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. The Cdc25 and Acr2p RHOD domains have the signature motif (H/YCxxxxxR).


Pssm-ID: 238720 [Multi-domain]  Cd Length: 113  Bit Score: 36.62  E-value: 7.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776941518  38 ELQEMI-----NQESDLVVLDVRtESEYLSGHIPNAILLP----YDQISEQAEASLPDKDAKIIVYCHS--GRRSAIATK 106
Cdd:cd01443     8 ELVALLensdsNAGKDFVVVDLR-RDDYEGGHIKGSINLPaqscYQTLPQVYALFSLAGVKLAIFYCGSsqGRGPRAARW 86


                  ....*
gi 1776941518 107 ELTAL 111
Cdd:cd01443    87 FADYL 91
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 35-95 8.28e-04

Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain superfamily. Included in this CD is the Saccharomyces cerevisiae arsenate reductase protein, Acr2p, and other yeast and plant homologs.


Pssm-ID: 238789 [Multi-domain]  Cd Length: 113  Bit Score: 36.62  E-value: 8.28e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776941518  35 TTSELQEMI-NQESDLVVLDVRTESeYLSGHIPNAILLPYD----QISEQAEASLPDKDAKIIVYC 95
Cdd:cd01531     5 SPAQLKGWIrNGRPPFQVVDVRDED-YAGGHIKGSWHYPSTrfkaQLNQLVQLLSGSKKDTVVFHC 69
lipo_SP0191 NF041193
SP0191 family lipoprotein;
4-37 1.98e-03

SP0191 family lipoprotein;


Pssm-ID: 469097  Cd Length: 190  Bit Score: 36.20  E-value: 1.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1776941518   4 KTKLLLIIVSLTILTGCGFNNESKESNHETPTTS 37
Cdd:NF041193    2 KKILILLGALLLLLTGCGQKKESKASSKSTTKSS 35
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 35-69 2.58e-03

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 35.34  E-value: 2.58e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1776941518  35 TTSELQEMINQ-ESDLVVLDVRTESEYLSGHIPNAI 69
Cdd:cd01446     3 DCAWLAALLREgGERLLLLDCRPFLEYSSSHIRGAV 38
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 33-95 6.18e-03

Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. Cdc25A phosphatase functions to regulate S phase entry and Cdc25B is required for G2/M phase transition of the cell cycle. The Cdc25 domain binds oxyanions at the catalytic site and has the signature motif (H/YCxxxxxR).


Pssm-ID: 238788 [Multi-domain]  Cd Length: 121  Bit Score: 34.12  E-value: 6.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776941518  33 TPTT--SELQ-EMINQESDLVVLDVRTESEYLSGHIPNAILLpYDQisEQAEASLPDKDAK--------IIVYC 95
Cdd:cd01530     5 SPETlaRLLQgKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNL-STK--DELEEFFLDKPGVaskkkrrvLIFHC 75
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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