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Conserved domains on  [gi|935515630|ref|WP_054430543|]
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MULTISPECIES: rhodanese-like domain-containing protein [Achromobacter]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 321-429 5.42e-43

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.


The actual alignment was detected with superfamily member cd01533:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 109  Bit Score: 151.07  E-value: 5.42e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 321 EVIEHEKHTPWIDVDDLHERVARGDDIVVVDSRTPEEFHNFTLPFSHSLPGAELVYRIRELAPDPKTFVVVNCAGRTRSI 400
Cdd:cd01533    1 ELVEAVRHTPSVSADELAALQARGAPLVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGELAPDPRTPIVVNCAGRTRSI 80

                         90       100
                 ....*....|....*....|....*....
gi 935515630 401 VGAQTLIDAGIPNRVASLRNGTMEWLLSG 429
Cdd:cd01533   81 IGAQSLINAGLPNPVAALRNGTQGWTLAG 109
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 15-192 1.51e-31

Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General function prediction only];


:

Pssm-ID: 444296  Cd Length: 179  Bit Score: 121.20  E-value: 1.51e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630  15 DTERARAVRDFIAQVKALVpDPARATPDQLAPVARLLEALGRRAELFPPQAFEVVPGRpTAIYRLAEDADGAYALYLSLG 94
Cdd:COG5553    3 TQRRPPRLRRFIAALRALV-DRGPDEREILAAVRPLLRRLVASDDWLPAEFAEPDPDR-YARYLLYADPDGRFSVVAFVW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630  95 EAGKAQPPHDHTTWAIIAGVSGNERNEVYARSagaePGRDVLTHVRRVDVAAGDSIVLGPS-DVHTIELVDGKPGAHLHF 173
Cdd:COG5553   81 GPGQKTPIHDHGTWGVIGVLRGAEKNTRYRRT----DDGARLEPGGEVVLGPGDVIALSPPgDIHQVENAGDEPAISLHV 156

                        170
                 ....*....|....*....
gi 935515630 174 YGLALDRLHgRVVFESTAG 192
Cdd:COG5553  157 YGGNIGRLV-RFVFDPETG 174
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 467-556 3.53e-29

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.


The actual alignment was detected with superfamily member cd01534:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 95  Bit Score: 111.41  E-value: 3.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 467 IDAATLRAFEAEqGTRTLYKFDVRTREEYETGHLPGWRWAPGGQLVQATDEYLATRRARVVLVDWDGVRAQTTGAWLAQL 546
Cdd:cd01534    1 IGAAELARWAAE-GDRTVYRFDVRTPEEYEAGHLPGFRHTPGGQLVQETDHFAPVRGARIVLADDDGVRADMTASWLAQM 79

                         90
                 ....*....|
gi 935515630 547 GaVEVYLYQP 556
Cdd:cd01534   80 G-WEVYVLEG 88
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 214-301 3.41e-18

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.


The actual alignment was detected with superfamily member cd01532:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 92  Bit Score: 79.84  E-value: 3.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 214 LQEALRGEAEIAVLDVREAGRYARRHLLYAVPAPLWRLEVLADRLVPRRDTRIVLVDDD--ETLAHQAAAKLTRLGWTDI 291
Cdd:cd01532    1 VRQALLAREEIALIDVREEDPFAQSHPLWAANLPLSRLELDAWVRIPRRDTPIVVYGEGggEDLAPRAARRLSELGYTDV 80

                         90
                 ....*....|
gi 935515630 292 SVLAGGTDGW 301
Cdd:cd01532   81 ALLEGGLQGW 90
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 597-725 1.14e-11

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.


The actual alignment was detected with superfamily member cd01535:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 145  Bit Score: 62.91  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 597 LFDIESRLAYERGHVPGARYAAPDRLQEFLPT--DTQRPIVLTSPDGVLAAVAAAELAwRSGRPVSYLLGGTRAWQAQGL 674
Cdd:cd01535   14 VVDVTASANYVKRHIPGAWWVLRAQLAQALEKlpAAERYVLTCGSSLLARFAAADLAA-LTVKPVFVLEGGTAAWIAAGL 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 935515630 675 PLAQGAEGVLTGDDDQSISPYlfDDLSARDQGFRDYLDWELGLVAQLERDG 725
Cdd:cd01535   93 PVESGETRLASPRIDRYRRPY--EGTDNPREAMQAYLDWEFGLVEQLGRDG 141
 
Name Accession Description Interval E-value
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
 321-429 5.42e-43

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: 151.07  E-value: 5.42e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 321 EVIEHEKHTPWIDVDDLHERVARGDDIVVVDSRTPEEFHNFTLPFSHSLPGAELVYRIRELAPDPKTFVVVNCAGRTRSI 400
Cdd:cd01533    1 ELVEAVRHTPSVSADELAALQARGAPLVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGELAPDPRTPIVVNCAGRTRSI 80

                         90       100
                 ....*....|....*....|....*....
gi 935515630 401 VGAQTLIDAGIPNRVASLRNGTMEWLLSG 429
Cdd:cd01533   81 IGAQSLINAGLPNPVAALRNGTQGWTLAG 109
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 15-192 1.51e-31

Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General function prediction only];


Pssm-ID: 444296  Cd Length: 179  Bit Score: 121.20  E-value: 1.51e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630  15 DTERARAVRDFIAQVKALVpDPARATPDQLAPVARLLEALGRRAELFPPQAFEVVPGRpTAIYRLAEDADGAYALYLSLG 94
Cdd:COG5553    3 TQRRPPRLRRFIAALRALV-DRGPDEREILAAVRPLLRRLVASDDWLPAEFAEPDPDR-YARYLLYADPDGRFSVVAFVW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630  95 EAGKAQPPHDHTTWAIIAGVSGNERNEVYARSagaePGRDVLTHVRRVDVAAGDSIVLGPS-DVHTIELVDGKPGAHLHF 173
Cdd:COG5553   81 GPGQKTPIHDHGTWGVIGVLRGAEKNTRYRRT----DDGARLEPGGEVVLGPGDVIALSPPgDIHQVENAGDEPAISLHV 156

                        170
                 ....*....|....*....
gi 935515630 174 YGLALDRLHgRVVFESTAG 192
Cdd:COG5553  157 YGGNIGRLV-RFVFDPETG 174
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 467-556 3.53e-29

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: 111.41  E-value: 3.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 467 IDAATLRAFEAEqGTRTLYKFDVRTREEYETGHLPGWRWAPGGQLVQATDEYLATRRARVVLVDWDGVRAQTTGAWLAQL 546
Cdd:cd01534    1 IGAAELARWAAE-GDRTVYRFDVRTPEEYEAGHLPGFRHTPGGQLVQETDHFAPVRGARIVLADDDGVRADMTASWLAQM 79

                         90
                 ....*....|
gi 935515630 547 GaVEVYLYQP 556
Cdd:cd01534   80 G-WEVYVLEG 88
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 214-301 3.41e-18

Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 1st repeat which does not contain the putative catalytic Cys residue.


Pssm-ID: 238790 [Multi-domain]  Cd Length: 92  Bit Score: 79.84  E-value: 3.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 214 LQEALRGEAEIAVLDVREAGRYARRHLLYAVPAPLWRLEVLADRLVPRRDTRIVLVDDD--ETLAHQAAAKLTRLGWTDI 291
Cdd:cd01532    1 VRQALLAREEIALIDVREEDPFAQSHPLWAANLPLSRLELDAWVRIPRRDTPIVVYGEGggEDLAPRAARRLSELGYTDV 80

                         90
                 ....*....|
gi 935515630 292 SVLAGGTDGW 301
Cdd:cd01532   81 ALLEGGLQGW 90
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 208-308 4.56e-16

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: 74.23  E-value: 4.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 208 RLSPAGLQEALRGEaEIAVLDVREAGRYARRHLLYAVPAPLWRLEVLADRLvpRRDTRIVLVDDDETLAHQAAAKLTRLG 287
Cdd:COG0607    5 EISPAELAELLESE-DAVLLDVREPEEFAAGHIPGAINIPLGELAERLDEL--PKDKPIVVYCASGGRSAQAAALLRRAG 81

                         90       100
                 ....*....|....*....|.
gi 935515630 288 WTDISVLAGGTDGWEREGREL 308
Cdd:COG0607   82 YTNVYNLAGGIEAWKAAGLPV 102
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 330-436 7.56e-16

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: 73.85  E-value: 7.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 330 PWIDVDDLHERVARgDDIVVVDSRTPEEFHNFTLPFSHSLPGAELVYRIRELAPDpKTFVVVnCAGRTRSIVGAQTLIDA 409
Cdd:COG0607    4 KEISPAELAELLES-EDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKD-KPIVVY-CASGGRSAQAAALLRRA 80

                         90       100
                 ....*....|....*....|....*..
gi 935515630 410 GIPNrVASLRNGTMEWLLSGRELAYGR 436
Cdd:COG0607   81 GYTN-VYNLAGGIEAWKAAGLPVEKGK 106
4RHOD_Repeat_4 cd01535
Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative ...
 597-725 1.14e-11

Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 4th repeat which, in general, contains the putative catalytic Cys residue.


Pssm-ID: 238793 [Multi-domain]  Cd Length: 145  Bit Score: 62.91  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 597 LFDIESRLAYERGHVPGARYAAPDRLQEFLPT--DTQRPIVLTSPDGVLAAVAAAELAwRSGRPVSYLLGGTRAWQAQGL 674
Cdd:cd01535   14 VVDVTASANYVKRHIPGAWWVLRAQLAQALEKlpAAERYVLTCGSSLLARFAAADLAA-LTVKPVFVLEGGTAAWIAAGL 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 935515630 675 PLAQGAEGVLTGDDDQSISPYlfDDLSARDQGFRDYLDWELGLVAQLERDG 725
Cdd:cd01535   93 PVESGETRLASPRIDRYRRPY--EGTDNPREAMQAYLDWEFGLVEQLGRDG 141
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 462-552 1.37e-10

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: 58.83  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 462 AGIGHIDAATLRAFEAEQGTRTLykfDVRTREEYETGHLPGWRWAPGGQLVQATDEYLATRraRVVLVDWDGVRAQTTGA 541
Cdd:COG0607    1 ASVKEISPAELAELLESEDAVLL---DVREPEEFAAGHIPGAINIPLGELAERLDELPKDK--PIVVYCASGGRSAQAAA 75

                         90
                 ....*....|.
gi 935515630 542 WLAQLGAVEVY 552
Cdd:COG0607   76 LLRRAGYTNVY 86
cupin_CDO cd10548
cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11. ...
 77-175 2.72e-10

cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11.20), which catalyzes the conversion of cysteine to cysteine sulfinic acid, the first step in the biosynthesis of essential oxidized cysteine metabolites such as sulfate, hypotaurine, and taurine. CDO also plays an important role in the regulation of intracellular cysteine levels in mammals; CDO expression is altered in cancer cells, and abnormal or deficient CDO activity has been linked to Parkinson's disease, Alzheimer's disease, and rheumatoid arthritis. CDO is an iron-dependent thiol dioxygenase that uses molecular oxygen to oxidize the sulfhydryl group of cysteine to generate cysteine sulfinic acid. The CDO active site contains an amino acid-derived cofactor. These enzymes are found in prokaryotes as well as eukaryotes and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380416 [Multi-domain]  Cd Length: 100  Bit Score: 57.70  E-value: 2.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630  77 YRLAEDADgaYALYLSLGEAGKAQPPHDHT-TWAIIAGVSGNERNEVYARSAGAEPGRDvlthvRRVDVAAGDSIVLGPS 155
Cdd:cd10548    4 NLLYRDPD--FELLLLCWPPGQGSPIHDHGgSWCVVKVLEGELTETRYRRPDDGSLSGE-----ETLEETPGDVTYINPD 76

                         90       100
                 ....*....|....*....|.
gi 935515630 156 -DVHTIELVDGKPGAHLHFYG 175
Cdd:cd10548   77 gGIHRVENPSDEPAVSLHLYS 97
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 220-301 3.80e-09

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: 54.41  E-value: 3.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630  220 GEAEIAVLDVREAGRYARRHLLYAVPAPLWRLEVLADRLVP--------RRDTRIVLVDDDETLAHQAAAKLTRLGWTDI 291
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLEllekllelLKDKPIVVYCNSGNRAAAAAALLKALGYKNV 81

                          90
                  ....*....|
gi 935515630  292 SVLAGGTDGW 301
Cdd:pfam00581  82 YVLDGGFEAW 91
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
332-437 7.26e-09

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 58.48  E-value: 7.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 332 IDVDDLHERVARGddIVVVDSRTPEEFHNFTLPFSHSLPGAELVYRIRELAPDPKTFVVVNCAGRTRSIVGAQTLIDAGI 411
Cdd:PRK08762   5 ISPAEARARAAQG--AVLIDVREAHERASGQAEGALRIPRGFLELRIETHLPDRDREIVLICASGTRSAHAAATLRELGY 82

                         90       100
                 ....*....|....*....|....*.
gi 935515630 412 PNrVASLRNGTMEWLLSGRELAYGRQ 437
Cdd:PRK08762  83 TR-VASVAGGFSAWKDAGLPLERPRL 107
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
208-308 8.98e-09

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 58.10  E-value: 8.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 208 RLSPAGLQEALRGEAeiAVLDVREAGRYARRHLLYAVPAPLWRLEVLADRLVPRRDTRIVLVDDDETLAHQAAAKLTRLG 287
Cdd:PRK08762   4 EISPAEARARAAQGA--VLIDVREAHERASGQAEGALRIPRGFLELRIETHLPDRDREIVLICASGTRSAHAAATLRELG 81

                         90       100
                 ....*....|....*....|.
gi 935515630 288 WTDISVLAGGTDGWEREGREL 308
Cdd:PRK08762  82 YTRVASVAGGFSAWKDAGLPL 102
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 487-554 1.66e-07

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: 49.40  E-value: 1.66e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 935515630  487 FDVRTREEYETGHLPG-------WRWAPGGQLVQATDEYLATRRAR-VVLVDWDGVRAQTTGAWLAQLGAVEVYLY 554
Cdd:pfam00581   9 IDVRPPEEYAKGHIPGavnvplsSLSLPPLPLLELLEKLLELLKDKpIVVYCNSGNRAAAAAALLKALGYKNVYVL 84
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 220-307 4.07e-07

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: 48.61  E-value: 4.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630   220 GEAEIAVLDVREAGRYARRHLLYAVPAPL------------WRLEVLADRLVPRRDTRIVLVDDDETLAHQAAAKLTRLG 287
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLselldrrgeldiLEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 935515630   288 WTDISVLAGGTDGWEREGRE 307
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAGPP 100
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 591-679 2.54e-06

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: 46.50  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 591 DAGAAELFDIESRLAYERGHVPGARYAAPDRLQEFLPT-DTQRPIVLTSPDGvlaavaaaelaWRSGR-----------P 658
Cdd:COG0607   16 ESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDElPKDKPIVVYCASG-----------GRSAQaaallrragytN 84

                         90       100
                 ....*....|....*....|.
gi 935515630 659 VSYLLGGTRAWQAQGLPLAQG 679
Cdd:COG0607   85 VYNLAGGIEAWKAAGLPVEKG 105
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 344-425 9.43e-06

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: 44.78  E-value: 9.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630  344 GDDIVVVDSRTPEEFHNFTLPFSHSLPGAELVYRIRELAPDPKTF--------VVVNCAGRTRSIVGAQTLIDAGIPNrV 415
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLlellkdkpIVVYCNSGNRAAAAAALLKALGYKN-V 81

                          90
                  ....*....|
gi 935515630  416 ASLRNGTMEW 425
Cdd:pfam00581  82 YVLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 488-555 1.52e-04

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: 41.29  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630   488 DVRTREEYETGHLPG--------WRWAPGGQLVQATDEYL----ATRRARVVLVDWDGVRAQTTGAWLAQLGAVEVYLYQ 555
Cdd:smart00450   9 DVRSPEEYEGGHIPGavniplseLLDRRGELDILEFEELLkrlgLDKDKPVVVYCRSGNRSAKAAWLLRELGFKNVYLLD 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 591-670 4.42e-04

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: 39.77  E-value: 4.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630  591 DAGAAELFDIESRLAYERGHVPGARYAAPDRL-----------QEFLPTDTQRPIVLTSPDGVLAAVAAAELAWRSGRPV 659
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLslpplpllellEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNV 81

                          90
                  ....*....|.
gi 935515630  660 SYLLGGTRAWQ 670
Cdd:pfam00581  82 YVLDGGFEAWK 92
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 344-431 4.25e-03

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: 37.44  E-value: 4.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630   344 GDDIVVVDSRTPEEF---H-----NFTLP----FSHSLPGAELVYRIRELAPDPKTFVVVNCAGRTRSIVGAQTLIDAGI 411
Cdd:smart00450   2 DEKVVLLDVRSPEEYeggHipgavNIPLSelldRRGELDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81

                           90       100
                   ....*....|....*....|
gi 935515630   412 PNrVASLRNGTMEWLLSGRE 431
Cdd:smart00450  82 KN-VYLLDGGYKEWSAAGPP 100
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
488-552 6.83e-03

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 39.61  E-value: 6.83e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 935515630 488 DVRTREEYETGHLPGWRWAPGGQLVQATDEYLATRRARVVLVDWDGVRAQTTGAWLAQLGAVEVY 552
Cdd:PRK08762  22 DVREAHERASGQAEGALRIPRGFLELRIETHLPDRDREIVLICASGTRSAHAAATLRELGYTRVA 86
 
Name Accession Description Interval E-value
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
 321-429 5.42e-43

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: 151.07  E-value: 5.42e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 321 EVIEHEKHTPWIDVDDLHERVARGDDIVVVDSRTPEEFHNFTLPFSHSLPGAELVYRIRELAPDPKTFVVVNCAGRTRSI 400
Cdd:cd01533    1 ELVEAVRHTPSVSADELAALQARGAPLVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGELAPDPRTPIVVNCAGRTRSI 80

                         90       100
                 ....*....|....*....|....*....
gi 935515630 401 VGAQTLIDAGIPNRVASLRNGTMEWLLSG 429
Cdd:cd01533   81 IGAQSLINAGLPNPVAALRNGTQGWTLAG 109
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 15-192 1.51e-31

Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General function prediction only];


Pssm-ID: 444296  Cd Length: 179  Bit Score: 121.20  E-value: 1.51e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630  15 DTERARAVRDFIAQVKALVpDPARATPDQLAPVARLLEALGRRAELFPPQAFEVVPGRpTAIYRLAEDADGAYALYLSLG 94
Cdd:COG5553    3 TQRRPPRLRRFIAALRALV-DRGPDEREILAAVRPLLRRLVASDDWLPAEFAEPDPDR-YARYLLYADPDGRFSVVAFVW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630  95 EAGKAQPPHDHTTWAIIAGVSGNERNEVYARSagaePGRDVLTHVRRVDVAAGDSIVLGPS-DVHTIELVDGKPGAHLHF 173
Cdd:COG5553   81 GPGQKTPIHDHGTWGVIGVLRGAEKNTRYRRT----DDGARLEPGGEVVLGPGDVIALSPPgDIHQVENAGDEPAISLHV 156

                        170
                 ....*....|....*....
gi 935515630 174 YGLALDRLHgRVVFESTAG 192
Cdd:COG5553  157 YGGNIGRLV-RFVFDPETG 174
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 467-556 3.53e-29

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: 111.41  E-value: 3.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 467 IDAATLRAFEAEqGTRTLYKFDVRTREEYETGHLPGWRWAPGGQLVQATDEYLATRRARVVLVDWDGVRAQTTGAWLAQL 546
Cdd:cd01534    1 IGAAELARWAAE-GDRTVYRFDVRTPEEYEAGHLPGFRHTPGGQLVQETDHFAPVRGARIVLADDDGVRADMTASWLAQM 79

                         90
                 ....*....|
gi 935515630 547 GaVEVYLYQP 556
Cdd:cd01534   80 G-WEVYVLEG 88
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 214-301 3.41e-18

Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 1st repeat which does not contain the putative catalytic Cys residue.


Pssm-ID: 238790 [Multi-domain]  Cd Length: 92  Bit Score: 79.84  E-value: 3.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 214 LQEALRGEAEIAVLDVREAGRYARRHLLYAVPAPLWRLEVLADRLVPRRDTRIVLVDDD--ETLAHQAAAKLTRLGWTDI 291
Cdd:cd01532    1 VRQALLAREEIALIDVREEDPFAQSHPLWAANLPLSRLELDAWVRIPRRDTPIVVYGEGggEDLAPRAARRLSELGYTDV 80

                         90
                 ....*....|
gi 935515630 292 SVLAGGTDGW 301
Cdd:cd01532   81 ALLEGGLQGW 90
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 208-308 4.56e-16

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: 74.23  E-value: 4.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 208 RLSPAGLQEALRGEaEIAVLDVREAGRYARRHLLYAVPAPLWRLEVLADRLvpRRDTRIVLVDDDETLAHQAAAKLTRLG 287
Cdd:COG0607    5 EISPAELAELLESE-DAVLLDVREPEEFAAGHIPGAINIPLGELAERLDEL--PKDKPIVVYCASGGRSAQAAALLRRAG 81

                         90       100
                 ....*....|....*....|.
gi 935515630 288 WTDISVLAGGTDGWEREGREL 308
Cdd:COG0607   82 YTNVYNLAGGIEAWKAAGLPV 102
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 330-436 7.56e-16

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: 73.85  E-value: 7.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 330 PWIDVDDLHERVARgDDIVVVDSRTPEEFHNFTLPFSHSLPGAELVYRIRELAPDpKTFVVVnCAGRTRSIVGAQTLIDA 409
Cdd:COG0607    4 KEISPAELAELLES-EDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKD-KPIVVY-CASGGRSAQAAALLRRA 80

                         90       100
                 ....*....|....*....|....*..
gi 935515630 410 GIPNrVASLRNGTMEWLLSGRELAYGR 436
Cdd:COG0607   81 GYTN-VYNLAGGIEAWKAAGLPVEKGK 106
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 217-302 5.15e-15

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: 70.79  E-value: 5.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 217 ALRGEAEIAVLDVREAGRYARRHLLYAVPAPLWRLEVLADRLVPRRDTRIVLVDDDETLAHQAAAKLTRLGWTDISVLAG 296
Cdd:cd00158    4 ELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLEG 83


                 ....*.
gi 935515630 297 GTDGWE 302
Cdd:cd00158   84 GMLAWK 89
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 336-427 5.93e-14

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: 68.09  E-value: 5.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 336 DLHERVARgddivVVDSRTPEEFHNFTLPFSHSLPGAELVYRIREL----APDPKTFVVVNCAGRTRSIVGAQTLIDAGI 411
Cdd:cd01529    7 GEHEPGTA-----LLDVRAEDEYAAGHLPGKRSIPGAALVLRSQELqaleAPGRATRYVLTCDGSLLARFAAQELLALGG 81

                         90
                 ....*....|....*.
gi 935515630 412 PNrVASLRNGTMEWLL 427
Cdd:cd01529   82 KP-VALLDGGTSAWVA 96
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 336-425 3.32e-12

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: 62.70  E-value: 3.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 336 DLHERVaRGDDIVVVDSRTPEEFHNFTLPFSHSLPGAELVYRIRELAPDPKTFVVVNCAGRTRSIVGAQTLIDAGIPNrV 415
Cdd:cd00158    1 ELKELL-DDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTN-V 78

                         90
                 ....*....|
gi 935515630 416 ASLRNGTMEW 425
Cdd:cd00158   79 YNLEGGMLAW 88
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 215-301 7.15e-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: 62.31  E-value: 7.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 215 QEALRGEAEIAVLDVREAGRYARRHLLYAVPAP-----LWRLEVLADRlVPRRDTRIVLVDDDETLAHQAAAKLTRLGWT 289
Cdd:cd01529    4 DWLGEHEPGTALLDVRAEDEYAAGHLPGKRSIPgaalvLRSQELQALE-APGRATRYVLTCDGSLLARFAAQELLALGGK 82

                         90
                 ....*....|..
gi 935515630 290 DISVLAGGTDGW 301
Cdd:cd01529   83 PVALLDGGTSAW 94
4RHOD_Repeat_4 cd01535
Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative ...
 597-725 1.14e-11

Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 4th repeat which, in general, contains the putative catalytic Cys residue.


Pssm-ID: 238793 [Multi-domain]  Cd Length: 145  Bit Score: 62.91  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 597 LFDIESRLAYERGHVPGARYAAPDRLQEFLPT--DTQRPIVLTSPDGVLAAVAAAELAwRSGRPVSYLLGGTRAWQAQGL 674
Cdd:cd01535   14 VVDVTASANYVKRHIPGAWWVLRAQLAQALEKlpAAERYVLTCGSSLLARFAAADLAA-LTVKPVFVLEGGTAAWIAAGL 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 935515630 675 PLAQGAEGVLTGDDDQSISPYlfDDLSARDQGFRDYLDWELGLVAQLERDG 725
Cdd:cd01535   93 PVESGETRLASPRIDRYRRPY--EGTDNPREAMQAYLDWEFGLVEQLGRDG 141
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 476-553 5.48e-11

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: 59.61  E-value: 5.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 476 EAEQGT--RTLYKFDVRTREEYETGHLPGWRWAPGGQLVQATDEYLAT----RRARVVLVDWDGVRAQTTGAWLAQLGAV 549
Cdd:cd01529    3 ADWLGEhePGTALLDVRAEDEYAAGHLPGKRSIPGAALVLRSQELQALeapgRATRYVLTCDGSLLARFAAQELLALGGK 82


                 ....
gi 935515630 550 EVYL 553
Cdd:cd01529   83 PVAL 86
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 462-552 1.37e-10

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: 58.83  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 462 AGIGHIDAATLRAFEAEQGTRTLykfDVRTREEYETGHLPGWRWAPGGQLVQATDEYLATRraRVVLVDWDGVRAQTTGA 541
Cdd:COG0607    1 ASVKEISPAELAELLESEDAVLL---DVREPEEFAAGHIPGAINIPLGELAERLDELPKDK--PIVVYCASGGRSAQAAA 75

                         90
                 ....*....|.
gi 935515630 542 WLAQLGAVEVY 552
Cdd:COG0607   76 LLRRAGYTNVY 86
cupin_CDO cd10548
cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11. ...
 77-175 2.72e-10

cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11.20), which catalyzes the conversion of cysteine to cysteine sulfinic acid, the first step in the biosynthesis of essential oxidized cysteine metabolites such as sulfate, hypotaurine, and taurine. CDO also plays an important role in the regulation of intracellular cysteine levels in mammals; CDO expression is altered in cancer cells, and abnormal or deficient CDO activity has been linked to Parkinson's disease, Alzheimer's disease, and rheumatoid arthritis. CDO is an iron-dependent thiol dioxygenase that uses molecular oxygen to oxidize the sulfhydryl group of cysteine to generate cysteine sulfinic acid. The CDO active site contains an amino acid-derived cofactor. These enzymes are found in prokaryotes as well as eukaryotes and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380416 [Multi-domain]  Cd Length: 100  Bit Score: 57.70  E-value: 2.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630  77 YRLAEDADgaYALYLSLGEAGKAQPPHDHT-TWAIIAGVSGNERNEVYARSAGAEPGRDvlthvRRVDVAAGDSIVLGPS 155
Cdd:cd10548    4 NLLYRDPD--FELLLLCWPPGQGSPIHDHGgSWCVVKVLEGELTETRYRRPDDGSLSGE-----ETLEETPGDVTYINPD 76

                         90       100
                 ....*....|....*....|.
gi 935515630 156 -DVHTIELVDGKPGAHLHFYG 175
Cdd:cd10548   77 gGIHRVENPSDEPAVSLHLYS 97
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 214-358 1.83e-09

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 59.03  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 214 LQEALrGEAEIAVLDVRE---AGR--YARRHL---LYA------------VPAPLWRLEVLADRL----VpRRDTRIVLV 269
Cdd:COG2897    1 LAAHL-DDPDVVILDVRWdlpDGRaaYEAGHIpgaVFLdldtdlsdprspGRHPLPSPEAFAALLgalgI-SNDTTVVVY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 270 DDDetlAHQAAAK----LTRLGWTDISVLAGGTDGWEREGRELFSGTNVPSKafGEVIEHEKHTPWIDVDDLHERVARGd 345
Cdd:COG2897   79 DDG---GGLFAARawwlLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAP--GDFTARPDPELLADADEVLAALGDP- 152

                        170
                 ....*....|...
gi 935515630 346 DIVVVDSRTPEEF 358
Cdd:COG2897  153 DAVLVDARSPERY 165
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 220-301 3.80e-09

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: 54.41  E-value: 3.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630  220 GEAEIAVLDVREAGRYARRHLLYAVPAPLWRLEVLADRLVP--------RRDTRIVLVDDDETLAHQAAAKLTRLGWTDI 291
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLEllekllelLKDKPIVVYCNSGNRAAAAAALLKALGYKNV 81

                          90
                  ....*....|
gi 935515630  292 SVLAGGTDGW 301
Cdd:pfam00581  82 YVLDGGFEAW 91
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
332-437 7.26e-09

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 58.48  E-value: 7.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 332 IDVDDLHERVARGddIVVVDSRTPEEFHNFTLPFSHSLPGAELVYRIRELAPDPKTFVVVNCAGRTRSIVGAQTLIDAGI 411
Cdd:PRK08762   5 ISPAEARARAAQG--AVLIDVREAHERASGQAEGALRIPRGFLELRIETHLPDRDREIVLICASGTRSAHAAATLRELGY 82

                         90       100
                 ....*....|....*....|....*.
gi 935515630 412 PNrVASLRNGTMEWLLSGRELAYGRQ 437
Cdd:PRK08762  83 TR-VASVAGGFSAWKDAGLPLERPRL 107
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
208-308 8.98e-09

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 58.10  E-value: 8.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 208 RLSPAGLQEALRGEAeiAVLDVREAGRYARRHLLYAVPAPLWRLEVLADRLVPRRDTRIVLVDDDETLAHQAAAKLTRLG 287
Cdd:PRK08762   4 EISPAEARARAAQGA--VLIDVREAHERASGQAEGALRIPRGFLELRIETHLPDRDREIVLICASGTRSAHAAATLRELG 81

                         90       100
                 ....*....|....*....|.
gi 935515630 288 WTDISVLAGGTDGWEREGREL 308
Cdd:PRK08762  82 YTRVASVAGGFSAWKDAGLPL 102
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 488-555 6.20e-08

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: 50.76  E-value: 6.20e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 935515630 488 DVRTREEYETGHLPGWRWAPGGQLVQATDEYLATRRARVVLVDWDGVRAQTTGAWLAQLGAVEVYLYQ 555
Cdd:cd00158   15 DVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLE 82
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 220-301 8.62e-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: 50.54  E-value: 8.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 220 GEAEIAVLDVREAGRYARRHLLYAVPAPLWRLEVLADRLVPRRDTRIVLVDDDETLAHQAAAKLTRLGWtDISVLAGGTD 299
Cdd:cd01534   13 GDRTVYRFDVRTPEEYEAGHLPGFRHTPGGQLVQETDHFAPVRGARIVLADDDGVRADMTASWLAQMGW-EVYVLEGGLA 91


                 ..
gi 935515630 300 GW 301
Cdd:cd01534   92 AA 93
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 487-554 1.66e-07

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: 49.40  E-value: 1.66e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 935515630  487 FDVRTREEYETGHLPG-------WRWAPGGQLVQATDEYLATRRAR-VVLVDWDGVRAQTTGAWLAQLGAVEVYLY 554
Cdd:pfam00581   9 IDVRPPEEYAKGHIPGavnvplsSLSLPPLPLLELLEKLLELLKDKpIVVYCNSGNRAAAAAALLKALGYKNVYVL 84
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 220-307 4.07e-07

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: 48.61  E-value: 4.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630   220 GEAEIAVLDVREAGRYARRHLLYAVPAPL------------WRLEVLADRLVPRRDTRIVLVDDDETLAHQAAAKLTRLG 287
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLselldrrgeldiLEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 935515630   288 WTDISVLAGGTDGWEREGRE 307
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAGPP 100
4RHOD_Repeat_4 cd01535
Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative ...
 214-315 1.67e-06

Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 4th repeat which, in general, contains the putative catalytic Cys residue.


Pssm-ID: 238793 [Multi-domain]  Cd Length: 145  Bit Score: 48.27  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 214 LQEALRGEAEIAVLDVREAGRYARRHLlyavPAPLWRLEV-LADRL--VPRRDtRIVLVDDDETLAHQAAAKLTRLGWTD 290
Cdd:cd01535    2 LAAWLGEGGQTAVVDVTASANYVKRHI----PGAWWVLRAqLAQALekLPAAE-RYVLTCGSSLLARFAAADLAALTVKP 76

                         90       100
                 ....*....|....*....|....*
gi 935515630 291 ISVLAGGTDGWEREGRELFSGTNVP 315
Cdd:cd01535   77 VFVLEGGTAAWIAAGLPVESGETRL 101
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 591-679 2.54e-06

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: 46.50  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 591 DAGAAELFDIESRLAYERGHVPGARYAAPDRLQEFLPT-DTQRPIVLTSPDGvlaavaaaelaWRSGR-----------P 658
Cdd:COG0607   16 ESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDElPKDKPIVVYCASG-----------GRSAQaaallrragytN 84

                         90       100
                 ....*....|....*....|.
gi 935515630 659 VSYLLGGTRAWQAQGLPLAQG 679
Cdd:COG0607   85 VYNLAGGIEAWKAAGLPVEKG 105
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 314-426 3.35e-06

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 49.87  E-value: 3.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 314 VPSKAFGEVIEHEKHTPWIDVDDLHERVARGDDIVVVDSRTPEEFHNFTLPFSHSLPGAELVYRIRELAPDPKTFVVVNC 393
Cdd:PRK05597 242 VLERVRGSTPVHGISGGFGEVLDVPRVSALPDGVTLIDVREPSEFAAYSIPGAHNVPLSAIREGANPPSVSAGDEVVVYC 321

                         90       100       110
                 ....*....|....*....|....*....|...
gi 935515630 394 AGRTRSIVGAQTLIDAGIPNrVASLRNGTMEWL 426
Cdd:PRK05597 322 AAGVRSAQAVAILERAGYTG-MSSLDGGIEGWL 353
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 344-425 9.43e-06

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: 44.78  E-value: 9.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630  344 GDDIVVVDSRTPEEFHNFTLPFSHSLPGAELVYRIRELAPDPKTF--------VVVNCAGRTRSIVGAQTLIDAGIPNrV 415
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLlellkdkpIVVYCNSGNRAAAAAALLKALGYKN-V 81

                          90
                  ....*....|
gi 935515630  416 ASLRNGTMEW 425
Cdd:pfam00581  82 YVLDGGFEAW 91
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 205-308 1.05e-05

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: 45.04  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 205 YHARLS----PAGLQEALRGEAE-IAVLDVREAGRYARRHLLYAVPAPLWRLEVLADRLVPRRDTRIVLVDDDE-TLAHQ 278
Cdd:cd01521    2 FEAKLAfetdCWDVAIALKNGKPdFVLVDVRSAEAYARGHVPGAINLPHREICENATAKLDKEKLFVVYCDGPGcNGATK 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 935515630 279 AAAKLTRLGWtDISVLAGGTDGWEREGREL 308
Cdd:cd01521   82 AALKLAELGF-PVKEMIGGLDWWKREGYAT 110
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 488-555 1.52e-04

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: 41.29  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630   488 DVRTREEYETGHLPG--------WRWAPGGQLVQATDEYL----ATRRARVVLVDWDGVRAQTTGAWLAQLGAVEVYLYQ 555
Cdd:smart00450   9 DVRSPEEYEGGHIPGavniplseLLDRRGELDILEFEELLkrlgLDKDKPVVVYCRSGNRSAKAAWLLRELGFKNVYLLD 88
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 208-303 2.97e-04

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: 40.32  E-value: 2.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 208 RLSPAGLQEALRGEAEIAVLDVR--EAGRYARRHLLYAVPAPLWRLEVLADRLvpRRDTRIVLVDDDETLAHQAAAKLTR 285
Cdd:cd01444    1 RISVDELAELLAAGEAPVLLDVRdpASYAALPDHIPGAIHLDEDSLDDWLGDL--DRDRPVVVYCYHGNSSAQLAQALRE 78

                         90
                 ....*....|....*...
gi 935515630 286 LGWTDISVLAGGTDGWER 303
Cdd:cd01444   79 AGFTDVRSLAGGFEAWRR 96
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 591-670 4.42e-04

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: 39.77  E-value: 4.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630  591 DAGAAELFDIESRLAYERGHVPGARYAAPDRL-----------QEFLPTDTQRPIVLTSPDGVLAAVAAAELAWRSGRPV 659
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLslpplpllellEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNV 81

                          90
                  ....*....|.
gi 935515630  660 SYLLGGTRAWQ 670
Cdd:pfam00581  82 YVLDGGFEAWK 92
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 332-395 1.07e-03

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: 39.26  E-value: 1.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 935515630 332 IDVDDLHERVARGD-DIVVVDSRTPEEFHNFTLPFSHSLPGAELVYRIRELAPDPKTFVVVnCAG 395
Cdd:cd01521   10 TDCWDVAIALKNGKpDFVLVDVRSAEAYARGHVPGAINLPHREICENATAKLDKEKLFVVY-CDG 73
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 332-425 1.91e-03

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: 38.01  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630 332 IDVDDLHERVARGDDIVVVDSRTPEEFhnfTLPFSHsLPGAeLVYRIRELA-----PDPKTFVVVNCAGRTRSIVGAQTL 406
Cdd:cd01444    2 ISVDELAELLAAGEAPVLLDVRDPASY---AALPDH-IPGA-IHLDEDSLDdwlgdLDRDRPVVVYCYHGNSSAQLAQAL 76

                         90
                 ....*....|....*....
gi 935515630 407 IDAGIPNrVASLRNGTMEW 425
Cdd:cd01444   77 REAGFTD-VRSLAGGFEAW 94
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 344-431 4.25e-03

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: 37.44  E-value: 4.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 935515630   344 GDDIVVVDSRTPEEF---H-----NFTLP----FSHSLPGAELVYRIRELAPDPKTFVVVNCAGRTRSIVGAQTLIDAGI 411
Cdd:smart00450   2 DEKVVLLDVRSPEEYeggHipgavNIPLSelldRRGELDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81

                           90       100
                   ....*....|....*....|
gi 935515630   412 PNrVASLRNGTMEWLLSGRE 431
Cdd:smart00450  82 KN-VYLLDGGYKEWSAAGPP 100
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
488-552 6.83e-03

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 39.61  E-value: 6.83e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 935515630 488 DVRTREEYETGHLPGWRWAPGGQLVQATDEYLATRRARVVLVDWDGVRAQTTGAWLAQLGAVEVY 552
Cdd:PRK08762  22 DVREAHERASGQAEGALRIPRGFLELRIETHLPDRDREIVLICASGTRSAHAAATLRELGYTRVA 86
 
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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