NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490376239|ref|WP_004255839|]
View 

MULTISPECIES: rhodanese-related sulfurtransferase [Providencia]

Protein Classification

tRNA uridine(34) hydroxylase( domain architecture ID 11478196)

tRNA uridine(34) hydroxylase catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs

CATH:  3.40.250.10
EC:  1.14.-.-
Gene Ontology:  GO:0016705|GO:0006400
PubMed:  12151332
SCOP:  4000452

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
22-337 2.30e-177

rhodanese-related sulfurtransferase;


:

Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 493.98  E-value: 2.30e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239  22 EPRTTISFYKYFNIQDPNEFRNQWYQQFKALSVFGRVYIAKEGINAQISVPESNVGALRELIYAtDPALDNLRLNIAiDD 101
Cdd:PRK00142   2 KPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKA-DPRFADIRFKIS-ED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 102 DGKSFWVLRMKVRERVVADGIEDETFNPANTGQYLKAHEVNEMIDDPNTVFVDMRNHYEYEVGRFDNAIEIPSDTFREQL 181
Cdd:PRK00142  80 DGHAFPRLSVKVRKEIVALGLDDDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 182 PMAVEMLQEQKDKNVVMYCTGGIRCEKASAYMLHNGFKNVYHVEGGIIEYARKAKEQGlpLRFKGKNFVFDNRMGERITE 261
Cdd:PRK00142 160 PWVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQG--LLWDGKLYVFDERMAVPIND 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490376239 262 -DTLAQCHQCGAPCDTHTNCRNDGCHLLFIQCPSCAEKYEGCCSSSCTEEMKLPEQEQRARRAGREVSNKIFNKSRH 337
Cdd:PRK00142 238 eVPIGHCHQCGTPCDRYVNCANPACNLLILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLIFNKERH 314
 
Name Accession Description Interval E-value
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
22-337 2.30e-177

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 493.98  E-value: 2.30e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239  22 EPRTTISFYKYFNIQDPNEFRNQWYQQFKALSVFGRVYIAKEGINAQISVPESNVGALRELIYAtDPALDNLRLNIAiDD 101
Cdd:PRK00142   2 KPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKA-DPRFADIRFKIS-ED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 102 DGKSFWVLRMKVRERVVADGIEDETFNPANTGQYLKAHEVNEMIDDPNTVFVDMRNHYEYEVGRFDNAIEIPSDTFREQL 181
Cdd:PRK00142  80 DGHAFPRLSVKVRKEIVALGLDDDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 182 PMAVEMLQEQKDKNVVMYCTGGIRCEKASAYMLHNGFKNVYHVEGGIIEYARKAKEQGlpLRFKGKNFVFDNRMGERITE 261
Cdd:PRK00142 160 PWVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQG--LLWDGKLYVFDERMAVPIND 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490376239 262 -DTLAQCHQCGAPCDTHTNCRNDGCHLLFIQCPSCAEKYEGCCSSSCTEEMKLPEQEQRARRAGREVSNKIFNKSRH 337
Cdd:PRK00142 238 eVPIGHCHQCGTPCDRYVNCANPACNLLILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLIFNKERH 314
TrhO COG1054
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ...
 22-326 1.88e-161

tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440674 [Multi-domain]  Cd Length: 304  Bit Score: 453.44  E-value: 1.88e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239  22 EPRTTISFYKYFNIQDPNEFRNQWYQQFKALSVFGRVYIAKEGINAQISVPESNVGALRELIYAtDPALDNLRLNIAiDD 101
Cdd:COG1054    2 KPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRA-DPRFADLEFKES-EA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 102 DGKSFWVLRMKVRERVVADGIEDetFNP-ANTGQYLKAHEVNEMIDDPNTVFVDMRNHYEYEVGRFDNAIEIPSDTFREQ 180
Cdd:COG1054   80 DGHPFPRLKVKLKKEIVTMGLPD--VDPnEGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFREF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 181 LPMAVEMLQEQKDKNVVMYCTGGIRCEKASAYMLHNGFKNVYHVEGGIIEYARKAKEQGlpLRFKGKNFVFDNRMGERI- 259
Cdd:COG1054  158 PEWVEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEG--SLWEGECFVFDERVAVDHn 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490376239 260 -TEDTLAQCHQCGAPCDTHTNCRNDGCHLLFIQCPSCAEKYEgCCSSSCTEEMKLPEQEQRARRAGRE 326
Cdd:COG1054  236 lEPGVIGLCHACGTPCDRYVNCANDPCYELGVSCPHCADKYE-CCSDECTEEQRARYERQRQLRLAKE 302
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 133-233 1.19e-54

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: 174.30  E-value: 1.19e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 133 GQYLKAHEVNEMIDDPNTVFVDMRNHYEYEVGRFDNAIEIPSDTFREQLPMAVEMLQEQKDKNVVMYCTGGIRCEKASAY 212
Cdd:cd01518    1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80

                         90       100
                 ....*....|....*....|.
gi 490376239 213 MLHNGFKNVYHVEGGIIEYAR 233
Cdd:cd01518   81 LKERGFKNVYQLKGGILKYLE 101
Rhodanese_C pfam12368
Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some ...
 245-308 2.72e-30

Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some members of the Rhodanase family. Rhodanase is pfam00581.


Pssm-ID: 463552 [Multi-domain]  Cd Length: 66  Bit Score: 110.10  E-value: 2.72e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490376239  245 KGKNFVFDNRM--GERITEDTLAQCHQCGAPCDTHTNCRNDGCHLLFIQCPSCAEKYEGCCSSSCT 308
Cdd:pfam12368   1 KGKLFVFDERLavVEPSDDDVIGKCYHCGKPCDRYVNCANPDCNRLFLQCEECAEKYEGCCSEECA 66
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 146-237 2.89e-21

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: 87.13  E-value: 2.89e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239   146 DDPNTVFVDMRNHYEYEVGRFDNAIEIPSDTFREQLPMAVEMLQEQ--------KDKNVVMYCTGGIRCEKASAYMLHNG 217
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEEllkrlgldKDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 490376239   218 FKNVYHVEGGIIEYARKAKE 237
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAGPP 100
 
Name Accession Description Interval E-value
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
22-337 2.30e-177

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 493.98  E-value: 2.30e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239  22 EPRTTISFYKYFNIQDPNEFRNQWYQQFKALSVFGRVYIAKEGINAQISVPESNVGALRELIYAtDPALDNLRLNIAiDD 101
Cdd:PRK00142   2 KPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKA-DPRFADIRFKIS-ED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 102 DGKSFWVLRMKVRERVVADGIEDETFNPANTGQYLKAHEVNEMIDDPNTVFVDMRNHYEYEVGRFDNAIEIPSDTFREQL 181
Cdd:PRK00142  80 DGHAFPRLSVKVRKEIVALGLDDDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 182 PMAVEMLQEQKDKNVVMYCTGGIRCEKASAYMLHNGFKNVYHVEGGIIEYARKAKEQGlpLRFKGKNFVFDNRMGERITE 261
Cdd:PRK00142 160 PWVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQG--LLWDGKLYVFDERMAVPIND 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490376239 262 -DTLAQCHQCGAPCDTHTNCRNDGCHLLFIQCPSCAEKYEGCCSSSCTEEMKLPEQEQRARRAGREVSNKIFNKSRH 337
Cdd:PRK00142 238 eVPIGHCHQCGTPCDRYVNCANPACNLLILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLIFNKERH 314
TrhO COG1054
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ...
 22-326 1.88e-161

tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440674 [Multi-domain]  Cd Length: 304  Bit Score: 453.44  E-value: 1.88e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239  22 EPRTTISFYKYFNIQDPNEFRNQWYQQFKALSVFGRVYIAKEGINAQISVPESNVGALRELIYAtDPALDNLRLNIAiDD 101
Cdd:COG1054    2 KPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRA-DPRFADLEFKES-EA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 102 DGKSFWVLRMKVRERVVADGIEDetFNP-ANTGQYLKAHEVNEMIDDPNTVFVDMRNHYEYEVGRFDNAIEIPSDTFREQ 180
Cdd:COG1054   80 DGHPFPRLKVKLKKEIVTMGLPD--VDPnEGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFREF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 181 LPMAVEMLQEQKDKNVVMYCTGGIRCEKASAYMLHNGFKNVYHVEGGIIEYARKAKEQGlpLRFKGKNFVFDNRMGERI- 259
Cdd:COG1054  158 PEWVEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEG--SLWEGECFVFDERVAVDHn 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490376239 260 -TEDTLAQCHQCGAPCDTHTNCRNDGCHLLFIQCPSCAEKYEgCCSSSCTEEMKLPEQEQRARRAGRE 326
Cdd:COG1054  236 lEPGVIGLCHACGTPCDRYVNCANDPCYELGVSCPHCADKYE-CCSDECTEEQRARYERQRQLRLAKE 302
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 133-233 1.19e-54

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: 174.30  E-value: 1.19e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 133 GQYLKAHEVNEMIDDPNTVFVDMRNHYEYEVGRFDNAIEIPSDTFREQLPMAVEMLQEQKDKNVVMYCTGGIRCEKASAY 212
Cdd:cd01518    1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80

                         90       100
                 ....*....|....*....|.
gi 490376239 213 MLHNGFKNVYHVEGGIIEYAR 233
Cdd:cd01518   81 LKERGFKNVYQLKGGILKYLE 101
PRK01415 PRK01415
hypothetical protein; Validated
 22-265 5.16e-36

hypothetical protein; Validated


Pssm-ID: 167229 [Multi-domain]  Cd Length: 247  Bit Score: 130.83  E-value: 5.16e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239  22 EPRTTISFYKYFNIQDPNEFRNQWYQQFKALSVFGRVYIAKEGINAQISVPESNVG-ALRELIYATDPALDNLRLNIAid 100
Cdd:PRK01415   3 EKIAILSAYSFVNIEEPANLIPKLLLIGKRKYVRGTILLANEGFNGSFSGSYENVNlVLEELIKLTGPKDVNVKINYS-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 101 dDGKSFWVLRMKVRERVVADGIEDETFNpANTGQYLKAHEVNEMIDDPNTVFVDMRNHYEYEVGRFDNAIEIPSDTFReQ 180
Cdd:PRK01415  81 -DVHPFQKLKVRLKKEIVAMNVDDLNVD-LFKGEYIEPKDWDEFITKQDVIVIDTRNDYEVEVGTFKSAINPNTKTFK-Q 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 181 LPMAVEMLQEQ-KDKNVVMYCTGGIRCEKASAYMLHNGFKNVYHVEGGIIEYARKAKEQGlpLRFKGKNFVFDNRmgeRI 259
Cdd:PRK01415 158 FPAWVQQNQELlKGKKIAMVCTGGIRCEKSTSLLKSIGYDEVYHLKGGILQYLEDTQNKN--NLWQGECFVFDDR---RA 232


                 ....*.
gi 490376239 260 TEDTLA 265
Cdd:PRK01415 233 VTDDLS 238
PRK05320 PRK05320
rhodanese superfamily protein; Provisional
 27-254 1.23e-31

rhodanese superfamily protein; Provisional


Pssm-ID: 235405 [Multi-domain]  Cd Length: 257  Bit Score: 119.36  E-value: 1.23e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239  27 ISFYKYFNIQDPNEFRNQWYQQFKALSVFGRVYIAKEGINAQISVPESNVGALRELIYAtDPALDNLRLNIAIDDDgKSF 106
Cdd:PRK05320   6 IAAYKFVSLDDPETLRPLVLARCEALGLKGTILLAPEGINLFLAGTREAIDAFYAWLRA-DARFADLQVKESLSDS-QPF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 107 WVLRMKVRERVVA---DGIEDE-----TFNPANTGQYL-KAHevnemiDDPN--TVFVDMRNHYEYEVGRFDNAIEIPSD 175
Cdd:PRK05320  84 RRMLVKLKREIITmkrPAIRPElgrapSVDAATLKRWLdQGH------DDAGrpVVMLDTRNAFEVDVGTFDGALDYRID 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 176 TFREqLPMAVEMLQ-EQKDKNVVMYCTGGIRCEKASAYMLHNGFKNVYHVEGGIIEYARKAKEQGlplrFKGKNFVFDNR 254
Cdd:PRK05320 158 KFTE-FPEALAAHRaDLAGKTVVSFCTGGIRCEKAAIHMQEVGIDNVYQLEGGILKYFEEVGGAH----YDGDCFVFDYR 232
Rhodanese_C pfam12368
Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some ...
 245-308 2.72e-30

Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some members of the Rhodanase family. Rhodanase is pfam00581.


Pssm-ID: 463552 [Multi-domain]  Cd Length: 66  Bit Score: 110.10  E-value: 2.72e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490376239  245 KGKNFVFDNRM--GERITEDTLAQCHQCGAPCDTHTNCRNDGCHLLFIQCPSCAEKYEGCCSSSCT 308
Cdd:pfam12368   1 KGKLFVFDERLavVEPSDDDVIGKCYHCGKPCDRYVNCANPDCNRLFLQCEECAEKYEGCCSEECA 66
UPF0176_N pfam17773
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family ...
 24-114 9.29e-25

UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family proteins. It adopts a fold similar to the pfam00708 family.


Pssm-ID: 465497 [Multi-domain]  Cd Length: 92  Bit Score: 96.02  E-value: 9.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239   24 RTTISFYKYFNIQDPNEFRNQWYQQFKALSVFGRVYIAKEGINAQISVPESNVGALRELIYAtDPALDNLRLNIAIDDDg 103
Cdd:pfam17773   1 YVVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLRA-DPGFADLDFKESYSDE- 78

                          90
                  ....*....|.
gi 490376239  104 KSFWVLRMKVR 114
Cdd:pfam17773  79 HPFRRLKVKLK 89
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 134-242 1.25e-22

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: 90.80  E-value: 1.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 134 QYLKAHEVNEMIDDPNTVFVDMRNHYEYEVGRFDNAIEIPSDTFREQLPmavemlQEQKDKNVVMYCTGGIRCEKASAYM 213
Cdd:COG0607    4 KEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLD------ELPKDKPIVVYCASGGRSAQAAALL 77

                         90       100
                 ....*....|....*....|....*....
gi 490376239 214 LHNGFKNVYHVEGGIIEYarkaKEQGLPL 242
Cdd:COG0607   78 RRAGYTNVYNLAGGIEAW----KAAGLPV 102
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 140-232 1.94e-21

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: 86.97  E-value: 1.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 140 EVNEMIDDPNTVFVDMRNHYEYEVGRFDNAIEIPSDTFREQLpmavEMLQEQKDKNVVMYCTGGIRCEKASAYMLHNGFK 219
Cdd:cd00158    1 ELKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERA----ALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGT 76

                         90
                 ....*....|...
gi 490376239 220 NVYHVEGGIIEYA 232
Cdd:cd00158   77 NVYNLEGGMLAWK 89
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 146-237 2.89e-21

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: 87.13  E-value: 2.89e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239   146 DDPNTVFVDMRNHYEYEVGRFDNAIEIPSDTFREQLPMAVEMLQEQ--------KDKNVVMYCTGGIRCEKASAYMLHNG 217
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEEllkrlgldKDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 490376239   218 FKNVYHVEGGIIEYARKAKE 237
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 145-232 2.39e-14

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: 67.89  E-value: 2.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239  145 IDDPNTVFVDMRNHYEYEVGRFDNAIEIPSDTFR----EQLPMAVEMLQEQKDKNVVMYCTGGIRCEKASAYMLHNGFKN 220
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSlpplPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|..
gi 490376239  221 VYHVEGGIIEYA 232
Cdd:pfam00581  81 VYVLDGGFEAWK 92
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 136-234 8.06e-12

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: 60.87  E-value: 8.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 136 LKAHEVNEMIDDP--NTVFVDMRNHYEYEVGRFDNAIEIPSDTFREQLPmavEMLQEQKDKNVVMYCTGGIRCEKASAYM 213
Cdd:cd01528    2 ISVAELAEWLADEreEPVLIDVREPEELEIAFLPGFLHLPMSEIPERSK---ELDSDNPDKDIVVLCHHGGRSMQVAQWL 78

                         90       100
                 ....*....|....*....|.
gi 490376239 214 LHNGFKNVYHVEGGIIEYARK 234
Cdd:cd01528   79 LRQGFENVYNLQGGIDAWSLE 99
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 147-232 8.09e-12

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: 61.13  E-value: 8.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 147 DPNTVFVDMRNHYEYEVGRFDNAIEIPSDTFREQLPMAVEMLQEQ-------KDKNVVMYCTGGIRCEKASAYMLHNGFK 219
Cdd:cd01519   13 HPNKVLIDVREPEELKTGKIPGAINIPLSSLPDALALSEEEFEKKygfpkpsKDKELIFYCKAGVRSKAAAELARSLGYE 92

                         90
                 ....*....|...
gi 490376239 220 NVYHVEGGIIEYA 232
Cdd:cd01519   93 NVGNYPGSWLDWA 105
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 139-231 4.02e-11

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: 58.82  E-value: 4.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 139 HEVNEMIDDpNTVFVDMRNHYEYEVGRFDNAIEIPSDTFREQlpmavemLQE-QKDKNVVMYCTGGIRCEKASAYMLHNG 217
Cdd:cd01524    4 HELDNYRAD-GVTLIDVRTPQEFEKGHIKGAINIPLDELRDR-------LNElPKDKEIIVYCAVGLRGYIAARILTQNG 75

                         90
                 ....*....|....
gi 490376239 218 FKnVYHVEGGIIEY 231
Cdd:cd01524   76 FK-VKNLDGGYKTY 88
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 130-234 4.02e-10

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 60.49  E-value: 4.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 130 ANTGQYLKAHEVNEMIDDPNTVF-VDMRNHYEYEVGRFDNAIEIPSDTFreqlpMAVEMLQE-QKDKNVVMYCTGGIRCE 207
Cdd:PRK07878 283 AAAGSTITPRELKEWLDSGKKIAlIDVREPVEWDIVHIPGAQLIPKSEI-----LSGEALAKlPQDRTIVLYCKTGVRSA 357

                         90       100
                 ....*....|....*....|....*..
gi 490376239 208 KASAYMLHNGFKNVYHVEGGIIEYARK 234
Cdd:PRK07878 358 EALAALKKAGFSDAVHLQGGVVAWAKQ 384
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
151-242 4.15e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 54.25  E-value: 4.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 151 VFVDMRNHYEYEVGRFDNAIEIPsdtfREQLPMAVEMLQEQKDKNVVMYCTGGIRCEKASAYMLHNGFKNVYHVEGGIIE 230
Cdd:PRK08762  19 VLIDVREAHERASGQAEGALRIP----RGFLELRIETHLPDRDREIVLICASGTRSAHAAATLRELGYTRVASVAGGFSA 94

                         90
                 ....*....|..
gi 490376239 231 YarkaKEQGLPL 242
Cdd:PRK08762  95 W----KDAGLPL 102
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 136-233 2.79e-07

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: 48.19  E-value: 2.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 136 LKAHEVNEMIDDPNTVFVDMRNHYEYE-VGRFDNAIEIPSDT--FR--EQLPMAVEMLQeqKDKNVVMYCTGGIRCEKAS 210
Cdd:cd01447    1 LSPEDARALLGSPGVLLVDVRDPRELErTGMIPGAFHAPRGMleFWadPDSPYHKPAFA--EDKPFVFYCASGWRSALAG 78

                         90       100
                 ....*....|....*....|...
gi 490376239 211 AYMLHNGFKNVYHVEGGIIEYAR 233
Cdd:cd01447   79 KTLQDMGLKPVYNIEGGFKDWKE 101
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 139-228 3.61e-07

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: 47.64  E-value: 3.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 139 HEVNEMIDDPNT-VFVDMR--NHYEYEVGRFDNAI---EIPSDTFREQLPmavemlqeqKDKNVVMYCTGGIRCEKASAY 212
Cdd:cd01444    5 DELAELLAAGEApVLLDVRdpASYAALPDHIPGAIhldEDSLDDWLGDLD---------RDRPVVVYCYHGNSSAQLAQA 75

                         90
                 ....*....|....*.
gi 490376239 213 MLHNGFKNVYHVEGGI 228
Cdd:cd01444   76 LREAGFTDVRSLAGGF 91
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 136-226 4.61e-07

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: 48.09  E-value: 4.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 136 LKAHEVneMIDDPNTVFVDMRNHYE-YEVGRFDNAIEIPSDTFreqLPMAVE--MLQE-----QKDKNVVMYCTGGIRCE 207
Cdd:cd01522    4 AEAWAL--LQADPQAVLVDVRTEAEwKFVGGVPDAVHVAWQVY---PDMEINpnFLAEleekvGKDRPVLLLCRSGNRSI 78

                         90       100
                 ....*....|....*....|
gi 490376239 208 KASAYMLHNGFKNVYHV-EG 226
Cdd:cd01522   79 AAAEAAAQAGFTNVYNVlEG 98
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
143-227 2.36e-06

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 45.78  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 143 EMIDDPNTVFVDMRNHYEYEVGRFDNAIEIPSDTfreqlpMAVEMLQEQKDKNVVMYCTGGIRCEKASAYMLHNGFKNVY 222
Cdd:PRK00162  14 QKLQEGGAVLVDIRDPQSFAMGHAPGAFHLTNDS------LGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQQGFDVVY 87


                 ....*
gi 490376239 223 HVEGG 227
Cdd:PRK00162  88 SIDGG 92
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 133-228 4.29e-05

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 44.86  E-value: 4.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 133 GQYLKAHEVNEMIDDpnTVFVDMRNHYEYEVGRFDNAIEIPSDTFREQL-PMAVEMLQEqkdknVVMYCTGGIRCEKASA 211
Cdd:PRK05597 260 GEVLDVPRVSALPDG--VTLIDVREPSEFAAYSIPGAHNVPLSAIREGAnPPSVSAGDE-----VVVYCAAGVRSAQAVA 332

                         90
                 ....*....|....*..
gi 490376239 212 YMLHNGFKNVYHVEGGI 228
Cdd:PRK05597 333 ILERAGYTGMSSLDGGI 349
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 135-233 1.85e-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: 40.47  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 135 YLKAHEVNEMIDDPNT------VFVDMRNHyEYEVGRFDNAIEIPSDTFREQLPMAVEMLQEQKDKNVVMYCTG----GI 204
Cdd:cd01443    3 YISPEELVALLENSDSnagkdfVVVDLRRD-DYEGGHIKGSINLPAQSCYQTLPQVYALFSLAGVKLAIFYCGSsqgrGP 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 490376239 205 R-CEKASAYMLHNGF--KNVYHVEGGIIEYAR 233
Cdd:cd01443   82 RaARWFADYLRKVGEslPKSYILTGGIKAWYH 113
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 135-227 5.99e-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: 38.93  E-value: 5.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 135 YLKAHEVNEMIDD--PNTVFVDMRNhYEYEVGRFDNAIEIPSDTFREQLPMAVEMLQEQKDKNVVMYCTGG-IRCEKASA 211
Cdd:cd01531    3 YISPAQLKGWIRNgrPPFQVVDVRD-EDYAGGHIKGSWHYPSTRFKAQLNQLVQLLSGSKKDTVVFHCALSqVRGPSAAR 81

                         90       100
                 ....*....|....*....|....
gi 490376239 212 YML--------HNGFKNVYHVEGG 227
Cdd:cd01531   82 KFLryldeedlETSKFEVYVLHGG 105
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 138-233 1.90e-03

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: 37.61  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 138 AHEVNEMIDDPNTVFVDMRNHYEYE-----------VGRFDNAIEIPSDTF---------REQLpmaVEMLQEQ---KDK 194
Cdd:cd01449    3 AEEVLANLDSGDVQLVDARSPERFRgevpeprpglrSGHIPGAVNIPWTSLldedgtfksPEEL---RALFAALgitPDK 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 490376239 195 NVVMYCTGGIRcekAS--AYMLHN-GFKNVYHVEGGIIEYAR 233
Cdd:cd01449   80 PVIVYCGSGVT---ACvlLLALELlGYKNVRLYDGSWSEWGS 118
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 147-229 2.02e-03

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: 37.27  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 147 DPNTVFVDMRNHYEYEVGRFDNAIEIPSdtfrEQLPMAVEMLQEQK----DKNVVMYCTGGIRCEKASAYMLHNGFKNVY 222
Cdd:cd01529   10 EPGTALLDVRAEDEYAAGHLPGKRSIPG----AALVLRSQELQALEapgrATRYVLTCDGSLLARFAAQELLALGGKPVA 85


                 ....*..
gi 490376239 223 HVEGGII 229
Cdd:cd01529   86 LLDGGTS 92
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 146-234 2.11e-03

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: 37.67  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 146 DDPNTVFVDMRNHYEYEVGRFDNAIEIPSDTFR----EQLPMAVEMLQEQKDKNVVMYCTGGIRCEKASAYMLHNGFK-N 220
Cdd:cd01526   21 AGKKHVLLDVRPKVHFEICRLPEAINIPLSELLskaaELKSLQELPLDNDKDSPIYVVCRRGNDSQTAVRKLKELGLErF 100

                         90
                 ....*....|....
gi 490376239 221 VYHVEGGIIEYARK 234
Cdd:cd01526  101 VRDIIGGLKAWADK 114
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
140-233 3.23e-03

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 38.95  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 140 EVNEMID--DPNTVFVDMRNHYEYEVGRFDNAIEIP-SDTfrEQLPmAVEMLQE-QKDKNVVMYCTGGIRCEKASAYMLH 215
Cdd:PRK07411 288 ELKALLDsgADDFVLIDVRNPNEYEIARIPGSVLVPlPDI--ENGP-GVEKVKElLNGHRLIAHCKMGGRSAKALGILKE 364

                         90
                 ....*....|....*...
gi 490376239 216 NGFKNVyHVEGGIIEYAR 233
Cdd:PRK07411 365 AGIEGT-NVKGGITAWSR 381
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 147-228 5.54e-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: 36.18  E-value: 5.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490376239 147 DPNTVFVDMRNHYEYEVGRFDNAIEIPSDTFREQlpmAVEMLqeQKDKNVVMYCTgGIRC---EKASAYMLHNGFKnVYH 223
Cdd:cd01521   23 KPDFVLVDVRSAEAYARGHVPGAINLPHREICEN---ATAKL--DKEKLFVVYCD-GPGCngaTKAALKLAELGFP-VKE 95


                 ....*
gi 490376239 224 VEGGI 228
Cdd:cd01521   96 MIGGL 100
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH