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Conserved domains on  [gi|2188688103|gb|UKG74087|]
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XdhC family protein [Serratia marcescens]

Protein Classification

XdhC family protein( domain architecture ID 11449431)

XdhC family protein may be involved in the attachment of molybdenum to xanthine dehydrogenase

CATH:  3.40.50.720
Gene Ontology:  GO:0070403
PubMed:  30945211|10217763

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
XdhC COG1975
Molybdoenzyme maturation factor PaoD (Mo cofactor insertion), XdhC/CoxF family ...
 7-323 1.96e-92

Molybdoenzyme maturation factor PaoD (Mo cofactor insertion), XdhC/CoxF family [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441578 [Multi-domain]  Cd Length: 303  Bit Score: 278.29  E-value: 1.96e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188688103   7 TVVSQAISWLQQ-QPVWLCTVLSTYGSSPRSPGALMAATRDGRYSGSLSGGCVEEDFLRRVAAGEYQAPSQVIRYGEGGM 85
Cdd:COG1975     2 DVLEALAALLAAgEPVVLATVVETRGSAPREPGAKMLVTADGRIAGTIGGGCLEADVIERAREALADGEPRLLRYGLGPE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188688103  86 TP-NVALPCGGVLDVLIEYLPAGEAsvayLQRIAGALEGHHALIKRLTLPHACHsleqshftsatqverRLEQITLHIAA 164
Cdd:COG1975    82 DAwDLGLCCGGTVEVLLEPLDAADA----LAALAAALAAREPVALVLDLAGGLG---------------EDGVFVEVLGP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188688103 165 APRLLIAGLSSVALYCADFAVALGFEVLVCESRPEAldnFAAELKPGV-TLLRQFPAKFIEDGGCHANTAVVALTHDPRM 243
Cdd:COG1975   143 PPRLLIFGAGHVARALARLAAALGFRVTVVDPRAEF---APPERFPGAdEVVADDPEDALAALALDPGTAVVVLTHDHAL 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188688103 244 DDLTLMEAIHTPAFYIGAMGSLRNSARRRQRLQQiAEFTPQELERIHAPIGLPLGSKTPAEIALAVMAAIVQQKNRRPAA 323
Cdd:COG1975   220 DLAALEAALRSPAAYIGLIGSRRKRARRRERLRE-EGVSEAQLARLHAPIGLDIGAKTPEEIAVSILAELIAVRRGASGA 298
 
Name Accession Description Interval E-value
XdhC COG1975
Molybdoenzyme maturation factor PaoD (Mo cofactor insertion), XdhC/CoxF family ...
 7-323 1.96e-92

Molybdoenzyme maturation factor PaoD (Mo cofactor insertion), XdhC/CoxF family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441578 [Multi-domain]  Cd Length: 303  Bit Score: 278.29  E-value: 1.96e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188688103   7 TVVSQAISWLQQ-QPVWLCTVLSTYGSSPRSPGALMAATRDGRYSGSLSGGCVEEDFLRRVAAGEYQAPSQVIRYGEGGM 85
Cdd:COG1975     2 DVLEALAALLAAgEPVVLATVVETRGSAPREPGAKMLVTADGRIAGTIGGGCLEADVIERAREALADGEPRLLRYGLGPE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188688103  86 TP-NVALPCGGVLDVLIEYLPAGEAsvayLQRIAGALEGHHALIKRLTLPHACHsleqshftsatqverRLEQITLHIAA 164
Cdd:COG1975    82 DAwDLGLCCGGTVEVLLEPLDAADA----LAALAAALAAREPVALVLDLAGGLG---------------EDGVFVEVLGP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188688103 165 APRLLIAGLSSVALYCADFAVALGFEVLVCESRPEAldnFAAELKPGV-TLLRQFPAKFIEDGGCHANTAVVALTHDPRM 243
Cdd:COG1975   143 PPRLLIFGAGHVARALARLAAALGFRVTVVDPRAEF---APPERFPGAdEVVADDPEDALAALALDPGTAVVVLTHDHAL 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188688103 244 DDLTLMEAIHTPAFYIGAMGSLRNSARRRQRLQQiAEFTPQELERIHAPIGLPLGSKTPAEIALAVMAAIVQQKNRRPAA 323
Cdd:COG1975   220 DLAALEAALRSPAAYIGLIGSRRKRARRRERLRE-EGVSEAQLARLHAPIGLDIGAKTPEEIAVSILAELIAVRRGASGA 298
XdhC_C pfam13478
XdhC Rossmann domain; This entry is the rossmann domain found in the Xanthine dehydrogenase ...
 168-313 1.38e-45

XdhC Rossmann domain; This entry is the rossmann domain found in the Xanthine dehydrogenase accessory protein.


Pssm-ID: 463891  Cd Length: 143  Bit Score: 152.27  E-value: 1.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188688103 168 LLIAGLSSVALYCADFAVALGFEVLVCESRPEALDnfAAELKPGVTLLRQFPAKFIEDGGCHANTAVVALTHDPRMDDLT 247
Cdd:pfam13478   1 LVIFGAGHVAQALARLAALLGFRVTVVDPRPEFAN--PERFPDADEVIVWDLEEALELLRIDARTAVVVLTHDHKLDLEA 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2188688103 248 LMEAIHTPAFYIGAMGSLRNSARRRQRLQQiAEFTPQELERIHAPIGLPLGSKTPAEIALAVMAAI 313
Cdd:pfam13478  79 LEAALRGDAAYIGMIGSRRKRARRLERLRA-AGGSEEQLARLHAPIGLDIGAKTPEEIAVSILAEI 143
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 167-208 8.82e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 37.30  E-value: 8.82e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2188688103 167 RLLIAGLSSVALYCADFAVALGFEVLVCESRPEALDnFAAEL 208
Cdd:cd05188   137 TVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLE-LAKEL 177
 
Name Accession Description Interval E-value
XdhC COG1975
Molybdoenzyme maturation factor PaoD (Mo cofactor insertion), XdhC/CoxF family ...
 7-323 1.96e-92

Molybdoenzyme maturation factor PaoD (Mo cofactor insertion), XdhC/CoxF family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441578 [Multi-domain]  Cd Length: 303  Bit Score: 278.29  E-value: 1.96e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188688103   7 TVVSQAISWLQQ-QPVWLCTVLSTYGSSPRSPGALMAATRDGRYSGSLSGGCVEEDFLRRVAAGEYQAPSQVIRYGEGGM 85
Cdd:COG1975     2 DVLEALAALLAAgEPVVLATVVETRGSAPREPGAKMLVTADGRIAGTIGGGCLEADVIERAREALADGEPRLLRYGLGPE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188688103  86 TP-NVALPCGGVLDVLIEYLPAGEAsvayLQRIAGALEGHHALIKRLTLPHACHsleqshftsatqverRLEQITLHIAA 164
Cdd:COG1975    82 DAwDLGLCCGGTVEVLLEPLDAADA----LAALAAALAAREPVALVLDLAGGLG---------------EDGVFVEVLGP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188688103 165 APRLLIAGLSSVALYCADFAVALGFEVLVCESRPEAldnFAAELKPGV-TLLRQFPAKFIEDGGCHANTAVVALTHDPRM 243
Cdd:COG1975   143 PPRLLIFGAGHVARALARLAAALGFRVTVVDPRAEF---APPERFPGAdEVVADDPEDALAALALDPGTAVVVLTHDHAL 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188688103 244 DDLTLMEAIHTPAFYIGAMGSLRNSARRRQRLQQiAEFTPQELERIHAPIGLPLGSKTPAEIALAVMAAIVQQKNRRPAA 323
Cdd:COG1975   220 DLAALEAALRSPAAYIGLIGSRRKRARRRERLRE-EGVSEAQLARLHAPIGLDIGAKTPEEIAVSILAELIAVRRGASGA 298
XdhC_C pfam13478
XdhC Rossmann domain; This entry is the rossmann domain found in the Xanthine dehydrogenase ...
 168-313 1.38e-45

XdhC Rossmann domain; This entry is the rossmann domain found in the Xanthine dehydrogenase accessory protein.


Pssm-ID: 463891  Cd Length: 143  Bit Score: 152.27  E-value: 1.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2188688103 168 LLIAGLSSVALYCADFAVALGFEVLVCESRPEALDnfAAELKPGVTLLRQFPAKFIEDGGCHANTAVVALTHDPRMDDLT 247
Cdd:pfam13478   1 LVIFGAGHVAQALARLAALLGFRVTVVDPRPEFAN--PERFPDADEVIVWDLEEALELLRIDARTAVVVLTHDHKLDLEA 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2188688103 248 LMEAIHTPAFYIGAMGSLRNSARRRQRLQQiAEFTPQELERIHAPIGLPLGSKTPAEIALAVMAAI 313
Cdd:pfam13478  79 LEAALRGDAAYIGMIGSRRKRARRLERLRA-AGGSEEQLARLHAPIGLDIGAKTPEEIAVSILAEI 143
XdhC_CoxI pfam02625
XdhC and CoxI family; This domain is often found in association with an NAD-binding region, ...
 15-81 2.25e-16

XdhC and CoxI family; This domain is often found in association with an NAD-binding region, related to TrkA-N (pfam02254; personal obs:C. Yeats). XdhC is believed to be involved in the attachment of molybdenum to Xanthine Dehydrogenase.


Pssm-ID: 460626 [Multi-domain]  Cd Length: 68  Bit Score: 72.52  E-value: 2.25e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2188688103  15 WLQQ-QPVWLCTVLSTYGSSPRSPGALMAATRDGRYSGSLSGGCVEEDFLRRV----AAGEyqapSQVIRYG 81
Cdd:pfam02625   1 LLAAgEPVALATVVATEGSAPRRPGAKMLVRADGRIAGTIGGGCLEAAVIEDArevlAAGR----PRLLRYG 68
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 167-208 8.82e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 37.30  E-value: 8.82e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2188688103 167 RLLIAGLSSVALYCADFAVALGFEVLVCESRPEALDnFAAEL 208
Cdd:cd05188   137 TVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLE-LAKEL 177
 
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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