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Conserved domains on  [gi|491040493|ref|WP_004902162|]
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MULTISPECIES: GTP-binding protein [Enterobacteriaceae]

Protein Classification

CobW family GTP-binding protein( domain architecture ID 11424901)

CobW family GTP-binding protein similar to GTPase CobW, which is involved in the synthesis of cobalamin, and zinc-binding GTPase YeiR which belongs to the G3E family of P-loop GTPases

Gene Ontology:  GO:0005525|GO:0003924|GO:0046872
PubMed:  34302342|11916378

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
1-376 8.69e-77

Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];


:

Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 240.46  E-value: 8.69e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493   1 MKRTPLIILNGFLGAGKTTLLKNLLTQAHKRRMAvsVIVNDMSELDVDGVLIANTEIvdaasnNFVSISADSI--SSRSG 78
Cdd:COG0523    1 DKRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIA--VIVNEFGEVGIDAALVRDTDE------EIVELSNGCIccTLRED 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493  79 iqkLDSALKNLLEKRSPDFILLETSGSSHPLPLVRYLREHPQVS----LKAFLSLVDTVMLNDDYDGgkklipvfqehln 154
Cdd:COG0523   73 ---LLPALRRLLRRGRFDRLLIETTGLADPAPVAQTFTFDPELRdrlrLDGVVTVVDARNLLDDLAD------------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493 155 rgtRGVESLLAEQIMFCNKLLLTKNDRLPFYVVTEVARAIHPLNPQVAIMAVPWGNLQLDELLSMPDYDFHRVALLIDEL 234
Cdd:COG0523  137 ---RTLHELLVDQIAFADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWL 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493 235 QDAIDAvlsdepDKKYDISWRVIEDDRPFHPQRLWDTCHRfMGAGVYRSKGFFWLPGRdDLALLWNQAAGSINLEFISYW 314
Cdd:COG0523  214 EELRDH------EHDDGIRSFVFRSDRPFDPERLADFLEE-LGPGVLRAKGFLWLAGR-PRRLVFQGVGGRLSLEPLGPW 285
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491040493 315 KAgvlthtdnsltkeeraairqqlakmpgrfGDRRCRLTVIGESGEIDDFALALRQCLLTEE 376
Cdd:COG0523  286 PA-----------------------------DDRRSRLVFIGRDLDEAALEAALDACLLTDA 318
 
Name Accession Description Interval E-value
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
1-376 8.69e-77

Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 240.46  E-value: 8.69e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493   1 MKRTPLIILNGFLGAGKTTLLKNLLTQAHKRRMAvsVIVNDMSELDVDGVLIANTEIvdaasnNFVSISADSI--SSRSG 78
Cdd:COG0523    1 DKRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIA--VIVNEFGEVGIDAALVRDTDE------EIVELSNGCIccTLRED 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493  79 iqkLDSALKNLLEKRSPDFILLETSGSSHPLPLVRYLREHPQVS----LKAFLSLVDTVMLNDDYDGgkklipvfqehln 154
Cdd:COG0523   73 ---LLPALRRLLRRGRFDRLLIETTGLADPAPVAQTFTFDPELRdrlrLDGVVTVVDARNLLDDLAD------------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493 155 rgtRGVESLLAEQIMFCNKLLLTKNDRLPFYVVTEVARAIHPLNPQVAIMAVPWGNLQLDELLSMPDYDFHRVALLIDEL 234
Cdd:COG0523  137 ---RTLHELLVDQIAFADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWL 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493 235 QDAIDAvlsdepDKKYDISWRVIEDDRPFHPQRLWDTCHRfMGAGVYRSKGFFWLPGRdDLALLWNQAAGSINLEFISYW 314
Cdd:COG0523  214 EELRDH------EHDDGIRSFVFRSDRPFDPERLADFLEE-LGPGVLRAKGFLWLAGR-PRRLVFQGVGGRLSLEPLGPW 285
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491040493 315 KAgvlthtdnsltkeeraairqqlakmpgrfGDRRCRLTVIGESGEIDDFALALRQCLLTEE 376
Cdd:COG0523  286 PA-----------------------------DDRRSRLVFIGRDLDEAALEAALDACLLTDA 318
chaper_GTP_ZigA NF038288
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ...
5-392 4.28e-50

zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc metallochaperone thought to be important for histidine utilization (HUT), supplying Zn to the histidine ammonia-lyase HutH when required under low-Zn conditions.


Pssm-ID: 468453 [Multi-domain]  Cd Length: 390  Bit Score: 173.43  E-value: 4.28e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493   5 PLIILNGFLGAGKTTLLKNLLTQAHKRRmaVSVIVNDMSELDVDGVLIANTEivdaasnnfVSISadsissRSGiQKL-- 82
Cdd:NF038288   2 PVTVLSGFLGAGKTTLLNHILNNREGRR--VAVIVNDMSEVNIDAALVRNGG---------ASLS------RTE-EKLve 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493  83 ------------DsalknLL--------EKRSpDFILLETSGSSHPLPLVRYL--REHPQVSLKAFLSL------VDTVM 134
Cdd:NF038288  64 msngcicctlreD-----LLvevrrlarEGRF-DYLVIESTGISEPLPVAETFtfADEDGVSLSDVARLdtmvtvVDAVN 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493 135 LNDDYDGGKKLipvfQEhlnRG-------TRGVESLLAEQIMFCNKLLLTKNDRLPFYVVTEVARAIHPLNPQVAIMAVP 207
Cdd:NF038288 138 FLRDYDSADSL----QE---RGeslgeedERTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPIS 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493 208 WGNLQLDELLSMPDYDFHRVALLIDELQDaidavLSDE--PD-KKYDISWRVIEDDRPFHPQRLWDTCHRFMGAGVYRSK 284
Cdd:NF038288 211 FGQVPLDKVLNTGLFDFERAAQAPGWLKE-----LRGEhtPEtEEYGISSFVYRARRPFHPQRFYDFLHSEWPGKVLRSK 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493 285 GFFWLPGRDDLALLWNQAAGSINLEFISYWKAGVLTH---TDnsltKEERAAIRQQlakMPGRFGDRRCRLTVIGESGEI 361
Cdd:NF038288 286 GFFWLASRPDFAGSWSQAGGIARHGPAGMWWAAVPRErwpQD----EESLAAIREN---WDEPFGDRRQELVFIGQDMDE 358
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 491040493 362 DDFALALRQCLLTEEEIL----WWQQggiFHDPWP 392
Cdd:NF038288 359 AALRAALDACLLTDEEMAagpeAWAT---LPDPFP 390
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
5-217 2.17e-36

cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino acid sequence of YjiA protein in E. coli contains several conserved motifs that characterizes it as a P-loop GTPase. YijA gene is among the genes significantly induced in response to DNA-damage caused by mitomycin. YijA gene is a homologue of the CobW gene which encodes the cobalamin synthesis protein/P47K.


Pssm-ID: 349766  Cd Length: 198  Bit Score: 131.49  E-value: 2.17e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493   5 PLIILNGFLGAGKTTLLKNLLTQAHKRRMAvsVIVNDMSELDVDGVLIANTEIVDaasnNFVSISADSI--SSRSgiqKL 82
Cdd:cd03112    1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIA--VIVNEFGEVGIDAALLADSGGGE----EVVELSNGCIccTLKG---DL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493  83 DSALKNLLEKRS-PDFILLETSGSSHPLPLVRYLREHPQVSLKAFLSLVDTVMlnddyDGGKklipvFQEHLNRGtrGVE 161
Cdd:cd03112   72 VKALEQLLERRGkFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVV-----DAKN-----FLKQLDEE--DVS 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491040493 162 SLLAEQIMFCNKLLLTKNDRLPFYVVTEVARAIHPLNPQVAIMAVPWGNLQLDELL 217
Cdd:cd03112  140 DLAVDQIAFADVIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELL 195
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
5-201 2.48e-23

CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase expression / formation protein, and UreG a urease accessory protein. Both these proteins contain a P-loop nucleotide binding motif. HypB has GTPase activity and is a guanine nucleotide binding protein. It is not known whether UreG binds GTP or some other nucleotide. Both enzymes are involved in nickel binding. HypB can store nickel and is required for nickel dependent hydrogenase expression. UreG is required for functional incorporation of the urease nickel metallocenter. GTP hydrolysis may required by these proteins for nickel incorporation into other nickel proteins. This family of domains also contains P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression, and the cobW gene product, which may be involved in cobalamin biosynthesis in Pseudomonas denitrificans.


Pssm-ID: 396860  Cd Length: 179  Bit Score: 95.78  E-value: 2.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493    5 PLIILNGFLGAGKTTLLKNLLTQ-AHKRRMAvsVIVNDMSELDVDGVLIANTEI-VDAASNNFV--SISADsissrsgiq 80
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLKQnRAGLRIA--VIVNEFGETGIDAELLSETGVlIVELSNGCIccTIRED--------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493   81 kLDSALKNLLE-KRSPDFILLETSGSSHPLPLVRYLReHPQVSLKAFLSLVDTVMlnddyDGGKklipvfqehlNRGTRG 159
Cdd:pfam02492  70 -LSMALEALLErEGRLDVIFIETTGLAEPAPVAQTFL-SPELRSPVLLDGVITVV-----DAAN----------EADGEK 132
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 491040493  160 VESLLAEQIMFCNKLLLTKNDRLP----FYVVTEVARAIHPLNPQV 201
Cdd:pfam02492 133 IPRKAGDQIAFADLIVLNKTDLAPevalLEVLEEDLRRLNPGAPVV 178
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
252-372 1.54e-21

Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal to the trimeric cobaltochelatase subunit CobN, which is essential for vitamin B12 (cobalamin) biosynthesis. They contain a P-loop nucleotide-binding loop in the N-terminal domain and a histidine-rich region in the C-terminal portion suggesting a role in metal binding, possibly as an intermediary between the cobalt transport and chelation systems. CobW might be involved in cobalt reduction leading to cobalt(I) corrinoids. This entry represents the C-terminal domain found in CobW, as well as in P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression.


Pssm-ID: 214844 [Multi-domain]  Cd Length: 92  Bit Score: 88.04  E-value: 1.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493   252 ISWRVIEDDRPFHPQRLWDTCHRFMGaGVYRSKGFFWLPGRDDLALLWNQAAGSINLEFISYWKAgvlthtdnsltkeer 331
Cdd:smart00833   1 ISSFVYRARRPFHPQRLLAALDELPE-GVLRAKGFFWLASRPDLPGVLSQAGGRLRIEPAGAWPA--------------- 64
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 491040493   332 aairqqlakmpgrFGDRRCRLTVIGESGEIDDFALALRQCL 372
Cdd:smart00833  65 -------------AGDRRTRLVFIGRDLDEEAIRAALDACL 92
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
1-262 4.34e-11

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 63.57  E-value: 4.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493   1 MKRTPLIILNGFLGAGKTTLLKNLLTQAHKRRMAvsVIVNDMSELDVDGVLIAnteivDAASnNFVSISADSI-SSRSgi 79
Cdd:PRK11537   1 MNPIAVTLLTGFLGAGKTTLLRHILNEQHGYKIA--VIENEFGEVSVDDQLIG-----DRAT-QIKTLTNGCIcCSRS-- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493  80 QKLDSALKNLLEKRSP-----DFILLETSGSSHPLPLVRYLREHPQVS----LKAFLSLVDTVMLnddydggkklipvfQ 150
Cdd:PRK11537  71 NELEDALLDLLDNLDKgniqfDRLVIECTGMADPGPIIQTFFSHEVLCqrylLDGVIALVDAVHA--------------D 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493 151 EHLNRGTrgvesLLAEQIMFCNKLLLTKNDRLPfyvVTEVARA-IHPLNPQVAIMAVPWGNLQLDELlsmpdydFHRVAL 229
Cdd:PRK11537 137 EQMNQFT-----IAQSQVGYADRILLTKTDVAG---EAEKLRErLARINARAPVYTVVHGDIDLSLL-------FNTNGF 201
                        250       260       270
                 ....*....|....*....|....*....|...
gi 491040493 230 LIDELQDAIDAVLSDEPDKKYDISWRVIEDDRP 262
Cdd:PRK11537 202 MLEENVVSTKPRFHFIADKQNDISSIVVELDYP 234
 
Name Accession Description Interval E-value
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
1-376 8.69e-77

Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 240.46  E-value: 8.69e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493   1 MKRTPLIILNGFLGAGKTTLLKNLLTQAHKRRMAvsVIVNDMSELDVDGVLIANTEIvdaasnNFVSISADSI--SSRSG 78
Cdd:COG0523    1 DKRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIA--VIVNEFGEVGIDAALVRDTDE------EIVELSNGCIccTLRED 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493  79 iqkLDSALKNLLEKRSPDFILLETSGSSHPLPLVRYLREHPQVS----LKAFLSLVDTVMLNDDYDGgkklipvfqehln 154
Cdd:COG0523   73 ---LLPALRRLLRRGRFDRLLIETTGLADPAPVAQTFTFDPELRdrlrLDGVVTVVDARNLLDDLAD------------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493 155 rgtRGVESLLAEQIMFCNKLLLTKNDRLPFYVVTEVARAIHPLNPQVAIMAVPWGNLQLDELLSMPDYDFHRVALLIDEL 234
Cdd:COG0523  137 ---RTLHELLVDQIAFADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWL 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493 235 QDAIDAvlsdepDKKYDISWRVIEDDRPFHPQRLWDTCHRfMGAGVYRSKGFFWLPGRdDLALLWNQAAGSINLEFISYW 314
Cdd:COG0523  214 EELRDH------EHDDGIRSFVFRSDRPFDPERLADFLEE-LGPGVLRAKGFLWLAGR-PRRLVFQGVGGRLSLEPLGPW 285
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491040493 315 KAgvlthtdnsltkeeraairqqlakmpgrfGDRRCRLTVIGESGEIDDFALALRQCLLTEE 376
Cdd:COG0523  286 PA-----------------------------DDRRSRLVFIGRDLDEAALEAALDACLLTDA 318
chaper_GTP_ZigA NF038288
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ...
5-392 4.28e-50

zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc metallochaperone thought to be important for histidine utilization (HUT), supplying Zn to the histidine ammonia-lyase HutH when required under low-Zn conditions.


Pssm-ID: 468453 [Multi-domain]  Cd Length: 390  Bit Score: 173.43  E-value: 4.28e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493   5 PLIILNGFLGAGKTTLLKNLLTQAHKRRmaVSVIVNDMSELDVDGVLIANTEivdaasnnfVSISadsissRSGiQKL-- 82
Cdd:NF038288   2 PVTVLSGFLGAGKTTLLNHILNNREGRR--VAVIVNDMSEVNIDAALVRNGG---------ASLS------RTE-EKLve 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493  83 ------------DsalknLL--------EKRSpDFILLETSGSSHPLPLVRYL--REHPQVSLKAFLSL------VDTVM 134
Cdd:NF038288  64 msngcicctlreD-----LLvevrrlarEGRF-DYLVIESTGISEPLPVAETFtfADEDGVSLSDVARLdtmvtvVDAVN 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493 135 LNDDYDGGKKLipvfQEhlnRG-------TRGVESLLAEQIMFCNKLLLTKNDRLPFYVVTEVARAIHPLNPQVAIMAVP 207
Cdd:NF038288 138 FLRDYDSADSL----QE---RGeslgeedERTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPIS 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493 208 WGNLQLDELLSMPDYDFHRVALLIDELQDaidavLSDE--PD-KKYDISWRVIEDDRPFHPQRLWDTCHRFMGAGVYRSK 284
Cdd:NF038288 211 FGQVPLDKVLNTGLFDFERAAQAPGWLKE-----LRGEhtPEtEEYGISSFVYRARRPFHPQRFYDFLHSEWPGKVLRSK 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493 285 GFFWLPGRDDLALLWNQAAGSINLEFISYWKAGVLTH---TDnsltKEERAAIRQQlakMPGRFGDRRCRLTVIGESGEI 361
Cdd:NF038288 286 GFFWLASRPDFAGSWSQAGGIARHGPAGMWWAAVPRErwpQD----EESLAAIREN---WDEPFGDRRQELVFIGQDMDE 358
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 491040493 362 DDFALALRQCLLTEEEIL----WWQQggiFHDPWP 392
Cdd:NF038288 359 AALRAALDACLLTDEEMAagpeAWAT---LPDPFP 390
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
5-217 2.17e-36

cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino acid sequence of YjiA protein in E. coli contains several conserved motifs that characterizes it as a P-loop GTPase. YijA gene is among the genes significantly induced in response to DNA-damage caused by mitomycin. YijA gene is a homologue of the CobW gene which encodes the cobalamin synthesis protein/P47K.


Pssm-ID: 349766  Cd Length: 198  Bit Score: 131.49  E-value: 2.17e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493   5 PLIILNGFLGAGKTTLLKNLLTQAHKRRMAvsVIVNDMSELDVDGVLIANTEIVDaasnNFVSISADSI--SSRSgiqKL 82
Cdd:cd03112    1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIA--VIVNEFGEVGIDAALLADSGGGE----EVVELSNGCIccTLKG---DL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493  83 DSALKNLLEKRS-PDFILLETSGSSHPLPLVRYLREHPQVSLKAFLSLVDTVMlnddyDGGKklipvFQEHLNRGtrGVE 161
Cdd:cd03112   72 VKALEQLLERRGkFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVV-----DAKN-----FLKQLDEE--DVS 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491040493 162 SLLAEQIMFCNKLLLTKNDRLPFYVVTEVARAIHPLNPQVAIMAVPWGNLQLDELL 217
Cdd:cd03112  140 DLAVDQIAFADVIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELL 195
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
5-201 2.48e-23

CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase expression / formation protein, and UreG a urease accessory protein. Both these proteins contain a P-loop nucleotide binding motif. HypB has GTPase activity and is a guanine nucleotide binding protein. It is not known whether UreG binds GTP or some other nucleotide. Both enzymes are involved in nickel binding. HypB can store nickel and is required for nickel dependent hydrogenase expression. UreG is required for functional incorporation of the urease nickel metallocenter. GTP hydrolysis may required by these proteins for nickel incorporation into other nickel proteins. This family of domains also contains P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression, and the cobW gene product, which may be involved in cobalamin biosynthesis in Pseudomonas denitrificans.


Pssm-ID: 396860  Cd Length: 179  Bit Score: 95.78  E-value: 2.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493    5 PLIILNGFLGAGKTTLLKNLLTQ-AHKRRMAvsVIVNDMSELDVDGVLIANTEI-VDAASNNFV--SISADsissrsgiq 80
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLKQnRAGLRIA--VIVNEFGETGIDAELLSETGVlIVELSNGCIccTIRED--------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493   81 kLDSALKNLLE-KRSPDFILLETSGSSHPLPLVRYLReHPQVSLKAFLSLVDTVMlnddyDGGKklipvfqehlNRGTRG 159
Cdd:pfam02492  70 -LSMALEALLErEGRLDVIFIETTGLAEPAPVAQTFL-SPELRSPVLLDGVITVV-----DAAN----------EADGEK 132
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 491040493  160 VESLLAEQIMFCNKLLLTKNDRLP----FYVVTEVARAIHPLNPQV 201
Cdd:pfam02492 133 IPRKAGDQIAFADLIVLNKTDLAPevalLEVLEEDLRRLNPGAPVV 178
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
252-372 1.54e-21

Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal to the trimeric cobaltochelatase subunit CobN, which is essential for vitamin B12 (cobalamin) biosynthesis. They contain a P-loop nucleotide-binding loop in the N-terminal domain and a histidine-rich region in the C-terminal portion suggesting a role in metal binding, possibly as an intermediary between the cobalt transport and chelation systems. CobW might be involved in cobalt reduction leading to cobalt(I) corrinoids. This entry represents the C-terminal domain found in CobW, as well as in P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression.


Pssm-ID: 214844 [Multi-domain]  Cd Length: 92  Bit Score: 88.04  E-value: 1.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493   252 ISWRVIEDDRPFHPQRLWDTCHRFMGaGVYRSKGFFWLPGRDDLALLWNQAAGSINLEFISYWKAgvlthtdnsltkeer 331
Cdd:smart00833   1 ISSFVYRARRPFHPQRLLAALDELPE-GVLRAKGFFWLASRPDLPGVLSQAGGRLRIEPAGAWPA--------------- 64
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 491040493   332 aairqqlakmpgrFGDRRCRLTVIGESGEIDDFALALRQCL 372
Cdd:smart00833  65 -------------AGDRRTRLVFIGRDLDEEAIRAALDACL 92
CobW_C pfam07683
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ...
256-372 9.44e-14

Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of putative metal chaperones that can be separated into up to 15 subgroups. In addition to known roles in cobalamin biosynthesis and the activation of the Fe-type nitrile hydratase, this family is also known to be involved in the response to zinc limitation. The CobW subgroup involved in cobalamin synthesis represents only a small sub-fraction of the family.


Pssm-ID: 462228 [Multi-domain]  Cd Length: 93  Bit Score: 66.49  E-value: 9.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493  256 VIEDDRPFHPQRLWDTCHRF-MGAGVYRSKGFFWLPGRDdLALLWNQAAGSINLEFISYWKagvlthtdnsltkeeraai 334
Cdd:pfam07683   5 VFRADRPFDPERLEAWLEDLlLPEGILRAKGILWLAGRP-RPLVFQGVGGRLSLEPAGRWW------------------- 64
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 491040493  335 rqqlakmpgRFGDRRCRLTVIGESGEIDDFALALRQCL 372
Cdd:pfam07683  65 ---------PDEDRRSRLVFIGRDLDREALRAALDACL 93
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
1-262 4.34e-11

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 63.57  E-value: 4.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493   1 MKRTPLIILNGFLGAGKTTLLKNLLTQAHKRRMAvsVIVNDMSELDVDGVLIAnteivDAASnNFVSISADSI-SSRSgi 79
Cdd:PRK11537   1 MNPIAVTLLTGFLGAGKTTLLRHILNEQHGYKIA--VIENEFGEVSVDDQLIG-----DRAT-QIKTLTNGCIcCSRS-- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493  80 QKLDSALKNLLEKRSP-----DFILLETSGSSHPLPLVRYLREHPQVS----LKAFLSLVDTVMLnddydggkklipvfQ 150
Cdd:PRK11537  71 NELEDALLDLLDNLDKgniqfDRLVIECTGMADPGPIIQTFFSHEVLCqrylLDGVIALVDAVHA--------------D 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491040493 151 EHLNRGTrgvesLLAEQIMFCNKLLLTKNDRLPfyvVTEVARA-IHPLNPQVAIMAVPWGNLQLDELlsmpdydFHRVAL 229
Cdd:PRK11537 137 EQMNQFT-----IAQSQVGYADRILLTKTDVAG---EAEKLRErLARINARAPVYTVVHGDIDLSLL-------FNTNGF 201
                        250       260       270
                 ....*....|....*....|....*....|...
gi 491040493 230 LIDELQDAIDAVLSDEPDKKYDISWRVIEDDRP 262
Cdd:PRK11537 202 MLEENVVSTKPRFHFIADKQNDISSIVVELDYP 234
 
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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