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Conserved domains on  [gi|2291339184|gb|UVT37964|]
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CobW domain-containing protein 1 [Karlodinium veneficum]

Protein Classification

chaper_GTP_ZigA superfamily-containing protein( domain architecture ID 1904169)

chaper_GTP_ZigA superfamily-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
chaper_GTP_ZigA super family cl45739
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ...
34-426 3.86e-179

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.


The actual alignment was detected with superfamily member NF038288:

Pssm-ID: 468453 [Multi-domain]  Cd Length: 390  Bit Score: 505.08  E-value: 3.86e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184  34 LPVTVLSGFLGAGKTTLMKHVLENLDGLRVAVVVNDMAEVNIDAALVDQADV---RQEkEKVVELSNGCICCTLREDLLT 110
Cdd:NF038288    1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGAslsRTE-EKLVEMSNGCICCTLREDLLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 111 TIMDFAQQNRFDHLLIESSGISEPLPVAETFTFDNKDtGVRLDQYARLDTLVTVVDGVNLFSELESIQTTATSGQAAYEG 190
Cdd:NF038288   80 EVRRLAREGRFDYLVIESTGISEPLPVAETFTFADED-GVSLSDVARLDTMVTVVDAVNFLRDYDSADSLQERGESLGEE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 191 DDRPLAQLLVDQIEFANVILLNKCDLLSDKQKLDVKTTLQSLNPNAAVFQTVRSVLPLKHVLGTGLFSMSDAEKNEQWLK 270
Cdd:NF038288  159 DERTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERAAQAPGWLK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 271 EARiGEHVAETEEFGIKSFMYRRRLPFHPERLRKLMDDaESLPGVIRAKGFCWIATRPRFVAVLSFVGSLrdMSQGQP-- 348
Cdd:NF038288  239 ELR-GEHTPETEEYGISSFVYRARRPFHPQRFYDFLHS-EWPGKVLRSKGFFWLASRPDFAGSWSQAGGI--ARHGPAgm 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 349 WWAAMETELWPEglSEDLRSSGL--WQEPFGDRSRELVVIGQ-YEQADIEARLDACLLTKDEMAQPQpwsfsDTWPAWED 425
Cdd:NF038288  315 WWAAVPRERWPQ--DEESLAAIRenWDEPFGDRRQELVFIGQdMDEAALRAALDACLLTDEEMAAGP-----EAWATLPD 387

                  .
gi 2291339184 426 P 426
Cdd:NF038288  388 P 388
 
Name Accession Description Interval E-value
chaper_GTP_ZigA NF038288
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ...
34-426 3.86e-179

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: 505.08  E-value: 3.86e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184  34 LPVTVLSGFLGAGKTTLMKHVLENLDGLRVAVVVNDMAEVNIDAALVDQADV---RQEkEKVVELSNGCICCTLREDLLT 110
Cdd:NF038288    1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGAslsRTE-EKLVEMSNGCICCTLREDLLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 111 TIMDFAQQNRFDHLLIESSGISEPLPVAETFTFDNKDtGVRLDQYARLDTLVTVVDGVNLFSELESIQTTATSGQAAYEG 190
Cdd:NF038288   80 EVRRLAREGRFDYLVIESTGISEPLPVAETFTFADED-GVSLSDVARLDTMVTVVDAVNFLRDYDSADSLQERGESLGEE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 191 DDRPLAQLLVDQIEFANVILLNKCDLLSDKQKLDVKTTLQSLNPNAAVFQTVRSVLPLKHVLGTGLFSMSDAEKNEQWLK 270
Cdd:NF038288  159 DERTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERAAQAPGWLK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 271 EARiGEHVAETEEFGIKSFMYRRRLPFHPERLRKLMDDaESLPGVIRAKGFCWIATRPRFVAVLSFVGSLrdMSQGQP-- 348
Cdd:NF038288  239 ELR-GEHTPETEEYGISSFVYRARRPFHPQRFYDFLHS-EWPGKVLRSKGFFWLASRPDFAGSWSQAGGI--ARHGPAgm 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 349 WWAAMETELWPEglSEDLRSSGL--WQEPFGDRSRELVVIGQ-YEQADIEARLDACLLTKDEMAQPQpwsfsDTWPAWED 425
Cdd:NF038288  315 WWAAVPRERWPQ--DEESLAAIRenWDEPFGDRRQELVFIGQdMDEAALRAALDACLLTDEEMAAGP-----EAWATLPD 387

                  .
gi 2291339184 426 P 426
Cdd:NF038288  388 P 388
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
32-404 6.38e-128

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 372.20  E-value: 6.38e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184  32 DRLPVTVLSGFLGAGKTTLMKHVLENLDGLRVAVVVNDMAEVNIDAALVDQADvrqekEKVVELSNGCICCTLREDLLTT 111
Cdd:COG0523     2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRDTD-----EEIVELSNGCICCTLREDLLPA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 112 IMDFAQQNRFDHLLIESSGISEPLPVAETFTFDnkdtgVRLDQYARLDTLVTVVDGVNLFSELesiqttatsgqaayegD 191
Cdd:COG0523    77 LRRLLRRGRFDRLLIETTGLADPAPVAQTFTFD-----PELRDRLRLDGVVTVVDARNLLDDL----------------A 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 192 DRPLAQLLVDQIEFANVILLNKCDLLSDKQKLDVKTTLQSLNPNAAVFQTVRSVLPLKHVLGTGLFSMSDAEKNEQWLKE 271
Cdd:COG0523   136 DRTLHELLVDQIAFADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWLEE 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 272 ARIGEHVAeteefGIKSFMYRRRLPFHPERLRKLMDDAesLPGVIRAKGFCWIATRPRfVAVLSFVGSLRDMSQGQPWWA 351
Cdd:COG0523   216 LRDHEHDD-----GIRSFVFRSDRPFDPERLADFLEEL--GPGVLRAKGFLWLAGRPR-RLVFQGVGGRLSLEPLGPWPA 287
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2291339184 352 ametelwpeglsedlrssglwqepfGDRSRELVVIGQ-YEQADIEARLDACLLT 404
Cdd:COG0523   288 -------------------------DDRRSRLVFIGRdLDEAALEAALDACLLT 316
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
35-255 3.61e-84

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: 256.29  E-value: 3.61e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184  35 PVTVLSGFLGAGKTTLMKHVLENLDGLRVAVVVNDMAEVNIDAALVDQADvrqEKEKVVELSNGCICCTLREDLLTTIMD 114
Cdd:cd03112     1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSG---GGEEVVELSNGCICCTLKGDLVKALEQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 115 FAQQ-NRFDHLLIESSGISEPLPVAETFTFDNkdtgvRLDQYARLDTLVTVVDGVNLFSELesiqttatsgqaayegDDR 193
Cdd:cd03112    78 LLERrGKFDYILIETTGLADPGPIAQTLWSDE-----ELESRLRLDGVVTVVDAKNFLKQL----------------DEE 136
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2291339184 194 PLAQLLVDQIEFANVILLNKCDLLSDKQKLDVKTTLQSLNPNAAVFQTVRSVLPLKHVLGTG 255
Cdd:cd03112   137 DVSDLAVDQIAFADVIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGTG 198
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
35-240 1.10e-63

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: 202.87  E-value: 1.10e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184  35 PVTVLSGFLGAGKTTLMKHVLENL-DGLRVAVVVNDMAEVNIDAALVDQADVrqekeKVVELSNGCICCTLREDLLTTIM 113
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLKQNrAGLRIAVIVNEFGETGIDAELLSETGV-----LIVELSNGCICCTIREDLSMALE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 114 DFAQQN-RFDHLLIESSGISEPLPVAETFTFDNkdtgvrLDQYARLDTLVTVVDgvnlfselesiqttatsgqAAYEGDD 192
Cdd:pfam02492  76 ALLEREgRLDVIFIETTGLAEPAPVAQTFLSPE------LRSPVLLDGVITVVD-------------------AANEADG 130
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2291339184 193 RPLAQLLVDQIEFANVILLNKCDLLSDKQKLDV-KTTLQSLNPNAAVFQ 240
Cdd:pfam02492 131 EKIPRKAGDQIAFADLIVLNKTDLAPEVALLEVlEEDLRRLNPGAPVVP 179
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
33-398 2.91e-45

cobalamin biosynthesis protein CobW; The family of proteins identified by this model is generally found proximal to the trimeric cobaltochelatase subunit CobN which is essential for vitamin B12 (cobalamin) biosynthesis. The protein contains an 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. A broader CobW family is delineated by two Pfam models which identify the N- and C-terminal domains (pfam02492 and pfam07683). [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274151 [Multi-domain]  Cd Length: 341  Bit Score: 160.30  E-value: 2.91e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184  33 RLPVTVLSGFLGAGKTTLMKHVLENLDGLRVAVVVNDMAEVNIDAALVDQ-ADVRQEKEKVVELSNGCICCTLREDLLTT 111
Cdd:TIGR02475   3 KIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKAcGIEGCSEENIVELANGCICCTVADDFIPT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 112 IMDF-AQQNRFDHLLIESSGISEPLPVAETFTFDNkdtgVRldQYARLDTLVTVVDGVNLFSELESIQTTATSGQAAYEG 190
Cdd:TIGR02475  83 MTKLlARRQRPDHILIETSGLALPKPLVQAFQWPE----IR--SRVTVDGVVTVVDGPAVAAGRFAADPDALDAQRAADD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 191 D---DRPLAQLLVDQIEFANVILLNKCDLLSDKQKLDVKTTLQSLNPNAA-VFQTVRSVLPLKHVLGTGLFSMSDAEKNE 266
Cdd:TIGR02475 157 NldhETPLEELFEDQLACADLVILNKADLLDAAGLARVRAEIAAELPRAVkIVEASHGEVDARVLLGLGAAAEDDLDNRP 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 267 QWLKEARIGEHvaETEEFgiKSFMYRRRLPFHPERLRKLMDDAESLPGVIRAKGFCWIATRPRFVaVLSFVGSLRDMSQG 346
Cdd:TIGR02475 237 SHHDFEGGEEH--DHDEF--DSVVVDLGEVADPAALRQRLERLAEEHDVLRIKGFAAVPGKPMRL-LVQGVGQRVDSYYD 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2291339184 347 QPWWAAMetelwpeglsedlrssglwqepfgDRSRELVVIGQ--YEQADIEARL 398
Cdd:TIGR02475 312 RPWQAAE------------------------TRQTRLVVIGLhdLDQAAIRAAL 341
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
34-400 4.27e-31

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 121.35  E-value: 4.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184  34 LPVTVLSGFLGAGKTTLMKHVLENLDGLRVAVVVNDMAEVNIDAALV-DQAdvrqekEKVVELSNGCICCTLREDLLTTI 112
Cdd:PRK11537    4 IAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLIgDRA------TQIKTLTNGCICCSRSNELEDAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 113 MDFAQ-----QNRFDHLLIESSGISEPLPVAETFTFDNkdtgvRLDQYARLDTLVTVVDGVNlfselesiqttatsgqAA 187
Cdd:PRK11537   78 LDLLDnldkgNIQFDRLVIECTGMADPGPIIQTFFSHE-----VLCQRYLLDGVIALVDAVH----------------AD 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 188 YEGDDRPLAQllvDQIEFANVILLNKCDLLSDKQKLDVKttLQSLNPNAAVFQTVRSVLPLKHVLGTGLFSMSDAekneq 267
Cdd:PRK11537  137 EQMNQFTIAQ---SQVGYADRILLTKTDVAGEAEKLRER--LARINARAPVYTVVHGDIDLSLLFNTNGFMLEEN----- 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 268 wLKEARIGEHVAETEEFGIKSFMYRRRLPFHPERLRKLMDD--AESLPGVIRAKGFCWIATRPRfvaVLSFVGSLRdmsq 345
Cdd:PRK11537  207 -VVSTKPRFHFIADKQNDISSIVVELDYPVDISEVSRVMENllLESADKLLRYKGMLWIDGEPN---RLLFQGVQR---- 278
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2291339184 346 gqpwwaameteLWpeglsedlrsSGLWQEPFGDRSRE--LVVIG-QYEQADIEARLDA 400
Cdd:PRK11537  279 -----------LY----------SADWDRPWGDETPHstLVFIGiQLPEEEIRAAFAG 315
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
286-402 2.07e-20

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: 85.34  E-value: 2.07e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184  286 IKSFMYRRRLPFHPERLRKLMDDAesLPGVIRAKGFCWIATRPRFVAVLSFVGSLRDMSQGQPWWAAmetelwpeglsed 365
Cdd:smart00833   1 ISSFVYRARRPFHPQRLLAALDEL--PEGVLRAKGFFWLASRPDLPGVLSQAGGRLRIEPAGAWPAA------------- 65
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2291339184  366 lrssglwqepfGDRSRELVVIGQ-YEQADIEARLDACL 402
Cdd:smart00833  66 -----------GDRRTRLVFIGRdLDEEAIRAALDACL 92
 
Name Accession Description Interval E-value
chaper_GTP_ZigA NF038288
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ...
34-426 3.86e-179

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: 505.08  E-value: 3.86e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184  34 LPVTVLSGFLGAGKTTLMKHVLENLDGLRVAVVVNDMAEVNIDAALVDQADV---RQEkEKVVELSNGCICCTLREDLLT 110
Cdd:NF038288    1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGAslsRTE-EKLVEMSNGCICCTLREDLLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 111 TIMDFAQQNRFDHLLIESSGISEPLPVAETFTFDNKDtGVRLDQYARLDTLVTVVDGVNLFSELESIQTTATSGQAAYEG 190
Cdd:NF038288   80 EVRRLAREGRFDYLVIESTGISEPLPVAETFTFADED-GVSLSDVARLDTMVTVVDAVNFLRDYDSADSLQERGESLGEE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 191 DDRPLAQLLVDQIEFANVILLNKCDLLSDKQKLDVKTTLQSLNPNAAVFQTVRSVLPLKHVLGTGLFSMSDAEKNEQWLK 270
Cdd:NF038288  159 DERTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERAAQAPGWLK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 271 EARiGEHVAETEEFGIKSFMYRRRLPFHPERLRKLMDDaESLPGVIRAKGFCWIATRPRFVAVLSFVGSLrdMSQGQP-- 348
Cdd:NF038288  239 ELR-GEHTPETEEYGISSFVYRARRPFHPQRFYDFLHS-EWPGKVLRSKGFFWLASRPDFAGSWSQAGGI--ARHGPAgm 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 349 WWAAMETELWPEglSEDLRSSGL--WQEPFGDRSRELVVIGQ-YEQADIEARLDACLLTKDEMAQPQpwsfsDTWPAWED 425
Cdd:NF038288  315 WWAAVPRERWPQ--DEESLAAIRenWDEPFGDRRQELVFIGQdMDEAALRAALDACLLTDEEMAAGP-----EAWATLPD 387

                  .
gi 2291339184 426 P 426
Cdd:NF038288  388 P 388
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
32-404 6.38e-128

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 372.20  E-value: 6.38e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184  32 DRLPVTVLSGFLGAGKTTLMKHVLENLDGLRVAVVVNDMAEVNIDAALVDQADvrqekEKVVELSNGCICCTLREDLLTT 111
Cdd:COG0523     2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRDTD-----EEIVELSNGCICCTLREDLLPA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 112 IMDFAQQNRFDHLLIESSGISEPLPVAETFTFDnkdtgVRLDQYARLDTLVTVVDGVNLFSELesiqttatsgqaayegD 191
Cdd:COG0523    77 LRRLLRRGRFDRLLIETTGLADPAPVAQTFTFD-----PELRDRLRLDGVVTVVDARNLLDDL----------------A 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 192 DRPLAQLLVDQIEFANVILLNKCDLLSDKQKLDVKTTLQSLNPNAAVFQTVRSVLPLKHVLGTGLFSMSDAEKNEQWLKE 271
Cdd:COG0523   136 DRTLHELLVDQIAFADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWLEE 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 272 ARIGEHVAeteefGIKSFMYRRRLPFHPERLRKLMDDAesLPGVIRAKGFCWIATRPRfVAVLSFVGSLRDMSQGQPWWA 351
Cdd:COG0523   216 LRDHEHDD-----GIRSFVFRSDRPFDPERLADFLEEL--GPGVLRAKGFLWLAGRPR-RLVFQGVGGRLSLEPLGPWPA 287
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2291339184 352 ametelwpeglsedlrssglwqepfGDRSRELVVIGQ-YEQADIEARLDACLLT 404
Cdd:COG0523   288 -------------------------DDRRSRLVFIGRdLDEAALEAALDACLLT 316
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
35-255 3.61e-84

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: 256.29  E-value: 3.61e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184  35 PVTVLSGFLGAGKTTLMKHVLENLDGLRVAVVVNDMAEVNIDAALVDQADvrqEKEKVVELSNGCICCTLREDLLTTIMD 114
Cdd:cd03112     1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSG---GGEEVVELSNGCICCTLKGDLVKALEQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 115 FAQQ-NRFDHLLIESSGISEPLPVAETFTFDNkdtgvRLDQYARLDTLVTVVDGVNLFSELesiqttatsgqaayegDDR 193
Cdd:cd03112    78 LLERrGKFDYILIETTGLADPGPIAQTLWSDE-----ELESRLRLDGVVTVVDAKNFLKQL----------------DEE 136
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2291339184 194 PLAQLLVDQIEFANVILLNKCDLLSDKQKLDVKTTLQSLNPNAAVFQTVRSVLPLKHVLGTG 255
Cdd:cd03112   137 DVSDLAVDQIAFADVIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGTG 198
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
35-240 1.10e-63

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: 202.87  E-value: 1.10e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184  35 PVTVLSGFLGAGKTTLMKHVLENL-DGLRVAVVVNDMAEVNIDAALVDQADVrqekeKVVELSNGCICCTLREDLLTTIM 113
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLKQNrAGLRIAVIVNEFGETGIDAELLSETGV-----LIVELSNGCICCTIREDLSMALE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 114 DFAQQN-RFDHLLIESSGISEPLPVAETFTFDNkdtgvrLDQYARLDTLVTVVDgvnlfselesiqttatsgqAAYEGDD 192
Cdd:pfam02492  76 ALLEREgRLDVIFIETTGLAEPAPVAQTFLSPE------LRSPVLLDGVITVVD-------------------AANEADG 130
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2291339184 193 RPLAQLLVDQIEFANVILLNKCDLLSDKQKLDV-KTTLQSLNPNAAVFQ 240
Cdd:pfam02492 131 EKIPRKAGDQIAFADLIVLNKTDLAPEVALLEVlEEDLRRLNPGAPVVP 179
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
33-398 2.91e-45

cobalamin biosynthesis protein CobW; The family of proteins identified by this model is generally found proximal to the trimeric cobaltochelatase subunit CobN which is essential for vitamin B12 (cobalamin) biosynthesis. The protein contains an 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. A broader CobW family is delineated by two Pfam models which identify the N- and C-terminal domains (pfam02492 and pfam07683). [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274151 [Multi-domain]  Cd Length: 341  Bit Score: 160.30  E-value: 2.91e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184  33 RLPVTVLSGFLGAGKTTLMKHVLENLDGLRVAVVVNDMAEVNIDAALVDQ-ADVRQEKEKVVELSNGCICCTLREDLLTT 111
Cdd:TIGR02475   3 KIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKAcGIEGCSEENIVELANGCICCTVADDFIPT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 112 IMDF-AQQNRFDHLLIESSGISEPLPVAETFTFDNkdtgVRldQYARLDTLVTVVDGVNLFSELESIQTTATSGQAAYEG 190
Cdd:TIGR02475  83 MTKLlARRQRPDHILIETSGLALPKPLVQAFQWPE----IR--SRVTVDGVVTVVDGPAVAAGRFAADPDALDAQRAADD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 191 D---DRPLAQLLVDQIEFANVILLNKCDLLSDKQKLDVKTTLQSLNPNAA-VFQTVRSVLPLKHVLGTGLFSMSDAEKNE 266
Cdd:TIGR02475 157 NldhETPLEELFEDQLACADLVILNKADLLDAAGLARVRAEIAAELPRAVkIVEASHGEVDARVLLGLGAAAEDDLDNRP 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 267 QWLKEARIGEHvaETEEFgiKSFMYRRRLPFHPERLRKLMDDAESLPGVIRAKGFCWIATRPRFVaVLSFVGSLRDMSQG 346
Cdd:TIGR02475 237 SHHDFEGGEEH--DHDEF--DSVVVDLGEVADPAALRQRLERLAEEHDVLRIKGFAAVPGKPMRL-LVQGVGQRVDSYYD 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2291339184 347 QPWWAAMetelwpeglsedlrssglwqepfgDRSRELVVIGQ--YEQADIEARL 398
Cdd:TIGR02475 312 RPWQAAE------------------------TRQTRLVVIGLhdLDQAAIRAAL 341
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
34-400 4.27e-31

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 121.35  E-value: 4.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184  34 LPVTVLSGFLGAGKTTLMKHVLENLDGLRVAVVVNDMAEVNIDAALV-DQAdvrqekEKVVELSNGCICCTLREDLLTTI 112
Cdd:PRK11537    4 IAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLIgDRA------TQIKTLTNGCICCSRSNELEDAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 113 MDFAQ-----QNRFDHLLIESSGISEPLPVAETFTFDNkdtgvRLDQYARLDTLVTVVDGVNlfselesiqttatsgqAA 187
Cdd:PRK11537   78 LDLLDnldkgNIQFDRLVIECTGMADPGPIIQTFFSHE-----VLCQRYLLDGVIALVDAVH----------------AD 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 188 YEGDDRPLAQllvDQIEFANVILLNKCDLLSDKQKLDVKttLQSLNPNAAVFQTVRSVLPLKHVLGTGLFSMSDAekneq 267
Cdd:PRK11537  137 EQMNQFTIAQ---SQVGYADRILLTKTDVAGEAEKLRER--LARINARAPVYTVVHGDIDLSLLFNTNGFMLEEN----- 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 268 wLKEARIGEHVAETEEFGIKSFMYRRRLPFHPERLRKLMDD--AESLPGVIRAKGFCWIATRPRfvaVLSFVGSLRdmsq 345
Cdd:PRK11537  207 -VVSTKPRFHFIADKQNDISSIVVELDYPVDISEVSRVMENllLESADKLLRYKGMLWIDGEPN---RLLFQGVQR---- 278
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2291339184 346 gqpwwaameteLWpeglsedlrsSGLWQEPFGDRSRE--LVVIG-QYEQADIEARLDA 400
Cdd:PRK11537  279 -----------LY----------SADWDRPWGDETPHstLVFIGiQLPEEEIRAAFAG 315
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
286-402 2.07e-20

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: 85.34  E-value: 2.07e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184  286 IKSFMYRRRLPFHPERLRKLMDDAesLPGVIRAKGFCWIATRPRFVAVLSFVGSLRDMSQGQPWWAAmetelwpeglsed 365
Cdd:smart00833   1 ISSFVYRARRPFHPQRLLAALDEL--PEGVLRAKGFFWLASRPDLPGVLSQAGGRLRIEPAGAWPAA------------- 65
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2291339184  366 lrssglwqepfGDRSRELVVIGQ-YEQADIEARLDACL 402
Cdd:smart00833  66 -----------GDRRTRLVFIGRdLDEEAIRAALDACL 92
CobW_C pfam07683
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ...
286-402 2.15e-18

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: 79.59  E-value: 2.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 286 IKSFMYRRRLPFHPERLRKLMDDAESLPGVIRAKGFCWIATRPRfVAVLSFVGSLRDMSQGQPWWaametelwpeglsed 365
Cdd:pfam07683   1 ISSFVFRADRPFDPERLEAWLEDLLLPEGILRAKGILWLAGRPR-PLVFQGVGGRLSLEPAGRWW--------------- 64
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2291339184 366 lrssglwqePFGDRSRELVVIGQ-YEQADIEARLDACL 402
Cdd:pfam07683  65 ---------PDEDRRSRLVFIGRdLDREALRAALDACL 93
HypB cd05390
nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the ...
44-239 9.37e-07

nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the maturation of nickel-dependent hydrogenases, like carbon monoxide dehydrogenase or urease. HypB is a GTP-binding protein and has GTP hyrolase activity. It forms homodimer and is capable of binding two nickel ions and two zinc ions. The active site is located on the dimer interface. Energy from hydrolysis of GTP is used to insert nickels into hydrogenases.


Pssm-ID: 349775  Cd Length: 203  Bit Score: 49.13  E-value: 9.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184  44 GAGKTTLMKHVLENL-DGLRVAVVVNDMaEVNIDAALVDQADVrqekeKVVELSNGCIcCTLREDLLTTIMDFAQQNRFD 122
Cdd:cd05390    31 GSGKTTLLERTIDALkDELKIAVIEGDL-ETDNDAERIRATGV-----PAIQINTGGA-CHLDADMVARALHDLDLDELD 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 123 HLLIESSGisePLPVAETFtfdnkDTGvrldqyarldTLVTVVdgvnLFSelesiqTTatsgqaayEGDDRPLAQLLVDQ 202
Cdd:cd05390   104 LLFIENVG---NLVCPAEF-----DLG----------EHKNVV----LLS------VT--------EGDDKPLKYPLMFQ 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2291339184 203 IefANVILLNKCDLLS----DKQKldVKTTLQSLNPNAAVF 239
Cdd:cd05390   148 V--ADVVLINKIDLLPyfdfDVEK--AKEDIKKLNPNAPII 184
HypB COG0378
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ...
44-241 2.03e-05

Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440147 [Multi-domain]  Cd Length: 200  Bit Score: 45.05  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184  44 GAGKTTLMKHVLENL-DGLRVAVVVNDMAEVNiDAALVDQADVRqekekVVELSNGCiCCTLREDLLTTIMDFAQQNRFD 122
Cdd:COG0378    23 GSGKTTLLEKTIRALkDRLRIAVIEGDIYTTE-DAERLRAAGVP-----VVQINTGG-CCHLDASMVLEALEELDLPDLD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2291339184 123 HLLIESSGIseplPVAETFTfdnkDTGVrldqyarlDTLVTVVDgvnlfselesiqTTatsgqaayEGDDRPL----Aql 198
Cdd:COG0378    96 LLFIENVGN----LVCPAFF----PLGE--------DLKVVVLS------------VT--------EGDDKPRkyppM-- 137
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2291339184 199 lvdqIEFANVILLNKCDLLS----DKQKLdvKTTLQSLNPNAAVFQT 241
Cdd:COG0378   138 ----FTAADLLVINKIDLAPyvgfDLEVM--EEDARRVNPGAPIFEV 178
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
38-65 2.16e-03

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 38.90  E-value: 2.16e-03
                          10        20
                  ....*....|....*....|....*...
gi 2291339184  38 VLSGFLGAGKTTLMKHVLENLDGLRVAV 65
Cdd:COG0194     6 VLSGPSGAGKTTLVKALLERDPDLRFSV 33
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
35-66 8.80e-03

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 38.42  E-value: 8.80e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2291339184  35 PVTVLSGFLGAGKTTLMKHVLENLD--GLRVAVV 66
Cdd:COG0507   141 RVSVLTGGAGTGKTTTLRALLAALEalGLRVALA 174
 
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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