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Conserved domains on  [gi|504095838|ref|WP_014329832|]
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GTP-binding protein [Sinorhizobium fredii]

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 ...
8-360 7.16e-144

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


:

Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 409.95  E-value: 7.16e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838   8 KPIPVTVLTGYLGAGKTTLLNRILSENHGRKYAVIVNEFGEIGIDNDLIVESDEEIYEMNNGCVCCTVRGDLIRVVEGLM 87
Cdd:COG0523    2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRDTDEEIVELSNGCICCTLREDLLPALRRLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  88 RRpGRFDAIIVETTGLADPVPVAQTFFMDDDVRAKTELDAVVALVDAKHLPLRLKD---SREAEDQIAFADVVLLNKTDL 164
Cdd:COG0523   82 RR-GRFDRLLIETTGLADPAPVAQTFTFDPELRDRLRLDGVVTVVDARNLLDDLADrtlHELLVDQIAFADVIVLNKTDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838 165 VSPEELERIEATVRVINPSARIYRTQRSDIDLGKVLDQGAFNLERALEnDPHFLDQGEQDDHVCGpdcdhdhhhhdhdhh 244
Cdd:COG0523  161 VDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALA-RPGWLEELRDHEHDDG--------------- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838 245 hhdhdhdhhhhhdhapspihdvtVQSISLR-GGEMNPERFFPWIQKItqtdGPNILRLKGIIAFAGDAERYVVQGVHMII 323
Cdd:COG0523  225 -----------------------IRSFVFRsDRPFDPERLADFLEEL----GPGVLRAKGFLWLAGRPRRLVFQGVGGRL 277
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 504095838 324 EGDHQRPWKEGEkRETRLVFIGRDLDREKLERTFKAC 360
Cdd:COG0523  278 SLEPLGPWPADD-RRSRLVFIGRDLDEAALEAALDAC 313
 
Name Accession Description Interval E-value
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
8-360 7.16e-144

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 409.95  E-value: 7.16e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838   8 KPIPVTVLTGYLGAGKTTLLNRILSENHGRKYAVIVNEFGEIGIDNDLIVESDEEIYEMNNGCVCCTVRGDLIRVVEGLM 87
Cdd:COG0523    2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRDTDEEIVELSNGCICCTLREDLLPALRRLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  88 RRpGRFDAIIVETTGLADPVPVAQTFFMDDDVRAKTELDAVVALVDAKHLPLRLKD---SREAEDQIAFADVVLLNKTDL 164
Cdd:COG0523   82 RR-GRFDRLLIETTGLADPAPVAQTFTFDPELRDRLRLDGVVTVVDARNLLDDLADrtlHELLVDQIAFADVIVLNKTDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838 165 VSPEELERIEATVRVINPSARIYRTQRSDIDLGKVLDQGAFNLERALEnDPHFLDQGEQDDHVCGpdcdhdhhhhdhdhh 244
Cdd:COG0523  161 VDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALA-RPGWLEELRDHEHDDG--------------- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838 245 hhdhdhdhhhhhdhapspihdvtVQSISLR-GGEMNPERFFPWIQKItqtdGPNILRLKGIIAFAGDAERYVVQGVHMII 323
Cdd:COG0523  225 -----------------------IRSFVFRsDRPFDPERLADFLEEL----GPGVLRAKGFLWLAGRPRRLVFQGVGGRL 277
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 504095838 324 EGDHQRPWKEGEkRETRLVFIGRDLDREKLERTFKAC 360
Cdd:COG0523  278 SLEPLGPWPADD-RRSRLVFIGRDLDEAALEAALDAC 313
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
11-201 2.89e-102

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: 299.82  E-value: 2.89e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  11 PVTVLTGYLGAGKTTLLNRILSENHGRKYAVIVNEFGEIGIDNDLIVESD--EEIYEMNNGCVCCTVRGDLIRVVEGLMR 88
Cdd:cd03112    1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSGggEEVVELSNGCICCTLKGDLVKALEQLLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  89 RPGRFDAIIVETTGLADPVPVAQTFFMDDDVRAKTELDAVVALVDAKHLPLRLKD---SREAEDQIAFADVVLLNKTDLV 165
Cdd:cd03112   81 RRGKFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVVDAKNFLKQLDEedvSDLAVDQIAFADVIVLNKTDLV 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 504095838 166 SPEELERIEATVRVINPSARIYRTQRSDIDLGKVLD 201
Cdd:cd03112  161 DEEELEALRARIRALNPGAKIVETTYGRVDLEELLG 196
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
11-188 1.61e-78

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: 238.69  E-value: 1.61e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838   11 PVTVLTGYLGAGKTTLLNRILSEN-HGRKYAVIVNEFGEIGIDNDLIVESDEEIYEMNNGCVCCTVRGDLIRVVEGLMRR 89
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLKQNrAGLRIAVIVNEFGETGIDAELLSETGVLIVELSNGCICCTIREDLSMALEALLER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838   90 PGRFDAIIVETTGLADPVPVAQTFFmDDDVRAKTELDAVVALVDAKHLPLRLKDSREAEDQIAFADVVLLNKTDLVSPEE 169
Cdd:pfam02492  81 EGRLDVIFIETTGLAEPAPVAQTFL-SPELRSPVLLDGVITVVDAANEADGEKIPRKAGDQIAFADLIVLNKTDLAPEVA 159
                         170       180
                  ....*....|....*....|
gi 504095838  170 -LERIEATVRVINPSARIYR 188
Cdd:pfam02492 160 lLEVLEEDLRRLNPGAPVVP 179
chaper_GTP_ZigA NF038288
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ...
10-210 6.63e-67

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: 216.18  E-value: 6.63e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  10 IPVTVLTGYLGAGKTTLLNRILSENHGRKYAVIVNEFGEIGIDNDLIVE-------SDEEIYEMNNGCVCCTVRGDLIRV 82
Cdd:NF038288   1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNggaslsrTEEKLVEMSNGCICCTLREDLLVE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  83 VEGLMRRpGRFDAIIVETTGLADPVPVAQTF-FMDDDVRAKTE---LDAVVALVDAKHLplrLKDSREAE---------- 148
Cdd:NF038288  81 VRRLARE-GRFDYLVIESTGISEPLPVAETFtFADEDGVSLSDvarLDTMVTVVDAVNF---LRDYDSADslqergeslg 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504095838 149 ------------DQIAFADVVLLNKTDLVSPEELERIEATVRVINPSARIYRTQRSDIDLGKVLDQGAFNLERA 210
Cdd:NF038288 157 eedertvvdllvDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERA 230
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
8-359 4.44e-63

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 203.78  E-value: 4.44e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838   8 KPIPVTVLTGYLGAGKTTLLNRILSENHGRKYAVIVNEFGEIGIDNDLIVESDEEIYEMNNGCVCCTVRGD----LIRVV 83
Cdd:PRK11537   2 NPIAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLIGDRATQIKTLTNGCICCSRSNEledaLLDLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  84 EGLMRRPGRFDAIIVETTGLADPVPVAQTFFMDDDVRAKTELDAVVALVDAKHLPLRLKDSREAEDQIAFADVVLLNKTD 163
Cdd:PRK11537  82 DNLDKGNIQFDRLVIECTGMADPGPIIQTFFSHEVLCQRYLLDGVIALVDAVHADEQMNQFTIAQSQVGYADRILLTKTD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838 164 LVSpeELERIEATVRVINPSARIYRTQRSDIDLGKVLDQGAFNLERALE-NDPHFLDQGEQDDHVcgpdcdhdhhhhdhd 242
Cdd:PRK11537 162 VAG--EAEKLRERLARINARAPVYTVVHGDIDLSLLFNTNGFMLEENVVsTKPRFHFIADKQNDI--------------- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838 243 hhhhdhdhDHHHHHDHAPSPIHDVT--VQSISLRGGEmnperffpwiqkitqtdgpNILRLKGIIAFAGDAERYVVQGVH 320
Cdd:PRK11537 225 --------SSIVVELDYPVDISEVSrvMENLLLESAD-------------------KLLRYKGMLWIDGEPNRLLFQGVQ 277
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 504095838 321 MIIEGDHQRPWkEGEKRETRLVFIGRDLDREKLERTFKA 359
Cdd:PRK11537 278 RLYSADWDRPW-GDETPHSTLVFIGIQLPEEEIRAAFAG 315
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
10-357 4.56e-61

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: 199.59  E-value: 4.56e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838   10 IPVTVLTGYLGAGKTTLLNRILSENHGRKYAVIVNEFGEIGIDNDLIVE------SDEEIYEMNNGCVCCTVRGDLIRVV 83
Cdd:TIGR02475   4 IPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKAcgiegcSEENIVELANGCICCTVADDFIPTM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838   84 EGLMRRPGRFDAIIVETTGLADPVPVAQTFFMdDDVRAKTELDAVVALVDAKHL--------PLRLKDSREA-------- 147
Cdd:TIGR02475  84 TKLLARRQRPDHILIETSGLALPKPLVQAFQW-PEIRSRVTVDGVVTVVDGPAVaagrfaadPDALDAQRAAddnldhet 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  148 ------EDQIAFADVVLLNKTDLVSPEELERIEATVRVINPSA-RIYRTQRSDIDLGKVLDQGAfNLERALENDPHFLDQ 220
Cdd:TIGR02475 163 pleelfEDQLACADLVILNKADLLDAAGLARVRAEIAAELPRAvKIVEASHGEVDARVLLGLGA-AAEDDLDNRPSHHDF 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  221 GEQDDHVcgpdcdhdhhhhdhdhhhhdhdhdhhhhhdhapspiHDvTVQSISLRGGEM-NPERFFPWIQKITQTdgPNIL 299
Cdd:TIGR02475 242 EGGEEHD------------------------------------HD-EFDSVVVDLGEVaDPAALRQRLERLAEE--HDVL 282
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 504095838  300 RLKGIIAFAGDAERYVVQGVHMIIEGDHQRPWKEGEKRETRLVFIG-RDLDREKLERTF 357
Cdd:TIGR02475 283 RIKGFAAVPGKPMRLLVQGVGQRVDSYYDRPWQAAETRQTRLVVIGlHDLDQAAIRAAL 341
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
268-360 6.29e-16

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: 72.24  E-value: 6.29e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838   268 VQSISLR-GGEMNPERFFPWIQKITqtdgPNILRLKGIIAFAGDAER-YVVQGVHMIIEGDHQRPWKEGEKRETRLVFIG 345
Cdd:smart00833   1 ISSFVYRaRRPFHPQRLLAALDELP----EGVLRAKGFFWLASRPDLpGVLSQAGGRLRIEPAGAWPAAGDRRTRLVFIG 76
                           90
                   ....*....|....*
gi 504095838   346 RDLDREKLERTFKAC 360
Cdd:smart00833  77 RDLDEEAIRAALDAC 91
 
Name Accession Description Interval E-value
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
8-360 7.16e-144

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 409.95  E-value: 7.16e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838   8 KPIPVTVLTGYLGAGKTTLLNRILSENHGRKYAVIVNEFGEIGIDNDLIVESDEEIYEMNNGCVCCTVRGDLIRVVEGLM 87
Cdd:COG0523    2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRDTDEEIVELSNGCICCTLREDLLPALRRLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  88 RRpGRFDAIIVETTGLADPVPVAQTFFMDDDVRAKTELDAVVALVDAKHLPLRLKD---SREAEDQIAFADVVLLNKTDL 164
Cdd:COG0523   82 RR-GRFDRLLIETTGLADPAPVAQTFTFDPELRDRLRLDGVVTVVDARNLLDDLADrtlHELLVDQIAFADVIVLNKTDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838 165 VSPEELERIEATVRVINPSARIYRTQRSDIDLGKVLDQGAFNLERALEnDPHFLDQGEQDDHVCGpdcdhdhhhhdhdhh 244
Cdd:COG0523  161 VDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALA-RPGWLEELRDHEHDDG--------------- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838 245 hhdhdhdhhhhhdhapspihdvtVQSISLR-GGEMNPERFFPWIQKItqtdGPNILRLKGIIAFAGDAERYVVQGVHMII 323
Cdd:COG0523  225 -----------------------IRSFVFRsDRPFDPERLADFLEEL----GPGVLRAKGFLWLAGRPRRLVFQGVGGRL 277
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 504095838 324 EGDHQRPWKEGEkRETRLVFIGRDLDREKLERTFKAC 360
Cdd:COG0523  278 SLEPLGPWPADD-RRSRLVFIGRDLDEAALEAALDAC 313
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
11-201 2.89e-102

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: 299.82  E-value: 2.89e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  11 PVTVLTGYLGAGKTTLLNRILSENHGRKYAVIVNEFGEIGIDNDLIVESD--EEIYEMNNGCVCCTVRGDLIRVVEGLMR 88
Cdd:cd03112    1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSGggEEVVELSNGCICCTLKGDLVKALEQLLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  89 RPGRFDAIIVETTGLADPVPVAQTFFMDDDVRAKTELDAVVALVDAKHLPLRLKD---SREAEDQIAFADVVLLNKTDLV 165
Cdd:cd03112   81 RRGKFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVVDAKNFLKQLDEedvSDLAVDQIAFADVIVLNKTDLV 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 504095838 166 SPEELERIEATVRVINPSARIYRTQRSDIDLGKVLD 201
Cdd:cd03112  161 DEEELEALRARIRALNPGAKIVETTYGRVDLEELLG 196
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
11-188 1.61e-78

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: 238.69  E-value: 1.61e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838   11 PVTVLTGYLGAGKTTLLNRILSEN-HGRKYAVIVNEFGEIGIDNDLIVESDEEIYEMNNGCVCCTVRGDLIRVVEGLMRR 89
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLKQNrAGLRIAVIVNEFGETGIDAELLSETGVLIVELSNGCICCTIREDLSMALEALLER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838   90 PGRFDAIIVETTGLADPVPVAQTFFmDDDVRAKTELDAVVALVDAKHLPLRLKDSREAEDQIAFADVVLLNKTDLVSPEE 169
Cdd:pfam02492  81 EGRLDVIFIETTGLAEPAPVAQTFL-SPELRSPVLLDGVITVVDAANEADGEKIPRKAGDQIAFADLIVLNKTDLAPEVA 159
                         170       180
                  ....*....|....*....|
gi 504095838  170 -LERIEATVRVINPSARIYR 188
Cdd:pfam02492 160 lLEVLEEDLRRLNPGAPVVP 179
chaper_GTP_ZigA NF038288
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ...
10-210 6.63e-67

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: 216.18  E-value: 6.63e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  10 IPVTVLTGYLGAGKTTLLNRILSENHGRKYAVIVNEFGEIGIDNDLIVE-------SDEEIYEMNNGCVCCTVRGDLIRV 82
Cdd:NF038288   1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNggaslsrTEEKLVEMSNGCICCTLREDLLVE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  83 VEGLMRRpGRFDAIIVETTGLADPVPVAQTF-FMDDDVRAKTE---LDAVVALVDAKHLplrLKDSREAE---------- 148
Cdd:NF038288  81 VRRLARE-GRFDYLVIESTGISEPLPVAETFtFADEDGVSLSDvarLDTMVTVVDAVNF---LRDYDSADslqergeslg 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504095838 149 ------------DQIAFADVVLLNKTDLVSPEELERIEATVRVINPSARIYRTQRSDIDLGKVLDQGAFNLERA 210
Cdd:NF038288 157 eedertvvdllvDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERA 230
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
8-359 4.44e-63

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 203.78  E-value: 4.44e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838   8 KPIPVTVLTGYLGAGKTTLLNRILSENHGRKYAVIVNEFGEIGIDNDLIVESDEEIYEMNNGCVCCTVRGD----LIRVV 83
Cdd:PRK11537   2 NPIAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLIGDRATQIKTLTNGCICCSRSNEledaLLDLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  84 EGLMRRPGRFDAIIVETTGLADPVPVAQTFFMDDDVRAKTELDAVVALVDAKHLPLRLKDSREAEDQIAFADVVLLNKTD 163
Cdd:PRK11537  82 DNLDKGNIQFDRLVIECTGMADPGPIIQTFFSHEVLCQRYLLDGVIALVDAVHADEQMNQFTIAQSQVGYADRILLTKTD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838 164 LVSpeELERIEATVRVINPSARIYRTQRSDIDLGKVLDQGAFNLERALE-NDPHFLDQGEQDDHVcgpdcdhdhhhhdhd 242
Cdd:PRK11537 162 VAG--EAEKLRERLARINARAPVYTVVHGDIDLSLLFNTNGFMLEENVVsTKPRFHFIADKQNDI--------------- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838 243 hhhhdhdhDHHHHHDHAPSPIHDVT--VQSISLRGGEmnperffpwiqkitqtdgpNILRLKGIIAFAGDAERYVVQGVH 320
Cdd:PRK11537 225 --------SSIVVELDYPVDISEVSrvMENLLLESAD-------------------KLLRYKGMLWIDGEPNRLLFQGVQ 277
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 504095838 321 MIIEGDHQRPWkEGEKRETRLVFIGRDLDREKLERTFKA 359
Cdd:PRK11537 278 RLYSADWDRPW-GDETPHSTLVFIGIQLPEEEIRAAFAG 315
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
10-357 4.56e-61

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: 199.59  E-value: 4.56e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838   10 IPVTVLTGYLGAGKTTLLNRILSENHGRKYAVIVNEFGEIGIDNDLIVE------SDEEIYEMNNGCVCCTVRGDLIRVV 83
Cdd:TIGR02475   4 IPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKAcgiegcSEENIVELANGCICCTVADDFIPTM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838   84 EGLMRRPGRFDAIIVETTGLADPVPVAQTFFMdDDVRAKTELDAVVALVDAKHL--------PLRLKDSREA-------- 147
Cdd:TIGR02475  84 TKLLARRQRPDHILIETSGLALPKPLVQAFQW-PEIRSRVTVDGVVTVVDGPAVaagrfaadPDALDAQRAAddnldhet 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  148 ------EDQIAFADVVLLNKTDLVSPEELERIEATVRVINPSA-RIYRTQRSDIDLGKVLDQGAfNLERALENDPHFLDQ 220
Cdd:TIGR02475 163 pleelfEDQLACADLVILNKADLLDAAGLARVRAEIAAELPRAvKIVEASHGEVDARVLLGLGA-AAEDDLDNRPSHHDF 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  221 GEQDDHVcgpdcdhdhhhhdhdhhhhdhdhdhhhhhdhapspiHDvTVQSISLRGGEM-NPERFFPWIQKITQTdgPNIL 299
Cdd:TIGR02475 242 EGGEEHD------------------------------------HD-EFDSVVVDLGEVaDPAALRQRLERLAEE--HDVL 282
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 504095838  300 RLKGIIAFAGDAERYVVQGVHMIIEGDHQRPWKEGEKRETRLVFIG-RDLDREKLERTF 357
Cdd:TIGR02475 283 RIKGFAAVPGKPMRLLVQGVGQRVDSYYDRPWQAAETRQTRLVVIGlHDLDQAAIRAAL 341
CobW_C pfam07683
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ...
268-361 1.14e-28

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: 106.94  E-value: 1.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  268 VQSISLR-GGEMNPERFFPWIQKITQtdGPNILRLKGIIAFAGDAERYVVQGVHMIIEGDHQRPWKEGEKRETRLVFIGR 346
Cdd:pfam07683   1 ISSFVFRaDRPFDPERLEAWLEDLLL--PEGILRAKGILWLAGRPRPLVFQGVGGRLSLEPAGRWWPDEDRRSRLVFIGR 78
                          90
                  ....*....|....*
gi 504095838  347 DLDREKLERTFKACE 361
Cdd:pfam07683  79 DLDREALRAALDACL 93
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
268-360 6.29e-16

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: 72.24  E-value: 6.29e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838   268 VQSISLR-GGEMNPERFFPWIQKITqtdgPNILRLKGIIAFAGDAER-YVVQGVHMIIEGDHQRPWKEGEKRETRLVFIG 345
Cdd:smart00833   1 ISSFVYRaRRPFHPQRLLAALDELP----EGVLRAKGFFWLASRPDLpGVLSQAGGRLRIEPAGAWPAAGDRRTRLVFIG 76
                           90
                   ....*....|....*
gi 504095838   346 RDLDREKLERTFKAC 360
Cdd:smart00833  77 RDLDEEAIRAALDAC 91
shulin_C20orf194-like cd22936
Tetrahymena thermophila shulin, human uncharacterized protein C20orf194, and similar proteins; ...
7-206 5.61e-13

Tetrahymena thermophila shulin, human uncharacterized protein C20orf194, and similar proteins; This family contains Tetrahymena thermophila shulin, human uncharacterized protein C20orf194, and similar proteins. Shulin is a negative regulator of the ciliary outer dynein arm (ODA). It binds newly synthesized ODAs, locks the dynein motors together by shutting off motor activity, and facilitates the delivery of ODAs from the cytoplasm to their final position in the cilia. ODAs, together with inner dynein arms (IDAs), are arrayed along a microtubule-based structure called the axoneme and drive the movement of cilia. Human C20orf194 interacts with the small GTPase Arf-like 3 (ARL3) and may act as its effector. The rs6051702 single nucleotide polymorphism (SNP) within the C20orf194 gene is associated with inosine triphosphatase (ITPA) functional gene polymorphisms that were found to influence RBV-induced hemoglobin (Hb)-decline during treatment of chronic hepatitis C patients with pegylated interferon (PEG-IFN) plus ribavirin (RBV).


Pssm-ID: 438574 [Multi-domain]  Cd Length: 1092  Bit Score: 70.46  E-value: 5.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838    7 QKPIPVTVLTGYLGAGKTTLLNrILSENHGRKYAVIVnefgeIGIDNDLIVESDEEIYEMNNGCVCCTVRgdlIRVVEGL 86
Cdd:cd22936   687 KDKIVITIVTGIPGSGKEKLAA-NLVSLAKEDNRWHV-----LRQDLRESSAFDDKSLQKQLSSVLSSQR---RQAARKR 757
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838   87 MRrpgrfdaIIVETTGLADPVPVAQTFFMDDDVRAKTELDAVVALVDAkhLPLRLKDSREAE----DQIA---FADVVLL 159
Cdd:cd22936   758 PR-------ILVVVPGYTDDVVIAAALHPDPEVSGSFKIGAVTTCVNP--LNFFMEHNRNTFpkllDQLAqgwVTNVVFT 828
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 504095838  160 NKTDlVSPEELERIEATVRVINPSARIYRTQRSDI----DLGKVLDQGAFN 206
Cdd:cd22936   829 STTD-NQDPELEEVQKLLRAVNPDAAFILALKGNVtrgeDAELILSENSFS 878
HypB COG0378
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ...
20-189 6.00e-06

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


Pssm-ID: 440147 [Multi-domain]  Cd Length: 200  Bit Score: 46.59  E-value: 6.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  20 GAGKTTLLNRILSENHGR-KYAVIVNefgeigidnDLIVESDEEIYE--------MNNGCVCCTVRGDLIRVVEGLmrRP 90
Cdd:COG0378   23 GSGKTTLLEKTIRALKDRlRIAVIEG---------DIYTTEDAERLRaagvpvvqINTGGCCHLDASMVLEALEEL--DL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  91 GRFDAIIVETTGladpVPVAQTFFmddDVRAktelDAVVALVD--------AKHLPLrlkdsreaedqIAFADVVLLNKT 162
Cdd:COG0378   92 PDLDLLFIENVG----NLVCPAFF---PLGE----DLKVVVLSvtegddkpRKYPPM-----------FTAADLLVINKI 149
                        170       180
                 ....*....|....*....|....*....
gi 504095838 163 DLVS--PEELERIEATVRVINPSARIYRT 189
Cdd:COG0378  150 DLAPyvGFDLEVMEEDARRVNPGAPIFEV 178
YjiA COG2403
Zn/Ni/Co-binding GTPase YjiA, predicted metallochaperone, CobW/Nha3/YciC family [Inorganic ion ...
154-189 1.82e-04

Zn/Ni/Co-binding GTPase YjiA, predicted metallochaperone, CobW/Nha3/YciC family [Inorganic ion transport and metabolism];


Pssm-ID: 441959  Cd Length: 441  Bit Score: 43.29  E-value: 1.82e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 504095838 154 ADVVLLNKTDLVSPEELERIEATVRVINPSARIYRT 189
Cdd:COG2403  262 ADVVVINKVDTADPEDIETVRENIRKVNPKAEIIEA 297
HypB cd05390
nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the ...
20-186 1.99e-03

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: 39.12  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  20 GAGKTTLLNRILSE-NHGRKYAVIVnefGEIGIDNDL--IVESDEEIYEMNNGCVCcTVRGDLI-RVVEGLmrRPGRFDA 95
Cdd:cd05390   31 GSGKTTLLERTIDAlKDELKIAVIE---GDLETDNDAerIRATGVPAIQINTGGAC-HLDADMVaRALHDL--DLDELDL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838  96 IIVETTG-LADPVpvaqTFFMDDDVRAK----TELDAVVAlvdaKHlPLRLKDsreaedqiafADVVLLNKTDLVSPEE- 169
Cdd:cd05390  105 LFIENVGnLVCPA----EFDLGEHKNVVllsvTEGDDKPL----KY-PLMFQV----------ADVVLINKIDLLPYFDf 165
                        170
                 ....*....|....*...
gi 504095838 170 -LERIEATVRVINPSARI 186
Cdd:cd05390  166 dVEKAKEDIKKLNPNAPI 183
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
12-161 7.83e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.58  E-value: 7.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504095838    12 VTVLTGYLGAGKTTLLNRILSENHGRKYAVIVnefgeIGIDNDLIVESDEEIYEMNNGCVCCTVRGDLIRVVEGLMRRPg 91
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIY-----IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKL- 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504095838    92 RFDAIIV-ETTGLADPVPVAQTFFMDDD-VRAKTELDAVVALVDAKHlplRLKDSREAEDQIAFADVVLLNK 161
Cdd:smart00382  78 KPDVLILdEITSLLDAEQEALLLLLEELrLLLLLKSEKNLTVILTTN---DEKDLGPALLRRRFDRRIVLLL 146
 
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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