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Conserved domains on  [gi|2273339399|ref|WP_254656342|]
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GTP-binding protein [Jannaschia sp. CCS1]

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 ...
1-270 3.70e-69

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


:

Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 216.96  E-value: 3.70e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399   1 MPLPLTVVAGYLGAGKTTFINRLLAGDHRLRLMVLVNDFGAINIDAGLIALADGDTIALTNGCVCCTMGADLFMALGDaL 80
Cdd:COG0523     2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRDTDEEIVELSNGCICCTLREDLLPALRR-L 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399  81 DRRPRPDHLIVEASGVADPARIANAALAEPDLA----YGGIVTIVDGQQIDGLCADPMIGAQVRDQIACADLVVVSKvCE 156
Cdd:COG0523    81 LRRGRFDRLLIETTGLADPAPVAQTFTFDPELRdrlrLDGVVTVVDARNLLDDLADRTLHELLVDQIAFADVIVLNK-TD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399 157 L-----SAVLAATLTTLSGASVLLSAD--VTDPATLLCAAPKPTPASAPHP-------------DYQSWSYTGDATLHRE 216
Cdd:COG0523   160 LvdeeeLAALEARLRALNPGAPIVRTShgEVDPALLLDLGLFDLEAALARPgwleelrdhehddGIRSFVFRSDRPFDPE 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2273339399 217 VLSQSVAKRPQALFRLKGHV-MDPNGGAWEVHAVGRHVSVTQAAP----QSHTQLVAIG 270
Cdd:COG0523   240 RLADFLEELGPGVLRAKGFLwLAGRPRRLVFQGVGGRLSLEPLGPwpadDRRSRLVFIG 298
 
Name Accession Description Interval E-value
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
1-270 3.70e-69

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 216.96  E-value: 3.70e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399   1 MPLPLTVVAGYLGAGKTTFINRLLAGDHRLRLMVLVNDFGAINIDAGLIALADGDTIALTNGCVCCTMGADLFMALGDaL 80
Cdd:COG0523     2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRDTDEEIVELSNGCICCTLREDLLPALRR-L 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399  81 DRRPRPDHLIVEASGVADPARIANAALAEPDLA----YGGIVTIVDGQQIDGLCADPMIGAQVRDQIACADLVVVSKvCE 156
Cdd:COG0523    81 LRRGRFDRLLIETTGLADPAPVAQTFTFDPELRdrlrLDGVVTVVDARNLLDDLADRTLHELLVDQIAFADVIVLNK-TD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399 157 L-----SAVLAATLTTLSGASVLLSAD--VTDPATLLCAAPKPTPASAPHP-------------DYQSWSYTGDATLHRE 216
Cdd:COG0523   160 LvdeeeLAALEARLRALNPGAPIVRTShgEVDPALLLDLGLFDLEAALARPgwleelrdhehddGIRSFVFRSDRPFDPE 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2273339399 217 VLSQSVAKRPQALFRLKGHV-MDPNGGAWEVHAVGRHVSVTQAAP----QSHTQLVAIG 270
Cdd:COG0523   240 RLADFLEELGPGVLRAKGFLwLAGRPRRLVFQGVGGRLSLEPLGPwpadDRRSRLVFIG 298
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
4-154 1.42e-55

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: 178.10  E-value: 1.42e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399   4 PLTVVAGYLGAGKTTFINRLLAGDHRLRLMVLVNDFGAINIDAGLIALADG--DTIALTNGCVCCTMGADLFMALGDALD 81
Cdd:cd03112     1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSGGgeEVVELSNGCICCTLKGDLVKALEQLLE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2273339399  82 RRPRPDHLIVEASGVADPARIANAALAEPDLA----YGGIVTIVDGQQIDGLCADPMIGAQVRDQIACADLVVVSKV 154
Cdd:cd03112    81 RRGKFDYILIETTGLADPGPIAQTLWSDEELEsrlrLDGVVTVVDAKNFLKQLDEEDVSDLAVDQIAFADVIVLNKT 157
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
4-154 1.14e-45

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: 152.02  E-value: 1.14e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399   4 PLTVVAGYLGAGKTTFINRLLA-GDHRLRLMVLVNDFGAINIDAGLIALADGDTIALTNGCVCCTMGADLFMALGDALDR 82
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLKqNRAGLRIAVIVNEFGETGIDAELLSETGVLIVELSNGCICCTIREDLSMALEALLER 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2273339399  83 RPRPDHLIVEASGVADPARIANAALAE---PDLAYGGIVTIVDGQQIDGLCADPMIGaqvRDQIACADLVVVSKV 154
Cdd:pfam02492  81 EGRLDVIFIETTGLAEPAPVAQTFLSPelrSPVLLDGVITVVDAANEADGEKIPRKA---GDQIAFADLIVLNKT 152
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
3-274 5.59e-29

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: 112.92  E-value: 5.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399   3 LPLTVVAGYLGAGKTTFINRLLAGDHRLRLMVLVNDFGAINIDA------GLIALADGDTIALTNGCVCCTMGADLFMAL 76
Cdd:TIGR02475   4 IPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGeilkacGIEGCSEENIVELANGCICCTVADDFIPTM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399  77 GDALDRRPRPDHLIVEASGVADPARIAnAALAEPDL----AYGGIVTIVDGQQIDG--LCADPMIGAQVR---------- 140
Cdd:TIGR02475  84 TKLLARRQRPDHILIETSGLALPKPLV-QAFQWPEIrsrvTVDGVVTVVDGPAVAAgrFAADPDALDAQRaaddnldhet 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399 141 -------DQIACADLVVVSKVCELSA-----VLAATLTTLSGASVLLSAD--VTDPATLL--CAAPKPTPASAP------ 198
Cdd:TIGR02475 163 pleelfeDQLACADLVILNKADLLDAaglarVRAEIAAELPRAVKIVEAShgEVDARVLLglGAAAEDDLDNRPshhdfe 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399 199 ------HPDYQSWSYTGDATLHREVLSQSVAK--RPQALFRLKGHVMDPNGGA-WEVHAVGRHVSVT-----QAAPQSHT 264
Cdd:TIGR02475 243 ggeehdHDEFDSVVVDLGEVADPAALRQRLERlaEEHDVLRIKGFAAVPGKPMrLLVQGVGQRVDSYydrpwQAAETRQT 322
                         330
                  ....*....|
gi 2273339399 265 QLVAIGLKSL 274
Cdd:TIGR02475 323 RLVVIGLHDL 332
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
2-153 5.68e-22

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 93.23  E-value: 5.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399   2 PLPLTVVAGYLGAGKTTFINRLLAGDHRLRLMVLVNDFGAINIDAGLIALADGDTIALTNGCVCCTMGADLFMALGDALD 81
Cdd:PRK11537    3 PIAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLIGDRATQIKTLTNGCICCSRSNELEDALLDLLD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399  82 RRPRP----DHLIVEASGVADPARIANAALAEPDLA----YGGIVTIVD----GQQIDGLCAdpmigAQvrDQIACADLV 149
Cdd:PRK11537   83 NLDKGniqfDRLVIECTGMADPGPIIQTFFSHEVLCqrylLDGVIALVDavhaDEQMNQFTI-----AQ--SQVGYADRI 155

                  ....
gi 2273339399 150 VVSK 153
Cdd:PRK11537  156 LLTK 159
chaper_GTP_ZigA NF038288
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ...
3-168 1.32e-20

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: 90.61  E-value: 1.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399   3 LPLTVVAGYLGAGKTTFINRLLAGDHRLRLMVLVNDFGAINIDAGLIALADGD-------TIALTNGCVCCTMGADLFMA 75
Cdd:NF038288    1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGASlsrteekLVEMSNGCICCTLREDLLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399  76 LGdALDRRPRPDHLIVEASGVADPARIAN------------AALAEPDLayggIVTIVDG-------QQIDGLC------ 130
Cdd:NF038288   81 VR-RLAREGRFDYLVIESTGISEPLPVAEtftfadedgvslSDVARLDT----MVTVVDAvnflrdyDSADSLQergesl 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2273339399 131 --------ADPMIgaqvrDQIACADLVVVSKVCELSAV----LAATLTTL 168
Cdd:NF038288  156 geedertvVDLLV-----DQVEFADVILLNKTDLVSEAelerLTAILRSL 200
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
203-270 9.67e-04

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: 37.58  E-value: 9.67e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2273339399  203 QSWSYTGDATLHREVLSQSVAKRPQALFRLKG--HVMDPNGGAWEVHAVGRHVSVTQAAP-----QSHTQLVAIG 270
Cdd:smart00833   2 SSFVYRARRPFHPQRLLAALDELPEGVLRAKGffWLASRPDLPGVLSQAGGRLRIEPAGAwpaagDRRTRLVFIG 76
 
Name Accession Description Interval E-value
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
1-270 3.70e-69

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 216.96  E-value: 3.70e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399   1 MPLPLTVVAGYLGAGKTTFINRLLAGDHRLRLMVLVNDFGAINIDAGLIALADGDTIALTNGCVCCTMGADLFMALGDaL 80
Cdd:COG0523     2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRDTDEEIVELSNGCICCTLREDLLPALRR-L 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399  81 DRRPRPDHLIVEASGVADPARIANAALAEPDLA----YGGIVTIVDGQQIDGLCADPMIGAQVRDQIACADLVVVSKvCE 156
Cdd:COG0523    81 LRRGRFDRLLIETTGLADPAPVAQTFTFDPELRdrlrLDGVVTVVDARNLLDDLADRTLHELLVDQIAFADVIVLNK-TD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399 157 L-----SAVLAATLTTLSGASVLLSAD--VTDPATLLCAAPKPTPASAPHP-------------DYQSWSYTGDATLHRE 216
Cdd:COG0523   160 LvdeeeLAALEARLRALNPGAPIVRTShgEVDPALLLDLGLFDLEAALARPgwleelrdhehddGIRSFVFRSDRPFDPE 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2273339399 217 VLSQSVAKRPQALFRLKGHV-MDPNGGAWEVHAVGRHVSVTQAAP----QSHTQLVAIG 270
Cdd:COG0523   240 RLADFLEELGPGVLRAKGFLwLAGRPRRLVFQGVGGRLSLEPLGPwpadDRRSRLVFIG 298
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
4-154 1.42e-55

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: 178.10  E-value: 1.42e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399   4 PLTVVAGYLGAGKTTFINRLLAGDHRLRLMVLVNDFGAINIDAGLIALADG--DTIALTNGCVCCTMGADLFMALGDALD 81
Cdd:cd03112     1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSGGgeEVVELSNGCICCTLKGDLVKALEQLLE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2273339399  82 RRPRPDHLIVEASGVADPARIANAALAEPDLA----YGGIVTIVDGQQIDGLCADPMIGAQVRDQIACADLVVVSKV 154
Cdd:cd03112    81 RRGKFDYILIETTGLADPGPIAQTLWSDEELEsrlrLDGVVTVVDAKNFLKQLDEEDVSDLAVDQIAFADVIVLNKT 157
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
4-154 1.14e-45

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: 152.02  E-value: 1.14e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399   4 PLTVVAGYLGAGKTTFINRLLA-GDHRLRLMVLVNDFGAINIDAGLIALADGDTIALTNGCVCCTMGADLFMALGDALDR 82
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLKqNRAGLRIAVIVNEFGETGIDAELLSETGVLIVELSNGCICCTIREDLSMALEALLER 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2273339399  83 RPRPDHLIVEASGVADPARIANAALAE---PDLAYGGIVTIVDGQQIDGLCADPMIGaqvRDQIACADLVVVSKV 154
Cdd:pfam02492  81 EGRLDVIFIETTGLAEPAPVAQTFLSPelrSPVLLDGVITVVDAANEADGEKIPRKA---GDQIAFADLIVLNKT 152
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
3-274 5.59e-29

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: 112.92  E-value: 5.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399   3 LPLTVVAGYLGAGKTTFINRLLAGDHRLRLMVLVNDFGAINIDA------GLIALADGDTIALTNGCVCCTMGADLFMAL 76
Cdd:TIGR02475   4 IPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGeilkacGIEGCSEENIVELANGCICCTVADDFIPTM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399  77 GDALDRRPRPDHLIVEASGVADPARIAnAALAEPDL----AYGGIVTIVDGQQIDG--LCADPMIGAQVR---------- 140
Cdd:TIGR02475  84 TKLLARRQRPDHILIETSGLALPKPLV-QAFQWPEIrsrvTVDGVVTVVDGPAVAAgrFAADPDALDAQRaaddnldhet 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399 141 -------DQIACADLVVVSKVCELSA-----VLAATLTTLSGASVLLSAD--VTDPATLL--CAAPKPTPASAP------ 198
Cdd:TIGR02475 163 pleelfeDQLACADLVILNKADLLDAaglarVRAEIAAELPRAVKIVEAShgEVDARVLLglGAAAEDDLDNRPshhdfe 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399 199 ------HPDYQSWSYTGDATLHREVLSQSVAK--RPQALFRLKGHVMDPNGGA-WEVHAVGRHVSVT-----QAAPQSHT 264
Cdd:TIGR02475 243 ggeehdHDEFDSVVVDLGEVADPAALRQRLERlaEEHDVLRIKGFAAVPGKPMrLLVQGVGQRVDSYydrpwQAAETRQT 322
                         330
                  ....*....|
gi 2273339399 265 QLVAIGLKSL 274
Cdd:TIGR02475 323 RLVVIGLHDL 332
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
2-153 5.68e-22

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 93.23  E-value: 5.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399   2 PLPLTVVAGYLGAGKTTFINRLLAGDHRLRLMVLVNDFGAINIDAGLIALADGDTIALTNGCVCCTMGADLFMALGDALD 81
Cdd:PRK11537    3 PIAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLIGDRATQIKTLTNGCICCSRSNELEDALLDLLD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399  82 RRPRP----DHLIVEASGVADPARIANAALAEPDLA----YGGIVTIVD----GQQIDGLCAdpmigAQvrDQIACADLV 149
Cdd:PRK11537   83 NLDKGniqfDRLVIECTGMADPGPIIQTFFSHEVLCqrylLDGVIALVDavhaDEQMNQFTI-----AQ--SQVGYADRI 155

                  ....
gi 2273339399 150 VVSK 153
Cdd:PRK11537  156 LLTK 159
chaper_GTP_ZigA NF038288
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ...
3-168 1.32e-20

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: 90.61  E-value: 1.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399   3 LPLTVVAGYLGAGKTTFINRLLAGDHRLRLMVLVNDFGAINIDAGLIALADGD-------TIALTNGCVCCTMGADLFMA 75
Cdd:NF038288    1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGASlsrteekLVEMSNGCICCTLREDLLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273339399  76 LGdALDRRPRPDHLIVEASGVADPARIAN------------AALAEPDLayggIVTIVDG-------QQIDGLC------ 130
Cdd:NF038288   81 VR-RLAREGRFDYLVIESTGISEPLPVAEtftfadedgvslSDVARLDT----MVTVVDAvnflrdyDSADSLQergesl 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2273339399 131 --------ADPMIgaqvrDQIACADLVVVSKVCELSAV----LAATLTTL 168
Cdd:NF038288  156 geedertvVDLLV-----DQVEFADVILLNKTDLVSEAelerLTAILRSL 200
CobW_C pfam07683
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ...
202-270 1.31e-06

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: 45.69  E-value: 1.31e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2273339399 202 YQSWSYTGDATLHREVLSQSVAK--RPQALFRLKGHV-MDPNGGAWEVHAVGRHVSVTQAAPQS-----HTQLVAIG 270
Cdd:pfam07683   1 ISSFVFRADRPFDPERLEAWLEDllLPEGILRAKGILwLAGRPRPLVFQGVGGRLSLEPAGRWWpdedrRSRLVFIG 77
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
203-270 9.67e-04

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: 37.58  E-value: 9.67e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2273339399  203 QSWSYTGDATLHREVLSQSVAKRPQALFRLKG--HVMDPNGGAWEVHAVGRHVSVTQAAP-----QSHTQLVAIG 270
Cdd:smart00833   2 SSFVYRARRPFHPQRLLAALDELPEGVLRAKGffWLASRPDLPGVLSQAGGRLRIEPAGAwpaagDRRTRLVFIG 76
 
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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