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Conserved domains on  [gi|1622868361|ref|XP_028690071|]
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COBW domain-containing protein 5 isoform X1 [Macaca mulatta]

Protein Classification

CobW family GTP-binding protein( domain architecture ID 10123116)

CobW family GTP-binding protein similar to Homo sapiens Zinc-regulated GTPase metalloprotein activator 1, a zinc chaperone that directly transfers zinc cofactor to target metalloproteins, thereby activating them

Gene Ontology:  GO:0005525|GO:0003924

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
43-235 1.76e-93

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: 277.87  E-value: 1.76e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361  43 PVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGEGSaLEKSLAVSQGGelYEEWLELRNGCLCCSVKDNGLRAIEN 122
Cdd:cd03112     1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVG-IDAALLADSGG--GEEVVELSNGCICCTLKGDLVKALEQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 123 LMQKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEEKpdgLINEATRQVALADIILI 202
Cdd:cd03112    78 LLERRGKFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVVDAKNFLKQLDEED---VSDLAVDQIAFADVIVL 154
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622868361 203 NKTDLVPEEDVKKLRMTIRSINGLGQILETQRS 235
Cdd:cd03112   155 NKTDLVDEEELEALRARIRALNPGAKIVETTYG 187
CobW_C pfam07683
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ...
255-354 1.48e-19

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: 82.29  E-value: 1.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 255 IVTITFEVPGNAKEEHLNIFIQNLLWEKNVrnkdnhcmevIRLKGLVSIKDKPQQVIVQGVHELYDLEETPVSWKDDtER 334
Cdd:pfam07683   1 ISSFVFRADRPFDPERLEAWLEDLLLPEGI----------LRAKGILWLAGRPRPLVFQGVGGRLSLEPAGRWWPDE-DR 69
                          90       100
                  ....*....|....*....|
gi 1622868361 335 TNRLVLIGRNLDKDILKQLF 354
Cdd:pfam07683  70 RSRLVFIGRDLDREALRAAL 89
 
Name Accession Description Interval E-value
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
43-235 1.76e-93

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: 277.87  E-value: 1.76e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361  43 PVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGEGSaLEKSLAVSQGGelYEEWLELRNGCLCCSVKDNGLRAIEN 122
Cdd:cd03112     1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVG-IDAALLADSGG--GEEVVELSNGCICCTLKGDLVKALEQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 123 LMQKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEEKpdgLINEATRQVALADIILI 202
Cdd:cd03112    78 LLERRGKFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVVDAKNFLKQLDEED---VSDLAVDQIAFADVIVL 154
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622868361 203 NKTDLVPEEDVKKLRMTIRSINGLGQILETQRS 235
Cdd:cd03112   155 NKTDLVDEEELEALRARIRALNPGAKIVETTYG 187
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
40-354 2.39e-88

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 269.35  E-value: 2.39e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361  40 AKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGE---GSALekslaVSQGGelyEEWLELRNGCLCCSVKDNG 116
Cdd:COG0523     2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEvgiDAAL-----VRDTD---EEIVELSNGCICCTLREDL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 117 LRAIENLMqKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEekpDGLINEATRQVAL 196
Cdd:COG0523    74 LPALRRLL-RRGRFDRLLIETTGLADPAPVAQTFTFDPELRDRLRLDGVVTVVDARNLLDDLAD---RTLHELLVDQIAF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 197 ADIILINKTDLVPEEDVKKLRMTIRSING-------------LGQILETQRSSLQKKLQHVPGTQP----HLDQSIVTIT 259
Cdd:COG0523   150 ADVIVLNKTDLVDEEELAALEARLRALNPgapivrtshgevdPALLLDLGLFDLEAALARPGWLEElrdhEHDDGIRSFV 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 260 FEVPGNAKEEHLNIFIqnllweknvrnkDNHCMEVIRLKGLVSIKDKPQQVIVQGVHELYDLEETPvSWKDDtERTNRLV 339
Cdd:COG0523   230 FRSDRPFDPERLADFL------------EELGPGVLRAKGFLWLAGRPRRLVFQGVGGRLSLEPLG-PWPAD-DRRSRLV 295
                         330
                  ....*....|....*
gi 1622868361 340 LIGRNLDKDILKQLF 354
Cdd:COG0523   296 FIGRDLDEAALEAAL 310
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
43-231 8.34e-60

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: 191.31  E-value: 8.34e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361  43 PVTIITGYLGAGKTTLLNYIL-TEQHSKRVAVILNEFGEGSaLEKSLAVSQGgelyEEWLELRNGCLCCSVKDNGLRAIE 121
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLkQNRAGLRIAVIVNEFGETG-IDAELLSETG----VLIVELSNGCICCTIREDLSMALE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 122 NLMQKKGKFDYILLETTGLADPGAVASMFWVDaELGSDIYLDGIITIVDSkyglKHLTEEKPdgLINEATRQVALADIIL 201
Cdd:pfam02492  76 ALLEREGRLDVIFIETTGLAEPAPVAQTFLSP-ELRSPVLLDGVITVVDA----ANEADGEK--IPRKAGDQIAFADLIV 148
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622868361 202 INKTDLVPEE-DVKKLRMTIRSINGLGQILE 231
Cdd:pfam02492 149 LNKTDLAPEVaLLEVLEEDLRRLNPGAPVVP 179
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
40-348 9.89e-47

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: 162.61  E-value: 9.89e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361  40 AKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGE----GSALeKSLAVSQGGElyEEWLELRNGCLCCSVKDN 115
Cdd:TIGR02475   2 AKIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDlgidGEIL-KACGIEGCSE--ENIVELANGCICCTVADD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 116 GLRAIENLMQKKGKFDYILLETTGLADPGAVASMF-WvdAELGSDIYLDGIITIVDSKYGLKHLTEEKPDGLinEATR-- 192
Cdd:TIGR02475  79 FIPTMTKLLARRQRPDHILIETSGLALPKPLVQAFqW--PEIRSRVTVDGVVTVVDGPAVAAGRFAADPDAL--DAQRaa 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 193 ----------------QVALADIILINKTDLVPEEDVKKLRMTIRS-INGLGQILETQRSSL------------------ 237
Cdd:TIGR02475 155 ddnldhetpleelfedQLACADLVILNKADLLDAAGLARVRAEIAAeLPRAVKIVEASHGEVdarvllglgaaaeddldn 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 238 QKKLQHVPGTQPHLDQSIVTITFEVPGNAKEEHLNIFIQNLLWEKNvrnkdnhcmeVIRLKGLVSIKDKPQQVIVQGVHE 317
Cdd:TIGR02475 235 RPSHHDFEGGEEHDHDEFDSVVVDLGEVADPAALRQRLERLAEEHD----------VLRIKGFAAVPGKPMRLLVQGVGQ 304
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1622868361 318 LYDlEETPVSWKDDTERTNRLVLIG-RNLDKD 348
Cdd:TIGR02475 305 RVD-SYYDRPWQAAETRQTRLVVIGlHDLDQA 335
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
42-356 2.71e-41

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 147.54  E-value: 2.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361  42 IPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGEGSALEKSLavsqgGELYEEWLELRNGCLCCS----VKDNGL 117
Cdd:PRK11537    4 IAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLI-----GDRATQIKTLTNGCICCSrsneLEDALL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 118 RAIENLMQKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEekpdglINEATRQVALA 197
Cdd:PRK11537   79 DLLDNLDKGNIQFDRLVIECTGMADPGPIIQTFFSHEVLCQRYLLDGVIALVDAVHADEQMNQ------FTIAQSQVGYA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 198 DIILINKTDLVPEEDvkKLRMTIRSING-------------LGQILETQRSSLQKKLqhvPGTQPHL------DQSIVTI 258
Cdd:PRK11537  153 DRILLTKTDVAGEAE--KLRERLARINArapvytvvhgdidLSLLFNTNGFMLEENV---VSTKPRFhfiadkQNDISSI 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 259 TFEVPGNAKEEHLNIFIQNLLweknVRNKDNhcmeVIRLKGLVSIKDKPQQVIVQGVHELYDLEetpvsWK---DDTERT 335
Cdd:PRK11537  228 VVELDYPVDISEVSRVMENLL----LESADK----LLRYKGMLWIDGEPNRLLFQGVQRLYSAD-----WDrpwGDETPH 294
                         330       340
                  ....*....|....*....|.
gi 1622868361 336 NRLVLIGRNLDKDILKQLFIA 356
Cdd:PRK11537  295 STLVFIGIQLPEEEIRAAFAG 315
CobW_C pfam07683
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ...
255-354 1.48e-19

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: 82.29  E-value: 1.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 255 IVTITFEVPGNAKEEHLNIFIQNLLWEKNVrnkdnhcmevIRLKGLVSIKDKPQQVIVQGVHELYDLEETPVSWKDDtER 334
Cdd:pfam07683   1 ISSFVFRADRPFDPERLEAWLEDLLLPEGI----------LRAKGILWLAGRPRPLVFQGVGGRLSLEPAGRWWPDE-DR 69
                          90       100
                  ....*....|....*....|
gi 1622868361 335 TNRLVLIGRNLDKDILKQLF 354
Cdd:pfam07683  70 RSRLVFIGRDLDREALRAAL 89
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
294-354 9.09e-09

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: 52.21  E-value: 9.09e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622868361  294 VIRLKGLVSIKDKPQQVIV-QGVHELYDLEETPVsWKDDTERTNRLVLIGRNLDKDILKQLF 354
Cdd:smart00833  28 VLRAKGFFWLASRPDLPGVlSQAGGRLRIEPAGA-WPAAGDRRTRLVFIGRDLDEEAIRAAL 88
 
Name Accession Description Interval E-value
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
43-235 1.76e-93

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: 277.87  E-value: 1.76e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361  43 PVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGEGSaLEKSLAVSQGGelYEEWLELRNGCLCCSVKDNGLRAIEN 122
Cdd:cd03112     1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVG-IDAALLADSGG--GEEVVELSNGCICCTLKGDLVKALEQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 123 LMQKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEEKpdgLINEATRQVALADIILI 202
Cdd:cd03112    78 LLERRGKFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVVDAKNFLKQLDEED---VSDLAVDQIAFADVIVL 154
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622868361 203 NKTDLVPEEDVKKLRMTIRSINGLGQILETQRS 235
Cdd:cd03112   155 NKTDLVDEEELEALRARIRALNPGAKIVETTYG 187
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
40-354 2.39e-88

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 269.35  E-value: 2.39e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361  40 AKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGE---GSALekslaVSQGGelyEEWLELRNGCLCCSVKDNG 116
Cdd:COG0523     2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEvgiDAAL-----VRDTD---EEIVELSNGCICCTLREDL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 117 LRAIENLMqKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEekpDGLINEATRQVAL 196
Cdd:COG0523    74 LPALRRLL-RRGRFDRLLIETTGLADPAPVAQTFTFDPELRDRLRLDGVVTVVDARNLLDDLAD---RTLHELLVDQIAF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 197 ADIILINKTDLVPEEDVKKLRMTIRSING-------------LGQILETQRSSLQKKLQHVPGTQP----HLDQSIVTIT 259
Cdd:COG0523   150 ADVIVLNKTDLVDEEELAALEARLRALNPgapivrtshgevdPALLLDLGLFDLEAALARPGWLEElrdhEHDDGIRSFV 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 260 FEVPGNAKEEHLNIFIqnllweknvrnkDNHCMEVIRLKGLVSIKDKPQQVIVQGVHELYDLEETPvSWKDDtERTNRLV 339
Cdd:COG0523   230 FRSDRPFDPERLADFL------------EELGPGVLRAKGFLWLAGRPRRLVFQGVGGRLSLEPLG-PWPAD-DRRSRLV 295
                         330
                  ....*....|....*
gi 1622868361 340 LIGRNLDKDILKQLF 354
Cdd:COG0523   296 FIGRDLDEAALEAAL 310
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
43-231 8.34e-60

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: 191.31  E-value: 8.34e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361  43 PVTIITGYLGAGKTTLLNYIL-TEQHSKRVAVILNEFGEGSaLEKSLAVSQGgelyEEWLELRNGCLCCSVKDNGLRAIE 121
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLkQNRAGLRIAVIVNEFGETG-IDAELLSETG----VLIVELSNGCICCTIREDLSMALE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 122 NLMQKKGKFDYILLETTGLADPGAVASMFWVDaELGSDIYLDGIITIVDSkyglKHLTEEKPdgLINEATRQVALADIIL 201
Cdd:pfam02492  76 ALLEREGRLDVIFIETTGLAEPAPVAQTFLSP-ELRSPVLLDGVITVVDA----ANEADGEK--IPRKAGDQIAFADLIV 148
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622868361 202 INKTDLVPEE-DVKKLRMTIRSINGLGQILE 231
Cdd:pfam02492 149 LNKTDLAPEVaLLEVLEEDLRRLNPGAPVVP 179
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
40-348 9.89e-47

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: 162.61  E-value: 9.89e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361  40 AKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGE----GSALeKSLAVSQGGElyEEWLELRNGCLCCSVKDN 115
Cdd:TIGR02475   2 AKIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDlgidGEIL-KACGIEGCSE--ENIVELANGCICCTVADD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 116 GLRAIENLMQKKGKFDYILLETTGLADPGAVASMF-WvdAELGSDIYLDGIITIVDSKYGLKHLTEEKPDGLinEATR-- 192
Cdd:TIGR02475  79 FIPTMTKLLARRQRPDHILIETSGLALPKPLVQAFqW--PEIRSRVTVDGVVTVVDGPAVAAGRFAADPDAL--DAQRaa 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 193 ----------------QVALADIILINKTDLVPEEDVKKLRMTIRS-INGLGQILETQRSSL------------------ 237
Cdd:TIGR02475 155 ddnldhetpleelfedQLACADLVILNKADLLDAAGLARVRAEIAAeLPRAVKIVEASHGEVdarvllglgaaaeddldn 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 238 QKKLQHVPGTQPHLDQSIVTITFEVPGNAKEEHLNIFIQNLLWEKNvrnkdnhcmeVIRLKGLVSIKDKPQQVIVQGVHE 317
Cdd:TIGR02475 235 RPSHHDFEGGEEHDHDEFDSVVVDLGEVADPAALRQRLERLAEEHD----------VLRIKGFAAVPGKPMRLLVQGVGQ 304
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1622868361 318 LYDlEETPVSWKDDTERTNRLVLIG-RNLDKD 348
Cdd:TIGR02475 305 RVD-SYYDRPWQAAETRQTRLVVIGlHDLDQA 335
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
42-356 2.71e-41

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 147.54  E-value: 2.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361  42 IPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGEGSALEKSLavsqgGELYEEWLELRNGCLCCS----VKDNGL 117
Cdd:PRK11537    4 IAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLI-----GDRATQIKTLTNGCICCSrsneLEDALL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 118 RAIENLMQKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEekpdglINEATRQVALA 197
Cdd:PRK11537   79 DLLDNLDKGNIQFDRLVIECTGMADPGPIIQTFFSHEVLCQRYLLDGVIALVDAVHADEQMNQ------FTIAQSQVGYA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 198 DIILINKTDLVPEEDvkKLRMTIRSING-------------LGQILETQRSSLQKKLqhvPGTQPHL------DQSIVTI 258
Cdd:PRK11537  153 DRILLTKTDVAGEAE--KLRERLARINArapvytvvhgdidLSLLFNTNGFMLEENV---VSTKPRFhfiadkQNDISSI 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 259 TFEVPGNAKEEHLNIFIQNLLweknVRNKDNhcmeVIRLKGLVSIKDKPQQVIVQGVHELYDLEetpvsWK---DDTERT 335
Cdd:PRK11537  228 VVELDYPVDISEVSRVMENLL----LESADK----LLRYKGMLWIDGEPNRLLFQGVQRLYSAD-----WDrpwGDETPH 294
                         330       340
                  ....*....|....*....|.
gi 1622868361 336 NRLVLIGRNLDKDILKQLFIA 356
Cdd:PRK11537  295 STLVFIGIQLPEEEIRAAFAG 315
CobW_C pfam07683
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ...
255-354 1.48e-19

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: 82.29  E-value: 1.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622868361 255 IVTITFEVPGNAKEEHLNIFIQNLLWEKNVrnkdnhcmevIRLKGLVSIKDKPQQVIVQGVHELYDLEETPVSWKDDtER 334
Cdd:pfam07683   1 ISSFVFRADRPFDPERLEAWLEDLLLPEGI----------LRAKGILWLAGRPRPLVFQGVGGRLSLEPAGRWWPDE-DR 69
                          90       100
                  ....*....|....*....|
gi 1622868361 335 TNRLVLIGRNLDKDILKQLF 354
Cdd:pfam07683  70 RSRLVFIGRDLDREALRAAL 89
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
294-354 9.09e-09

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: 52.21  E-value: 9.09e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622868361  294 VIRLKGLVSIKDKPQQVIV-QGVHELYDLEETPVsWKDDTERTNRLVLIGRNLDKDILKQLF 354
Cdd:smart00833  28 VLRAKGFFWLASRPDLPGVlSQAGGRLRIEPAGA-WPAAGDRRTRLVFIGRDLDEEAIRAAL 88
YjiA COG2403
Zn/Ni/Co-binding GTPase YjiA, predicted metallochaperone, CobW/Nha3/YciC family [Inorganic ion ...
196-232 3.05e-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: 42.52  E-value: 3.05e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622868361 196 LADIILINKTDLVPEEDVKKLRMTIRSINGLGQILET 232
Cdd:COG2403   261 MADVVVINKVDTADPEDIETVRENIRKVNPKAEIIEA 297
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
43-73 2.36e-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: 39.96  E-value: 2.36e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1622868361  43 PVTIITGYLGAGKTTLLNYIL--TEQHSKRVAV 73
Cdd:COG0507   141 RVSVLTGGAGTGKTTTLRALLaaLEALGLRVAL 173
HypB COG0378
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ...
194-232 2.91e-03

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


Pssm-ID: 440147 [Multi-domain]  Cd Length: 200  Bit Score: 38.50  E-value: 2.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622868361 194 VALADIILINKTDLVP--EEDVKKLRMTIRSINGLGQILET 232
Cdd:COG0378   138 FTAADLLVINKIDLAPyvGFDLEVMEEDARRVNPGAPIFEV 178
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
162-226 8.24e-03

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 36.89  E-value: 8.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622868361 162 LDGIITIVDSKYGLKHLTEEkpdgLINEAtRQVALADIILINKTDLVPEEDVKKLRMTIRSINGL 226
Cdd:cd00881    86 ADGALLVVDANEGVEPQTRE----HLNIA-LAGGLPIIVAVNKIDRVGEEDFDEVLREIKELLKL 145
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
43-73 9.08e-03

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 36.38  E-value: 9.08e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1622868361  43 PVTIITGYLGAGKTTLLNYILT--EQHSKRVAV 73
Cdd:cd17933    13 RVSVLTGGAGTGKTTTLKALLAalEAEGKRVVL 45
 
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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