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Conserved domains on  [gi|22122605|ref|NP_666209|]
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zinc-regulated GTPase metalloprotein activator 1 [Mus musculus]

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 ...
41-244 1.76e-99

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: 293.66  E-value: 1.76e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605  41 PVTIVTGYLGAGKTTLLNYILTEQHNRKIAVILNEFGEGSaVEKSLAVSQGGelYEEWLELRNGCLCCSVKDSGLRAIEN 120
Cdd:cd03112   1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVG-IDAALLADSGG--GEEVVELSNGCICCTLKGDLVKALEQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605 121 LMQKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITVVDSKYGLKHLTEEKpdgLVNEATRQVALADMILI 200
Cdd:cd03112  78 LLERRGKFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVVDAKNFLKQLDEED---VSDLAVDQIAFADVIVL 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 22122605 201 NKTDLVSEEELNNLRTTIRSINGLGKVLETQRSRVHLSNILDLH 244
Cdd:cd03112 155 NKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGTG 198
CobW_C pfam07683
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ...
271-374 5.72e-18

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


:

Pssm-ID: 462228 [Multi-domain]  Cd Length: 93  Bit Score: 78.43  E-value: 5.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605   271 IVTVTFEVPGSAKEECLNVFIQNLLWEKNVknkdghcmevIRLKGLVSIKDKPQQMIVQGIHELYDLEESLVNWKDDaER 350
Cdd:pfam07683   1 ISSFVFRADRPFDPERLEAWLEDLLLPEGI----------LRAKGILWLAGRPRPLVFQGVGGRLSLEPAGRWWPDE-DR 69
                          90       100
                  ....*....|....*....|....
gi 22122605   351 ACQLVFIGRNLDKDVLQQLFLTAV 374
Cdd:pfam07683  70 RSRLVFIGRDLDREALRAALDACL 93
 
Name Accession Description Interval E-value
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
41-244 1.76e-99

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: 293.66  E-value: 1.76e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605  41 PVTIVTGYLGAGKTTLLNYILTEQHNRKIAVILNEFGEGSaVEKSLAVSQGGelYEEWLELRNGCLCCSVKDSGLRAIEN 120
Cdd:cd03112   1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVG-IDAALLADSGG--GEEVVELSNGCICCTLKGDLVKALEQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605 121 LMQKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITVVDSKYGLKHLTEEKpdgLVNEATRQVALADMILI 200
Cdd:cd03112  78 LLERRGKFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVVDAKNFLKQLDEED---VSDLAVDQIAFADVIVL 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 22122605 201 NKTDLVSEEELNNLRTTIRSINGLGKVLETQRSRVHLSNILDLH 244
Cdd:cd03112 155 NKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGTG 198
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
38-378 2.08e-96

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 290.54  E-value: 2.08e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605  38 TKIPVTIVTGYLGAGKTTLLNYILTEQHNRKIAVILNEFGEgsavekslaVSQGGELY----EEWLELRNGCLCCSVKDS 113
Cdd:COG0523   2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGE---------VGIDAALVrdtdEEIVELSNGCICCTLRED 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605 114 GLRAIENLMqKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITVVDSKYGLKHLTEekpDGLVNEATRQVA 193
Cdd:COG0523  73 LLPALRRLL-RRGRFDRLLIETTGLADPAPVAQTFTFDPELRDRLRLDGVVTVVDARNLLDDLAD---RTLHELLVDQIA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605 194 LADMILINKTDLVSEEELNNLRTTIRSINGLGKVLETQRSRVHLSNILDLHAYDILSGISLQKKLQHVSTAPHlDQSIVT 273
Cdd:COG0523 149 FADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWLEELRDHEH-DDGIRS 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605 274 VTFEVPGSAKEECLNVFIQNLlweknvknkdGHcmEVIRLKGLVSIKDKPQQMIVQGIHELYDLEEsLVNWKDDaERACQ 353
Cdd:COG0523 228 FVFRSDRPFDPERLADFLEEL----------GP--GVLRAKGFLWLAGRPRRLVFQGVGGRLSLEP-LGPWPAD-DRRSR 293
                       330       340
                ....*....|....*....|....*
gi 22122605 354 LVFIGRNLDKDVLQQLFLTAVAEAE 378
Cdd:COG0523 294 LVFIGRDLDEAALEAALDACLLTDA 318
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
41-229 2.58e-59

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: 190.54  E-value: 2.58e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605    41 PVTIVTGYLGAGKTTLLNYIL-TEQHNRKIAVILNEFGEGSaVEKSLAVSQGgelyEEWLELRNGCLCCSVKDSGLRAIE 119
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLkQNRAGLRIAVIVNEFGETG-IDAELLSETG----VLIVELSNGCICCTIREDLSMALE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605   120 NLMQKKGKFDYILLETTGLADPGAVASMFWVDaELGSDIYLDGIITVVDSkyglKHLTEEKPdgLVNEATRQVALADMIL 199
Cdd:pfam02492  76 ALLEREGRLDVIFIETTGLAEPAPVAQTFLSP-ELRSPVLLDGVITVVDA----ANEADGEK--IPRKAGDQIAFADLIV 148
                         170       180       190
                  ....*....|....*....|....*....|.
gi 22122605   200 INKTDLVSEEELNN-LRTTIRSINGLGKVLE 229
Cdd:pfam02492 149 LNKTDLAPEVALLEvLEEDLRRLNPGAPVVP 179
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
37-366 4.57e-45

cobalamin biosynthesis protein CobW; The family of proteins identified by this model is generally found proximal to the trimeric cobaltochelatase subunit CobN which is essential for vitamin B12 (cobalamin) biosynthesis. The protein contains an P-loop nucleotide-binding loop in the N-terminal domain and a histidine-rich region in the C-terminal portion suggesting a role in metal binding, possibly as an intermediary between the cobalt transport and chelation systems. A broader CobW family is delineated by two Pfam models which identify the N- and C-terminal domains (pfam02492 and pfam07683). [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274151 [Multi-domain]  Cd Length: 341  Bit Score: 158.76  E-value: 4.57e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605    37 ITKIPVTIVTGYLGAGKTTLLNYILTEQHNRKIAVILNEFGE---GSAVEKSLAVSQGGElyEEWLELRNGCLCCSVKDS 113
Cdd:TIGR02475   1 LAKIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDlgiDGEILKACGIEGCSE--ENIVELANGCICCTVADD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605   114 GLRAIENLMQKKGKFDYILLETTGLADPGAVASMF-WvdAELGSDIYLDGIITVVDSKYGLKHLTEEKPDGLvnEATR-- 190
Cdd:TIGR02475  79 FIPTMTKLLARRQRPDHILIETSGLALPKPLVQAFqW--PEIRSRVTVDGVVTVVDGPAVAAGRFAADPDAL--DAQRaa 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605   191 ----------------QVALADMILINKTDLVSEEELNNLRTTIRS-INGLGKVLETQRSRVHLSNILDLHAY---DIls 250
Cdd:TIGR02475 155 ddnldhetpleelfedQLACADLVILNKADLLDAAGLARVRAEIAAeLPRAVKIVEASHGEVDARVLLGLGAAaedDL-- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605   251 gisLQKKLQHVSTAP--HLDQSIVTVTFEVPGSAKEECLNVFIQNLLWEKNvknkdghcmeVIRLKGLVSIKDKPQQMIV 328
Cdd:TIGR02475 233 ---DNRPSHHDFEGGeeHDHDEFDSVVVDLGEVADPAALRQRLERLAEEHD----------VLRIKGFAAVPGKPMRLLV 299
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 22122605   329 QGIHE----LYDLEeslvnWKDDAERACQLVFIG-RNLDKDVL 366
Cdd:TIGR02475 300 QGVGQrvdsYYDRP-----WQAAETRQTRLVVIGlHDLDQAAI 337
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
37-370 1.12e-43

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 154.09  E-value: 1.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605   37 ITKIPVTIVTGYLGAGKTTLLNYILTEQHNRKIAVILNEFGEgSAVEKSLAvsqgGELYEEWLELRNGCLCCS----VKD 112
Cdd:PRK11537   1 MNPIAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGE-VSVDDQLI----GDRATQIKTLTNGCICCSrsneLED 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605  113 SGLRAIENLMQKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITVVDSKYGLKHLTEekpdglVNEATRQV 192
Cdd:PRK11537  76 ALLDLLDNLDKGNIQFDRLVIECTGMADPGPIIQTFFSHEVLCQRYLLDGVIALVDAVHADEQMNQ------FTIAQSQV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605  193 ALADMILINKTDLVSEEElnNLRTTIRSINGLGKVLETQRSRVHLSNILDlhaydiLSGISLQKKLqhVSTAPHLD---- 268
Cdd:PRK11537 150 GYADRILLTKTDVAGEAE--KLRERLARINARAPVYTVVHGDIDLSLLFN------TNGFMLEENV--VSTKPRFHfiad 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605  269 -----QSIVtVTFEVP------GSAKEECLNVFIQNLLweknvknkdghcmeviRLKGLVSIKDKPQQMIVQGIHELYDl 337
Cdd:PRK11537 220 kqndiSSIV-VELDYPvdisevSRVMENLLLESADKLL----------------RYKGMLWIDGEPNRLLFQGVQRLYS- 281
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 22122605  338 eeslVNWK---DDAERACQLVFIGRNLDKDVLQQLF 370
Cdd:PRK11537 282 ----ADWDrpwGDETPHSTLVFIGIQLPEEEIRAAF 313
CobW_C pfam07683
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ...
271-374 5.72e-18

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


Pssm-ID: 462228 [Multi-domain]  Cd Length: 93  Bit Score: 78.43  E-value: 5.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605   271 IVTVTFEVPGSAKEECLNVFIQNLLWEKNVknkdghcmevIRLKGLVSIKDKPQQMIVQGIHELYDLEESLVNWKDDaER 350
Cdd:pfam07683   1 ISSFVFRADRPFDPERLEAWLEDLLLPEGI----------LRAKGILWLAGRPRPLVFQGVGGRLSLEPAGRWWPDE-DR 69
                          90       100
                  ....*....|....*....|....
gi 22122605   351 ACQLVFIGRNLDKDVLQQLFLTAV 374
Cdd:pfam07683  70 RSRLVFIGRDLDREALRAALDACL 93
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
310-373 2.01e-07

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: 48.36  E-value: 2.01e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22122605    310 VIRLKGLVSIKDKPQQ-MIVQGIHELYDLEeSLVNWKDDAERACQLVFIGRNLDKDVLQQLFLTA 373
Cdd:smart00833  28 VLRAKGFFWLASRPDLpGVLSQAGGRLRIE-PAGAWPAAGDRRTRLVFIGRDLDEEAIRAALDAC 91
 
Name Accession Description Interval E-value
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
41-244 1.76e-99

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: 293.66  E-value: 1.76e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605  41 PVTIVTGYLGAGKTTLLNYILTEQHNRKIAVILNEFGEGSaVEKSLAVSQGGelYEEWLELRNGCLCCSVKDSGLRAIEN 120
Cdd:cd03112   1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVG-IDAALLADSGG--GEEVVELSNGCICCTLKGDLVKALEQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605 121 LMQKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITVVDSKYGLKHLTEEKpdgLVNEATRQVALADMILI 200
Cdd:cd03112  78 LLERRGKFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVVDAKNFLKQLDEED---VSDLAVDQIAFADVIVL 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 22122605 201 NKTDLVSEEELNNLRTTIRSINGLGKVLETQRSRVHLSNILDLH 244
Cdd:cd03112 155 NKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGTG 198
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
38-378 2.08e-96

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 290.54  E-value: 2.08e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605  38 TKIPVTIVTGYLGAGKTTLLNYILTEQHNRKIAVILNEFGEgsavekslaVSQGGELY----EEWLELRNGCLCCSVKDS 113
Cdd:COG0523   2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGE---------VGIDAALVrdtdEEIVELSNGCICCTLRED 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605 114 GLRAIENLMqKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITVVDSKYGLKHLTEekpDGLVNEATRQVA 193
Cdd:COG0523  73 LLPALRRLL-RRGRFDRLLIETTGLADPAPVAQTFTFDPELRDRLRLDGVVTVVDARNLLDDLAD---RTLHELLVDQIA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605 194 LADMILINKTDLVSEEELNNLRTTIRSINGLGKVLETQRSRVHLSNILDLHAYDILSGISLQKKLQHVSTAPHlDQSIVT 273
Cdd:COG0523 149 FADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWLEELRDHEH-DDGIRS 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605 274 VTFEVPGSAKEECLNVFIQNLlweknvknkdGHcmEVIRLKGLVSIKDKPQQMIVQGIHELYDLEEsLVNWKDDaERACQ 353
Cdd:COG0523 228 FVFRSDRPFDPERLADFLEEL----------GP--GVLRAKGFLWLAGRPRRLVFQGVGGRLSLEP-LGPWPAD-DRRSR 293
                       330       340
                ....*....|....*....|....*
gi 22122605 354 LVFIGRNLDKDVLQQLFLTAVAEAE 378
Cdd:COG0523 294 LVFIGRDLDEAALEAALDACLLTDA 318
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
41-229 2.58e-59

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: 190.54  E-value: 2.58e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605    41 PVTIVTGYLGAGKTTLLNYIL-TEQHNRKIAVILNEFGEGSaVEKSLAVSQGgelyEEWLELRNGCLCCSVKDSGLRAIE 119
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLkQNRAGLRIAVIVNEFGETG-IDAELLSETG----VLIVELSNGCICCTIREDLSMALE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605   120 NLMQKKGKFDYILLETTGLADPGAVASMFWVDaELGSDIYLDGIITVVDSkyglKHLTEEKPdgLVNEATRQVALADMIL 199
Cdd:pfam02492  76 ALLEREGRLDVIFIETTGLAEPAPVAQTFLSP-ELRSPVLLDGVITVVDA----ANEADGEK--IPRKAGDQIAFADLIV 148
                         170       180       190
                  ....*....|....*....|....*....|.
gi 22122605   200 INKTDLVSEEELNN-LRTTIRSINGLGKVLE 229
Cdd:pfam02492 149 LNKTDLAPEVALLEvLEEDLRRLNPGAPVVP 179
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
37-366 4.57e-45

cobalamin biosynthesis protein CobW; The family of proteins identified by this model is generally found proximal to the trimeric cobaltochelatase subunit CobN which is essential for vitamin B12 (cobalamin) biosynthesis. The protein contains an P-loop nucleotide-binding loop in the N-terminal domain and a histidine-rich region in the C-terminal portion suggesting a role in metal binding, possibly as an intermediary between the cobalt transport and chelation systems. A broader CobW family is delineated by two Pfam models which identify the N- and C-terminal domains (pfam02492 and pfam07683). [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274151 [Multi-domain]  Cd Length: 341  Bit Score: 158.76  E-value: 4.57e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605    37 ITKIPVTIVTGYLGAGKTTLLNYILTEQHNRKIAVILNEFGE---GSAVEKSLAVSQGGElyEEWLELRNGCLCCSVKDS 113
Cdd:TIGR02475   1 LAKIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDlgiDGEILKACGIEGCSE--ENIVELANGCICCTVADD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605   114 GLRAIENLMQKKGKFDYILLETTGLADPGAVASMF-WvdAELGSDIYLDGIITVVDSKYGLKHLTEEKPDGLvnEATR-- 190
Cdd:TIGR02475  79 FIPTMTKLLARRQRPDHILIETSGLALPKPLVQAFqW--PEIRSRVTVDGVVTVVDGPAVAAGRFAADPDAL--DAQRaa 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605   191 ----------------QVALADMILINKTDLVSEEELNNLRTTIRS-INGLGKVLETQRSRVHLSNILDLHAY---DIls 250
Cdd:TIGR02475 155 ddnldhetpleelfedQLACADLVILNKADLLDAAGLARVRAEIAAeLPRAVKIVEASHGEVDARVLLGLGAAaedDL-- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605   251 gisLQKKLQHVSTAP--HLDQSIVTVTFEVPGSAKEECLNVFIQNLLWEKNvknkdghcmeVIRLKGLVSIKDKPQQMIV 328
Cdd:TIGR02475 233 ---DNRPSHHDFEGGeeHDHDEFDSVVVDLGEVADPAALRQRLERLAEEHD----------VLRIKGFAAVPGKPMRLLV 299
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 22122605   329 QGIHE----LYDLEeslvnWKDDAERACQLVFIG-RNLDKDVL 366
Cdd:TIGR02475 300 QGVGQrvdsYYDRP-----WQAAETRQTRLVVIGlHDLDQAAI 337
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
37-370 1.12e-43

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 154.09  E-value: 1.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605   37 ITKIPVTIVTGYLGAGKTTLLNYILTEQHNRKIAVILNEFGEgSAVEKSLAvsqgGELYEEWLELRNGCLCCS----VKD 112
Cdd:PRK11537   1 MNPIAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGE-VSVDDQLI----GDRATQIKTLTNGCICCSrsneLED 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605  113 SGLRAIENLMQKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITVVDSKYGLKHLTEekpdglVNEATRQV 192
Cdd:PRK11537  76 ALLDLLDNLDKGNIQFDRLVIECTGMADPGPIIQTFFSHEVLCQRYLLDGVIALVDAVHADEQMNQ------FTIAQSQV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605  193 ALADMILINKTDLVSEEElnNLRTTIRSINGLGKVLETQRSRVHLSNILDlhaydiLSGISLQKKLqhVSTAPHLD---- 268
Cdd:PRK11537 150 GYADRILLTKTDVAGEAE--KLRERLARINARAPVYTVVHGDIDLSLLFN------TNGFMLEENV--VSTKPRFHfiad 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605  269 -----QSIVtVTFEVP------GSAKEECLNVFIQNLLweknvknkdghcmeviRLKGLVSIKDKPQQMIVQGIHELYDl 337
Cdd:PRK11537 220 kqndiSSIV-VELDYPvdisevSRVMENLLLESADKLL----------------RYKGMLWIDGEPNRLLFQGVQRLYS- 281
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 22122605  338 eeslVNWK---DDAERACQLVFIGRNLDKDVLQQLF 370
Cdd:PRK11537 282 ----ADWDrpwGDETPHSTLVFIGIQLPEEEIRAAF 313
CobW_C pfam07683
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ...
271-374 5.72e-18

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


Pssm-ID: 462228 [Multi-domain]  Cd Length: 93  Bit Score: 78.43  E-value: 5.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605   271 IVTVTFEVPGSAKEECLNVFIQNLLWEKNVknkdghcmevIRLKGLVSIKDKPQQMIVQGIHELYDLEESLVNWKDDaER 350
Cdd:pfam07683   1 ISSFVFRADRPFDPERLEAWLEDLLLPEGI----------LRAKGILWLAGRPRPLVFQGVGGRLSLEPAGRWWPDE-DR 69
                          90       100
                  ....*....|....*....|....
gi 22122605   351 ACQLVFIGRNLDKDVLQQLFLTAV 374
Cdd:pfam07683  70 RSRLVFIGRDLDREALRAALDACL 93
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
310-373 2.01e-07

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: 48.36  E-value: 2.01e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22122605    310 VIRLKGLVSIKDKPQQ-MIVQGIHELYDLEeSLVNWKDDAERACQLVFIGRNLDKDVLQQLFLTA 373
Cdd:smart00833  28 VLRAKGFFWLASRPDLpGVLSQAGGRLRIE-PAGAWPAAGDRRTRLVFIGRDLDEEAIRAALDAC 91
shulin_C20orf194-like cd22936
Tetrahymena thermophila shulin, human uncharacterized protein C20orf194, and similar proteins; ...
39-382 1.34e-05

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: 47.35  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605   39 KIPVTIVTGYLGAGKTTLLNYIlteqhnrkiavilnefgegsavekslaVSQGGELYEeWLELRNGCLCCSVKDSGLRAI 118
Cdd:cd22936  689 KIVITIVTGIPGSGKEKLAANL---------------------------VSLAKEDNR-WHVLRQDLRESSAFDDKSLQK 740
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605  119 ENLM-------QKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITVVD--------SKYGLKHLTEEKPDG 183
Cdd:cd22936  741 QLSSvlssqrrQAARKRPRILVVVPGYTDDVVIAAALHPDPEVSGSFKIGAVTTCVNplnffmehNRNTFPKLLDQLAQG 820
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605  184 LVNeatrQValadmILINKTDlVSEEELNNLRTTIRSINGLGKVLETQRSRVHLSNILDLhaydILSGIS----LQKKLQ 259
Cdd:cd22936  821 WVT----NV-----VFTSTTD-NQDPELEEVQKLLRAVNPDAAFILALKGNVTRGEDAEL----ILSENSfsspEMNRAR 886
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122605  260 HVSTaPHLDQS--------IVTVTFEVPGSAKEE-CLNVFIQNLLWEK-NVKNKDGHCmEVIRLKGLVSIKDKPQQMIVQ 329
Cdd:cd22936  887 RLLY-PGWSEGlfssgplvPKMIQVTLPFSRDRPlERDLFILRLKALKsSLKPSPFTG-NIYCIEGTVKFTDEEEKIEVL 964
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 22122605  330 GI----HELYDLEESLVNWKDDAERACQLVFIGRNLDKDVLQQLFLTAVAEAEEQRT 382
Cdd:cd22936  965 NNtlsnNLRLVPVPTPPSPNDETPQELGLVFTGCNLNEEKLKELLRQCAKQKPSKKA 1021
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
41-71 4.74e-03

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


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 38.80  E-value: 4.74e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 22122605  41 PVTIVTGYLGAGKTTLLNYIL--TEQHNRKIAV 71
Cdd:COG0507 141 RVSVLTGGAGTGKTTTLRALLaaLEALGLRVAL 173
 
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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