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Conserved domains on  [gi|2462625369|ref|XP_054219260|]
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zinc-regulated GTPase metalloprotein activator 1A isoform X2 [Homo sapiens]

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 ...
40-324 3.05e-64

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


:

Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 206.18  E-value: 3.05e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369  40 AKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGE---GSALekslaVSQGGelyEEWLELRNGCLCCSVKDSG 116
Cdd:COG0523     2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEvgiDAAL-----VRDTD---EEIVELSNGCICCTLREDL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 117 LRAIENLMqKKGKFDYILLETTGLADP--------------------GIITIVDSKYGLKHLTEE--------------- 161
Cdd:COG0523    74 LPALRRLL-RRGRFDRLLIETTGLADPapvaqtftfdpelrdrlrldGVVTVVDARNLLDDLADRtlhellvdqiafadv 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 162 ----KPDgLINEAT--------RSINGLGQILETQRSRVDLSNVLDLHAFDSLSGISLQKKLQhvPGTQPHLDQSIVTIT 229
Cdd:COG0523   153 ivlnKTD-LVDEEElaalearlRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWLE--ELRDHEHDDGIRSFV 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 230 FEVPGNAKEEHLNMFIqnllweknvrnkDNHCMEVIRLKGLVSIKDKSQQVIVQGVHELYDLEETPvSWKDDtERTNRLV 309
Cdd:COG0523   230 FRSDRPFDPERLADFL------------EELGPGVLRAKGFLWLAGRPRRLVFQGVGGRLSLEPLG-PWPAD-DRRSRLV 295
                         330
                  ....*....|....*
gi 2462625369 310 LLGRNLDKDILKQLF 324
Cdd:COG0523   296 FIGRDLDEAALEAAL 310
 
Name Accession Description Interval E-value
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
40-324 3.05e-64

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 206.18  E-value: 3.05e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369  40 AKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGE---GSALekslaVSQGGelyEEWLELRNGCLCCSVKDSG 116
Cdd:COG0523     2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEvgiDAAL-----VRDTD---EEIVELSNGCICCTLREDL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 117 LRAIENLMqKKGKFDYILLETTGLADP--------------------GIITIVDSKYGLKHLTEE--------------- 161
Cdd:COG0523    74 LPALRRLL-RRGRFDRLLIETTGLADPapvaqtftfdpelrdrlrldGVVTVVDARNLLDDLADRtlhellvdqiafadv 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 162 ----KPDgLINEAT--------RSINGLGQILETQRSRVDLSNVLDLHAFDSLSGISLQKKLQhvPGTQPHLDQSIVTIT 229
Cdd:COG0523   153 ivlnKTD-LVDEEElaalearlRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWLE--ELRDHEHDDGIRSFV 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 230 FEVPGNAKEEHLNMFIqnllweknvrnkDNHCMEVIRLKGLVSIKDKSQQVIVQGVHELYDLEETPvSWKDDtERTNRLV 309
Cdd:COG0523   230 FRSDRPFDPERLADFL------------EELGPGVLRAKGFLWLAGRPRRLVFQGVGGRLSLEPLG-PWPAD-DRRSRLV 295
                         330
                  ....*....|....*
gi 2462625369 310 LLGRNLDKDILKQLF 324
Cdd:COG0523   296 FIGRDLDEAALEAAL 310
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
43-197 2.62e-63

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: 199.67  E-value: 2.62e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369  43 PVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGEGSaLEKSLAVSQGGelYEEWLELRNGCLCCSVKDSGLRAIEN 122
Cdd:cd03112     1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVG-IDAALLADSGG--GEEVVELSNGCICCTLKGDLVKALEQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 123 LMQKKGKFDYILLETTGLADP--------------------GIITIVDSKYGLKHLTEE-------------------KP 163
Cdd:cd03112    78 LLERRGKFDYILIETTGLADPgpiaqtlwsdeelesrlrldGVVTVVDAKNFLKQLDEEdvsdlavdqiafadvivlnKT 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462625369 164 DgLINEAT--------RSINGLGQILETQRSRVDLSNVLDLH 197
Cdd:cd03112   158 D-LVDEEElealrariRALNPGAKIVETTYGRVDLEELLGTG 198
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
43-152 4.75e-37

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: 131.22  E-value: 4.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369  43 PVTIITGYLGAGKTTLLNYIL-TEQHSKRVAVILNEFGEGSaLEKSLAVSQGgelyEEWLELRNGCLCCSVKDSGLRAIE 121
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLkQNRAGLRIAVIVNEFGETG-IDAELLSETG----VLIVELSNGCICCTIREDLSMALE 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462625369 122 NLMQKKGKFDYILLETTGLADP-------------------GIITIVDSK 152
Cdd:pfam02492  76 ALLEREGRLDVIFIETTGLAEPapvaqtflspelrspvlldGVITVVDAA 125
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
40-318 5.84e-34

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: 127.94  E-value: 5.84e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369  40 AKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGE----GSALeKSLAVSQGGElyEEWLELRNGCLCCSVKDS 115
Cdd:TIGR02475   2 AKIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDlgidGEIL-KACGIEGCSE--ENIVELANGCICCTVADD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 116 GLRAIENLMQKKGKFDYILLETTGLADP-------------------GIITIVDSKY---------------------GL 155
Cdd:TIGR02475  79 FIPTMTKLLARRQRPDHILIETSGLALPkplvqafqwpeirsrvtvdGVVTVVDGPAvaagrfaadpdaldaqraaddNL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 156 KHLT--EE---------------KPDGLINEATRSING-LGQ-------ILETQRSRVDLSNVLDLHAFDSLSgISLQKK 210
Cdd:TIGR02475 159 DHETplEElfedqlacadlvilnKADLLDAAGLARVRAeIAAelpravkIVEASHGEVDARVLLGLGAAAEDD-LDNRPS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 211 LQHVPGTQPHLDQSIVTITFEVPGNAKEEHLNMFIQNLLWEKNvrnkdnhcmeVIRLKGLVSIKDKSQQVIVQGVHELYD 290
Cdd:TIGR02475 238 HHDFEGGEEHDHDEFDSVVVDLGEVADPAALRQRLERLAEEHD----------VLRIKGFAAVPGKPMRLLVQGVGQRVD 307
                         330       340
                  ....*....|....*....|....*....
gi 2462625369 291 lEETPVSWKDDTERTNRLVLLG-RNLDKD 318
Cdd:TIGR02475 308 -SYYDRPWQAAETRQTRLVVIGlHDLDQA 335
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
42-326 3.65e-25

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 103.24  E-value: 3.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369  42 IPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGEGSALEKSLavsqgGELYEEWLELRNGCLCCS----VKDSGL 117
Cdd:PRK11537    4 IAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLI-----GDRATQIKTLTNGCICCSrsneLEDALL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 118 RAIENLMQKKGKFDYILLETTGLADP--------------------GIITIVDSKYGLKHL------------------- 158
Cdd:PRK11537   79 DLLDNLDKGNIQFDRLVIECTGMADPgpiiqtffshevlcqrylldGVIALVDAVHADEQMnqftiaqsqvgyadrillt 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 159 -TEEKPDG-LINEATRSINGLGQILETQRSRVDLSNVLDLHAF---DSLsgISLQKKLQHVPGTQPHLdQSIVtITFEVP 233
Cdd:PRK11537  159 kTDVAGEAeKLRERLARINARAPVYTVVHGDIDLSLLFNTNGFmleENV--VSTKPRFHFIADKQNDI-SSIV-VELDYP 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 234 GNAKEehLNMFIQNLLweknVRNKDNhcmeVIRLKGLVSIKDKSQQVIVQGVHELYDLEetpvsWK---DDTERTNRLVL 310
Cdd:PRK11537  235 VDISE--VSRVMENLL----LESADK----LLRYKGMLWIDGEPNRLLFQGVQRLYSAD-----WDrpwGDETPHSTLVF 299
                         330
                  ....*....|....*.
gi 2462625369 311 LGRNLDKDILKQLFIA 326
Cdd:PRK11537  300 IGIQLPEEEIRAAFAG 315
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
264-324 1.08e-06

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: 46.05  E-value: 1.08e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462625369  264 VIRLKGLVSIKDKSQQVIV-QGVHELYDLEETPVsWKDDTERTNRLVLLGRNLDKDILKQLF 324
Cdd:smart00833  28 VLRAKGFFWLASRPDLPGVlSQAGGRLRIEPAGA-WPAAGDRRTRLVFIGRDLDEEAIRAAL 88
 
Name Accession Description Interval E-value
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
40-324 3.05e-64

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 206.18  E-value: 3.05e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369  40 AKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGE---GSALekslaVSQGGelyEEWLELRNGCLCCSVKDSG 116
Cdd:COG0523     2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEvgiDAAL-----VRDTD---EEIVELSNGCICCTLREDL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 117 LRAIENLMqKKGKFDYILLETTGLADP--------------------GIITIVDSKYGLKHLTEE--------------- 161
Cdd:COG0523    74 LPALRRLL-RRGRFDRLLIETTGLADPapvaqtftfdpelrdrlrldGVVTVVDARNLLDDLADRtlhellvdqiafadv 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 162 ----KPDgLINEAT--------RSINGLGQILETQRSRVDLSNVLDLHAFDSLSGISLQKKLQhvPGTQPHLDQSIVTIT 229
Cdd:COG0523   153 ivlnKTD-LVDEEElaalearlRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWLE--ELRDHEHDDGIRSFV 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 230 FEVPGNAKEEHLNMFIqnllweknvrnkDNHCMEVIRLKGLVSIKDKSQQVIVQGVHELYDLEETPvSWKDDtERTNRLV 309
Cdd:COG0523   230 FRSDRPFDPERLADFL------------EELGPGVLRAKGFLWLAGRPRRLVFQGVGGRLSLEPLG-PWPAD-DRRSRLV 295
                         330
                  ....*....|....*
gi 2462625369 310 LLGRNLDKDILKQLF 324
Cdd:COG0523   296 FIGRDLDEAALEAAL 310
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
43-197 2.62e-63

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: 199.67  E-value: 2.62e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369  43 PVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGEGSaLEKSLAVSQGGelYEEWLELRNGCLCCSVKDSGLRAIEN 122
Cdd:cd03112     1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVG-IDAALLADSGG--GEEVVELSNGCICCTLKGDLVKALEQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 123 LMQKKGKFDYILLETTGLADP--------------------GIITIVDSKYGLKHLTEE-------------------KP 163
Cdd:cd03112    78 LLERRGKFDYILIETTGLADPgpiaqtlwsdeelesrlrldGVVTVVDAKNFLKQLDEEdvsdlavdqiafadvivlnKT 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462625369 164 DgLINEAT--------RSINGLGQILETQRSRVDLSNVLDLH 197
Cdd:cd03112   158 D-LVDEEElealrariRALNPGAKIVETTYGRVDLEELLGTG 198
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
43-152 4.75e-37

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: 131.22  E-value: 4.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369  43 PVTIITGYLGAGKTTLLNYIL-TEQHSKRVAVILNEFGEGSaLEKSLAVSQGgelyEEWLELRNGCLCCSVKDSGLRAIE 121
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLkQNRAGLRIAVIVNEFGETG-IDAELLSETG----VLIVELSNGCICCTIREDLSMALE 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462625369 122 NLMQKKGKFDYILLETTGLADP-------------------GIITIVDSK 152
Cdd:pfam02492  76 ALLEREGRLDVIFIETTGLAEPapvaqtflspelrspvlldGVITVVDAA 125
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
40-318 5.84e-34

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: 127.94  E-value: 5.84e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369  40 AKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGE----GSALeKSLAVSQGGElyEEWLELRNGCLCCSVKDS 115
Cdd:TIGR02475   2 AKIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDlgidGEIL-KACGIEGCSE--ENIVELANGCICCTVADD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 116 GLRAIENLMQKKGKFDYILLETTGLADP-------------------GIITIVDSKY---------------------GL 155
Cdd:TIGR02475  79 FIPTMTKLLARRQRPDHILIETSGLALPkplvqafqwpeirsrvtvdGVVTVVDGPAvaagrfaadpdaldaqraaddNL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 156 KHLT--EE---------------KPDGLINEATRSING-LGQ-------ILETQRSRVDLSNVLDLHAFDSLSgISLQKK 210
Cdd:TIGR02475 159 DHETplEElfedqlacadlvilnKADLLDAAGLARVRAeIAAelpravkIVEASHGEVDARVLLGLGAAAEDD-LDNRPS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 211 LQHVPGTQPHLDQSIVTITFEVPGNAKEEHLNMFIQNLLWEKNvrnkdnhcmeVIRLKGLVSIKDKSQQVIVQGVHELYD 290
Cdd:TIGR02475 238 HHDFEGGEEHDHDEFDSVVVDLGEVADPAALRQRLERLAEEHD----------VLRIKGFAAVPGKPMRLLVQGVGQRVD 307
                         330       340
                  ....*....|....*....|....*....
gi 2462625369 291 lEETPVSWKDDTERTNRLVLLG-RNLDKD 318
Cdd:TIGR02475 308 -SYYDRPWQAAETRQTRLVVIGlHDLDQA 335
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
42-326 3.65e-25

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 103.24  E-value: 3.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369  42 IPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGEGSALEKSLavsqgGELYEEWLELRNGCLCCS----VKDSGL 117
Cdd:PRK11537    4 IAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLI-----GDRATQIKTLTNGCICCSrsneLEDALL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 118 RAIENLMQKKGKFDYILLETTGLADP--------------------GIITIVDSKYGLKHL------------------- 158
Cdd:PRK11537   79 DLLDNLDKGNIQFDRLVIECTGMADPgpiiqtffshevlcqrylldGVIALVDAVHADEQMnqftiaqsqvgyadrillt 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 159 -TEEKPDG-LINEATRSINGLGQILETQRSRVDLSNVLDLHAF---DSLsgISLQKKLQHVPGTQPHLdQSIVtITFEVP 233
Cdd:PRK11537  159 kTDVAGEAeKLRERLARINARAPVYTVVHGDIDLSLLFNTNGFmleENV--VSTKPRFHFIADKQNDI-SSIV-VELDYP 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 234 GNAKEehLNMFIQNLLweknVRNKDNhcmeVIRLKGLVSIKDKSQQVIVQGVHELYDLEetpvsWK---DDTERTNRLVL 310
Cdd:PRK11537  235 VDISE--VSRVMENLL----LESADK----LLRYKGMLWIDGEPNRLLFQGVQRLYSAD-----WDrpwGDETPHSTLVF 299
                         330
                  ....*....|....*.
gi 2462625369 311 LGRNLDKDILKQLFIA 326
Cdd:PRK11537  300 IGIQLPEEEIRAAFAG 315
CobW_C pfam07683
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ...
225-324 6.47e-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: 77.66  E-value: 6.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625369 225 IVTITFEVPGNAKEEHLNMFIQNLLWEKNVrnkdnhcmevIRLKGLVSIKDKSQQVIVQGVHELYDLEETPVSWKDDtER 304
Cdd:pfam07683   1 ISSFVFRADRPFDPERLEAWLEDLLLPEGI----------LRAKGILWLAGRPRPLVFQGVGGRLSLEPAGRWWPDE-DR 69
                          90       100
                  ....*....|....*....|
gi 2462625369 305 TNRLVLLGRNLDKDILKQLF 324
Cdd:pfam07683  70 RSRLVFIGRDLDREALRAAL 89
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
264-324 1.08e-06

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: 46.05  E-value: 1.08e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462625369  264 VIRLKGLVSIKDKSQQVIV-QGVHELYDLEETPVsWKDDTERTNRLVLLGRNLDKDILKQLF 324
Cdd:smart00833  28 VLRAKGFFWLASRPDLPGVlSQAGGRLRIEPAGA-WPAAGDRRTRLVFIGRDLDEEAIRAAL 88
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
43-73 1.79e-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: 1.79e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462625369  43 PVTIITGYLGAGKTTLLNYIL--TEQHSKRVAV 73
Cdd:COG0507   141 RVSVLTGGAGTGKTTTLRALLaaLEALGLRVAL 173
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 7.08e-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: 36.76  E-value: 7.08e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462625369  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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