NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2217376072|ref|XP_047278918|]
View 

zinc-regulated GTPase metalloprotein activator 1E isoform X6 [Homo sapiens]

Protein Classification

GTP-binding protein( domain architecture ID 10123105)

GTP-binding protein similar to GTPase YjiA, a GTP dependent regulatory protein, and CobW, which is involved in the synthesis of cobalamin

Gene Ontology:  GO:0005525|GO:0003924
PubMed:  11916378

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
43-206 5.36e-69

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: 211.61  E-value: 5.36e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376072  43 PVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNESGEGSaLEKSLAVSQGGelYEEWLELRNGCLCCSVKDNGLRAIEN 122
Cdd:cd03112     1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVG-IDAALLADSGG--GEEVVELSNGCICCTLKGDLVKALEQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376072 123 LMQKKGKFDDILLETTGLADPGAVTSMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEE-------------------KP 183
Cdd:cd03112    78 LLERRGKFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVVDAKNFLKQLDEEdvsdlavdqiafadvivlnKT 157
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217376072 184 DgLINEAT--------RSINGLGQILETQRS 206
Cdd:cd03112   158 D-LVDEEElealrariRALNPGAKIVETTYG 187
 
Name Accession Description Interval E-value
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
43-206 5.36e-69

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: 211.61  E-value: 5.36e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376072  43 PVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNESGEGSaLEKSLAVSQGGelYEEWLELRNGCLCCSVKDNGLRAIEN 122
Cdd:cd03112     1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVG-IDAALLADSGG--GEEVVELSNGCICCTLKGDLVKALEQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376072 123 LMQKKGKFDDILLETTGLADPGAVTSMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEE-------------------KP 183
Cdd:cd03112    78 LLERRGKFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVVDAKNFLKQLDEEdvsdlavdqiafadvivlnKT 157
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217376072 184 DgLINEAT--------RSINGLGQILETQRS 206
Cdd:cd03112   158 D-LVDEEElealrariRALNPGAKIVETTYG 187
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
40-180 1.41e-46

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 158.03  E-value: 1.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376072  40 AKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNESGE---GSALekslaVSQGGelyEEWLELRNGCLCCSVKDNG 116
Cdd:COG0523     2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEvgiDAAL-----VRDTD---EEIVELSNGCICCTLREDL 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217376072 117 LRAIENLMqKKGKFDDILLETTGLADPGAVTSMFWVDAELGSDIYLDGIITIVDSKYGLKHLTE 180
Cdd:COG0523    74 LPALRRLL-RRGRFDRLLIETTGLADPAPVAQTFTFDPELRDRLRLDGVVTVVDARNLLDDLAD 136
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
43-172 7.82e-43

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: 144.32  E-value: 7.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376072  43 PVTIITGYLGAGKTTLLNYIL-TEQHSKRVAVILNESGEGSaLEKSLAVSQGgelyEEWLELRNGCLCCSVKDNGLRAIE 121
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLkQNRAGLRIAVIVNEFGETG-IDAELLSETG----VLIVELSNGCICCTIREDLSMALE 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217376072 122 NLMQKKGKFDDILLETTGLADPGAVTSMFWVDaELGSDIYLDGIITIVDSK 172
Cdd:pfam02492  76 ALLEREGRLDVIFIETTGLAEPAPVAQTFLSP-ELRSPVLLDGVITVVDAA 125
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
40-171 2.29e-30

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: 116.00  E-value: 2.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376072  40 AKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNESGE----GSALeKSLAVSQGGElyEEWLELRNGCLCCSVKDN 115
Cdd:TIGR02475   2 AKIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDlgidGEIL-KACGIEGCSE--ENIVELANGCICCTVADD 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217376072 116 GLRAIENLMQKKGKFDDILLETTGLADPGAVTSMF-WvdAELGSDIYLDGIITIVDS 171
Cdd:TIGR02475  79 FIPTMTKLLARRQRPDHILIETSGLALPKPLVQAFqW--PEIRSRVTVDGVVTVVDG 133
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
42-171 1.78e-27

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 107.87  E-value: 1.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376072  42 IPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNESGEGSALEKSLavsqgGELYEEWLELRNGCLCCS----VKDNGL 117
Cdd:PRK11537    4 IAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLI-----GDRATQIKTLTNGCICCSrsneLEDALL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217376072 118 RAIENLMQKKGKFDDILLETTGLADPGAVTSMFWVDAELGSDIYLDGIITIVDS 171
Cdd:PRK11537   79 DLLDNLDKGNIQFDRLVIECTGMADPGPIIQTFFSHEVLCQRYLLDGVIALVDA 132
 
Name Accession Description Interval E-value
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
43-206 5.36e-69

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: 211.61  E-value: 5.36e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376072  43 PVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNESGEGSaLEKSLAVSQGGelYEEWLELRNGCLCCSVKDNGLRAIEN 122
Cdd:cd03112     1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVG-IDAALLADSGG--GEEVVELSNGCICCTLKGDLVKALEQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376072 123 LMQKKGKFDDILLETTGLADPGAVTSMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEE-------------------KP 183
Cdd:cd03112    78 LLERRGKFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVVDAKNFLKQLDEEdvsdlavdqiafadvivlnKT 157
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217376072 184 DgLINEAT--------RSINGLGQILETQRS 206
Cdd:cd03112   158 D-LVDEEElealrariRALNPGAKIVETTYG 187
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
40-180 1.41e-46

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 158.03  E-value: 1.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376072  40 AKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNESGE---GSALekslaVSQGGelyEEWLELRNGCLCCSVKDNG 116
Cdd:COG0523     2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEvgiDAAL-----VRDTD---EEIVELSNGCICCTLREDL 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217376072 117 LRAIENLMqKKGKFDDILLETTGLADPGAVTSMFWVDAELGSDIYLDGIITIVDSKYGLKHLTE 180
Cdd:COG0523    74 LPALRRLL-RRGRFDRLLIETTGLADPAPVAQTFTFDPELRDRLRLDGVVTVVDARNLLDDLAD 136
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
43-172 7.82e-43

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: 144.32  E-value: 7.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376072  43 PVTIITGYLGAGKTTLLNYIL-TEQHSKRVAVILNESGEGSaLEKSLAVSQGgelyEEWLELRNGCLCCSVKDNGLRAIE 121
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLkQNRAGLRIAVIVNEFGETG-IDAELLSETG----VLIVELSNGCICCTIREDLSMALE 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217376072 122 NLMQKKGKFDDILLETTGLADPGAVTSMFWVDaELGSDIYLDGIITIVDSK 172
Cdd:pfam02492  76 ALLEREGRLDVIFIETTGLAEPAPVAQTFLSP-ELRSPVLLDGVITVVDAA 125
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
40-171 2.29e-30

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: 116.00  E-value: 2.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376072  40 AKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNESGE----GSALeKSLAVSQGGElyEEWLELRNGCLCCSVKDN 115
Cdd:TIGR02475   2 AKIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDlgidGEIL-KACGIEGCSE--ENIVELANGCICCTVADD 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217376072 116 GLRAIENLMQKKGKFDDILLETTGLADPGAVTSMF-WvdAELGSDIYLDGIITIVDS 171
Cdd:TIGR02475  79 FIPTMTKLLARRQRPDHILIETSGLALPKPLVQAFqW--PEIRSRVTVDGVVTVVDG 133
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
42-171 1.78e-27

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 107.87  E-value: 1.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376072  42 IPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNESGEGSALEKSLavsqgGELYEEWLELRNGCLCCS----VKDNGL 117
Cdd:PRK11537    4 IAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLI-----GDRATQIKTLTNGCICCSrsneLEDALL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217376072 118 RAIENLMQKKGKFDDILLETTGLADPGAVTSMFWVDAELGSDIYLDGIITIVDS 171
Cdd:PRK11537   79 DLLDNLDKGNIQFDRLVIECTGMADPGPIIQTFFSHEVLCQRYLLDGVIALVDA 132
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
43-73 9.24e-04

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: 40.35  E-value: 9.24e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2217376072  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 5.36e-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: 5.36e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2217376072  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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH