NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1720395082|ref|XP_030106750|]
View 

zinc-regulated GTPase metalloprotein activator 1 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
YejR super family cl33931
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
2-182 3.71e-29

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


The actual alignment was detected with superfamily member COG0523:

Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 109.88  E-value: 3.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395082   2 ILINKTDLVSEEELNNLRTTIRSINGLGKVLETQRSRVHLSNILDLHAYDILSGISLQKKLQHVSTAPHlDQSIVTVTFE 81
Cdd:COG0523   153 IVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWLEELRDHEH-DDGIRSFVFR 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395082  82 VPGSAKEECLNVFIQNLlweknvknkdGHcmEVIRLKGLVSIKDKPQQMIVQGIHELYDLEEsLVNWKDDaERACQLVFI 161
Cdd:COG0523   232 SDRPFDPERLADFLEEL----------GP--GVLRAKGFLWLAGRPRRLVFQGVGGRLSLEP-LGPWPAD-DRRSRLVFI 297
                         170       180
                  ....*....|....*....|.
gi 1720395082 162 GRNLDKDVLQQLFLTAVAEAE 182
Cdd:COG0523   298 GRDLDEAALEAALDACLLTDA 318
 
Name Accession Description Interval E-value
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
2-182 3.71e-29

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 109.88  E-value: 3.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395082   2 ILINKTDLVSEEELNNLRTTIRSINGLGKVLETQRSRVHLSNILDLHAYDILSGISLQKKLQHVSTAPHlDQSIVTVTFE 81
Cdd:COG0523   153 IVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWLEELRDHEH-DDGIRSFVFR 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395082  82 VPGSAKEECLNVFIQNLlweknvknkdGHcmEVIRLKGLVSIKDKPQQMIVQGIHELYDLEEsLVNWKDDaERACQLVFI 161
Cdd:COG0523   232 SDRPFDPERLADFLEEL----------GP--GVLRAKGFLWLAGRPRRLVFQGVGGRLSLEP-LGPWPAD-DRRSRLVFI 297
                         170       180
                  ....*....|....*....|.
gi 1720395082 162 GRNLDKDVLQQLFLTAVAEAE 182
Cdd:COG0523   298 GRDLDEAALEAALDACLLTDA 318
CobW_C pfam07683
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ...
75-178 7.05e-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: 77.28  E-value: 7.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395082  75 IVTVTFEVPGSAKEECLNVFIQNLLWEKNVknkdghcmevIRLKGLVSIKDKPQQMIVQGIHELYDLEESLVNWKDDaER 154
Cdd:pfam07683   1 ISSFVFRADRPFDPERLEAWLEDLLLPEGI----------LRAKGILWLAGRPRPLVFQGVGGRLSLEPAGRWWPDE-DR 69
                          90       100
                  ....*....|....*....|....
gi 1720395082 155 ACQLVFIGRNLDKDVLQQLFLTAV 178
Cdd:pfam07683  70 RSRLVFIGRDLDREALRAALDACL 93
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
1-48 1.23e-12

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: 63.31  E-value: 1.23e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720395082   1 MILINKTDLVSEEELNNLRTTIRSINGLGKVLETQRSRVHLSNILDLH 48
Cdd:cd03112   151 VIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGTG 198
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
114-177 1.02e-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: 47.98  E-value: 1.02e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720395082  114 VIRLKGLVSIKDKPQQ-MIVQGIHELYDLEeSLVNWKDDAERACQLVFIGRNLDKDVLQQLFLTA 177
Cdd:smart00833  28 VLRAKGFFWLASRPDLpGVLSQAGGRLRIE-PAGAWPAAGDRRTRLVFIGRDLDEEAIRAALDAC 91
 
Name Accession Description Interval E-value
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
2-182 3.71e-29

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 109.88  E-value: 3.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395082   2 ILINKTDLVSEEELNNLRTTIRSINGLGKVLETQRSRVHLSNILDLHAYDILSGISLQKKLQHVSTAPHlDQSIVTVTFE 81
Cdd:COG0523   153 IVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWLEELRDHEH-DDGIRSFVFR 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395082  82 VPGSAKEECLNVFIQNLlweknvknkdGHcmEVIRLKGLVSIKDKPQQMIVQGIHELYDLEEsLVNWKDDaERACQLVFI 161
Cdd:COG0523   232 SDRPFDPERLADFLEEL----------GP--GVLRAKGFLWLAGRPRRLVFQGVGGRLSLEP-LGPWPAD-DRRSRLVFI 297
                         170       180
                  ....*....|....*....|.
gi 1720395082 162 GRNLDKDVLQQLFLTAVAEAE 182
Cdd:COG0523   298 GRDLDEAALEAALDACLLTDA 318
CobW_C pfam07683
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ...
75-178 7.05e-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: 77.28  E-value: 7.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395082  75 IVTVTFEVPGSAKEECLNVFIQNLLWEKNVknkdghcmevIRLKGLVSIKDKPQQMIVQGIHELYDLEESLVNWKDDaER 154
Cdd:pfam07683   1 ISSFVFRADRPFDPERLEAWLEDLLLPEGI----------LRAKGILWLAGRPRPLVFQGVGGRLSLEPAGRWWPDE-DR 69
                          90       100
                  ....*....|....*....|....
gi 1720395082 155 ACQLVFIGRNLDKDVLQQLFLTAV 178
Cdd:pfam07683  70 RSRLVFIGRDLDREALRAALDACL 93
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
1-48 1.23e-12

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: 63.31  E-value: 1.23e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720395082   1 MILINKTDLVSEEELNNLRTTIRSINGLGKVLETQRSRVHLSNILDLH 48
Cdd:cd03112   151 VIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGTG 198
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
114-177 1.02e-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: 47.98  E-value: 1.02e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720395082  114 VIRLKGLVSIKDKPQQ-MIVQGIHELYDLEeSLVNWKDDAERACQLVFIGRNLDKDVLQQLFLTA 177
Cdd:smart00833  28 VLRAKGFFWLASRPDLpGVLSQAGGRLRIE-PAGAWPAAGDRRTRLVFIGRDLDEEAIRAALDAC 91
 
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