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Conserved domains on  [gi|568942480|ref|XP_006506479|]
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vitamin K-dependent gamma-carboxylase isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VKG_Carbox super family cl27079
Vitamin K-dependent gamma-carboxylase; Using reduced vitamin K, oxygen, and carbon dioxide, ...
 8-276 3.21e-116

Vitamin K-dependent gamma-carboxylase; Using reduced vitamin K, oxygen, and carbon dioxide, gamma-glutamyl carboxylase post-translationally modifies certain glutamates by adding carbon dioxide to the gamma position of those amino acids. In vertebrates, the modification of glutamate residues of target proteins is facilitated by an interaction between a propeptide present on target proteins and the gamma-glutamyl carboxylase.


The actual alignment was detected with superfamily member pfam05090:

Pssm-ID: 461546  Cd Length: 432  Bit Score: 349.95  E-value: 3.21e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942480    8 WLFSPFKLV----LSEELTSLLVVHWCGLLLDLSAGFLLFFDASRPVGLFFVSYFHCMNSQLFSIGMFPYVMLASSPLFC 83
Cdd:pfam05090 168 WLFSPFDLPligpLLQELWVAYIVSWGGFLFDLSIGFLLLFKKTRPLAFLFVIFFHLMNSILFPIGMFPYVMLATALIFF 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942480   84 SAEWPRKLVARCPKRLQELLPTKAAPRPSascvykrsrgKAGPKPGLRHQLGAIFTLLYLLEQLFLPYSHFLTQGYNNWT 163
Cdd:pfam05090 248 SPEWPRKLLARLPSRLRKLLPKARPPSSA----------KKKKIPSKKKKLVLALLLLYFVLQLLLPLRHFLYPGYVFWT 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942480  164 NGLYGYSWDMMVHSrSHQHVKITYRDGLTGELGYLNPGVFT---QSRRWKDHADMLKQYATCLSLLLPKYNVTEPQIYFD 240
Cdd:pfam05090 318 EEGYRFSWRMMLHE-KTGYVTFKVVDNKTGEVGYVDPSDFLtprQEKRMSTQPDMILQYAHCLKRNYKKKGIKNPSVYAD 396

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 568942480  241 IWVSINDRFQQRLFDPRVDIVQAVWSPFQRTPWVQP 276
Cdd:pfam05090 397 SWVSLNGRFSQRLIDPNVDLAKAEWSPFKHKPWILP 432
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 284-376 2.33e-05

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


The actual alignment was detected with superfamily member cd02235:

Pssm-ID: 477354 [Multi-domain]  Cd Length: 100  Bit Score: 43.34  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942480 284 WRTKLQDIKSSLDNHTEVVFIADFP-----GLHLENfvsedlGNTSIQLLQGEVTVElVAEQKNQTLQEGEKMQLPAGEY 358
Cdd:cd02235    3 KRTVLQRTDLSVPGREVVQVRVEIPpgavaGRHTHP------GEESGYVLEGSLELE-VDGQPPVTLKAGDSFFIPAGTV 75

                         90
                 ....*....|....*...
gi 568942480 359 HKVYTVSSSPSCYMYVYV 376
Cdd:cd02235   76 HNAKNVGSGPAKLLATYI 93
 
Name Accession Description Interval E-value
VKG_Carbox pfam05090
Vitamin K-dependent gamma-carboxylase; Using reduced vitamin K, oxygen, and carbon dioxide, ...
 8-276 3.21e-116

Vitamin K-dependent gamma-carboxylase; Using reduced vitamin K, oxygen, and carbon dioxide, gamma-glutamyl carboxylase post-translationally modifies certain glutamates by adding carbon dioxide to the gamma position of those amino acids. In vertebrates, the modification of glutamate residues of target proteins is facilitated by an interaction between a propeptide present on target proteins and the gamma-glutamyl carboxylase.


Pssm-ID: 461546  Cd Length: 432  Bit Score: 349.95  E-value: 3.21e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942480    8 WLFSPFKLV----LSEELTSLLVVHWCGLLLDLSAGFLLFFDASRPVGLFFVSYFHCMNSQLFSIGMFPYVMLASSPLFC 83
Cdd:pfam05090 168 WLFSPFDLPligpLLQELWVAYIVSWGGFLFDLSIGFLLLFKKTRPLAFLFVIFFHLMNSILFPIGMFPYVMLATALIFF 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942480   84 SAEWPRKLVARCPKRLQELLPTKAAPRPSascvykrsrgKAGPKPGLRHQLGAIFTLLYLLEQLFLPYSHFLTQGYNNWT 163
Cdd:pfam05090 248 SPEWPRKLLARLPSRLRKLLPKARPPSSA----------KKKKIPSKKKKLVLALLLLYFVLQLLLPLRHFLYPGYVFWT 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942480  164 NGLYGYSWDMMVHSrSHQHVKITYRDGLTGELGYLNPGVFT---QSRRWKDHADMLKQYATCLSLLLPKYNVTEPQIYFD 240
Cdd:pfam05090 318 EEGYRFSWRMMLHE-KTGYVTFKVVDNKTGEVGYVDPSDFLtprQEKRMSTQPDMILQYAHCLKRNYKKKGIKNPSVYAD 396

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 568942480  241 IWVSINDRFQQRLFDPRVDIVQAVWSPFQRTPWVQP 276
Cdd:pfam05090 397 SWVSLNGRFSQRLIDPNVDLAKAEWSPFKHKPWILP 432
HTTM smart00752
Horizontally Transferred TransMembrane Domain; Sequence analysis of vitamin K dependent ...
 4-87 1.26e-31

Horizontally Transferred TransMembrane Domain; Sequence analysis of vitamin K dependent gamma-carboxylases (VKGC) revealed the presence of a novel domain, HTTM (Horizontally Transferred TransMembrane) in its N-terminus. In contrast to most known domains, HTTM contains four transmembrane regions. Its occurrence in eukaryotes, bacteria and archaea is more likely caused by horizontal gene transfer than by early invention. The conservation of VKGC catalytic sites indicates an enzymatic function also for the other family members.


Pssm-ID: 214802  Cd Length: 271  Bit Score: 122.82  E-value: 1.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942480     4 LSRHWLFSPFKLVLSEELTSLLVVHWCGLLLDLSAGFLLFFDASRPVGLFFVSYFHCMNSQLFSIGMFPYVMLASSPLFC 83
Cdd:smart00752 188 LSLDWFFSPLDLVLLEFPPLLLAVTWGGLLFDLFFPFLLFNRRTRPIGLVVFIAFHLGNAVLFGIGMFPFVMIGALPLFL 267


                   ....
gi 568942480    84 SAEW 87
Cdd:smart00752 268 PPEW 271
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
 284-376 2.33e-05

Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLL4011, a Bradyrhizobium diazoefficiens protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380363 [Multi-domain]  Cd Length: 100  Bit Score: 43.34  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942480 284 WRTKLQDIKSSLDNHTEVVFIADFP-----GLHLENfvsedlGNTSIQLLQGEVTVElVAEQKNQTLQEGEKMQLPAGEY 358
Cdd:cd02235    3 KRTVLQRTDLSVPGREVVQVRVEIPpgavaGRHTHP------GEESGYVLEGSLELE-VDGQPPVTLKAGDSFFIPAGTV 75

                         90
                 ....*....|....*...
gi 568942480 359 HKVYTVSSSPSCYMYVYV 376
Cdd:cd02235   76 HNAKNVGSGPAKLLATYI 93
 
Name Accession Description Interval E-value
VKG_Carbox pfam05090
Vitamin K-dependent gamma-carboxylase; Using reduced vitamin K, oxygen, and carbon dioxide, ...
 8-276 3.21e-116

Vitamin K-dependent gamma-carboxylase; Using reduced vitamin K, oxygen, and carbon dioxide, gamma-glutamyl carboxylase post-translationally modifies certain glutamates by adding carbon dioxide to the gamma position of those amino acids. In vertebrates, the modification of glutamate residues of target proteins is facilitated by an interaction between a propeptide present on target proteins and the gamma-glutamyl carboxylase.


Pssm-ID: 461546  Cd Length: 432  Bit Score: 349.95  E-value: 3.21e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942480    8 WLFSPFKLV----LSEELTSLLVVHWCGLLLDLSAGFLLFFDASRPVGLFFVSYFHCMNSQLFSIGMFPYVMLASSPLFC 83
Cdd:pfam05090 168 WLFSPFDLPligpLLQELWVAYIVSWGGFLFDLSIGFLLLFKKTRPLAFLFVIFFHLMNSILFPIGMFPYVMLATALIFF 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942480   84 SAEWPRKLVARCPKRLQELLPTKAAPRPSascvykrsrgKAGPKPGLRHQLGAIFTLLYLLEQLFLPYSHFLTQGYNNWT 163
Cdd:pfam05090 248 SPEWPRKLLARLPSRLRKLLPKARPPSSA----------KKKKIPSKKKKLVLALLLLYFVLQLLLPLRHFLYPGYVFWT 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942480  164 NGLYGYSWDMMVHSrSHQHVKITYRDGLTGELGYLNPGVFT---QSRRWKDHADMLKQYATCLSLLLPKYNVTEPQIYFD 240
Cdd:pfam05090 318 EEGYRFSWRMMLHE-KTGYVTFKVVDNKTGEVGYVDPSDFLtprQEKRMSTQPDMILQYAHCLKRNYKKKGIKNPSVYAD 396

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 568942480  241 IWVSINDRFQQRLFDPRVDIVQAVWSPFQRTPWVQP 276
Cdd:pfam05090 397 SWVSLNGRFSQRLIDPNVDLAKAEWSPFKHKPWILP 432
HTTM smart00752
Horizontally Transferred TransMembrane Domain; Sequence analysis of vitamin K dependent ...
 4-87 1.26e-31

Horizontally Transferred TransMembrane Domain; Sequence analysis of vitamin K dependent gamma-carboxylases (VKGC) revealed the presence of a novel domain, HTTM (Horizontally Transferred TransMembrane) in its N-terminus. In contrast to most known domains, HTTM contains four transmembrane regions. Its occurrence in eukaryotes, bacteria and archaea is more likely caused by horizontal gene transfer than by early invention. The conservation of VKGC catalytic sites indicates an enzymatic function also for the other family members.


Pssm-ID: 214802  Cd Length: 271  Bit Score: 122.82  E-value: 1.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942480     4 LSRHWLFSPFKLVLSEELTSLLVVHWCGLLLDLSAGFLLFFDASRPVGLFFVSYFHCMNSQLFSIGMFPYVMLASSPLFC 83
Cdd:smart00752 188 LSLDWFFSPLDLVLLEFPPLLLAVTWGGLLFDLFFPFLLFNRRTRPIGLVVFIAFHLGNAVLFGIGMFPFVMIGALPLFL 267


                   ....
gi 568942480    84 SAEW 87
Cdd:smart00752 268 PPEW 271
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
 284-376 2.33e-05

Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLL4011, a Bradyrhizobium diazoefficiens protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380363 [Multi-domain]  Cd Length: 100  Bit Score: 43.34  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942480 284 WRTKLQDIKSSLDNHTEVVFIADFP-----GLHLENfvsedlGNTSIQLLQGEVTVElVAEQKNQTLQEGEKMQLPAGEY 358
Cdd:cd02235    3 KRTVLQRTDLSVPGREVVQVRVEIPpgavaGRHTHP------GEESGYVLEGSLELE-VDGQPPVTLKAGDSFFIPAGTV 75

                         90
                 ....*....|....*...
gi 568942480 359 HKVYTVSSSPSCYMYVYV 376
Cdd:cd02235   76 HNAKNVGSGPAKLLATYI 93
cupin_dsy2733 cd06983
Desulfitobacterium hafniense dsy2733 and related proteins, cupin domain; This family includes ...
 316-362 4.96e-03

Desulfitobacterium hafniense dsy2733 and related proteins, cupin domain; This family includes bacterial proteins homologous to dsy2733, a Desulfitobacterium hafniense protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380388 [Multi-domain]  Cd Length: 81  Bit Score: 36.07  E-value: 4.96e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568942480 316 VSED--LGNTSIQLLQGEVTVELvaEQKNQTLQEGEKMQLPAGEYHKVY 362
Cdd:cd06983   23 VSEEeyFGDTLYYVLEGEAEITI--GDEKHRLKAGDVLAVPAGVLHAIG 69
 
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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