NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1052789140|ref|NP_001317043|]
View 

voltage-dependent L-type calcium channel subunit beta-4 isoform g [Homo sapiens]

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
Guanylate_kin super family cl30083
Guanylate kinase;
1-180 4.88e-57

Guanylate kinase;


The actual alignment was detected with superfamily member pfam00625:

Pssm-ID: 395500  Cd Length: 182  Bit Score: 181.81  E-value: 4.88e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052789140   1 MRPVVLVGPSLKGyevTDMMQKALFDFLKHRFdgRISITRVTADISL-----------AKRSVLNNPSKRAIIERSN-TR 68
Cdd:pfam00625   2 RRPVVLSGPSGVG---KSHIKKALLSEYPDKF--GYSVPHTTRPPRKgevdgkdyyfvSKEEMERDISANEFLEYAQfSG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052789140  69 SSLAEVQSEIERIFELARSlqlVVLDADtINHPAQLIKTSLAPIIVHVKVSSPKVLQRLIKSRGKSQSKHLNVQLVAADK 148
Cdd:pfam00625  77 NMYGTSVETIEQIHEQGKI---VILDVD-PQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQ 152
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1052789140 149 LAQCPPemFDVILDENQLEDACEHLGEYLEAY 180
Cdd:pfam00625 153 EFQHYE--FDVIIVNDDLEEAYKKLKEALEAE 182
 
Name Accession Description Interval E-value
Guanylate_kin pfam00625
Guanylate kinase;
1-180 4.88e-57

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 181.81  E-value: 4.88e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052789140   1 MRPVVLVGPSLKGyevTDMMQKALFDFLKHRFdgRISITRVTADISL-----------AKRSVLNNPSKRAIIERSN-TR 68
Cdd:pfam00625   2 RRPVVLSGPSGVG---KSHIKKALLSEYPDKF--GYSVPHTTRPPRKgevdgkdyyfvSKEEMERDISANEFLEYAQfSG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052789140  69 SSLAEVQSEIERIFELARSlqlVVLDADtINHPAQLIKTSLAPIIVHVKVSSPKVLQRLIKSRGKSQSKHLNVQLVAADK 148
Cdd:pfam00625  77 NMYGTSVETIEQIHEQGKI---VILDVD-PQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQ 152
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1052789140 149 LAQCPPemFDVILDENQLEDACEHLGEYLEAY 180
Cdd:pfam00625 153 EFQHYE--FDVIIVNDDLEEAYKKLKEALEAE 182
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
10-181 5.57e-29

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 108.92  E-value: 5.57e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052789140   10 SLKGYEVTDMMQK---ALFDFLKHRFDGRISITRVTADISLAKRSVLNNPSKRA-IIERSNTRSSLaeVQSEIERIFELA 85
Cdd:smart00072   3 VGKGTLLAELIQEipdAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGlFLEWGEYEGNY--YGTSKETIRQVA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052789140   86 RSLQLVVLDADtINHPAQLIKTSLAPIIVHVKVSSPKVLQRLIKSRGKSQSKHLNVQLVAADKLAQCPpEMFDVILDENQ 165
Cdd:smart00072  81 EKGKHCLLDID-PQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAQEY-HLFDYVIVNDD 158
                          170
                   ....*....|....*.
gi 1052789140  166 LEDACEHLGEYLEAYW 181
Cdd:smart00072 159 LEDAYEELKEILEAEQ 174
 
Name Accession Description Interval E-value
Guanylate_kin pfam00625
Guanylate kinase;
1-180 4.88e-57

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 181.81  E-value: 4.88e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052789140   1 MRPVVLVGPSLKGyevTDMMQKALFDFLKHRFdgRISITRVTADISL-----------AKRSVLNNPSKRAIIERSN-TR 68
Cdd:pfam00625   2 RRPVVLSGPSGVG---KSHIKKALLSEYPDKF--GYSVPHTTRPPRKgevdgkdyyfvSKEEMERDISANEFLEYAQfSG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052789140  69 SSLAEVQSEIERIFELARSlqlVVLDADtINHPAQLIKTSLAPIIVHVKVSSPKVLQRLIKSRGKSQSKHLNVQLVAADK 148
Cdd:pfam00625  77 NMYGTSVETIEQIHEQGKI---VILDVD-PQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKINKRMAAAEQ 152
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1052789140 149 LAQCPPemFDVILDENQLEDACEHLGEYLEAY 180
Cdd:pfam00625 153 EFQHYE--FDVIIVNDDLEEAYKKLKEALEAE 182
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
10-181 5.57e-29

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 108.92  E-value: 5.57e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052789140   10 SLKGYEVTDMMQK---ALFDFLKHRFDGRISITRVTADISLAKRSVLNNPSKRA-IIERSNTRSSLaeVQSEIERIFELA 85
Cdd:smart00072   3 VGKGTLLAELIQEipdAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGlFLEWGEYEGNY--YGTSKETIRQVA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052789140   86 RSLQLVVLDADtINHPAQLIKTSLAPIIVHVKVSSPKVLQRLIKSRGKSQSKHLNVQLVAADKLAQCPpEMFDVILDENQ 165
Cdd:smart00072  81 EKGKHCLLDID-PQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRGTETSERIQKRLAAAQKEAQEY-HLFDYVIVNDD 158
                          170
                   ....*....|....*.
gi 1052789140  166 LEDACEHLGEYLEAYW 181
Cdd:smart00072 159 LEDAYEELKEILEAEQ 174
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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