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Conserved domains on  [gi|21356905|ref|NP_649540|]
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polymerase (DNA-directed), delta interacting protein 2, isoform A [Drosophila melanogaster]

Protein Classification

YccV-like and DUF525 domain-containing protein( domain architecture ID 10236861)

YccV-like and DUF525 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF525 super family cl01119
ApaG domain; The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins ...
 268-386 4.39e-36

ApaG domain; The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins and in eukaryotic F-box proteins. The domain is named after the bacterial apaG protein, of which it forms the core. The domain also occurs in the C-terminal part of eukaryotic proteins with an N-terminal F-box domain. The Salmonella typhimurium apaG domain protein corD is involved in Co(2+) resistance and Mg(2+) efflux. Tertiary structures from different apaG proteins show a fold of several beta-sheets. The apaG domain may be involved in protein-protein interactions which could be implicated in substrate-specificity.


The actual alignment was detected with superfamily member PRK05461:

Pssm-ID: 470082  Cd Length: 127  Bit Score: 128.34  E-value: 4.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356905  268 TTENVRITVIPFYMGCRETPASSVYWWRYCIRLENLGELSVQLRERHWRIFSLSGTLETVRGRGVVGQEPILSPRlPAFQ 347
Cdd:PRK05461   5 VTYGIEVSVQPRYLEEQSDPEEGRYVFAYTITIENLGRVPVQLLSRHWLITDANGRVQEVRGEGVVGEQPVLAPG-ESFE 83

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 21356905  348 YSSHVSLQAPSGHMWGTFRLEREDGYSFDCKIPPFSLES 386
Cdd:PRK05461  84 YTSGAVLETPSGTMQGHYQMVDEDGERFEVPIPPFRLAV 122
YccV-like super family cl01548
Hemimethylated DNA-binding protein YccV like; YccV is a hemimethylated DNA binding protein ...
 51-237 1.36e-07

Hemimethylated DNA-binding protein YccV like; YccV is a hemimethylated DNA binding protein which has been shown to regulate dnaA gene expression. The structure of one of the hypothetical proteins in this family has been solved and it forms a beta sheet structure with a terminating alpha helix.


The actual alignment was detected with superfamily member smart00992:

Pssm-ID: 445467  Cd Length: 98  Bit Score: 49.16  E-value: 1.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356905     51 RYETGQLFLHRIFGYRGVIlFPWtarvyDRDLHNPgkisattttsaNPTQQNRTKEASLRvkantsasptaataqsadap 130
Cdd:smart00992   3 KFRIGQVVRHKLFGYRGVV-FDW-----DPEFANT-----------EEWYDEIPEDSRPP-------------------- 45

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356905    131 tstafetnaaestgttnlgttsqvdpkevkgKVQTFYQVLIDTRDCPYIRaqteavtflgnqdsnrslyaipgldYVAHE 210
Cdd:smart00992  46 -------------------------------RDQPFYHVLVENDDSSYVA-------------------------YVSEQ 69

                          170       180
                   ....*....|....*....|....*..
gi 21356905    211 DIMPYSSSEksPLQHELFDKFLTHAPD 237
Cdd:smart00992  70 NLEPDTSGE--PIDHPLLDELFDEFDG 94
 
Name Accession Description Interval E-value
apaG PRK05461
CO2+/MG2+ efflux protein ApaG; Reviewed
 268-386 4.39e-36

CO2+/MG2+ efflux protein ApaG; Reviewed


Pssm-ID: 180098  Cd Length: 127  Bit Score: 128.34  E-value: 4.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356905  268 TTENVRITVIPFYMGCRETPASSVYWWRYCIRLENLGELSVQLRERHWRIFSLSGTLETVRGRGVVGQEPILSPRlPAFQ 347
Cdd:PRK05461   5 VTYGIEVSVQPRYLEEQSDPEEGRYVFAYTITIENLGRVPVQLLSRHWLITDANGRVQEVRGEGVVGEQPVLAPG-ESFE 83

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 21356905  348 YSSHVSLQAPSGHMWGTFRLEREDGYSFDCKIPPFSLES 386
Cdd:PRK05461  84 YTSGAVLETPSGTMQGHYQMVDEDGERFEVPIPPFRLAV 122
DUF525 pfam04379
ApaG domain; The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins ...
 287-369 1.01e-35

ApaG domain; The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins and in eukaryotic F-box proteins. The domain is named after the bacterial apaG protein, of which it forms the core. The domain also occurs in the C-terminal part of eukaryotic proteins with an N-terminal F-box domain. The Salmonella typhimurium apaG domain protein corD is involved in Co(2+) resistance and Mg(2+) efflux. Tertiary structures from different apaG proteins show a fold of several beta-sheets. The apaG domain may be involved in protein-protein interactions which could be implicated in substrate-specificity.


Pssm-ID: 461283  Cd Length: 87  Bit Score: 126.04  E-value: 1.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356905   287 PASSVYWWRYCIRLENLGELSVQLRERHWRIFSLSGTLETVRGRGVVGQEPILSPRlPAFQYSSHVSLQAPSGHMWGTFR 366
Cdd:pfam04379   6 PEEGRYVFAYTIRIENLGDSSVQLLSRHWIITDANGKVEEVRGEGVVGEQPVLAPG-ESFEYTSGCPLETPSGSMEGSYT 84


                  ...
gi 21356905   367 LER 369
Cdd:pfam04379  85 MVR 87
ApaG COG2967
Uncharacterized conserved protein ApaG affecting Mg2+/Co2+ transport [Inorganic ion transport ...
 270-384 3.81e-35

Uncharacterized conserved protein ApaG affecting Mg2+/Co2+ transport [Inorganic ion transport and metabolism];


Pssm-ID: 442207  Cd Length: 119  Bit Score: 125.60  E-value: 3.81e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356905 270 ENVRITVIPFYMGCRETPASSVYWWRYCIRLENLGELSVQLRERHWRIFSLSGTLETVRGRGVVGQEPILSPRlPAFQYS 349
Cdd:COG2967   1 YGIKVSVETEYLPEQSDPEEGRYVFAYTITIENLGDVTVQLLSRHWIITDANGKVQEVEGEGVVGEQPVLAPG-ESFEYT 79

                        90       100       110
                ....*....|....*....|....*....|....*
gi 21356905 350 SHVSLQAPSGHMWGTFRLEREDGYSFDCKIPPFSL 384
Cdd:COG2967  80 SGCVLETPVGTMQGSYQMVDEDGERFDVPIPPFSL 114
YccV-like smart00992
Hemimethylated DNA-binding protein YccV like; YccV is a hemimethylated DNA binding protein ...
 51-237 1.36e-07

Hemimethylated DNA-binding protein YccV like; YccV is a hemimethylated DNA binding protein which has been shown to regulate dnaA gene expression. The structure of one of the hypothetical proteins in this family has been solved and it forms a beta sheet structure with a terminating alpha helix.


Pssm-ID: 214961  Cd Length: 98  Bit Score: 49.16  E-value: 1.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356905     51 RYETGQLFLHRIFGYRGVIlFPWtarvyDRDLHNPgkisattttsaNPTQQNRTKEASLRvkantsasptaataqsadap 130
Cdd:smart00992   3 KFRIGQVVRHKLFGYRGVV-FDW-----DPEFANT-----------EEWYDEIPEDSRPP-------------------- 45

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356905    131 tstafetnaaestgttnlgttsqvdpkevkgKVQTFYQVLIDTRDCPYIRaqteavtflgnqdsnrslyaipgldYVAHE 210
Cdd:smart00992  46 -------------------------------RDQPFYHVLVENDDSSYVA-------------------------YVSEQ 69

                          170       180
                   ....*....|....*....|....*..
gi 21356905    211 DIMPYSSSEksPLQHELFDKFLTHAPD 237
Cdd:smart00992  70 NLEPDTSGE--PIDHPLLDELFDEFDG 94
YccV-like pfam08755
Hemimethylated DNA-binding protein YccV like; YccV is a hemimethylated DNA binding protein ...
 51-83 2.17e-04

Hemimethylated DNA-binding protein YccV like; YccV is a hemimethylated DNA binding protein which has been shown to regulate dnaA gene expression. The structure of one of the hypothetical proteins in this family has been solved and it forms a beta sheet structure with a terminating alpha helix.


Pssm-ID: 430193  Cd Length: 96  Bit Score: 39.88  E-value: 2.17e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 21356905    51 RYETGQLFLHRIFGYRGVIL---------FPWTARVYDRDLH 83
Cdd:pfam08755   2 KFRIGQVVRHRRYGYRGVIVgwdpecaasEEWIEQMGVDSLG 43
 
Name Accession Description Interval E-value
apaG PRK05461
CO2+/MG2+ efflux protein ApaG; Reviewed
 268-386 4.39e-36

CO2+/MG2+ efflux protein ApaG; Reviewed


Pssm-ID: 180098  Cd Length: 127  Bit Score: 128.34  E-value: 4.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356905  268 TTENVRITVIPFYMGCRETPASSVYWWRYCIRLENLGELSVQLRERHWRIFSLSGTLETVRGRGVVGQEPILSPRlPAFQ 347
Cdd:PRK05461   5 VTYGIEVSVQPRYLEEQSDPEEGRYVFAYTITIENLGRVPVQLLSRHWLITDANGRVQEVRGEGVVGEQPVLAPG-ESFE 83

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 21356905  348 YSSHVSLQAPSGHMWGTFRLEREDGYSFDCKIPPFSLES 386
Cdd:PRK05461  84 YTSGAVLETPSGTMQGHYQMVDEDGERFEVPIPPFRLAV 122
DUF525 pfam04379
ApaG domain; The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins ...
 287-369 1.01e-35

ApaG domain; The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins and in eukaryotic F-box proteins. The domain is named after the bacterial apaG protein, of which it forms the core. The domain also occurs in the C-terminal part of eukaryotic proteins with an N-terminal F-box domain. The Salmonella typhimurium apaG domain protein corD is involved in Co(2+) resistance and Mg(2+) efflux. Tertiary structures from different apaG proteins show a fold of several beta-sheets. The apaG domain may be involved in protein-protein interactions which could be implicated in substrate-specificity.


Pssm-ID: 461283  Cd Length: 87  Bit Score: 126.04  E-value: 1.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356905   287 PASSVYWWRYCIRLENLGELSVQLRERHWRIFSLSGTLETVRGRGVVGQEPILSPRlPAFQYSSHVSLQAPSGHMWGTFR 366
Cdd:pfam04379   6 PEEGRYVFAYTIRIENLGDSSVQLLSRHWIITDANGKVEEVRGEGVVGEQPVLAPG-ESFEYTSGCPLETPSGSMEGSYT 84


                  ...
gi 21356905   367 LER 369
Cdd:pfam04379  85 MVR 87
ApaG COG2967
Uncharacterized conserved protein ApaG affecting Mg2+/Co2+ transport [Inorganic ion transport ...
 270-384 3.81e-35

Uncharacterized conserved protein ApaG affecting Mg2+/Co2+ transport [Inorganic ion transport and metabolism];


Pssm-ID: 442207  Cd Length: 119  Bit Score: 125.60  E-value: 3.81e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356905 270 ENVRITVIPFYMGCRETPASSVYWWRYCIRLENLGELSVQLRERHWRIFSLSGTLETVRGRGVVGQEPILSPRlPAFQYS 349
Cdd:COG2967   1 YGIKVSVETEYLPEQSDPEEGRYVFAYTITIENLGDVTVQLLSRHWIITDANGKVQEVEGEGVVGEQPVLAPG-ESFEYT 79

                        90       100       110
                ....*....|....*....|....*....|....*
gi 21356905 350 SHVSLQAPSGHMWGTFRLEREDGYSFDCKIPPFSL 384
Cdd:COG2967  80 SGCVLETPVGTMQGSYQMVDEDGERFDVPIPPFSL 114
YccV-like smart00992
Hemimethylated DNA-binding protein YccV like; YccV is a hemimethylated DNA binding protein ...
 51-237 1.36e-07

Hemimethylated DNA-binding protein YccV like; YccV is a hemimethylated DNA binding protein which has been shown to regulate dnaA gene expression. The structure of one of the hypothetical proteins in this family has been solved and it forms a beta sheet structure with a terminating alpha helix.


Pssm-ID: 214961  Cd Length: 98  Bit Score: 49.16  E-value: 1.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356905     51 RYETGQLFLHRIFGYRGVIlFPWtarvyDRDLHNPgkisattttsaNPTQQNRTKEASLRvkantsasptaataqsadap 130
Cdd:smart00992   3 KFRIGQVVRHKLFGYRGVV-FDW-----DPEFANT-----------EEWYDEIPEDSRPP-------------------- 45

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356905    131 tstafetnaaestgttnlgttsqvdpkevkgKVQTFYQVLIDTRDCPYIRaqteavtflgnqdsnrslyaipgldYVAHE 210
Cdd:smart00992  46 -------------------------------RDQPFYHVLVENDDSSYVA-------------------------YVSEQ 69

                          170       180
                   ....*....|....*....|....*..
gi 21356905    211 DIMPYSSSEksPLQHELFDKFLTHAPD 237
Cdd:smart00992  70 NLEPDTSGE--PIDHPLLDELFDEFDG 94
YccV-like pfam08755
Hemimethylated DNA-binding protein YccV like; YccV is a hemimethylated DNA binding protein ...
 51-83 2.17e-04

Hemimethylated DNA-binding protein YccV like; YccV is a hemimethylated DNA binding protein which has been shown to regulate dnaA gene expression. The structure of one of the hypothetical proteins in this family has been solved and it forms a beta sheet structure with a terminating alpha helix.


Pssm-ID: 430193  Cd Length: 96  Bit Score: 39.88  E-value: 2.17e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 21356905    51 RYETGQLFLHRIFGYRGVIL---------FPWTARVYDRDLH 83
Cdd:pfam08755   2 KFRIGQVVRHRRYGYRGVIVgwdpecaasEEWIEQMGVDSLG 43
 
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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