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Conserved domains on  [gi|588480525|ref|NP_001277074|]
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polymerase delta-interacting protein 2 isoform 2 [Homo sapiens]

Protein Classification

ApaG domain-containing protein( domain architecture ID 5117)

ApaG domain-containing protein similar to Homo sapiens polymerase delta-interacting protein 2 (Poldip2) isoform 2, which is a nuclear-encoded mitochondrial protein required for oxidative metabolism

CATH:  2.60.40.1470
Gene Ontology:  GO:0005515
SCOP:  4007551

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 ...
 216-337 1.21e-32

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: 118.33  E-value: 1.21e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480525 216 HRETTENIRVTVIPFYMGMREAQNSHVYWWRYCIRLENLDSDVVQLRERHWRIFSLSGTLETVRGRGVVGREPVLskeQP 295
Cdd:PRK05461   2 YSAVTYGIEVSVQPRYLEEQSDPEEGRYVFAYTITIENLGRVPVQLLSRHWLITDANGRVQEVRGEGVVGEQPVL---AP 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 588480525 296 --AFQYSSHVSLQASSGHMWGTFRFERPDGSHFDVRIPPFSLES 337
Cdd:PRK05461  79 geSFEYTSGAVLETPSGTMQGHYQMVDEDGERFEVPIPPFRLAV 122
 
Name Accession Description Interval E-value
apaG PRK05461
CO2+/MG2+ efflux protein ApaG; Reviewed
 216-337 1.21e-32

CO2+/MG2+ efflux protein ApaG; Reviewed


Pssm-ID: 180098  Cd Length: 127  Bit Score: 118.33  E-value: 1.21e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480525 216 HRETTENIRVTVIPFYMGMREAQNSHVYWWRYCIRLENLDSDVVQLRERHWRIFSLSGTLETVRGRGVVGREPVLskeQP 295
Cdd:PRK05461   2 YSAVTYGIEVSVQPRYLEEQSDPEEGRYVFAYTITIENLGRVPVQLLSRHWLITDANGRVQEVRGEGVVGEQPVL---AP 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 588480525 296 --AFQYSSHVSLQASSGHMWGTFRFERPDGSHFDVRIPPFSLES 337
Cdd:PRK05461  79 geSFEYTSGAVLETPSGTMQGHYQMVDEDGERFEVPIPPFRLAV 122
ApaG COG2967
Uncharacterized conserved protein ApaG affecting Mg2+/Co2+ transport [Inorganic ion transport ...
 221-335 1.31e-32

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


Pssm-ID: 442207  Cd Length: 119  Bit Score: 117.89  E-value: 1.31e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480525 221 ENIRVTVIPFYMGMREAQNSHVYWWRYCIRLENLDSDVVQLRERHWRIFSLSGTLETVRGRGVVGREPVLskeQP--AFQ 298
Cdd:COG2967    1 YGIKVSVETEYLPEQSDPEEGRYVFAYTITIENLGDVTVQLLSRHWIITDANGKVQEVEGEGVVGEQPVL---APgeSFE 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 588480525 299 YSSHVSLQASSGHMWGTFRFERPDGSHFDVRIPPFSL 335
Cdd:COG2967   78 YTSGCVLETPVGTMQGSYQMVDEDGERFDVPIPPFSL 114
DUF525 pfam04379
ApaG domain; The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins ...
 239-320 1.08e-30

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: 111.79  E-value: 1.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480525  239 NSHVYWWRYCIRLENLDSDVVQLRERHWRIFSLSGTLETVRGRGVVGREPVLsKEQPAFQYSSHVSLQASSGHMWGTFRF 318
Cdd:pfam04379   7 EEGRYVFAYTIRIENLGDSSVQLLSRHWIITDANGKVEEVRGEGVVGEQPVL-APGESFEYTSGCPLETPSGSMEGSYTM 85


                  ..
gi 588480525  319 ER 320
Cdd:pfam04379  86 VR 87
 
Name Accession Description Interval E-value
apaG PRK05461
CO2+/MG2+ efflux protein ApaG; Reviewed
 216-337 1.21e-32

CO2+/MG2+ efflux protein ApaG; Reviewed


Pssm-ID: 180098  Cd Length: 127  Bit Score: 118.33  E-value: 1.21e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480525 216 HRETTENIRVTVIPFYMGMREAQNSHVYWWRYCIRLENLDSDVVQLRERHWRIFSLSGTLETVRGRGVVGREPVLskeQP 295
Cdd:PRK05461   2 YSAVTYGIEVSVQPRYLEEQSDPEEGRYVFAYTITIENLGRVPVQLLSRHWLITDANGRVQEVRGEGVVGEQPVL---AP 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 588480525 296 --AFQYSSHVSLQASSGHMWGTFRFERPDGSHFDVRIPPFSLES 337
Cdd:PRK05461  79 geSFEYTSGAVLETPSGTMQGHYQMVDEDGERFEVPIPPFRLAV 122
ApaG COG2967
Uncharacterized conserved protein ApaG affecting Mg2+/Co2+ transport [Inorganic ion transport ...
 221-335 1.31e-32

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


Pssm-ID: 442207  Cd Length: 119  Bit Score: 117.89  E-value: 1.31e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480525 221 ENIRVTVIPFYMGMREAQNSHVYWWRYCIRLENLDSDVVQLRERHWRIFSLSGTLETVRGRGVVGREPVLskeQP--AFQ 298
Cdd:COG2967    1 YGIKVSVETEYLPEQSDPEEGRYVFAYTITIENLGDVTVQLLSRHWIITDANGKVQEVEGEGVVGEQPVL---APgeSFE 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 588480525 299 YSSHVSLQASSGHMWGTFRFERPDGSHFDVRIPPFSL 335
Cdd:COG2967   78 YTSGCVLETPVGTMQGSYQMVDEDGERFDVPIPPFSL 114
DUF525 pfam04379
ApaG domain; The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins ...
 239-320 1.08e-30

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: 111.79  E-value: 1.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480525  239 NSHVYWWRYCIRLENLDSDVVQLRERHWRIFSLSGTLETVRGRGVVGREPVLsKEQPAFQYSSHVSLQASSGHMWGTFRF 318
Cdd:pfam04379   7 EEGRYVFAYTIRIENLGDSSVQLLSRHWIITDANGKVEEVRGEGVVGEQPVL-APGESFEYTSGCPLETPSGSMEGSYTM 85


                  ..
gi 588480525  319 ER 320
Cdd:pfam04379  86 VR 87
 
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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