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Database: UniProt
Entry: A0A3Q2GGJ6_CYPVA
LinkDB: A0A3Q2GGJ6_CYPVA
Original site: A0A3Q2GGJ6_CYPVA 
ID   A0A3Q2GGJ6_CYPVA        Unreviewed;       845 AA.
AC   A0A3Q2GGJ6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=PMS1 homolog 1, mismatch repair system component {ECO:0000313|Ensembl:ENSCVAP00000025380.1};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000025380.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000025380.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC       {ECO:0000256|ARBA:ARBA00006082}.
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DR   AlphaFoldDB; A0A3Q2GGJ6; -.
DR   STRING; 28743.ENSCVAP00000025380; -.
DR   Ensembl; ENSCVAT00000001762.1; ENSCVAP00000025380.1; ENSCVAG00000010271.1.
DR   GeneTree; ENSGT00940000157085; -.
DR   Proteomes; UP000265020; Unplaced.
DR   GO; GO:0032300; C:mismatch repair complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR   CDD; cd16926; HATPase_MutL-MLH-PMS-like; 1.
DR   CDD; cd03485; MutL_Trans_hPMS_1_like; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR014762; DNA_mismatch_repair_CS.
DR   InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR002099; MutL/Mlh/PMS.
DR   InterPro; IPR038973; MutL/Mlh/Pms-like.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00585; mutl; 1.
DR   PANTHER; PTHR10073; DNA MISMATCH REPAIR PROTEIN MLH, PMS, MUTL; 1.
DR   PANTHER; PTHR10073:SF54; PMS1 PROTEIN HOMOLOG 1; 1.
DR   Pfam; PF01119; DNA_mis_repair; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM01340; DNA_mis_repair; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00267}; Reference proteome {ECO:0000313|Proteomes:UP000265020}.
FT   DOMAIN          482..550
FT                   /note="HMG box"
FT                   /evidence="ECO:0000259|PROSITE:PS50118"
FT   DNA_BIND        482..550
FT                   /note="HMG box"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT   REGION          307..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..418
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..547
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   845 AA;  93040 MW;  79905925E61D9C37 CRC64;
     ALFAVLKENF GLERTEVRDN GCGIKAADAP VMAVRHFTSK ICSHEDLERL ESYGFRGEAL
     GSICAVAEVS VTTKTQEDDI STQYTLDHTG RVVSQRPSHL GQGTSVSVTK LFKNLPVRRQ
     FYSSTKKCKE ELKKVQDLLM AYALIKPELR LMLVHNKAVL WQKARAADLR SALVATLGSG
     AVANLLPCHQ EQPEMVLDGF LPKPGADLSS TSCSASEKTF IFINRRPVQQ KEIMKLLRQH
     YCAQYAEDAA RHRFPILLLS ISVSPSSLDV NLTPDKTQVL LDNKEAVLTA LEALLVSLYG
     FRSSSAEQQL NHEAPPPPSA RSEAKEDQNI RVHEDAPTAE PKHGGGADPQ AALQRQASSC
     SSSSSTADDW IINPPPSELC SVSSLCGDET AAARPKPEQT GSEPEKPEEE RETRKISAQD
     WSRGTALTDP VTGDPLRPVL VHRPSGPGSP GPQEARSKKL INSVTEKGAT LTAYDMISSR
     AMRAPPSPAS LFEKEARSEV LRERPAASLQ EVSAAVQERW RNLREEDRKT YEEKAKKKHD
     LHEQRTKLAS DGGPQGPTER AKAQSVKRKA PPSNQQLLDE LFSAQPQKKT KTPPPKPSRP
     LLCSMAALRL GLQRLSSQSS APPRGLRLVN RLGSQSCWAV MAGRRLLLFN PYRVEEALLF
     KRLQENHVLP AAVLQNPLRL TDGNLGGAEF ETLCSMKKGA AELDGSVFFS DPRLLANGFR
     VRLPAGLPSA EKHLEVAAMA DCVPFLGVED LREVLSAVLH RKASRPQDCR PLKVTNYLKA
     EAVRLARQLP SSLRRGDVEE LVGRMERRLG GTERTCIHGR RFFHHLVDVP STDEEAEALL
     RPLEL
//
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