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Database: UniProt
Entry: A0A0B7MXF1_9FUNG
LinkDB: A0A0B7MXF1_9FUNG
Original site: A0A0B7MXF1_9FUNG 
ID   A0A0B7MXF1_9FUNG        Unreviewed;      1143 AA.
AC   A0A0B7MXF1;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   05-JUN-2019, entry version 25.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   Name=PARPA_03356.1 scaffold 7264 {ECO:0000313|EMBL:CEP09802.1};
OS   Parasitella parasitica.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX   NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP09802.1, ECO:0000313|Proteomes:UP000054107};
RN   [1] {ECO:0000313|EMBL:CEP09802.1, ECO:0000313|Proteomes:UP000054107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP09802.1,
RC   ECO:0000313|Proteomes:UP000054107};
RA   Ellenberger Sabrina;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000256|RuleBase:RU000442};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU000442};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000442}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|RuleBase:RU000442}.
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DR   EMBL; LN722203; CEP09802.1; -; Genomic_DNA.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000054107; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR042087; DNA_pol_B_C.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   Pfam; PF14260; zf-C4pol; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|RuleBase:RU000442};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054107};
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU000442};
KW   Iron {ECO:0000256|RuleBase:RU000442};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU000442};
KW   Metal-binding {ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU000442};
KW   Nucleus {ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN      107    445       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      509    940       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN      977   1049       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION        1     40       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0B7MXF1}.
FT   COILED     1049   1069       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS      1     21       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0B7MXF1}.
SQ   SEQUENCE   1143 AA;  129433 MW;  E9754B251F887E4F CRC64;
     MTSLQSDKDI MLSSQPFEPG STIKKRKTAH TTSKEGANGT NFEQELKSLN DDMDVDIKIE
     NTEATWGRSA APALDPAKDK LVFQQIEIDE YMDWKAQQPV VRFYGVTTNG NSVVCHVRDF
     LPYFYFPAPY GFQHRHLPAL KQSLSSAIGQ PGAVFDVSIL MKQSIYGYHG DSKSPYIRVT
     VKDPRDISKC KNKVEQGLYV SDFDRPCQSD TTFESNLSYV LRFMIDCKVP GSNWIELPAG
     TWSFINEPTS LAQYEVQTRY DKFISHPPEG EWSDMAPLRV LSFDIECAGR KGIFPEANVD
     PVIQIASVVQ VQGQKKPFIR NVFTLNTCAH IVGSQVLSFD DEKDLLQKWS DFIRVVDPDV
     VIGYNTTNFD FPYLLDRAKH LGVTKFPFLG RIKGVHTDAK DTKFTSKAYG TRENKAINLE
     GRLQLDMLQA IQRDYKLRSY TLNSVSAEFL GEQKEDVHHS IITELQNGNE ETRRRLAVYC
     LKDAFLPLRL MDKLMLLFNY TEMARVTGVP FNYILVRGQQ IKVISQLYRR ALEEDLVIPV
     IKSEMSDEAY EGATVIEPER GYYDVPITTL DFTSLYPSIM QAHNLCYTTL LNPEIVKNLN
     LVKDVDYEVT PNSDMFVKAS RRKGLLPAIL SDLLAARKRA KNDLKKETDP FKRAVLDGRQ
     LALKISANSV YGFTGATVGK LPCLQISSSV TAYGRVMILK TKETVEEHFT VKNGYKHDAK
     VIYGDTDSVM IKFGVDNLKE AMALGKEGAS LVTTKFIRPI NLDFEKVYFP YLLINKKRYA
     GLYWTREDKY DKLDAKGIET VRRDNCRLVQ NIISKCLDKL LIERDVAGAQ AFVKQTISDL
     LQNKVDLSQL VITKALSKSD YANKQAHVEL AERMKKRDAG SAPALGDRVA YVIIKASNNT
     PAYERSEDPL YVLDNNIPID TKYYLENQLS KPLLRIFEPI LGDKAESLLS GAHTRTVNIS
     TPTIGGLMRF AVKTATCLGC KAPLPKGDTS AACKQCSDRL PELYQHQLDT VNKLEVKFSR
     LWTQCQRCQE SLHQDVICSN NDCPIFYMRK KAQKDMDEAS ERLDRFDYEC TRPQRILHLA
     TQKRSTSIST PTTPNRKQQR VINALMQHYT IDVATANMFY VEIVCSGAIR ANTYTALLVQ
     ISS
//
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