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Database: UniProt
Entry: A0A2H2ZNW4_9HYPO
LinkDB: A0A2H2ZNW4_9HYPO
Original site: A0A2H2ZNW4_9HYPO 
ID   A0A2H2ZNW4_9HYPO        Unreviewed;      1481 AA.
AC   A0A2H2ZNW4;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   05-JUN-2019, entry version 9.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=A9Z42_0000970 {ECO:0000313|EMBL:OTA08409.1};
OS   Trichoderma parareesei.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae;
OC   Trichoderma.
OX   NCBI_TaxID=858221 {ECO:0000313|EMBL:OTA08409.1, ECO:0000313|Proteomes:UP000219286};
RN   [1] {ECO:0000313|EMBL:OTA08409.1, ECO:0000313|Proteomes:UP000219286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 125925 {ECO:0000313|EMBL:OTA08409.1};
RX   PubMed=26272569;
RA   Yang D., Pomraning K., Kopchinskiy A., Karimi Aghcheh R.,
RA   Atanasova L., Chenthamara K., Baker S.E., Zhang R., Shen Q.,
RA   Freitag M., Kubicek C.P., Druzhinina I.S.;
RT   "Genome Sequence and Annotation of Trichoderma parareesei, the
RT   Ancestor of the Cellulase Producer Trichoderma reesei.";
RL   Genome Announc. 3:e00885-15(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OTA08409.1}.
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DR   EMBL; LFMI01000847; OTA08409.1; -; Genomic_DNA.
DR   Proteomes; UP000219286; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; IEA:InterPro.
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   GO; GO:0019985; P:translesion synthesis; IEA:InterPro.
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; IPR030559; PolZ_Rev3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   PANTHER; PTHR45812; PTHR45812; 2.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 2.
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:UP000219286};
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   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN       49    190       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      639    822       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      890   1335       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1376   1449       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION      426    460       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A2H2ZNW4}.
FT   REGION      608    633       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A2H2ZNW4}.
FT   COILED     1403   1423       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    615    633       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A2H2ZNW4}.
SQ   SEQUENCE   1481 AA;  169503 MW;  FB7ECE867A78793D CRC64;
     MVLFRVRLNC IDHYQALPSR HDPQLRNDLQ APLLNATRVP VIRIFGSTEF GQKVCAHVHG
     VFPYLYVEYD GDLNQDAVGA FIYRLHLSID HALAISYRRD QDGDKAKFVA RITLVKGVPF
     YGYTVGYKPF LKIYMFNPLV MTRLADLLQQ GVIMKRKFQP YEAHLQYLLQ FMVDYNLYGC
     DYVESSQTFF RSPVPPRHEG DAASSQLWDE GTVPVGFITD DLALPRESYC SIEVDILAEN
     IINREKVKER LLHQDFSEFL KPPSEDTKLV SSMAGLWKAE ARRRQRQLPP GQTPAQHLVS
     SFPREALVSM SADSRSSEPQ AWMHEEDYRR KVENLISKEQ EQFHDSGLSL GTFLKPLPHE
     SSIKTSLQSV EDLHPSNLSA ALGLSLISAR PNEDPSSNIE VDEQKLQMSQ SDEDAWLAIN
     ADGSDFEQES RKEHSVPSLE NIDTGPPKPT MAQPTRDPEA GRLDARFVGI GESGLLTGRI
     PRLPLLSIER GCPDVIYQDA FYSEEADVPL RRREYAGREF HLISNTLPFL PDFDPTGNAA
     PAGISHDSDM SLSREADMWQ NEQRLKEHCS WRGWEIVRSP PSCDEVARWM VQNATDVRRA
     KPRLTRPWLS QIDGPTPRTK HNFKYSQRQP SSAVPHEAQY MSTMSLEIHV NTRGNFVPNP
     EEDEIQCIFW HWKDDEATSS ATPELPGSSG SGVLVQSVDS VLAERIRSLV PDEVAEESSE
     LDLLNRMVEI VRFYDPDILT GYEVHGSSWG YLIERARLKY DYDLCSEFSR MKTQSNGRFG
     KENDQWGFNT TSSIRVTGRH MINIWRAMRG EVNLLQYTME NVVWHLLHRR IPHYPWRCLT
     SWHRSGKLQD VVRLVRYYRT RTRLDLEILE SNELISRTSE QARLLGVDFF SVFSRGSQFK
     VESIMFRIAK PENFMLVSPS RKQVGQQNAL ECLPLVMEPQ SAFYSSPLVV LDFQSLYPSI
     MIAYNYCYST FLGRIPDWRG KSKMGFAEYR RQDGLLSLLA KHINIAPNGM MYAKAEVRKS
     LLAKMLTEIL ETRIMVKSGM KQDREDKTLQ RLLNNRQLAL KLLANVTYGY TSASFSGRMP
     CSEIADSIVQ TGRETLERAT AYIHSVERWG AEVVYGDTDS LFVYLKGRSR DEAFVIGQEI
     AQVITERNPK PVKLKFEKVY HPCVLLAKKR YVGYKYESKD QVKPDFDAKG IETVRRDGTP
     AEQKIEEKAL RLLFETADLS QVKDYFQEQC RKVMGGRVSI QDFCFAKEVR LGSYSEHGLP
     PAGAMISARK MLQDSRAEPQ YGERVPYVVV TGAPGARLID RCVSPEELLR NPHWQLDADY
     YITKNLIPPL ERIFNLVGAN VRQWYEAMPK IRRIQRTKGH GHKKRTLEAY MQSINCLVCG
     RKVVSSAEMS LCSFCFAKVP DSLLALQSKL VAVERKYDEI RRICQSCEGL GPLEEVACDS
     HDCPVFWTRT RLRSKMHHEQ VVTEPLINEL HARMEGVSLD W
//
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