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Database: UniProt
Entry: A0A0A2L598_PENIT
LinkDB: A0A0A2L598_PENIT
Original site: A0A0A2L598_PENIT 
ID   A0A0A2L598_PENIT        Unreviewed;      1699 AA.
AC   A0A0A2L598;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   05-JUN-2019, entry version 22.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=PITC_001360 {ECO:0000313|EMBL:KGO75272.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO75272.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO75272.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO75272.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L.,
RA   Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium
RT   expansum provide new insights into secondary metabolism and
RT   pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(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:KGO75272.1}.
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DR   EMBL; JQGA01000480; KGO75272.1; -; Genomic_DNA.
DR   EnsemblFungi; KGO75272; KGO75272; PITC_001360.
DR   OrthoDB; 20210at2759; -.
DR   PhylomeDB; A0A0A2L598; -.
DR   Proteomes; UP000030104; 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; 1.
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   Complete proteome {ECO:0000313|Proteomes:UP000030104};
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:UP000030104};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442,
KW   ECO:0000313|EMBL:KGO75272.1}.
FT   DOMAIN       49    191       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      840   1032       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN     1098   1545       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1596   1668       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION      332    354       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0A2L598}.
FT   REGION      476    585       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0A2L598}.
FT   REGION      602    621       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0A2L598}.
FT   REGION      627    650       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0A2L598}.
FT   REGION      803    830       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0A2L598}.
FT   COMPBIAS    476    499       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0A2L598}.
FT   COMPBIAS    500    522       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0A2L598}.
FT   COMPBIAS    533    556       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0A2L598}.
FT   COMPBIAS    557    571       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0A2L598}.
FT   COMPBIAS    627    646       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0A2L598}.
SQ   SEQUENCE   1699 AA;  193038 MW;  75B7D4B0BCDB9CDB CRC64;
     MESFRVRLNY IDHYQATASE LDPPLPFRDE VSEKDFKPKV PVIRIFGATE TGQRVCVHVH
     GAFPYLYIEY NGSLAPEDVN SAIRTLHLSI DHALAVSFRR NAYDRRTAFV AHITLVKGVP
     FYGYHVGWRF FFKIYLLNPF HTTRLVDLLH QGAVMKRPLQ PYEAHVQYIP QWMCDYNLYG
     CATMRCSQVK FRAPVPDYFE LSNLAHRWHD RSIPPESILD HPALQKQSYC ALEVDVCVQD
     ILNRLDVKER PLHQDFTELL KPVAVNERLV PSMAGLWQDE TRRRKMRMGI TDPGGTPFGP
     EELVSMSADP RNQSRGGWIH EEEFREMASQ LAANEKHEDH KKDTTFGTFL DPDDHAKNVK
     TALDSVEDFF PDKISTLTFD SSRSQESAEQ NPPEISVDED LALSSQANGQ YYSDSDQGGD
     SSGGRIEQEL ETKQDALGDS FYDEVFDEMP FSDMAALAEP AEINNPEATK HGVYKEGNSV
     TQQKRPRDQS QSKSVAPKRN LENLDSHHSP TKRPRHVEKN GLSDGSLESP NTLKRQQDDK
     RKSVSFDSKL DTHAENPSSE PKSSSSQKTV RPKAHSHTRV LKFPVVKDPN DPLTILRYSQ
     DEACSSRKDP ESSQPFLSSF SSGSTVELSG KTCEPQSSSE LHSSATVMGP ASIDPHLAET
     MKKIHQSFNF TRNTSLHCFK FASPTCSEVS STINEHGRPS VVYQKAFYSD ETDVPERPRE
     YGGREFRLES NTIHYLPDFD PTAEAPAMFG EQIPTTHDRD QQEKVDQQLR EGCTARVWEF
     APVPPSRSEV TQWLEELEAS QVSKQKAAQT KPAETKPDFL SQIEGPTQKN AHGFKYSQKG
     VSTSVEHQAQ HMSTMSLEVH VNTRGTLMPN PEEDEITSLF WCIQSEDEDV EVNSHLPGVH
     VGMVYCGEGE RPEAKISKAL TIDVECEPSE LDLINRLIDI VRQYDPDIIT GYEVHNASWG
     YVIERARKKY DFDICEELSR TKSQSNGRFG KEADSWGFNH SSSVRITGRH MFNIWRAMKG
     ELNLLQYTME NVVFHVLHRR IPHYSPKDLT QWHQSGKPRN LLKVVEYFSS RVQMNLEILE
     ANELVPRTSE QARLLGIDFA SVVSRGSQFK VESLMFRIAK PENFLLVSPS RKQVGQQNAL
     ECLPLVLEPQ SDFYTSPLLV LDFQSLYPSV MIAYNYCYST FLGRAMHWRG RDKMGFMDYK
     RQPRLLELLK DKINISPNGM MYAKQEVRQS LLAKMLSEIL ETRVMVKNGM KADKDDKVLQ
     RLLNNRQLAL KLIANVTYGY TSASFSGRMP CSEIADSIVQ TGRETLEKAI AFIHSIERWG
     AEVVYGDTDS IFVYLKGRTR DQAFDIGEEI AQAVTDLNPR PIKLKFEKVY HPCILLAKKR
     YVGFKYEDRN QKEPEFDAKG IETVRRDGTP AEQKIEEKAL KTLFRTADLS QVKSYFQRQC
     AKIVQGRISI QDFCFAREVR LGTYAERSSL PAGAMISTKR MMEDPRSEPQ TGERVPYVVV
     TGAPGARLID RCVAPQTLLH DAQLEIDAEY YITKNLIPPL ERIFNLVGAN VRQWYDEMPK
     VQRIRRVEGS ALARPNSRAG GVTRKTLESY MRSSSCVVCR ARLSDAAVLV CGDCLQKPHI
     TLLDVVSRLQ RAEKRVVDLE AICRSCMGVS PGDEVSCDSL DCPVFYSRTR DAANWRHSRA
     VLEPVVELLE QKGDEGLDW
//
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