UniProt: B6QT88

Database: UniProt
Entry: B6QT88_TALMQ

LinkDB:  B6QT88_TALMQ 
Original site:  B6QT88_TALMQ

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Ontology (9)   
   GO (9)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (29)   

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ID   B6QT88_TALMQ            Unreviewed;      1655 AA.
AC   B6QT88;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=PMAA_003140 {ECO:0000313|EMBL:EEA19524.1};
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA19524.1, ECO:0000313|Proteomes:UP000001294};
RN   [1] {ECO:0000313|Proteomes:UP000001294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC   {ECO:0000313|Proteomes:UP000001294};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; 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|ARBA:ARBA00001966,
CC         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|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR   EMBL; DS995905; EEA19524.1; -; Genomic_DNA.
DR   RefSeq; XP_002152461.1; XM_002152425.1.
DR   STRING; 441960.B6QT88; -.
DR   VEuPathDB; FungiDB:PMAA_003140; -.
DR   HOGENOM; CLU_000203_3_1_1; -.
DR   OrthoDB; 211439at2759; -.
DR   PhylomeDB; B6QT88; -.
DR   Proteomes; UP000001294; 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   CDD; cd05778; DNA_polB_zeta_exo; 1.
DR   CDD; cd05534; POLBc_zeta; 1.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR   Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR   Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR   Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR042087; DNA_pol_B_thumb.
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; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR45812:SF1; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
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; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|RuleBase:RU000442};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU000442};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000442};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU000442};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442}; Nucleus {ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001294};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          825..986
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          1053..1499
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1551..1625
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
FT   REGION          285..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          536..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..515
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..571
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..607
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1655 AA;  188686 MW;  2C3F66A06EEBAB8F CRC64;
     MDIFRVRLNC IDHYQAVPTE FDPPVPFTNG ASQRTARPKV PVIRAFGATE TGQKVCAHVH
     GAFPYLYIEY RGGLGQDEVN NAIRNLHASI DHALANSYRQ NAYDGRVAYV AHISLVKGVP
     FYGYHVGYRF YLKIYLLNPM NIIRLADLLR QGAVMKTMLQ PYESHLQFIP QWMCDYNLYG
     CAYMDCAKVK FRSPVPEYLE LSNLDHRWHD RTIPPKYITS ETVLPKQSHC TLEVDVCVQD
     ILNRNAIKER PLHHDFIERK HPITAEEKLV QSMAGLWQDE TRRRKKRLGI KDPGSSPFTA
     EELVSMSASP RDQNKAGWIH EEEFRGHLLR VVDEEKKADD TSTISFDDYV KHNTLEDTIQ
     SAIDSVEDLY PQKLEPLMTQ IALADVDNAT RTNAYDTTIF PDGFDVDNEL EAEYSEPEDA
     YDNDDDGLPS SSFQFDDELL DALAEEMNEK DATKRQHDRK KIDQEDFRLG YSGASQFRLS
     KRARTGDLSS SEERLTKRPK NGYVESPKDG SKPKPLDDSF SSFDVAAILQ EAEEDGERIG
     PDDTPPLHPQ NGVDSSQKTV RASQNQRLSF PVVKDPNDPM TILRFSQRNG LSKENSRLSQ
     ASADLDSRES NGLEKSSSEL ALESSGNTVI KLHMGGRMTG VYEAFDIPAN HKALFYGFPC
     PTAAEVKASI QDEGRPAVIY QKPFYSDDND VPERSREYAG RDFRLVSNSI RYLPEFGRQG
     RNIHLFSETL PPILSLDEQR KEDQKLREHS SARIWEFAQL PPSRNEVLEW FENEEKAQEN
     EMTAPRISLP VSKPNVMSQI DGATQKNPYG FKYSQKQQST SVNHQTQYMS VMSLEVHVNT
     REGLAPNPEE DEISVHLGIL AQPADVLVPV AASLSVEIQT EASELDLITS LVDIVRNHDP
     DIITGYEVHN GSWGYLIERA RVKYEYDLCN ELSRVKASAH GRFGKDSDRW GFNNTSSISV
     TGRHMINIWR AMRSELNLLG YTMENVVFHL LHRRIPHYPF KDLTRWFTGS KPRNIMKVVE
     YYLSRVQLDL EILDTNELIP RTSEQARLLG VDFFSVFSRG SQFKVESLMF RIAKPENFIL
     ISPSRKQVGQ QNALECLPLV MEPQSDFYTS PLLVLDFQSL YPSIIIAYNY CYSTFLGRLD
     NWRGRGKMGF TEYKRQERIL ELLKDHVNIA PNGMIYAKPE IRKSLLARML SEILETRVMV
     KSGMKADKDD KTLQQLLNHR QLALKMIANV TYGYTSASFS GRMPCSEIAD SIVQTARETL
     ERAIAFIHSV DRWGAEVVYG DTDSLFISLK GRTRDEAFTI GEEISKAVTK MNPRPVKLKF
     EKVYHPCVLL AKKRYVGFKY EHRDQVEPDF DAKGIETVRR DGTPAEQKIE EKALKILFRT
     ADLSRVKDYF QKQCLKIMQG RVSVQDFCFA REVRLGTYSE NGTLPAGALI STKKMLEDPR
     LEPQYGERVP YVVVTGAPGA RLIDRCVAPG VLLNNAHLEL DAEYYITKNL IPPLERIFNL
     VGANVRQWYD EMPKIQRIRR IEGAFTGLGG GNNNAAISKK TLESYMKSST CLICKDKLQD
     NNNDLPLCNS CASLPHISLF KLTSQLQQAE RRTSNLHKIC RSCMGVPFGD EVSCDSKDCP
     VFYSRTREMS NWKSSNSVLE PVIRELERRD ERLDW
//

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