UniProt: A0A1E3IHE0

Database: UniProt
Entry: A0A1E3IHE0_9TREE

LinkDB:  A0A1E3IHE0_9TREE 
Original site:  A0A1E3IHE0_9TREE

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Ontology (9)   
   GO (9)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
All databases (27)   

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ID   A0A1E3IHE0_9TREE        Unreviewed;      1986 AA.
AC   A0A1E3IHE0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=L203_03152 {ECO:0000313|EMBL:ODN87948.1};
OS   Cryptococcus depauperatus CBS 7841.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus.
OX   NCBI_TaxID=1295531 {ECO:0000313|EMBL:ODN87948.1, ECO:0000313|Proteomes:UP000094043};
RN   [1] {ECO:0000313|EMBL:ODN87948.1, ECO:0000313|Proteomes:UP000094043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 7841 {ECO:0000313|EMBL:ODN87948.1,
RC   ECO:0000313|Proteomes:UP000094043};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (JUN-2016) 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-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ODN87948.1}.
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DR   EMBL; AWGK01000012; ODN87948.1; -; Genomic_DNA.
DR   STRING; 1295531.A0A1E3IHE0; -.
DR   VEuPathDB; FungiDB:L203_03152; -.
DR   OrthoDB; 211439at2759; -.
DR   Proteomes; UP000094043; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000094043};
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          1123..1311
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          1377..1823
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1881..1950
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          460..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          631..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          904..923
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1953..1980
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        471..490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..663
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..919
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1986 AA;  224401 MW;  A939445DB3980370 CRC64;
     MDNNPLRGPA EPLSSLLSDT SNPPSISNPL LRLRITHITS DQAAPIPTLR QYYSPSRFAT
     AIPPGCLPQN VAIIRVFGTT TSFQKVCVNT HLCYPYFYVP FPMDDEDPLR PERVVNLCQR
     FAVSLNHAIC LALRQDPLSA GNKANYSGGV DPRHLHVMSV MLVKGIPFYG YHLGYNYFLK
     VNLANPARLH IALEQLRKPN VLGREWQPHE AHLNHVLQFM CDFDIYGCGW LELGGGIFRD
     PVPEGNPHIP SPESSRDGQL SALDSLTIPA SMLYPPGLSP PKESFTALEI DVLPHQLLNR
     QRLVPRLLHH DFIELFHKPL DPNEKFVPAV AELWEDERRR RELRGLSTGT DSMMPESLRI
     DRMAMRELGH KVQKEGLDIK EESINIGGNW KISEELWGMI EERMIDEKKK KGPLTLEKFI
     QSARRGKNGE KAEWDKWIMT TFDAISAHWP KQPHKFKAKE LTEKSVSLRS PRTVEETSSP
     MNPAASSGID HSFSQPGVLD RELQFTTQWK HLTNTRPFED FEAEEETKNP FETCAMTQAS
     QNFKPNPELS THVQPANEEQ AYDYDQYYLD EREDDSDEKR HLEEAKLHAE QTNKIRATQI
     PARQDTGDDE MYDDEELEEL FRQTIAAGLG VSSLPSTPKK SNTFERCAGW TPTKRSGSTN
     GSSFHSRKRK RDQELLEKAG LGDLSDIIDH STISISPFNN SYNERLQPIT TPTKSKTPVS
     EKATPSSLIR NAFTRSHQVL PTKSPGGKSS KIKYDSAETI MLPLPKRTRS SIQTSFSSLV
     DKRNNLNTQG GVQQKLKDEA IRAAAEPGQQ ASGEAKNLSL NIGTDQKKVH LSLPAAGAGL
     YEPTSRMEKD NQSVLPLSTM LLKETNRSGA NSRAALPGTR FAMSATFPMN VVSDPTLSPT
     LQYNRPPPTL QQATSSKKSI DGDKLQHKRI RLAEQELISA SQVPLLPFAD YHRVRTFGDG
     NTGNEMAADT TPISLSWQYR DLPPLLEVVA NTMEQKGVAS VVYQVPFYSD PADVPPKGKI
     LTGKMFNFKS NKSVELLDFE AYVGDKKLSK NTSMENVGIR QLRSDYYQST TAYKFGWEYS
     PMPPSMACVR HWCAKTNMEA RLACKLQLAN ATQKNKYGFK FSQKKKVRNV NELQAMTVLT
     LEVFAQSRGH LLPDPEKDAI TAIFYCFQSH DDSLQDTTVH PGYHAGYVVV GALANAARLC
     LEGIPFEVVE DELELVNWVI DTVKYWDPDI LAGWEIHNSS WGYLSLRAYE LFAMDFANEM
     SRVLSGRSDP KNDGYLAHHS SNFKVVGRHT LNIWRICRSE VNLAQYTFEN VVFHFLHQRI
     PYYPTVSLTA LWKSKTPEHA TRVLKYFFQR VVLCMEIIDK AEIIVKTAEF ARVFGVDFAS
     VMTRGSQYKV ESFLARIAKP ESFVFVTPSK QQVGLQNAPF AVPLIAEPES KYYTDPVIVL
     DFQSLYPSII IAYNICYSTC LGRVEKFKGT DKFGFTELKV ASGLLELLKD YLIVTPNGMI
     FVKPAVRKSL LAKMLTEILD TRVMIKSAMK EAKDDKFLTS MLNARQLGLK LMANVTYGYT
     SATYSGRMPC IEIADSIVQT GRETLEKAQE MIHSRREWNA RVVYGDTDSL FVVLPGRTKE
     QAFKIGHTIA DTVTAMNPKP VKLKFEKVYM GSVLMAKKRY VGFKYENPDE TTPVFDAKGI
     ETVRRDGFAA QQMMEEVCLK ILFRTQDLSQ IKEYCRQEWK KILDGRISIQ DFIVAKEVRL
     GTYSEKGVPP PGAAVAYRRI LKDPRDEPQY AERVPYLISN ADGRRLIDRA RQPEELLSNR
     YLNIDAEYYI RNLLIPPLAR IFNLVGADVE EWYDSMPRTK RAGKYGRVVK YGKNKDRTTG
     VKDKHKATKS KIDSHFNSSH CMLCGTECQK LLCSECLSDP SVASHTLLFR QQIAQSKMVS
     LQRICASCCG TLPGEKILCS SIDCPLTYAR SAAQRDLEDL EEIDDQIRRL SEANGEEIER
     WQDESI
//

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