UniProt: A0A135SH03

Database: UniProt
Entry: A0A135SH03_9PEZI

LinkDB:  A0A135SH03_9PEZI 
Original site:  A0A135SH03_9PEZI

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Ontology (10)   
   GO (10)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
All databases (28)   

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ID   A0A135SH03_9PEZI        Unreviewed;      1716 AA.
AC   A0A135SH03;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=CNYM01_08112 {ECO:0000313|EMBL:KXH35067.1};
OS   Colletotrichum nymphaeae SA-01.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH35067.1, ECO:0000313|Proteomes:UP000070054};
RN   [1] {ECO:0000313|EMBL:KXH35067.1, ECO:0000313|Proteomes:UP000070054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA-01 {ECO:0000313|EMBL:KXH35067.1,
RC   ECO:0000313|Proteomes:UP000070054};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL   Submitted (FEB-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-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:KXH35067.1}.
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DR   EMBL; JEMN01001513; KXH35067.1; -; Genomic_DNA.
DR   Proteomes; UP000070054; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442}; Nucleus {ECO:0000256|RuleBase:RU000442};
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          871..1053
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          1120..1566
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1613..1684
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
FT   REGION          428..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          833..863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..543
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..651
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1716 AA;  193056 MW;  4E72C1B2A0802F8D CRC64;
     MDLFRVRLNC IDHYQATPTH YDPQLRNDVG PAQAKKGPKV PVVRVFGSTE TGQKVCAHIH
     GAFPYVYVEY RGSLEPEDVG AYIYRLHLSI DHALAVSYRR DQFGENAKFV ARITLVKGVP
     FYGFHVGYRF FLKIYMFNPI VMTRLSDLLQ QGVILKQKFQ PYEAHLQYLL QFMTDYNLYG
     CGYLDVSDVY FRGPIPSFDQ EGNSQHLWHD RTIPKTRVLD DLTLPRVSHC SIEVDICVQH
     ITNRRLVKER QLHHDFVERA KPLPADIKLV YSMAGLWKDE TRRRKMKMPN ADPGSSPFPA
     EVLVSMSANK RDSQPQGWIH EEEYKEEVAK LIETEKGLED SAPPSFENFV ERSPLEAAVK
     TALQSVEDLY PANLLPALGL PSNHAPANKN PASSIEVDEQ GVLDLGVDDY DPYPADSDEE
     ALIQMGEPKA RQDDQINSTG IKGKPLVASG TGSRSQPVAG DLTVRKTVNG LGSIYEGVCA
     SRLKTGNPPT VPVWDDLLDV AEEEGLVSKL SDPSSLGHRR TESVKRSISP HAIASSTKRS
     RTEPPVAPAS DAVVPKPSLK GILSNSTASE KHQVTMLPPN SQDKPRSSQN AGSKSAANQL
     LGFPVVKSQE DPGTKLRLSQ MNPPRASQQA EKDSPKHVSF NVASEETRSK PSPVTPAKKV
     RIATPTTDSL GTEAGTETIL HRIQTAIGSF SAKRQCVIGV LPPAPKLIMS TMKDLQIPDM
     IYQDAYYSEE KDVPARPREY AGREFRLESN TLPYLAEFDP TGTSAASMGI KSDTPIDKAK
     NDVRYDAQAS LCSYRSWEIA QPPPSAKEVQ DWWNKKHPLQ KAQKNVTAKI TGTPQATRRD
     LSQIDGPTPK NKHGFKYSPK KKSTSVKHEA QYMSTMALEV HVNTRGKFVP NPDEDEVQCI
     FWSIKADGTA SSSQEASGGI IAGVVVLSPD GSLAQRMRRY VSAEVIEESS ELDVMVRMVQ
     IVRDHDPDIL TGYEVHGSSW GYLIERARVK YDYDLCDEFS RMKSNSHGRI GKENDRWGFN
     TTSTIRVTGR HMINIWRAMR GELNLLQYTM ENVVWHVLHR RIPHYSWRTL TQWYNSSRQR
     DLDKLTRYYL TRTRIDIQIL ESNELIPRTS EQARLLGVDF FSVFSRGSQF KVESIMFRIA
     KPENFMLVSP SRKQVGGQNA LECLPLVMEP QSDFYNSPLL VLDFQSLYPS VMIAYNLCYS
     TFLGRIVNWR GMNKMGFTEY QRHKRLLELL KDHINITPNG MMYVRPEIRK SLLAKMLGEI
     LETRVMVKSG MKQDKDDKTL QALLNNRQLA LKLLANVTYG YTSASFSGRM PCSEIADSIV
     QTGRETLERA IAFIHSQEQW GAEVVYGDTD SLFVYLKGRT RDQAFDIGNE IAKAITDMNP
     RPVKLKFEKV YHPCVLLAKK RYVGYKYESK DQVTPEFDAK GIETVRRDGT PAEQKIEEKA
     LKLLFETANL SEVKAYFQKQ CEKIMRGSVS VQDFCYAREV KLGTYSDKGP PPPGALISTK
     KMLEDARAEP QYGERVPYVV ITGAPGARLI DRCVAPEDLL NDSHSQLDAE YYISKNLIPP
     LERIFNLVGA NVRQWYDEMP KVQRIRRVDQ TLGAAGGLGS KKTLESYLKS ASCISCNIKM
     HVEGVLCGRC QQDAPSSLFN LQTRLKDEER KYMDVLRVCR SCSALPAADE VPCDSKDCPV
     FYSRVKQSAR LKTEKSALEP VIRELVAKAG RAALEW
//

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