ID A0A175VZQ5_9PEZI Unreviewed; 1743 AA.
AC A0A175VZQ5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-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=MMYC01_208327 {ECO:0000313|EMBL:KXX76254.1};
OS Madurella mycetomatis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX76254.1, ECO:0000313|Proteomes:UP000078237};
RN [1] {ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA van de Sande W.W.J.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KXX76254.1, ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA Van De Sande W.;
RT "Madurella mycetomatis genome sequencing.";
RL Submitted (JAN-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:KXX76254.1}.
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DR EMBL; LCTW02000220; KXX76254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175VZQ5; -.
DR STRING; 100816.A0A175VZQ5; -.
DR VEuPathDB; FungiDB:MMYC01_208327; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000078237; 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; 2.
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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000078237};
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 864..1050
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 1117..1459
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1477..1543
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1593..1693
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 426..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1743 AA; 196236 MW; 8384BD6DDB8BBF28 CRC64;
MDVFRVRLNC IDHYQATPTR YDPQLRKDVH PSQAARQPKV PVIRVFGSTE TGQKVCAHIH
GAFPYLYVEY RGPLDRATVS EYILRFHLSV DHALAVSFRK EDKRQSYVAR VTLVKGIPFY
GFYVGYRFYL KIYMLNPLFM TRLADLLLQG LIMGRKFQPY EAHLQYLLQF MTDYNLYGCD
YIEAGKVKFR APVPDPAGPE DPPRIWDSNT IQPEAITADS SLPRVSYCSI EVDICVQDIL
NRKAVQERRL HHDFIERESP IPPGLKLVHS MAGLWADETK RRKKRMGKST GGSPFTEEAL
VSMSADPRDS QPPGWIHEAE YREQIQRLIE LESEQDNSEF TFSNYVEPEP FEETVQTAIE
SVEDLFPEKL LPALGLERRL LQGHQDVASS IQVDEKGIIE FEAAPKDKRL FPDDDPDEDI
VEEGQAAVEA GRSDKDKKSG DSGRTAAGND MLVGNTSQSM ERDSDAQQQK IIADLKWTVG
GLTGGIAISG LRSGKRPCIL LSSQLVDEAM VWELASRDDD PDSSQTVRPG DLKRFTSDLG
NNEPHKRPRF DSQDQTCPPS PDKPVFPAKD SRVSTRSGGF EPKGTPSGRS QSSQSSRPAL
KGASAKSFRN RTLNFPVVKD PSDPNTTLRL SQQGASQGSE DGIAKKQVSF GPPVSISEIS
TGNSPSLSSM SSSNPYTALP APRLHWSGSV TMFLINNTPP STAEVCSTMQ SYGLPDVIYQ
DAFYSNDKDV PPRVREYAGR EYRLEGNTVP YLPDFDATGQ SPAAFGLKPE LGRDSSEMEA
GFEKQQSRCI LRSWEIAEPT PTFSEVNRWW AEKQKKKTPD HSGSTRPRSL TQAGRPELSQ
IAGATPKNTH GFKYSQKQKS TSVQHEAQYM STMSLEIHVN SRGQLVPNPE EDEVQCIFWC
LRSDEQCLYG SQAPDRTMSG IVVLSEDGSL AKKIRSQISV SVVEESSELD VMVRMVEIVR
THDPDILTGY EVHGSSWGYL IERAMRKYEY DLCNEFSRMK AESHGKSGKE ADRWGFNTTS
MIHVTGRHMI NVWRAMRGEL SLLQYSMENV VWHLLHRRIP HYSWQTLTNW YRSGRPGDLG
KLLRYYLKRT RMDIEILEAN ELIPRTSEQA RLLGVDFFSV FSRGSQFKVE SIMFRIAKPE
NFIFTSPSRK QVGAQNALEC LPLVMEPQSA FYPSPLLVLD FQSLYPSVMI AYNYCYSTFL
GRIVDWRGTN KMGFTEFKRR NGLLKLLKDH INIAPNGMMY TKAEIRKSLL AKMLTEILET
RVMVKSGMKQ DKDDRTLQKL LNNRQLALKL LANVTYGYTS ASFSGRMPCS EIADSIVQTG
RETLERAIAY IHSVERWGAE VVYGDTDSLF VYLKGRTREQ AFEIGAEIAK EVTDMNPRPV
KLKFEKVYHP CVLLAKKRYV GYKYESRDQT VPEFDAKGIE TVRRDGTPAE QKIEEKALKI
LFDTADLSQV KEYFQSQCSK IMLARGPDRR GRLISTKRML EDARAEPQYG ERVPYVVITG
APGARLIDRC VAPEDLLDSP HASLDAEYYI SKNIIPPLER IFNLVGANVR AWYDEMPKVQ
HVRRLDTSSA FSALDSNGNK KKTLEWFMNS TACIACSVKM SKPTTTTTTA TTTTTTTTTS
RRNITDRLSL CGRCAADPAA TMVLLQARLN VEQRGYADVV GVCQSCAGFA PLEAEAEAGV
PCDSKDCPVF YTRVKQRARM RAERAAVEPV VRRLGEMVAM MALAEEGKGK GNGKGKRREG
LDW
//
