ID Q8X1U8_NEUCS Unreviewed; 1926 AA.
AC Q8X1U8;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN Name=UPR1 {ECO:0000313|EMBL:BAB83627.1};
OS Neurospora crassa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=5141 {ECO:0000313|EMBL:BAB83627.1};
RN [1] {ECO:0000313|EMBL:BAB83627.1}
RP NUCLEOTIDE SEQUENCE.
RA Sakai W., Ishii C., Inoue H.;
RT "The upr-1 gene encodes a catalytic subunit of the DNA polymerase zeta
RT which is involved in damage-induced mutagenesis in Neurospora crassa.";
RL Submitted (JAN-2002) 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}.
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DR EMBL; AB077040; BAB83627.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:NCU01951; -.
DR HOGENOM; CLU_000203_3_1_1; -.
DR PhylomeDB; Q8X1U8; -.
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 924..1109
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 1176..1625
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1754..1817
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 464..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..738
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 COMPBIAS 480..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1926 AA; 218733 MW; 0D67C43E9F629E4A CRC64;
MEFLRLRLNC IDHYQATPTR YDPQFDQDVR FSRSRKAAKV PVIRVFGSTD KGQKVCAHIH
GAFPYLYVEY DGNLEPNKDH ALAISYRKDP IRDRPKYVAR ISLTKGIPFY GFHVGYRFYL
KIYLFNPVVM SRLVDLLQQG VIMSRKFQPY EAHLQYLLQF MADYNLYGCN YLDAAMATFR
APVPKHDSNI EGREAEHHWD DTTIPSELIT DNYSLPRASH CSLEVDICVE DILNRKQVKE
RRLHHDFIEK EQPVSSQEKL VHSMAGLWTD ETNRRKKRMG ITDPEVNPFP PEVLVSMSAD
PRQSQVMGWV HEAEYRAGIQ QLVAQEQNNT DGRQETFSRF VQPVPFEETI KTTLESVEDL
YPDNLSQALQ IEAQFFHMNA HHLISIDVDE RSIFQLTREP YAKHTRHEYA GRISPEEPLN
GVGEGFGVGD SMIYPMDGRI RVYQPRASIR HKLLKIAQTY SSNIPANTGR QAGILGPGER
QRRSLKHPRP PGEVDHGAPA KRQVLQAEYS RESLHIKADP PQRALRKAPR NAHEQTQGAG
QPGPQRKLQS NPPERVYEEP NKRVHEEAQP KVHRKAQQRS REHDQKQGQQ IIQEQTQDHD
QGGCQKEVPE DSAFTTPALT VQPMKPNNQD PAGEELSVNS LRVEPPKPKT SQPMKSAMKQ
SFTQEFQNRT INFPVVKDPQ DPNTRARLSQ KSGSQKNEGN VTRKQLAFDP QPTILGPSAQ
AKPGQTKSNL KSSSRPLDSA PVALAPALLW SGSKKMFVLN NKPPSLSEVR CTMQVHGLPD
VIYQDAYYSK DEDVPSRPRE YAGREYRLDG SSVPWLSDFD PTGTSSATYG EKPTSGADWP
MLEAIYEAQQ EECAMRGWEI ADPPPSFKEV SNWWTDEQND RNPKRCHSTP LRIKTYRSQI
AGVTPKNKHG FEHPEKTKSE SKQDQAQYMS AMSLEVHVNT RGKLVPDPEE DEVQCVFWYL
RSEVNALRGT QTPDDTARGI IVFSEDSLLA DRIRKHTSVP VVQETTELDM MVRMVEIVRN
HDPDIFTGYE VHGSSWGYLI ERARIKYELD LCDEFSRMKS QSNGRIGKDA DRWGFNTTSS
IRITGRHMIN IWRAMRGELN LLQYTMENVV WHLLHRRIPH YSWKTLSDWY LSDRPKDLDK
VLRYYLTRTR LDIEILEKNE LIPRTSEQAR LLGVDFFSVF SRGSQFKVES IMFRIAKPEN
FLLPSPSRKQ VGAQNALECL PLVMEPQSAF YSSPLLVLDF QSLYPSVMIA YNYCYSTFLG
RIVSWRGRNK MGFMDYKRQE GLLSLLKDYI NIAPNGMMYT KPHIRKSLLA KMLTEILETR
IMVKSGMKQD KDDRAIQQLL NNRQLALKLL ANVTYGYTSA SFSGRMPCSE IADSIVQTGR
ETLERAIAFI HSVQKWDADV VYGDTDSLFV SLKGRTREQA FEIGQEIADA VTKLNPRPVK
LKFEKVYHPC VLLAKKRYVG YKYESRDQTV PVFDAKGIET VRRDGTPAEQ RIEEKALKIL
FETADLSQVK SYFQEQCHKI MRGAVSVQDF CFAREVKLGT YSTSGRGGPA PAGALIATKK
MKEDARAEPQ YGERVPYVVM AGAPGMRLVD RCVEPEELLN NAHATLDADY YINKNIIPPL
ERIFNLVGAN VRTWYEEMPK VQVLRKVAED EDADDDASKG PLLGLLGASP SKKGTAAAEA
AAAAAELEME DMLGEDGELL PPDVAAAQAQ ARKTLEAFLN TTICTACGVK IKRPLGVGLA
RELGMLEEGE GAVDRGLPLC HRCASDPPTL MVDMQAKVNR AEKSYVEIMK VCQSCAGFAL
SEEVPCDSKD CPVFYSRVKQ RTKVTAVKRV MEPLIKLFGE LELDKASSED EGGDEEGNWD
LEGRGEVVDE SGVEMQEDAR VRYEEEKVRF ETIVKGKVRA MSEELVERKE IIDNSYKSLK
AASLEW
//
