ID N1RUJ9_FUSC4 Unreviewed; 1453 AA.
AC N1RUJ9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=FOC4_g10008759 {ECO:0000313|EMBL:EMT70313.1};
OS Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT70313.1, ECO:0000313|Proteomes:UP000016929};
RN [1] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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; KB726324; EMT70313.1; -; Genomic_DNA.
DR SMR; N1RUJ9; -.
DR STRING; 1229665.N1RUJ9; -.
DR HOGENOM; CLU_001718_1_0_1; -.
DR Proteomes; UP000016929; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IEA:InterPro.
DR CDD; cd05776; DNA_polB_alpha_exo; 1.
DR CDD; cd05532; POLBc_alpha; 1.
DR Gene3D; 2.40.50.730; -; 1.
DR Gene3D; 3.30.70.2820; -; 1.
DR Gene3D; 1.10.3200.20; DNA Polymerase alpha, zinc finger; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 2.
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; IPR024647; DNA_pol_a_cat_su_N.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR038256; Pol_alpha_znc_sf.
DR InterPro; IPR045846; POLBc_alpha.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR015088; Znf_DNA-dir_DNA_pol_B_alpha.
DR NCBIfam; TIGR00592; pol2; 1.
DR PANTHER; PTHR45861; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR45861:SF1; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR Pfam; PF12254; DNA_pol_alpha_N; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF08996; zf-DNA_Pol; 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 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000016929};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 7..72
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 402..711
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 778..1215
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1255..1444
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 77..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1453 AA; 163898 MW; 9BF31AC24CD00CF6 CRC64;
MSHRARLAEL KALRESGKKV FDTYKVADVD NLYDEVDEDG YKKVVRERLN QDDFVVDDNG
EGYADDGRED WDRVQAYGSE SEEEATLRGR PSKTAKKNRQ EEQAKRAATD KDISEYFNGA
NRAQPKPKVV KTKEDDDFLS NLLGEVDNNI PAPAPHTSRV ERSGGRRKAR ALSPAPEPVP
KKTKTLDTRL PSPLPPAPDD DGFFPSADDD ILETADVPMS DPAPSSPAAK VAQRKAQIKQ
EPKEDDDDED MMEVAHAGTI ATTSVNLASS RPIKKIQKAE SYPTPASSSP VKPNGAQVDS
ASWNALTERL NVVTSSPAET KTIGKIDYKE AIEEDGSLNF FWTDYTEVNG SLCLFGKVLN
KKTRSYVSCF VKVDNILRKL YFLPRQHRLQ DGEETGEEVE MMNVYDEIDT MMTKMNVGMY
KIKACTRKYA FELRDVPKEA QYMKLLYPYN KPEVDPNRPG ETYSHVFGSN TALFEQFVLW
KNIMGPCWLK IEDADFDKLK NASHCKLEVL ADHPNMVSVL SESDNLDAPP LTLMSVSLRT
AFNEKDNKQE ILAISARIYE KVSLSDTTPA EKLPCRTFTV IRPHGQAFPM GFDHLAKKRN
RGLIVLKKQE ADILAFFLAQ LDVADPDVIL GHQLEGVDYS VLLNRLYEKK IPGWSRLGRL
RRSQWPSSIG KTGGNVFAER QILSGRLLCD LANDAGKSVM FKCQSWSLTE MCSLYLSGDN
RRRDFDNEVA LKTWAREKQG LLDYITHMEA DTHYIAALAL GVQMLPLTKV LTNLAGNSWA
RTLTGTRAER NEYILLHEFY RNKYICPDKQ TFRSRQRAEE AQREEEAVEG KKKDKYKGGL
VFEPEKGLYD KFVLVMDFNS LYPSIIQEFN ICFTTVDRPA TNGEEDEVPE VPINQDQGIL
PRLIATLVSR RRQVKSLMKD KKATPEELAT WDIKQLALKL TANSMYGCLG YTKSRFYARP
LAVLTTFKGR EILRSTKELA ESNSLQVIYG DTDSVMINAN VDNVADAFKV GNDFKKAVNE
QYKLLEIDID NVFRRILLQA KKKYAAINLV EKDGKFIEKM EVKGLDMKRR EYCALSKEIS
QHLLNEILSG DDTEVSIARI HEYLSDIAGK MREQTIPVQK YIIHTQLGKA PNDYPDSNSM
PQVQVALREM AKGKTVRKGD VIAYVITGDS KSSEPAPKRA YTPGDLKADP TLLPDVEWYI
GKQIFPPVER LCANIVGTST SQLAEHLGLD IKRYSSFQTQ QNSSSNDLEI YPLDSQIPDE
VRFGDCARLS LRCRKCKTPF AFEGLATSPN HVSQSGVICG SCGSSISTLS VVAQMEHAIR
TQTSRYYEGW LVCDDSQCGN RTRQMSVYGS RCLGPKGLAR DCLGRMRYEY TEKAIYTQLL
YFASLWDVDK AKAKATSTEM SRQDRENILA LAEHNRVRFG NVKGIVDKYL DKCGRQWVAM
DTLFTKLGFK PMA
//