ID A0A3M9XXX0_9PEZI Unreviewed; 1474 AA.
AC A0A3M9XXX0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN Name=POL1 {ECO:0000313|EMBL:RNJ52622.1};
GN ORFNames=D7B24_003157 {ECO:0000313|EMBL:RNJ52622.1};
OS Verticillium nonalfalfae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=1051616 {ECO:0000313|EMBL:RNJ52622.1, ECO:0000313|Proteomes:UP000267145};
RN [1] {ECO:0000313|EMBL:RNJ52622.1, ECO:0000313|Proteomes:UP000267145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VnAa140 {ECO:0000313|EMBL:RNJ52622.1,
RC ECO:0000313|Proteomes:UP000267145};
RA Stajich J.E., Kasson M.T.;
RT "Genome sequence of Verticillium nonalfalfae VnAa140.";
RL Submitted (OCT-2018) 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 -!- 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}.
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:RNJ52622.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RBVV01000187; RNJ52622.1; -; Genomic_DNA.
DR STRING; 1051616.A0A3M9XXX0; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000267145; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 10..75
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 417..723
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 791..1225
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1265..1461
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 81..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1474 AA; 165497 MW; BC7811C790C10D3A CRC64;
MGKTDRRAKL AELKALRQAG KKAFDNYQVD DINELYEEVD ETQYKKIVRD RLNEDDFVVD
DNGEGYADDG REEWDRVQQY HYASDSEEDG SGARGRPTKA SKKKQADDAA RREANDRDIS
TYFTSGAGKT QAKPKVAKTK EDDDFLADLL GEVDTNVPAP VPRSTKRHRS PDRQQRRVRV
ASPPPHERSQ PLAKRSKIRD DRPSSPPAAD DMLVDDNSVP TMDDDELPTQ FPMGDPAPSS
PAAKVAERKA QIKKEPDDDD DDMMEVAHAG TVTAASVNIT GSRPPKKLIK PEPYPAPITS
SPVKQESAID PSAWNDITNN LNIVSNSVSE VKSIRKIDYK DAIEEDGSLN MFWTDYTEVS
GSLCLFGKVL NKKTGQHVSC FVKIDNILRK LFFLPRETRV QGGIDTCDEV GMVDVYSEVD
ALMTKMKIGK YKTKSCNRKY AFELPDIPKE GQYLKCLYPY SMAPVDAGET GETFSHVFGT
NTALFEQFVL WKNIMGPCWL NIKDADFSSL QNASHCKLEV LVEHPNMVAS LRDSENLDTP
PLTLMSLAMR TTFNAKDNKL EILALSARVY EKVSLSDTTP AEKLPCRTFT LVRPNGSAFP
GGFEKLAKDR SNKGLIKTFK QESEILMFFL AQLDIVDPDV ILGHQLEGVD YSVLLNRIHE
KKTPQWSRLG RLRRTVWPSS IGKTGGNVFA ERQVMSGRLL CDLANDAGKS AMYKCQSWSL
TEMCSLYLSG NNHRRELDND AALKTWASHS KEGFMDYVTH IEADTYFIAA LALQVQLLPL
TKVLTNLAGN SWARTLTGTR AERNEYILLH EFHRNKYICP DKQGFQRGKG AKEDEEGDSK
KKDKFKGGLV FDPEKGLYDK FVLVMDFNSL YPSIIQEFNI CFTTVDRTAK LEDEEEVPEV
PVDQEQGILP KLIATLVSRR KQVKSLMKDK TATPEQLATW DIKQLALKLT ANSMYGCLGY
TKSRFYARPL AVLTTYKGRE ILRSTKELAE SRALQVIYGD TDSVMINANV ENVADAFKVG
AEFKKAVNER YRLLEIDIDN VFRRILLQAK KKYAAINLVE NNGKYIEKME VKGLDMKRRE
YCGLSKEISG KLLDEILSGE DTEVSISRIH DYLREIAAKM REQSIPAQKY IIFTQLGKGP
KEYPNGDTMP QVQVALRDIA RGKNVRKGDV ISYIITGDGQ SSEPAPKRAY TPSDVLKPES
GLAPDVEWYI AKQIFPPVER LCANIVGTST MQLAECLGLD IKRYDTSRRR DDGVEKDMEV
HPLESQIPDD VRFADCTRLS LRCRTCKKSS VFEGLYSQPT RVSPAGVLCD HCGATISPLS
VVAQVEHAIR VQTARYYEGW LICDDSSCGI RTRQMNVYGT RCLGPKGLAR DCLGRMRYDY
SEKAIYNQLV YFTSLWDVDK ARDKAIAAAA PSSEEALSQA DRENILALAE HNRVRFGTVK
GVVDKYLDKC GRQWVAMDTL FAKLGFSKAL APAA
//
