ID A0A0D2SHQ5_GOSRA Unreviewed; 1588 AA.
AC A0A0D2SHQ5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=B456_007G214600 {ECO:0000313|EMBL:KJB43754.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB43754.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB43754.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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; CM001746; KJB43754.1; -; Genomic_DNA.
DR STRING; 29730.A0A0D2SHQ5; -.
DR EnsemblPlants; KJB43754; KJB43754; B456_007G214600.
DR Gramene; KJB43754; KJB43754; B456_007G214600.
DR eggNOG; KOG0970; Eukaryota.
DR Proteomes; UP000032304; Chromosome 7.
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; 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; 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 Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304};
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 88..157
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 508..812
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 878..1341
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1380..1584
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 47..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1588 AA; 178098 MW; F9693A3BD8D78918 CRC64;
MCSILTGIMI SYLEEDRMVK FPNSFPNFTG KNPIEIKGIQ QLFHRKKNKK ETKSSRLMDF
DGPIDQPTDT GGRRRGRGAE AEKRAGALER LRALRQGGRR SDASVPAYLV KLDEPVFDNC
DEDAYQEIVN KRRKEAEDFI ENDDEYGDFG YGDDGNEVDW TQASHYLSSD DEGSDGGRYS
RKKKVEKKEK KENNNNNSSR VSKSSASLSA AAAMMGKQRV SSMFTSSAFN KKGKETDKVK
CESIVDDVIK QFAPDESDRE HRRRGQNSQL TSVRPFKVAP SVVTSVKSEG ELVSEGLNEL
VEKYPSNNEE AVVESSEIEV DKVEPEVELK VEIVEEKKEE KEGSVLKLNA KISEEKKDEA
LSATAGWKAV KGDGNGNVNG SVEGINGFTG EGQSEFELDV DGSMPFYILD AHEEFYGANM
GTLYLFGKVK VRSGYQSCCV VVKNIQRCVY AIPVSSIFHN EDIVKLEKDA EESKISLSSF
QSKLHDMASE LKNEVANHLL NLNVSGFTMA PVKRRYAFER SDVPVGENYV LKINYPFKDP
PLPSDLKGEK FCALLGTHNS ALELFLVKRK VKGPSWLSVS KFSACPAPQR VSWCKYEIIV
DSPKDIKVSS SSKKTTEIPP IVVSAINLKT IINERQNVNE IVSASIICCH RAKIDTPMLA
SEWKKPGLLS HFTVVRKLDG GIFPMGFTKE VTDRNSKAGS NVLVSESSER ALLNRLVIEL
YKLDSDVLVG HNISGFDLDV LLHRAQACKV PSSMWSKVGR LKRSVMPRLT KGSTIYGSGA
SPGIMSCIAG RLLCDTYLCS RDLLKEVSYS LTQLSKTQLN KDRKEITPQD IPQMFQTSEL
LMELIEYGET DAWLSMELMF HLSVLPLTRQ LTNISGNLWE KTLQGARAQR VEYLLLHAFH
AKKYIVPDKF SSHTKGTKVA KRRINHGVEN GNSDEVDNND MNFEEETHNE RGKGKKGPAY
AGGLVLEPKR GLYDKYVLLL DFNSLYPSII QEYNICFTTV ERFPDGLIRR LPSSKTAGVL
PELLKNLVQR RRMVKSWMKN ASGIKVQQLD IQQQALKLTA NSMYGCLGFS NSRFYAKPLA
ELITQQGREI LQSTVDLVQN NLNLEVIYGD TDSIMVYSGL DDIAKAKAIA GKVIQEVNKK
YRCLEIDLDG LYKRMLLLKK KKYAAVKVQF KDGMTYEVIE RKGLDMVRRD WSLLSKELGD
FCLAQILSGG SCEYVVESIH NSLMKVQEEM RNGQVELQKY IITKTLTKPP EAYPDAKNQP
HVQVALRMKQ SGYSTGCSAG DTIPYIICCE QGTSSSNSTG IAYRARHPDE LKKDEGKWMI
DIDYYLSQQI HPVVSRLCAS IQGTSPERLA DCLGLDSSKF QSKSSVAVSN DTANTLLFAV
DDEERYRGCE PLTLLCPSCS ATFTCPAVFS SIHTIGEKPK KMQQEESTSN FWRTLRCPQC
PEEGDMGRMS PGMIANQVKR QVDGFISMYY RGLMTCDDET CKHTTRSLNL RLFGDSEKGT
VCPNYPRCNG HLVRKYTEAD LYKQLAYFCY LLDTSRCIEK MDTSARIAVE KELAKVRPVV
DLAASTVKRI RDRCAFGWVQ INDLIVTF
//