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Database: UniProt
Entry: B4NF82_DROWI
LinkDB: B4NF82_DROWI
Original site: B4NF82_DROWI 
ID   B4NF82_DROWI            Unreviewed;       616 AA.
AC   B4NF82;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=DNA polymerase alpha subunit B {ECO:0000256|ARBA:ARBA00018596, ECO:0000256|PIRNR:PIRNR018300};
GN   Name=Dwil\GK22573 {ECO:0000313|EMBL:EDW82949.1};
GN   ORFNames=Dwil_GK22573 {ECO:0000313|EMBL:EDW82949.1};
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260 {ECO:0000313|EMBL:EDW82949.1, ECO:0000313|Proteomes:UP000007798};
RN   [1] {ECO:0000313|EMBL:EDW82949.1, ECO:0000313|Proteomes:UP000007798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24 {ECO:0000313|Proteomes:UP000007798};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Accessory subunit of the DNA polymerase alpha complex (also
CC       known as the alpha DNA polymerase-primase complex) which plays an
CC       essential role in the initiation of DNA synthesis.
CC       {ECO:0000256|PIRNR:PIRNR018300}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR018300}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase alpha subunit B family.
CC       {ECO:0000256|ARBA:ARBA00007299, ECO:0000256|PIRNR:PIRNR018300}.
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DR   EMBL; CH964251; EDW82949.1; -; Genomic_DNA.
DR   RefSeq; XP_002071963.1; XM_002071927.1.
DR   AlphaFoldDB; B4NF82; -.
DR   SMR; B4NF82; -.
DR   STRING; 7260.B4NF82; -.
DR   EnsemblMetazoa; FBtr0253224; FBpp0251716; FBgn0224550.
DR   GeneID; 6649823; -.
DR   KEGG; dwi:6649823; -.
DR   eggNOG; KOG1625; Eukaryota.
DR   HOGENOM; CLU_014923_3_0_1; -.
DR   InParanoid; B4NF82; -.
DR   OrthoDB; 49016at2759; -.
DR   PhylomeDB; B4NF82; -.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0005658; C:alpha DNA polymerase:primase complex; IEA:EnsemblMetazoa.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:EnsemblMetazoa.
DR   Gene3D; 3.60.21.60; -; 2.
DR   Gene3D; 1.10.8.530; DNA polymerase alpha-primase, subunit B, N-terminal domain; 1.
DR   InterPro; IPR007185; DNA_pol_a/d/e_bsu.
DR   InterPro; IPR043034; DNA_pol_alpha_B_N_sf.
DR   InterPro; IPR016722; DNA_pol_alpha_bsu.
DR   PANTHER; PTHR23061; DNA POLYMERASE 2 ALPHA 70 KDA SUBUNIT; 1.
DR   PANTHER; PTHR23061:SF12; DNA POLYMERASE ALPHA SUBUNIT B; 1.
DR   Pfam; PF04042; DNA_pol_E_B; 1.
DR   PIRSF; PIRSF018300; DNA_pol_alph_2; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|PIRNR:PIRNR018300};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:EDW82949.1};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR018300};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007798};
KW   Transferase {ECO:0000313|EMBL:EDW82949.1}.
FT   DOMAIN          366..564
FT                   /note="DNA polymerase alpha/delta/epsilon subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF04042"
FT   REGION          74..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   616 AA;  68184 MW;  6B5E8888C9110ADD CRC64;
     MDAEIKQQFD EMGVEPTEVV LDKCMELALS YNVNDATEFV EQWMAFSLSH LHGDEPTIEN
     LGEFERKVLQ LRRDKVGSRQ NNQKSRSSTL STPTVASASI IDSSSLATYG VKEDESMLGL
     NYDYSADNGP DSAMHTPKAN KNSARTGSLK SGVLFSPASY TPHSAKRTPT STDTVVGRPG
     DIVDTFGHPK LISGSSWQAQ VEHSVPVTQK MLHKESPLTA DNLCYMHDLL SERCNDLYDR
     FLDIGEGLVE KKLGAEGAAE CNWYPQDRHS LEALHMLHAV GMVHSEDDGP LDPHSALLAV
     LDADEPQNSF LTLNFSRIKS ASIFPGQVVL LKGFVPKGNT FVVEEIYTER KLTPPLPLKL
     DRELQFVVAA GPFTHSTDLF YDPLHDLLKY LKDHRPDVLL LTGPFVEAEH KMVAELAEGF
     DSFFEKMIVG IMEVVGCHTQ VLMVSSQRDA MAHSVYPTPP PVMRRIYPNL HLLPDPSIVD
     LDGITVGVTS TDIVSHLLSH EFALNAGERL HRAINHLFNQ GSFYPMCPPG DENMCYDSLL
     AQKYAQLKQL PNILILPSDQ RHFIRLVSDC LVINPGRLAN TKGGTFARFL VTPTAPTATA
     KTVNMFNSAA CQVQRI
//
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