GenomeNet

Database: UniProt
Entry: B3LZH4_DROAN
LinkDB: B3LZH4_DROAN
Original site: B3LZH4_DROAN 
ID   B3LZH4_DROAN            Unreviewed;      1031 AA.
AC   B3LZH4;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Uncharacterized protein, isoform A {ECO:0000313|EMBL:EDV41916.1};
DE   SubName: Full=Uncharacterized protein, isoform C {ECO:0000313|EMBL:KPU79434.1};
DE            EC=6.3.4.15 {ECO:0000313|EMBL:EDV41916.1, ECO:0000313|EMBL:KPU79434.1};
GN   Name=Dana\GF17255 {ECO:0000313|EMBL:EDV41916.1};
GN   Synonyms=dana_GLEANR_18522 {ECO:0000313|EMBL:EDV41916.1};
GN   ORFNames=GF17255 {ECO:0000313|EMBL:EDV41916.1};
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV41916.1, ECO:0000313|Proteomes:UP000007801};
RN   [1] {ECO:0000313|EMBL:EDV41916.1, ECO:0000313|Proteomes:UP000007801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV41916.1}, and Tucson
RC   14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
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).
RN   [2] {ECO:0000313|EMBL:EDV41916.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV41916.1};
RX   PubMed=18057021; DOI=10.1093/bioinformatics/btm542;
RA   Zimin A.V., Smith D.R., Sutton G., Yorke J.A.;
RT   "Assembly reconciliation.";
RL   Bioinformatics 24:42-45(2008).
RN   [3] {ECO:0000313|EMBL:EDV41916.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV41916.1};
RG   FlyBase;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC       {ECO:0000256|ARBA:ARBA00009934}.
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DR   EMBL; CH902617; EDV41916.1; -; Genomic_DNA.
DR   EMBL; CH902617; KPU79434.1; -; Genomic_DNA.
DR   RefSeq; XP_001953333.1; XM_001953298.2.
DR   RefSeq; XP_014766347.1; XM_014910861.1.
DR   AlphaFoldDB; B3LZH4; -.
DR   STRING; 7217.B3LZH4; -.
DR   EnsemblMetazoa; FBtr0121955; FBpp0120447; FBgn0094273.
DR   EnsemblMetazoa; FBtr0392093; FBpp0351492; FBgn0094273.
DR   GeneID; 6500040; -.
DR   KEGG; dan:6500040; -.
DR   eggNOG; KOG1536; Eukaryota.
DR   HOGENOM; CLU_006150_2_1_1; -.
DR   OMA; HEQYGVL; -.
DR   OrthoDB; 317678at2759; -.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0000791; C:euchromatin; IEA:EnsemblMetazoa.
DR   GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006325; P:chromatin organization; IEA:EnsemblMetazoa.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:EnsemblMetazoa.
DR   CDD; cd16442; BPL; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR   InterPro; IPR003142; BPL_C.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   NCBIfam; TIGR00121; birA_ligase; 1.
DR   PANTHER; PTHR12835; BIOTIN PROTEIN LIGASE; 1.
DR   PANTHER; PTHR12835:SF5; BIOTIN--PROTEIN LIGASE; 1.
DR   Pfam; PF02237; BPL_C; 1.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EDV41916.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007801}.
FT   DOMAIN          766..955
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
FT   REGION          263..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          318..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..409
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1031 AA;  114641 MW;  2593A32AFE90361A CRC64;
     MLTLYYVGAT VLQSWRIQKA CSKIAEHLAQ PSSISFYALQ PGHDDGFDPL FASSELCGNR
     NAAKVTEILW LHANQRGCCL RPLQSLHITP WISFPPAPSL LPFAYSSETL TPVASPDESP
     PQQRVSLSDQ GEHRMQLLLE AQVEPMQRPS SQDTTCVRLE DYGKLIAWKI DSHLAVLLET
     DVEHFTQLLI TTFLRNNLCI NDQLPLMRIE SVRREGEPQP FELLANHLKR QSRVTVELDK
     EGWKKHLEDL RAASVLAHQA TEFESHKNRT EGKSKSDILG QASEPLPKAV AVVEPTNKAA
     LSPARIPVTV PKTEAKIEVK TSPAKSEAKV SPVYKTESKS TPTKGTPKKL DSQPSELEKL
     AAAQAAQQQN TPQEATPIKV VAAPKAAIPE IPDKTDSPKK PEKIAAEAPK PSKTFEVAKP
     LNSPVTATPP RPVLKRNKDS LQESKPLNVL VYSDSASARD STLATLEQLL ERNVYTIYPL
     MPQQAAQKYW TEQTALLVVC GSVAPGIGQV LVDYFLQGGK VLSLCSDILH FILPNYRTAE
     VREHELVQFS YDKWQRVKMM HHIFCYQPSP VKKHFSTDSE ESTKSHSRKP SMELKDLAGH
     NHNLDVQVLG TEETWNTPSL LLAKSLQSGG KAVFSQVHLE TNPSEFETDE IKYSILKQNE
     STRLEIFADL LRKYLDVQVQ GGDGPPQPGV VYQQAYFLGR HESKFELLEK LRLRCSGPDN
     VIATPKLTIK FCGKDDKPPV ANNNVLPILI HSCPEDFSTV DYFDQLKTEH IGRLVIYAPV
     VSSSMHVINN LELINGLAVL PLQQTAGVGR SNNQWLSPLG CAMFSLQLHL AMDSPLGSRL
     PLLQHIIGAA IVNSLRSHPQ YGILDISIKW PNDIYANGNQ KIGGLVINTT LQGSQAIVNI
     GSGINLNNSK PTVCINDLIR EHNQHSPNNK LPLLKYELFI AMIFNEIERL LGEVQNGDFD
     SFYDLYYSLW LHSGQTVKIC LPNQQEREAE IVGIDDFGFL KVKLPSGAIE TVQPDGNSFD
     MLKGLIVPKY H
//
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