ID   B3MR87_DROAN            Unreviewed;      1189 AA.
AC   B3MR87;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 2.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=UBP-type domain-containing protein {ECO:0000259|PROSITE:PS50271};
GN   Name=Dana\GF21044 {ECO:0000313|EMBL:EDV34292.2};
GN   Synonyms=dana_GLEANR_4272 {ECO:0000313|EMBL:EDV34292.2};
GN   ORFNames=GF21044 {ECO:0000313|EMBL:EDV34292.2};
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:EDV34292.2, ECO:0000313|Proteomes:UP000007801};
RN   [1] {ECO:0000313|EMBL:EDV34292.2, ECO:0000313|Proteomes:UP000007801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC         [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC         COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:61930; EC=3.5.1.98;
CC         Evidence={ECO:0000256|ARBA:ARBA00001028};
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DR   EMBL; CH902622; EDV34292.2; -; Genomic_DNA.
DR   RefSeq; XP_001963843.2; XM_001963807.2.
DR   STRING; 7217.B3MR87; -.
DR   EnsemblMetazoa; FBtr0386930; FBpp0346758; FBgn0098049.
DR   GeneID; 6503733; -.
DR   KEGG; dan:6503733; -.
DR   eggNOG; KOG1343; Eukaryota.
DR   eggNOG; KOG1867; Eukaryota.
DR   HOGENOM; CLU_007727_2_0_1; -.
DR   InParanoid; B3MR87; -.
DR   OrthoDB; 124800at2759; -.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd10002; HDAC10_HDAC6-dom1; 1.
DR   CDD; cd10003; HDAC6-dom2; 1.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR10625:SF4; HISTONE DEACETYLASE 6, ISOFORM G; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF00850; Hist_deacetyl; 2.
DR   Pfam; PF02148; zf-UBP; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00502};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007801};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00502};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00502}.
FT   DOMAIN          994..1095
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          936..963
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1189 AA;  131594 MW;  DDC17B9CB396D25A CRC64;
     MSPPIVTRRS AQQAKIQTRA MVNKTKTSTG GGTTSAATAA GVIGSAAGGG SGGPSGGDSR
     KSNKPSAALL EAKRRARNLL KSQNNAMATQ ECVTDIFQNA VNAKGLVRRP TALIYDESMS
     QHCCLWDKEH YECPERFTRV LERCRELNLA DRCLQLPSRA ATKAEVLRLH TEEHFDRLKA
     TSGIRDDDRM EELSSRYDSI YIHPSTFELS LLATGSTIEL VDQLIAGSAQ NGMAIIRPPG
     HHAMKAEFNG YCFFNNVALA AQHALDVHKL QRILIIDYDV HHGQGTQRFF YNDPRVLYFS
     IHRFEYGSFW PHLHESDYHA IGSGPGTGYT FNVPLNSTGM TNGDYLAIFQ QLLLPVALEF
     QPELIMVSAG YDAALGCPEG EMEVTPACYP HLLNPLLRLA DSKVAVVLEG GYCLDSLAEG
     AALTLRSLLG DPCPPLVEEL ALPRQELADA LLNCICAHRP HWRCLQIQKT YEADELMATD
     AVQPKDLHRV RRIWIGGPPP VERYPTRDTA IPLPAEKIAS NSARLQVLRA ETKLSVPPVR
     VCYAYDTQML QHCNLHDGGH PEQPFRIQSI HQMHKEYALL ERMKQLSARA ATTDEICLAH
     TRSHVNSVRR LLGRDPEELH QLGSTYNSVY LHPRTFDCAT LAAGSVLQAV DSVLRGESRS
     GICNVRPPGH HAEPDQPHGF CIFNNVAIAA QYAIRDYGLQ RVLIVDWDVH HGNGTQHIFE
     SNPKVLYVSV HRYEHGAFFP KGPDGNFDVV GKGAGRGFNV NIPWNKKGMG DLEYALAFQQ
     VIMPIAYEFN PQLVLVSAGF DAAIGDPLGG CKVTPEGYGM LTHWLSALAG GKIVVCLEGG
     YNVNSISYAM TMCTKTLLGD PVPTPQLGAA SLQKPATVAY QSCIETLQAC LEVQRAHWQS
     LEFAGRRLPR DFDPLVGENN NEDFLTASLR QLNISSDQIP EAAPGGPGGD RPDCGEERPS
     GSKPKVKVKT LTEYLQENKE ALENNEMFAV YPLKTCPHLS LLRPEEVPPS INTGAACSQC
     ESSEENWMCL SCRTVACGRY VNEHMQMHCL ESEHPLAMSL RDFSVWCYAC SSYIDHPRLY
     AFLNAAHLDK FREPMAWTHV CPQRADGCYP IGADGRDEDD SAAGCSNICI QLERNQNNXP
     LAIRVLDGIT DYICTLCPPL RHLLQFLAEH LWPIVERIYL SLLHYFLAH
//