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Database: UniProt
Entry: B4MUZ2_DROWI
LinkDB: B4MUZ2_DROWI
Original site: B4MUZ2_DROWI 
ID   B4MUZ2_DROWI            Unreviewed;       673 AA.
AC   B4MUZ2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   13-FEB-2019, entry version 66.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDW76337.1};
DE            EC=3.2.1.23 {ECO:0000313|EMBL:EDW76337.1};
GN   Name=Dwil\GK15404 {ECO:0000313|EMBL:EDW76337.1};
GN   ORFNames=Dwil_GK15404 {ECO:0000313|EMBL:EDW76337.1};
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260 {ECO:0000313|EMBL:EDW76337.1, ECO:0000313|Proteomes:UP000007798};
RN   [1] {ECO:0000313|EMBL:EDW76337.1, 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.,
RA   Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N.,
RA   Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P.,
RA   Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W.,
RA   Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A.,
RA   Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D.,
RA   Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D.,
RA   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.,
RA   Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H.,
RA   Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S.,
RA   Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A.,
RA   Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S.,
RA   Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J.,
RA   Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W.,
RA   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.,
RA   Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S.,
RA   Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H.,
RA   Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F.,
RA   Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S.,
RA   Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J.,
RA   Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A.,
RA   Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A.,
RA   Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B.,
RA   McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P.,
RA   Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B.,
RA   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.,
RA   Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D.,
RA   Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H.,
RA   Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A.,
RA   Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H.,
RA   Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L.,
RA   Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C.,
RA   Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M.,
RA   Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E.,
RA   Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D.,
RA   Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N.,
RA   Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C.,
RA   Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B.,
RA   Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A.,
RA   Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D.,
RA   Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P.,
RA   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.,
RA   An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P.,
RA   Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J.,
RA   Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A.,
RA   Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M.,
RA   Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G.,
RA   DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M.,
RA   Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D.,
RA   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.,
RA   LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T.,
RA   Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V.,
RA   Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J.,
RA   Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V.,
RA   Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T.,
RA   Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B.,
RA   Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P.,
RA   Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C.,
RA   Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L.,
RA   Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N.,
RA   Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T.,
RA   Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A.,
RA   Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C.,
RA   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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
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DR   EMBL; CH963857; EDW76337.1; -; Genomic_DNA.
DR   RefSeq; XP_002065351.1; XM_002065315.2.
DR   ProteinModelPortal; B4MUZ2; -.
DR   SMR; B4MUZ2; -.
DR   STRING; 7260.FBpp0244547; -.
DR   EnsemblMetazoa; FBtr0246055; FBpp0244547; FBgn0217409.
DR   GeneID; 6642659; -.
DR   KEGG; dwi:6642659; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   eggNOG; COG1874; LUCA.
DR   InParanoid; B4MUZ2; -.
DR   KO; K12309; -.
DR   OMA; ACDFSYM; -.
DR   OrthoDB; 179316at2759; -.
DR   PhylomeDB; B4MUZ2; -.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblMetazoa.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:EnsemblMetazoa.
DR   Gene3D; 2.60.120.260; -; 2.
DR   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007798};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888,
KW   ECO:0000313|EMBL:EDW76337.1};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869,
KW   ECO:0000313|EMBL:EDW76337.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007798};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     12     36       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       56    379       Glyco_hydro_35. {ECO:0000259|Pfam:
FT                                PF01301}.
FT   DOMAIN      561    639       BetaGal_dom4_5. {ECO:0000259|Pfam:
FT                                PF13364}.
FT   ACT_SITE    205    205       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
FT   ACT_SITE    286    286       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
SQ   SEQUENCE   673 AA;  75233 MW;  1070D98368605EFD CRC64;
     MSGGCRCTRK LTLAMSGCVI ILVIALTVGL CVGLGGDDEV KREDTPKFTI DHEANTFLLD
     GEPFQYVSGS FHYFRALPDA WRSRLQTMRA SGLNALDTYI EWSLHNPHDG VYNWEGIADV
     VKFLEMAQEE GFYIVLRPGP YICAERDNGG LPHWLFTKYP NIKVRTNDSN YLAEVEKWYD
     ILMPRIQHLF IGNGGKIIMV QVENEYGAFD ACDHDYLNWL RDETEKHVSG NALLFTVDIP
     NERMSCGKIE NVFATTDFGI DRIHEIDEIW KMLRNLQPTG PLVNSEFYPG WLTHWQEENQ
     RRDGQVVADA LKTILSYNAS VNLYMFFGGT NFGFTAGANW NLDGGIGYAA DVTSYDYDAV
     MDEAGGVTSK YELVKKAIGE LWTLPEITLT PAKRLSYGKV ELTPSLQLLS SEGRAALSKG
     VPVESEKPKT FEELDQYSGL VLYETTLPDM DLDPALLKVE QINDRAQVFV DQELVGTLSR
     EANIYALPLS KGWGSTLQLL VENQGRVNYD LLNDTKGIFG DVSLQLHNGG YLTLENWKST
     SFPLEEAAVA SWLKQRTNKE LDSLITRQRI LRNGPILYSG TVKVDEIGDT YLNMAGWGKG
     VAYVNGFNLG RYWPVAGPQV TLYVPNELLK VGDNSIAILE YQRANKTTSG TDLPAVQFDA
     VAQLDGQSGD VKK
//
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