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Database: UniProt
Entry: B3MLU1_DROAN
LinkDB: B3MLU1_DROAN
Original site: B3MLU1_DROAN 
ID   B3MLU1_DROAN            Unreviewed;      2105 AA.
AC   B3MLU1;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 2.
DT   24-JAN-2024, entry version 75.
DE   SubName: Full=Uncharacterized protein, isoform G {ECO:0000313|EMBL:EDV30812.2};
DE            EC=3.5.-.- {ECO:0000313|EMBL:EDV30812.2};
GN   Name=Dana\GF14860 {ECO:0000313|EMBL:EDV30812.2};
GN   Synonyms=dana_GLEANR_15623 {ECO:0000313|EMBL:EDV30812.2};
GN   ORFNames=GF14860 {ECO:0000313|EMBL:EDV30812.2};
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:EDV30812.2, ECO:0000313|Proteomes:UP000007801};
RN   [1] {ECO:0000313|EMBL:EDV30812.2, 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).
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DR   EMBL; CH902620; EDV30812.2; -; Genomic_DNA.
DR   RefSeq; XP_001961591.2; XM_001961555.2.
DR   STRING; 7217.B3MLU1; -.
DR   EnsemblMetazoa; FBtr0391271; FBpp0350733; FBgn0091887.
DR   eggNOG; ENOG502QW08; Eukaryota.
DR   HOGENOM; CLU_000345_0_0_1; -.
DR   InParanoid; B3MLU1; -.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd10975; CE4_CDA_like_2; 1.
DR   Gene3D; 2.170.140.10; Chitin binding domain; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR002557; Chitin-bd_dom.
DR   InterPro; IPR036508; Chitin-bd_dom_sf.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR45985; -; 1.
DR   PANTHER; PTHR45985:SF12; CHITIN DEACETYLASE-LIKE 5, ISOFORM B; 1.
DR   Pfam; PF01607; CBM_14; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SMART; SM00494; ChtBD2; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 1.
DR   PROSITE; PS50940; CHIT_BIND_II; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:EDV30812.2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007801};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          132..187
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   REGION          188..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          356..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          513..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          547..773
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          791..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          938..964
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          980..1013
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1048..1084
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1144..1169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1209..1304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1501..1565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1594..1613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1663..1707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..453
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..584
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..615
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..641
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..719
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..773
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        948..964
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        980..1010
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1147..1161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1209..1231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1242..1256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1501..1539
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1540..1557
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1663..1697
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2105 AA;  231363 MW;  31AB450B3AAA9387 CRC64;
     MHRTGQQRSF SQRRQLLLPR RSVAELLAEV VVVVVVAVLP PIRWYFKFCE PTSKNATAPT
     TSRKFTVTVT TTRNTCNMGH STGRLSILWL LGLCLLLFKA GYTEAQSKRS SRVTSSRSFG
     TNVKSSSSNG LSFDCPEEFG YYPHPTDCTQ YYVCVFGGAL LESCTGGLMY SHELQTCDWP
     RNVGCELVDS SSAPERSPTR SQAQTQAQQQ QQHVPSRVRF GAAFSSPGAG ASKAPTVAPQ
     YHRSPPQVIQ AQVQHIPPPP ELRVPPNPVV TSRGQPKPLL DSQEDIAKLY AEAQETLPPV
     EEEESDRQQR VYRGQPSTVS QVQRDRDGII HQASINAIPQ AGKIGSYAFG TAYRVESSSP
     SSLGAPPPPA NIFVQPTPQA QPQPQELSRN YYNASIYNHG SGNGGGYQQH HQQQVPQQQQ
     QLQPTPFQQA QVQQAPQQQP PHQQQQAQAP PHPYDSSYYS IYDDDIDLYR DIEYQQQQQQ
     DQRDQQQQPP PATQYQPVVR QQQTQSTYRP LELAATPTPP QKGSYGNQPT LVYSTDYDED
     INAQIEQDNV YDQPTRSPPR PEQVAIQRLA TPSSAPSSTT PAARPDIRNY YDTLTTPEGP
     GFSQPDYSYS SSAEYAYGSP EDYDQSEATL TRTKPRSEAD DYDLTANVVG PTGKSATAAP
     TRSKSSKSTP AIVRSPTKSS SFPTTQAVKV TKPTTTTTTT TTSTTTPPPS TTTTKRYSSK
     AHANKPHKPH EPQKSKTKST TSTPATTTTP QAPRKPPTTT TLPKLNPSTY SSNPFLKSKL
     QSLAQSLVSL VSPSQSSPQN LTRSRLPAPH PPPSSTTQWP LGTESAGSSQ VDQVETVFDE
     SQNIQVHTVE APSSRSFETS TAPRFLDFIN AAAYGTSPRG NLLHSVSEKP VKTAPREALY
     RPLEGAHPAP STELPQQRKR IQTYILSDVE PQSFRIPGIE RKAPSQEELM ESSSTSRPNK
     HPIQYSLQSG SHGFSLFVEQ PENKTTTTTT TTTTTTTTTT TTTPAATPQA DSSDDYVEIV
     PTTYAPPLRI WRNGRPTIQQ GFYRPTTSGA ITTADTRTPP PAPFVSNTPD SVESSSTLRS
     TTVPKAQITP STEKIVGMIP SFTARASFLK ESLNRVTPNP ATRFVSPYKS LENLLQEERQ
     HQHNLRTTSR PRYTNAPASP PFLQTTPKPP KSLFLTPTSR NSSQDVLATM AAGNARNFSV
     SDAILSTFSP QRPAPTMLRT TTSTTTSTTT TEPPPPTVPT TTTPTTVSSV VASSPLRVSL
     SPGRPRGRSR YTVPTSNSLG DAADEPTTYA PKLRLPSGYE PSPYLKRKPQ RIRVFREPTA
     KPQEKYEVYK AALQAKDSGY DQLSAKSLKR KPIENEASLP DEPRAEALIS HPLEARQQNS
     LEETVSSTEH VVAITERPTV KFLYSNKYRQ QTAERTLAES LQNAGYISRA QKFRSANVLE
     QLKQFLAGSD SSSTSDESGT SHFVDEYAVP EINAAVDEIK HLYQPKEQTT LRSTTLPIAA
     PRSTAVTSSP KTYSSLPSTV PTSTSTVRTT TGTPELSTPR TPPIASPAHP TPLNPPTPAS
     ATATATPPVT FALPTARASR VNNVIKSSIA AVQSGVGASP PSPAGFQPQQ GLAAGKGKVP
     KFQFGFDPSI SKHSSSSISN PAAAAATSSA SVKCSDSTLN AKCNEIPSRN NNRNRGSAIY
     TNQDRDVVST PNRGTHPPRT RPTLKPSGTI VSKAQEFVDI YRYPPTRPDP IYPQPTPDKT
     AAKCRKDVCL LPDCYCGGKD IPGELPVESI PQIVLLTFDD SVNDLNKQLY TDLFEKGRVN
     PNGCPITATF YVSHEWTDYS QVQNLYADGH EMASHTVSHS FGEQFSQKKW TREIAGQREI
     LAAYGGVKLS DVRGMRAPFL SVGGNKMYKM LYDSNFTYDS SMPVYENRPP SWPYTLDYKI
     FHDCMIPPCP TRSYPGVWQV PMVMWQDLNG GRCSMGDACS NPSDAEGVTK MIMKNFERHY
     TTNRAPFGLF YHAAWFTQPH HKEGFIKFLD AINAMPDVWI VTNWQALQWV RDPTPISRIN
     SFQPFQCDYS DRPKRCNNPK VCNLWHKSGV RYMKTCQPCP DIYPWTGKSG IRSSRIDNEV
     EEPAP
//
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