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Database: UniProt
Entry: A0A0Q9XHA4_DROMO
LinkDB: A0A0Q9XHA4_DROMO
Original site: A0A0Q9XHA4_DROMO 
ID   A0A0Q9XHA4_DROMO        Unreviewed;      1936 AA.
AC   A0A0Q9XHA4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   13-SEP-2023, entry version 38.
DE   SubName: Full=Uncharacterized protein, isoform H {ECO:0000313|EMBL:KRG02867.1};
GN   Name=Dmoj\GI17301 {ECO:0000313|EMBL:KRG02867.1};
GN   ORFNames=Dmoj_GI17301 {ECO:0000313|EMBL:KRG02867.1};
OS   Drosophila mojavensis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7230 {ECO:0000313|EMBL:KRG02867.1, ECO:0000313|Proteomes:UP000009192};
RN   [1] {ECO:0000313|EMBL:KRG02867.1, ECO:0000313|Proteomes:UP000009192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15081-1352.22 {ECO:0000313|Proteomes:UP000009192};
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   -!- SIMILARITY: Belongs to the RBR family. {ECO:0000256|ARBA:ARBA00008278}.
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DR   EMBL; CH933807; KRG02867.1; -; Genomic_DNA.
DR   RefSeq; XP_015020574.1; XM_015165088.1.
DR   SMR; A0A0Q9XHA4; -.
DR   EnsemblMetazoa; FBtr0431217; FBpp0388515; FBgn0140045.
DR   GeneID; 6576287; -.
DR   OrthoDB; 2909614at2759; -.
DR   Proteomes; UP000009192; Unassembled WGS sequence.
DR   GO; GO:0071797; C:LUBAC complex; IEA:InterPro.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd19815; Bbox1_HOIP; 1.
DR   CDD; cd20337; BRcat_RBR_HOIP; 1.
DR   CDD; cd16631; mRING-HC-C4C4_RBR_HOIP; 1.
DR   CDD; cd20351; Rcat_RBR_HOIP; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR047543; Bbox1_RNF31-like.
DR   InterPro; IPR047540; BRcat_RBR_RNF31-like.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR047542; Rcat_RBR_RNF31-like.
DR   InterPro; IPR026254; RNF31-like.
DR   InterPro; IPR032065; RNF31-UBA.
DR   InterPro; IPR041031; RNF31_C.
DR   InterPro; IPR047541; RNF31_RBR_mRING-HC-like.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR16004:SF2; E3 UBIQUITIN-PROTEIN LIGASE RNF31; 1.
DR   PANTHER; PTHR16004; RING FINGER PROTEIN 31-RELATED; 1.
DR   Pfam; PF18091; E3_UbLigase_RBR; 1.
DR   Pfam; PF16678; HOIP-UBA; 1.
DR   Pfam; PF01485; IBR; 1.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00184; RING; 2.
DR   SMART; SM00547; ZnF_RBZ; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009192};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          1554..1792
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          1558..1607
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          129..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          482..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          646..737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..850
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          952..991
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1272..1373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1387..1411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..564
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..588
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..630
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..671
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        685..699
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..850
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        959..973
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1294..1310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1311..1337
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1350..1373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1936 AA;  215202 MW;  7F7E61C5010ED576 CRC64;
     MTTHQLLNRN VRTMPDWVNE ANDRIGPKPP PTPMNGNASM NGAQLKVPAL PPKTKNTPEP
     DYEIIEFSNQ QQYSNEPMKT TQIRTKTPDN KLKCTLCGSQ NPWVTCAECA GQIFCASCDD
     MFHKHPKRKN HIRKAAKQGT PPIPPKASAA GAAPPVAPPR RSKRGLLTPF LGRKEQMLPP
     PSPTPSHKSS GGWRGPAAGP QMNNRPLPEP PRPAPSEGGG SSRSGTPKSV FDSISRPPSV
     QLEKIKSKAN ATLDRMAQLQ QRYRQQKAQH EAGNPDQQLN FEHWSNISPS PSHFRSGSMS
     SGLNSSHFDL SDDSHNFHNS LLFQQQQQLR RQAVGAQRRQ MSTSVFNLNS MSPRRPLAEN
     QPIGSAWVAN QRMQQAQSMA HLNCAGCQSQ QPNWPGQPHP HDEWSQFGSQ QQFNSSNLSL
     NVGPGYLPQH QQLMQQQHPH YPPPVFMTQR GIMPNMYPGA AGYPMMHPGV MGMPPTAVSR
     AASRARYAAS PTPSRKSMSM RRKRSSYVDD ELTDDEDSDQ DDRRSLVSNR SGMTSASRAH
     QHHQRQRRMS SASQLISNGN GGNDELDGEQ RHAGSRQHKM RDRRGSIAKS VQSEWLPERR
     DSNASGGGTG TLKRSQQQDA PKTSRIYSDL ESEGSGARAL VQAKIQQKLQ EADQQKVKRT
     ESKRKPETKD ENTQAAAVVQ KVIETPVKSR EKSDSEYEEV VEEVTASETE EEQPAAAAPT
     EVDAGDDELG PPPSTPDHEW ECEFCTFVNE PNIKICAICC KTPCKQPVKP NKATTPPAKA
     AAVEPKATQA KSEVKLVRKS SMKTTTKPTV QKAIQPASQS PAKTQAPATA KPKQTTTATA
     TATTTTSTVT NKKPTTAIKS KLKSTAGNQA DKPLGSSFLN KESVENIWNT LDESIQAQAE
     QVLKQSKKVS TGCGGTPPRE LPTKMEAREM GTSPPPQSIS TQTYDALPFV GQPEIPPEPE
     RFRTPEPAKM ERKPYYRSSS QLTQENERYR SSNDLRNMES ISNQLTRRPN FINDLKMLQH
     QTSSPFDLPH ESVGYKHEPA RDPEIEMHII LKELELYKFT VDELEAALKY CGPDIHPIQW
     LRENWHKLVQ TVQSLSTKYG QERAENTIGT VSQNEAREAL RSSGGNVWQA VADCIQQRQQ
     KYRKLAAKGN FLSEDIVNAL TAHQGNVEQA LVELNRTQLK PFLMRIWGSP NGVENESAAV
     DNQSGSTALE ATIETEPAVA AAAASIASTE EAKAAVSENT ALEPPLIPLT ENRPAELPAE
     IVLETKPQAE EPIALPIIPD PPIVDSETRP LELPSETVLE EPKKVNPKKT TKTDAPNTAK
     ANSTPKASKI PKLTTNDNNT TPPPPPTTTT TATTTTTTNK KLPLRSKSFS APIGISSVKR
     IQQEYLQKQT QSNGSSNSRV PLKSSPSNRK SLSDAIKKFN TKTTLDDGPS TSAAVNALLK
     PRSQPRIPKK KYHETCFSDD DYETSASEEA EQEQQSEMLQ RKLSMPVFRA YPSVQEPVIE
     EPAVLARKYV EQQLVTSIAE AQIAATLVNM KFQEDVALWA ARECSDLDQA ISMLQQECEL
     CMNSYPMNQI VSMLKCTHKC CKQCAKSYFT VQITDRSIND CSCPFCKLPE LSNAVQHEDE
     HLEYFSNLDI FLKSILDNDV HELFQRKLRD RTLLQDPNFK WCIQCSSGFF ARPKQKRLIC
     PDCGSVTCAQ CRKPWERQHE GTSCEAYLEW KRENDPELQA QGVQEHLAQN GIDCPKCKFR
     YSLARGGCMH FTCTQCKFEF CYGCARPFMM GAKCTISPYC AKLGLHAHHP RNCLFYLRDK
     IPMQLQFLLK EHNVKFDTEP MELADEPSSS SKARAQARCP IPLQKETPQG LVDTVCNSEV
     PDKHAGMCRT HYVEYLAGKV AKASIDPLPI FDLTDCVQEL RRRGIALPER GPWDTDEIYK
     TMCSEVIKQR IPLKSA
//
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