ID A0A0Q9XFD0_DROMO Unreviewed; 2930 AA.
AC A0A0Q9XFD0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 18-JUN-2025, entry version 50.
DE SubName: Full=Uncharacterized protein, isoform D {ECO:0000313|EMBL:KRG02864.1};
DE SubName: Full=Uncharacterized protein, isoform E {ECO:0000313|EMBL:KRG02865.1};
GN Name=Dmoj\GI17301 {ECO:0000313|EMBL:KRG02865.1};
GN ORFNames=Dmoj_GI17301 {ECO:0000313|EMBL:KRG02865.1};
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:KRG02865.1, ECO:0000313|Proteomes:UP000009192};
RN [1] {ECO:0000313|EMBL:KRG02865.1, ECO:0000313|Proteomes:UP000009192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSC#15081-1352.22 {ECO:0000313|EMBL:KRG02865.1}, and Tucson
RC 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).
RN [2] {ECO:0000313|EMBL:KRG02865.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#15081-1352.22 {ECO:0000313|EMBL:KRG02865.1};
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:KRG02865.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#15081-1352.22 {ECO:0000313|EMBL:KRG02865.1};
RG FlyBase;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the RBR family. {ECO:0000256|ARBA:ARBA00008278}.
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DR EMBL; CH933807; KRG02864.1; -; Genomic_DNA.
DR EMBL; CH933807; KRG02865.1; -; Genomic_DNA.
DR RefSeq; XP_015020571.1; XM_015165085.1.
DR RefSeq; XP_015020572.1; XM_015165086.1.
DR SMR; A0A0Q9XFD0; -.
DR FunCoup; A0A0Q9XFD0; 10.
DR EnsemblMetazoa; FBtr0424446; FBpp0382300; FBgn0140045.
DR EnsemblMetazoa; FBtr0426201; FBpp0383907; FBgn0140045.
DR KEGG; dmo:Dmoj_GI17301; -.
DR CTD; 33950; -.
DR InParanoid; A0A0Q9XFD0; -.
DR OrthoDB; 9978677at2759; -.
DR Proteomes; UP000009192; Unassembled WGS sequence.
DR GO; GO:0071797; C:LUBAC complex; IEA:InterPro.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IEA:EnsemblMetazoa.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IEA:EnsemblMetazoa.
DR GO; GO:1990450; F:linear polyubiquitin binding; IEA:EnsemblMetazoa.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:EnsemblMetazoa.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:EnsemblMetazoa.
DR GO; GO:0010286; P:heat acclimation; IEA:EnsemblMetazoa.
DR GO; GO:0061059; P:positive regulation of peptidoglycan recognition protein signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0097039; P:protein linear polyubiquitination; IEA:EnsemblMetazoa.
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 LUBEL; 1.
DR PANTHER; PTHR16004; RING FINGER PROTEIN 31-RELATED; 1.
DR Pfam; PF18091; E3_UbLigase_RBR; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF16678; UBA_HOIP; 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 2548..2786
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 2552..2601
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 953..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1493..1657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1690..1709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1763..1799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1959..2005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2018..2038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2073..2118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2145..2195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2266..2405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..306
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..497
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..520
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..548
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..582
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..791
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..850
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..974
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1496..1510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1616..1627
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1646..1657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1770..1784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1959..1973
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2020..2033
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2076..2115
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2145..2161
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2162..2181
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2308..2320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2342..2353
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2378..2404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2930 AA; 324915 MW; 9C6C787F6AD3B2EA 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
DNQSDIHEFL NTHALDCLQV QNSESPALAY PFDDNSSPAK SAYATPSPYQ LEDGTLKNLE
ILIGNMEQNQ AKQNQEVLRS IETMLETFKG KPDQEYETDP EVMRILTKSP ISTLKSPSAL
PEKSSDDVKN FVWQHIQEIV PNLVQQVEQE LMAPTEVAQA PVTVVPTEAV PQKEATPPPD
PGVYIMEEFI KPNLRESTIR EELPPNFIYA TEIANFKLEF DRGVERVHEL EFELDDLEDA
KHIVYKSYLA PKLGAVKEEI VPENVVSEER NPNSETLESK VSASILVNEE ILAKNPDSDE
KNQNSEDLES KVSVVGVTEV EAAQNENSTE PIAPQVKQET AEATTKEVTL EKPINLPDEA
PLAANSVSSS KAETAAEQII AAPTPTEPKS KENAIAAETQ AKLDDKPSTS REVYKRNKRS
QLPKKGRARD QSQRPTNRNR LPNNIEKVER EIEAKEQKDA VIKTTNEIVP GSKIAVVEVE
EQIKAIEKEA EPEAIKSEPA EGKVEPRPET QTEIDVIIEA EDQEEAKTVA QAEVTQTEVT
QTEVVQSEVV RAEVTQAEVP VEPQAGVLTV PQSVEPNPTT TTESVDTDPK EVPSETLPLI
PNSAIETPIE RAEVEISQVV QSVSSTIANI EITPNQTQEQ PQEVEQPRSV VQVNEEAIIA
PTTPSAESLQ IEPATATTIE LIPTIAVTSN QKRSPKRFSK IPVRTLSTQS LHRESRNNTP
VEVEVNSELQ QNVEQDMPKA EETAVESAVV SVVVTPSEEA SEEIFEDAAE FSGEEQQLHD
DSPSEAELYS LDSEEHPPKS PDGAEVLLVL NPEQPMQNLS LAQSASNTSI SSHSSDEVEP
VVFKEFIPSG DPAKQNLSEL VEDTQRLIKQ MRDEISMDEF ESTDEDEYSE DYSDEYDEGE
EEDWYDSEGE EEEGTYNEQA SFIEEASSGA AGFVDEDGTE IEDIMEEDEL EAENEEAEEA
AAESSADIQQ TVTSTSSVTP TNHEDETAHG ATENVSFTGS TALEATIETE PAVAAAAASI
ASTEEAKAAV SENTALEPPL IPLTENRPAE LPAEIVLETK PQAEEPIALP IIPDPPIVDS
ETRPLELPSE TVLEEPKKVN PKKTTKTDAP NTAKANSTPK ASKIPKLTTN DNNTTPPPPP
TTTTTATTTT TTNKKLPLRS KSFSAPIGIS SVKRIQQEYL QKQTQSNGSS NSRVPLKSSP
SNRKSLSDAI KKFNTKTTLD DGPSTSAAVN ALLKPRSQPR IPKKKYHETC FSDDDYETSA
SEEAEQEQQS EMLQRKLSMP VFRAYPSVQE PVIEEPAVLA RKYVEQQLVT SIAEAQIAAT
LVNMKFQEDV ALWAARECSD LDQAISMLQQ ECELCMNSYP MNQIVSMLKC THKCCKQCAK
SYFTVQITDR SINDCSCPFC KLPELSNAVQ HEDEHLEYFS NLDIFLKSIL DNDVHELFQR
KLRDRTLLQD PNFKWCIQCS SGFFARPKQK RLICPDCGSV TCAQCRKPWE RQHEGTSCEA
YLEWKRENDP ELQAQGVQEH LAQNGIDCPK CKFRYSLARG GCMHFTCTQC KFEFCYGCAR
PFMMGAKCTI SPYCAKLGLH AHHPRNCLFY LRDKIPMQLQ FLLKEHNVKF DTEPMELADE
PSSSSKARAQ ARCPIPLQKE TPQGLVDTVC NSEVPDKHAG MCRTHYVEYL AGKVAKASID
PLPIFDLTDC VQELRRRGIA LPERGPWDTD EIYKTMCSEV IKQRIPLKSA
//
