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TRA1_DROME
ID   TRA1_DROME              Reviewed;        3790 AA.
AC   Q8I8U7; A0A140SQB4; A8DY44; Q2EZ47; Q8T3L7; Q9V9E9;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 4.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Transcription-associated protein 1;
DE   AltName: Full=dTRA1;
GN   Name=Nipped-A; Synonyms=Tra1; ORFNames=CG2905;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM F), TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND INTERACTION WITH SPT3; GCN5; ADA3 AND ADA2B.
RX   PubMed=12697829; DOI=10.1128/mcb.23.9.3305-3319.2003;
RA   Kusch T., Guelman S., Abmayr S.M., Workman J.L.;
RT   "Two Drosophila Ada2 homologues function in different multiprotein
RT   complexes.";
RL   Mol. Cell. Biol. 23:3305-3319(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E), FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16508010; DOI=10.1128/mcb.26.6.2347-2359.2006;
RA   Gause M., Eissenberg J.C., Macrae A.F., Dorsett M., Misulovin Z.,
RA   Dorsett D.;
RT   "Nipped-A, the Tra1/TRRAP subunit of the Drosophila SAGA and Tip60
RT   complexes, has multiple roles in Notch signaling during wing development.";
RL   Mol. Cell. Biol. 26:2347-2359(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 357-593 (ISOFORM F).
RC   STRAIN=Berkeley; TISSUE=Ovary;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [6]
RP   IDENTIFICATION IN THE TIP60 COMPLEX, AND FUNCTION.
RX   PubMed=15528408; DOI=10.1126/science.1103455;
RA   Kusch T., Florens L., Macdonald W.H., Swanson S.K., Glaser R.L.,
RA   Yates J.R. III, Abmayr S.M., Washburn M.P., Workman J.L.;
RT   "Acetylation by Tip60 is required for selective histone variant exchange at
RT   DNA lesions.";
RL   Science 306:2084-2087(2004).
CC   -!- FUNCTION: Part of the Tip60 chromatin-remodeling complex which is
CC       involved in DNA repair (PubMed:15528408). Upon induction of DNA double-
CC       strand breaks, this complex acetylates phosphorylated H2AV in
CC       nucleosomes and exchanges it with unmodified H2AV (PubMed:15528408).
CC       During wing development, required for activity of Notch and its
CC       coactivator mam (PubMed:16508010). Function in promoting mam function
CC       is likely to involve both the Tip60 and SAGA complexes
CC       (PubMed:16508010). {ECO:0000269|PubMed:15528408,
CC       ECO:0000269|PubMed:16508010}.
CC   -!- SUBUNIT: Component of the Tip60 chromatin-remodeling complex which
CC       contains the catalytic subunit Tip60 and the subunits Domino, Tra1,
CC       Brd8, E(Pc), DMAP1, Pontin, Reptin, Ing3, Act87E, BAP55, Mrg15, MrgBP,
CC       Gas41 and YL-1 (PubMed:15528408). Probable component of some SAGA
CC       complex (PubMed:12697829). Interacts with Spt3, Gcn5, Ada3 and Ada2b
CC       (PubMed:12697829). {ECO:0000269|PubMed:12697829,
CC       ECO:0000269|PubMed:15528408}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16508010}. Cytoplasm
CC       {ECO:0000269|PubMed:16508010}. Chromosome
CC       {ECO:0000269|PubMed:16508010}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=E {ECO:0000312|FlyBase:FBgn0053554};
CC         IsoId=Q8I8U7-1; Sequence=Displayed;
CC       Name=F {ECO:0000312|FlyBase:FBgn0053554};
CC         IsoId=Q8I8U7-2; Sequence=VSP_059312;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12697829}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       {ECO:0000269|PubMed:12697829}.
CC   -!- MISCELLANEOUS: Although strongly related to the PI3/PI4-kinase family,
CC       it lacks the typical motifs that constitute the catalytic site of
CC       PI3/PI4-kinase proteins, suggesting that it probably lacks such
CC       activity.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. TRA1 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM11122.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAN52145.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Insertion of several transposable element sequences.; Evidence={ECO:0000305};
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DR   EMBL; AY142217; AAN52145.1; ALT_SEQ; mRNA.
DR   EMBL; AE013599; ABI31023.2; -; Genomic_DNA.
DR   EMBL; AE013599; ABV53702.2; -; Genomic_DNA.
DR   EMBL; AY094769; AAM11122.1; ALT_INIT; mRNA.
DR   EMBL; DQ352451; ABD22987.1; -; mRNA.
DR   RefSeq; NP_001097192.2; NM_001103722.3. [Q8I8U7-1]
DR   RefSeq; NP_001303335.1; NM_001316406.1. [Q8I8U7-2]
DR   SMR; Q8I8U7; -.
DR   BioGRID; 61398; 31.
DR   IntAct; Q8I8U7; 20.
DR   MINT; Q8I8U7; -.
DR   STRING; 7227.FBpp0085431; -.
DR   PaxDb; Q8I8U7; -.
DR   PRIDE; Q8I8U7; -.
DR   EnsemblMetazoa; FBtr0303293; FBpp0292385; FBgn0053554. [Q8I8U7-1]
DR   EnsemblMetazoa; FBtr0347556; FBpp0312589; FBgn0053554. [Q8I8U7-2]
DR   GeneID; 35483; -.
DR   KEGG; dme:Dmel_CG33554; -.
DR   UCSC; CG33554-RA; d. melanogaster.
DR   UCSC; CG33554-RD; d. melanogaster.
DR   CTD; 35483; -.
DR   FlyBase; FBgn0053554; Nipped-A.
DR   VEuPathDB; VectorBase:FBgn0053554; -.
DR   eggNOG; KOG0889; Eukaryota.
DR   GeneTree; ENSGT00390000017961; -.
DR   InParanoid; Q8I8U7; -.
DR   OMA; NPIFAMD; -.
DR   PhylomeDB; Q8I8U7; -.
DR   SignaLink; Q8I8U7; -.
DR   BioGRID-ORCS; 35483; 1 hit in 3 CRISPR screens.
DR   ChiTaRS; Nipped-A; fly.
DR   GenomeRNAi; 35483; -.
DR   PRO; PR:Q8I8U7; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0053554; Expressed in eye disc (Drosophila) and 30 other tissues.
DR   ExpressionAtlas; Q8I8U7; baseline and differential.
DR   Genevisible; Q8I8U7; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR   GO; GO:0005703; C:polytene chromosome puff; IDA:FlyBase.
DR   GO; GO:0000124; C:SAGA complex; IDA:FlyBase.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
DR   GO; GO:0043486; P:histone exchange; IDA:UniProtKB.
DR   GO; GO:0043966; P:histone H3 acetylation; IDA:FlyBase.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0035222; P:wing disc pattern formation; IGI:FlyBase.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003152; FATC_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR003151; PIK-rel_kinase_FAT.
DR   InterPro; IPR014009; PIK_FAT.
DR   InterPro; IPR033317; TRA1/TRRAP.
DR   PANTHER; PTHR11139:SF1; PTHR11139:SF1; 2.
DR   Pfam; PF02259; FAT; 1.
DR   Pfam; PF02260; FATC; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   SMART; SM01343; FATC; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; SSF48371; 2.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Chromatin regulator; Chromosome;
KW   Cytoplasm; Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..3790
FT                   /note="Transcription-associated protein 1"
FT                   /id="PRO_0000088853"
FT   REPEAT          98..136
FT                   /note="HEAT 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          335..381
FT                   /note="HEAT 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          740..778
FT                   /note="HEAT 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1185..1223
FT                   /note="HEAT 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1332..1370
FT                   /note="HEAT 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1826..1864
FT                   /note="HEAT 6"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          2610..3173
FT                   /note="FAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT   DOMAIN          3429..3753
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   DOMAIN          3758..3790
FT                   /note="FATC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00535"
FT   REGION          3435..3441
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          3616..3624
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          3636..3661
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   VAR_SEQ         1999..2048
FT                   /note="VGSHTKPDDILRSIDKSYCDTVLNFLIRLACQVNDPQAPILSPGESLSRR
FT                   -> K (in isoform F)"
FT                   /id="VSP_059312"
FT   CONFLICT        468
FT                   /note="A -> T (in Ref. 5; AAM11122)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   3790 AA;  435330 MW;  366CF25BBC7C5435 CRC64;
     MSVIENVPVN TFRNYLNILN DSSSKDELKL KATQELSEHF EMIMQSPAYP SFLDNSLKIF
     MRILQDGEPQ FIQENTMQHI RKLILEMIHR LPITESLRQH VKTIITMMLK ILKTDNEENV
     LVCLRIIIEL HKHFRPSFNS EIQLFLGFVK EIYTNLPNHL TSIFETSNDV WVTDLKDLNL
     EVLLSESYSV RTIHVEKALD SNSQQQIYNL LPRGILSLKV LQELPIIVVL MYQIYKNAVH
     QEVSEFIPLI LTTINLQPTV TRRNSPQKEI YVEFMGAQIK TLSFLAYIVR IFQEVVIASS
     LSVTSGMLNL MKNCPKEAAH LRKELLIAAR HIFATDLRQK FIPSIEQLFD EDLLIGKGVT
     LDSIRPLAYS TLADLAHHVR QSLNIDVLIK AVNLFSKNVH DESLAVGIQT MSCKLLLNLV
     DCLRHHSETE PQRSKALLSK LLKVFVKKFE TIAKIQLPLI IQKCKGHAFS GALVNSSGNA
     SLSHINAPDL KDDISNIQVS ASGSQWIYSV NVAEFRSLVK TLVGGVKTIT WGFFNSKFQL
     TDTKLANHEK IFGPEIVCSY IDLVYYAMEA LDIYTINVNP NQQRTSGLIS RSKEEKEVLE
     HFSGIFLMMH SQNFQEIFST TINFLVERIY KNQSLQVIAN SFLANPTTSP LFATVLVEYL
     LNKMEEMGSN LERSNLYLRL FKLVFGSVSL FPVENEQMLR PHLHKIVNRS MELALISEEP
     YNYFLLLRAL FRSIGGGSHD LLYQEFLPLL PNLLEGLNRL QSGFHKQHMR DLFVELCLTV
     PVRLSSLLPY LPMLMDPLVS ALNGSPTLIS QGLRTLELCV DNLQPDFLYD HIQPVRAALM
     QALWKTLRNQ DNAALVAFRV LGKFGGGNRK MMVEPQALSY IINDKPTISI VTYFQEYETP
     IDFPVDEAIK SAFRALGSNS TDQFYRRQSW EVIRCFLAAF ISLDDEKHML LKLFTHVDFV
     ENKIMNWSTF QHKAGNETVR ETHQTALIGM LVASATKDLR DSVCPVMAAV VRHYTMVAIA
     QQAGPFPQKG YQATHGIDPM ILIDALASCM GHEEKELCKP GIACMGIILD TATNIMGNKD
     RACKLPIIQY LAEKMVSLCY DRPWYSKVGG CQAIQFLCKH MSLRALFQNL FNFLKAFMFV
     LMDLEGDVSN GAIEITKSYM KSMLEICLTP INECYKNIDL KDLQAKATYE VIHELVRHIT
     SPNTIVREES MVLLKHIGTI QSKTVSEVMD PHKDVLADII PPKKHLLRHQ PANAQIGLMD
     GNTFCTTLEP RLFTIDLTNT YHKLFFHELL TLSEAEDATL AKLDCYKNVP NLIPLRTSAL
     RALAACHYIS DIGYKEKIIN IIFKVMESDK SELQTTAFHC MKHFITGVTL EKEKVQSAMR
     PLLLKLGDHR NLSIPAIKRL SYFTQIFPQM FNEKLSEQIL QHCSKIMEIF VSEYKSTSPN
     VNFFASSKGG EYEQKIVILI EMFFYISASV KYIEKLCQLV LKTEKNLMIE ASSPYREALI
     KFLQRFPTET VDLFLTESLM IDPQWNRLFI YLLKHETGVS FRAVIKSSRY NNLIHYLNTH
     TEFPEALKYE IQHQAVLIIF TLMESDDQWI PTRQDIVDAL KNCWQNYLST LSSEDVLCDL
     WHLIGKILLH YFSNNTNDIE LLFQLLRALC FRFIPDVYFL RDFLQHTVAQ SFTVNWKRNA
     FFYFVENFNN SFLSEELKAK IITAVIIPCF AVSFDKGEGN KLIGAPPTPY QEDEKNIVSV
     FINKVFDPDK QYDDAVRIAL LQLACLLVER ASQHIHDGDA NNKRQGNKLR RLMTFAWPCL
     LSKSSVDPTA RYHGHLLLSH IIARLAIHKK IVLQVFHSLL KGHALEARSI VKQALDVLTP
     AMPLRMEDGN TMLTHWTKKI IVEEGHAMQQ LFHILQLIIR HYKVYFPVRH QLVQHLINYM
     QRLGFPPTAS IEHKKLAVDL AEVIIKWELH RIKDDRETKT DGTEEELIQE SSVKRSGIDL
     VETRKKSFDI IRETTVQGVG SHTKPDDILR SIDKSYCDTV LNFLIRLACQ VNDPQAPILS
     PGESLSRRCV MLLKMAMRPE IWPQPFDIKL NWLDKVLATV ETPHHNLNNI CTGIDFLTFL
     TTILSPDQLV SIIRPVQRGL SLCIIHQNTR IVRLMHMFLT RIMAIFPPDT QHKHEDLDLL
     YTAVSKMIAE NLTSYEKSPQ PNASSLFGTL MILKACTTNN ASYIDRILVQ FIRVLNHLTR
     DHINTIGGNT VISQSPDSNA LPLELLVLSL ELIKNRIFVM SVEIRKLFIG TILVSLIEKS
     TEVKIIKCII KMLDEWIKTK EPNVMTQVPS IREKSALLVK LMQNVEKKFT DEIELNIQFL
     EIINFIYRDE ILKQTELTNK LEGAFLNGLR FQNPNVRSKF FEILDSSMRR RLHDRLLYII
     CSQAWDTIGS HYWIKQCIEL LILTANTMMQ IQCSNEQFKI PSITSVIPVN SSETQENSFV
     SFLSSHSESF DIIQTVDDKD DVYDIDLNAD RKEDCQQILP NRRVTLVELV YKQAEFLEAN
     RNIRTDQMLV ATSQLCHIDT QLAQSVWLSM FPRIWSIFTE DQRCNITKEL IPFLSSGTNV
     NQKDCHPSTL NTFVESLTKC APPIYIPPNL LAYLGKSHNL WHRAILVLED MAVNQSMQSK
     DIDGGENQFS DLDVQQSNNI FDSLSKMYSS MHEEDLWAGL WLKFAHYPET NIAVSYEQMG
     FFEEAQGAYD LAMTKFKQDL SNGVVNTYVN SELLLWENHW MRCAKELNQW DILLDYAQTN
     KDKNMFLILE SSWRVPDWNL MKIALAKTEQ CYLKHYGFKI NLYKGYLSIL HQEERQTGNI
     ERYVEIASSL CIREWRRLPN IVSHIHLPYL QASQQIMELH EASQIHQGLA QSRNNSLHDM
     KAIVKTWRNR LPIISDDLSH WSDIFTWRQH HYQIITQHLE QQSDQGSTML GVHASAQAII
     SFGKIARKHN LTGVCQETLS RIYTIPSVPI VDCFQKIRQQ VKCYLQMPST SGKNEINEAL
     EVIESTNLKY FTGEMNAEFY ALKGLLLAQI GRSEEAGKSF SVAAQLHDGL TKAWAMWGDY
     MEQIFLKERK ITLAVDALIC YLQASRNQIE SKTRKYIAKV LWFLSYDNNT KILISTLEKH
     VAGIPPSYWL PWIPQLLCCL EQFEGDVILN LLSQIGRLYP QAVYFPIRTL YLTLKIEQRE
     KHKTAEQAVK SSCSNIDGTT LSFGRGASHG NIPSINPIKA TPPMWRCSKV MQLQREVHPT
     ILSSLEGIVD QMVWFRESWT EEVLRQLRQG LIKCYAIAFE KRDTVQHSTI TPHTLHFVKK
     LGSTFGIGIE NVPGSVTSSI SNSAASESLA RRAQVTFQDP VFQKMKEQFT NDFDFSKPGA
     MKLHNLISKL KTWIKVLETK VKKLPTSFLI EDKCRFLSNF SQKTAEVELP GELLIPLSSH
     YYVRIARFMP RVEIVQKNNT AARRLYIRGT NGKIYPYLVV LDSGLGDARR EERVLQLKRM
     LNYYLEKQKE TSRRFLNITV PRVVPISPQM RLAEDNPNSI SLLKIFKKCC QSMQVDYDMP
     IVKYYDRLSE VQARGTPTTH TLLREIFSEI QWTMVPKTLL KHWALKTFLA ATDFWHFRKM
     LTLQLALAFL CEHALNLTRL NADMMYLHQD SGLMNISYFK FDVNDDKCQL NQHRPVPFRL
     TPNVGEFITH FGITGPLSAA IVATARCFIQ PNYKLSSILQ TILRDEIIAL QKKGFRECKL
     IEGSEDRYSD GNCMEHSVNI VNSAVDIIMT RFNKISYFDS IENKKISVLV QSATNIDNLC
     RMDPAWHPWL
 
 
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