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Database: UniProt
Entry: L5LVP3_MYODS
LinkDB: L5LVP3_MYODS
Original site: L5LVP3_MYODS 
ID   L5LVP3_MYODS            Unreviewed;      2677 AA.
AC   L5LVP3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=E3 SUMO-protein ligase RanBP2 {ECO:0000313|EMBL:ELK30137.1};
GN   ORFNames=MDA_GLEAN10004208 {ECO:0000313|EMBL:ELK30137.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK30137.1, ECO:0000313|Proteomes:UP000010556};
RN   [1] {ECO:0000313|Proteomes:UP000010556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
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DR   EMBL; KB107320; ELK30137.1; -; Genomic_DNA.
DR   eggNOG; KOG0864; Eukaryota.
DR   eggNOG; KOG0865; Eukaryota.
DR   Proteomes; UP000010556; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR   GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd14684; RanBD1_RanBP2-like; 1.
DR   CDD; cd13177; RanBD2_RanBP2-like; 1.
DR   CDD; cd14685; RanBD3_RanBP2-like; 1.
DR   CDD; cd13178; RanBD4_RanBP2-like; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 4.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR022011; IR1-M.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR000156; Ran_bind_dom.
DR   InterPro; IPR045255; RanBP1-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   PANTHER; PTHR23138:SF169; E3 SUMO-PROTEIN LIGASE RANBP2; 1.
DR   PANTHER; PTHR23138; RAN BINDING PROTEIN; 1.
DR   Pfam; PF12185; IR1-M; 2.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   Pfam; PF00638; Ran_BP1; 4.
DR   Pfam; PF00641; zf-RanBP; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00160; RanBD; 4.
DR   SMART; SM00028; TPR; 1.
DR   SMART; SM00547; ZnF_RBZ; 1.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 4.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50196; RANBD1; 4.
DR   PROSITE; PS50005; TPR; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:ELK30137.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT   REPEAT          49..82
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          1083..1219
FT                   /note="RanBD1"
FT                   /evidence="ECO:0000259|PROSITE:PS50196"
FT   DOMAIN          1262..1291
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          1494..1630
FT                   /note="RanBD1"
FT                   /evidence="ECO:0000259|PROSITE:PS50196"
FT   DOMAIN          1791..1927
FT                   /note="RanBD1"
FT                   /evidence="ECO:0000259|PROSITE:PS50196"
FT   DOMAIN          2387..2522
FT                   /note="RanBD1"
FT                   /evidence="ECO:0000259|PROSITE:PS50196"
FT   DOMAIN          2543..2677
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   REGION          740..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1057..1084
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1391..1410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1673..1706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1758..1789
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2039..2070
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        748..779
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1067..1084
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1680..1706
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1758..1777
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2053..2067
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2677 AA;  300722 MW;  CEA34346D6CB2BF5 CRC64;
     MEFIFLLSID MCLKSMKGFY FAKLYYEAKE YDLAKKYIST YINVQERDPK AHRFLGLLYE
     VEENIDKAVE CYKRSVELNP TQKDLVLKIA ELLCKNDVTD GRAKYWVERA AKLFPGSPAI
     YKLKEQLLDC KGEDGWNKLF DLIQSELYAR PDDVYVNIRL VELYRSNKRL KDAVAHCHEA
     ERNVALRSSL EWNLCVVQTL KEYLESSDKS NWQATNKDLL LAYANLMLLT LSTRDIQESR
     DLLESFDGAL QSVKSCVGGN DELSAVFLEI KGHFYMHAGS LLLKMGQHSD VQWRALSELA
     ALCYLIAFQV PRPKIKLIKG EGGQNLLETM AFDRLSQSGH MLLNLSRDKQ DFLKEVVESF
     ANKSGQSALY DALFSGQSPK DSSFLGSDDI GNIDVQAPKI DDLARYDVGA IRAHNGSLQH
     LTWLGLQWNL LPTLPAIRKW LKQLFHHLPQ ETSRLETNAP ESICILDLEV FLLGVIYNSQ
     LQLKEKCSSH YNFYQPLCLP FPVCKQLYTE RQKSWWDAVC NLIHRKAIPG TSAKLRLLVQ
     RDINALRGQE KHGLQPALLI HWATYLQKTG SDLNSFYDQR EYIGRSVHYW KKVLPLLKMI
     KKKISIPEPT DPLFKHFHSA DIQASEIGEY EEEAHITFAI LDAVNGNIED AMTAFESIKN
     VVSYWNLALI FHRKAEDIEN EAHSPEEQEE CKNYLRKTRD YLMKILDDSD SNLSVVKKLP
     VPLESVKDML NSVKQQLDDY SEGGPLYKNG SLRNTDSEMK YSTPSPTKYS LSPSKSYKYS
     PKAPPQWAED QNSLLKMICQ EVEAIKKEMQ ELKLNSSNLG SPHRWPTEGY GPDSVPDGYQ
     GSQTFHGAPL TVATTGTSVY YSQSPAYNSQ YLLRPAANVT PTKGPVYGMN RLPPQQHIYA
     YSQQMHTPPV QSTSACMFSQ EMYGPPLRFE SPATGILSPR GDDYFNYNIQ QTSTNPPLPE
     PGYFTKPPVA AHASRSAESK VIEFGKTNFV QPMPGEGIRP SLTAPAHTTQ PPFKFNSNFK
     SNDGDFTFSS PQVVTQPPSM TYNNSESLLG KSVFGTPAPE VANKNHEADG GSAHGDDDDD
     GPHFEPVVPL PDKIEVKTGE EDEEEFFCNR AKLFRFDAES KEWKERGIGN VKILRHKTSG
     KIRLLMRREQ VLKICANHYI SPDMKLTPNA GSDRSFVWHA LDYADEFPKP EQLAIRFKTP
     EEAALFKCKF EEAQNILKTS GAKFSTSETS KATKSGFEGM FTKKEETCKA TKSGFEGMFT
     KKEGQWDCSV CFVQNESSSL KCVACDASKP THKPNPEASS AFTLGSKAKL SDSSGNQVGT
     GFKSNFSEKA FKFGITEQGF KFGHMDQENT PSFTFQSSNT DSNSTIEGFN FSVPVLADGF
     KFGIQELGNQ EKKSEKPLEN DNDFQAQGVS SQKNDTGVVF GQTGSTFTFA DLAKSTSGEG
     FQFGKKDPNF KGFSGAGEKL FSLQSGKKAD KADTSTDIEK DDDAYKTEDS DDIHFEPVVQ
     MPEKVELVTG EEDEKVLYSQ RVKLFRFDAE ISQWKERGLG NLKILKNEVN GKLRMLMRRE
     QVLKVCANHW ITTTMNLKPL SGSDRAWMWL ASDFSDGDAK LEQLAAKFKT PELAEEFKQK
     FEECQRLLLD IPLQTPHKLV DTGRAAKLIQ RAEEMKSGLK DFKTVLTNDQ TKVTEEESKN
     SDAGAVSVSD ITTKPNPENT GPTVEWSNYD LREDALDDSV SSSSVHASPL ASSPVRKNLF
     RFGESTTGFN FSFKSALSPS KSPALLNQSG TTVGNDEESD VTQEEERDGQ YFEPVVPLPD
     LVEVSSGEEN EQVVFSHRAK LYRYDKDVGQ WKERGIGDIK ILQNYDNKQV RIVMRRDQVL
     KLCANHRITP DMTLQNMKGT ERVWVWTACD FADGERKVEH LAVRFKLQDV ADSFKKIFDE
     AKIAQEKDSL ITPHVSFSTT PRESPCGRIA VAVLEETTKE RTDLLQGDDI ADATSEVGDV
     SSTSEIATKA VVSPPKFVFG SESVKSIFGS EKSKPFTFGN SSATGSLFGF SFNAPLKTSE
     TSSGVQSGSE REVEPNNCEE SKNSDIKQSP DGKVQNLFAA FPKEEFSTNY TFKTPEKAKE
     KIKPEDPPSD EDVLIVYELT PTPEHRALAS KLKLPPTFFC YKNRPDYVSE EEEDDEDFET
     AVKKLNGKLY LDDSEKYKPL EKSVTENEKE CIIVWEKKPT VEEKAKADTL KLPPTFFCGV
     GSDTDEDNGN GEDFQSELQK VQEAQKSHNE EITSMADSVC TGGTKVTVPF LCKSEEPDFI
     TKSICSSSTF SGTVDKPVDL STRKDNDADS TSQVESKTIS FGFGNNTGLS FADLASSNSG
     DFAFGSKDKN FQWANTGATV FGTQSTNKVG EEEDGSDEEV VYNEDIHFEP IVSLPEVEVK
     SGEEDEEILF KERAKLYRWD RDVNQWKERG VGDIKILWHT LKNYYRILMR RDQVFKVCAN
     HVITKTMELK PLNVSNNALV WTASDYADGE AKVEQLAVRF KTKEMADCFK RKFEECQQNL
     LKLQKGQVSL TAELSKETNP VVFFDVCADD EPLGRITMEL FSNIVPQTAE NFRALCTGEK
     GFGFKNSIFH RVIPDFVCQG GDITKHDGTG GRSIYGDKFE DENFNLARHL DYVQMHTNTS
     DMPQTKVRSY PSGVDHPGEP SIWLDATCTR DAVVTRQ
//
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