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UFSP2_DROPS
ID   UFSP2_DROPS             Reviewed;         608 AA.
AC   Q2M1D1;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Probable Ufm1-specific protease 2 {ECO:0000250|UniProtKB:Q9NUQ7};
DE            Short=UfSP2 {ECO:0000250|UniProtKB:Q9NUQ7};
DE            EC=3.4.22.- {ECO:0000250|UniProtKB:Q99K23, ECO:0000250|UniProtKB:Q9NUQ7};
GN   ORFNames=GA14252;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Thiol protease which recognizes and hydrolyzes the peptide
CC       bond at the C-terminal Gly of UFM1, a ubiquitin-like modifier protein
CC       bound to a number of target proteins. Does not hydrolyze SUMO1 or ISG15
CC       ubiquitin-like proteins. {ECO:0000250|UniProtKB:Q99K23,
CC       ECO:0000250|UniProtKB:Q9NUQ7}.
CC   -!- SIMILARITY: Belongs to the peptidase C78 family. {ECO:0000305}.
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DR   EMBL; CH379069; EAL30643.1; -; Genomic_DNA.
DR   RefSeq; XP_001353142.1; XM_001353106.3.
DR   AlphaFoldDB; Q2M1D1; -.
DR   SMR; Q2M1D1; -.
DR   STRING; 7237.FBpp0274790; -.
DR   MEROPS; C78.A01; -.
DR   EnsemblMetazoa; FBtr0276352; FBpp0274790; FBgn0074281.
DR   GeneID; 4812951; -.
DR   KEGG; dpo:Dpse_GA14252; -.
DR   eggNOG; KOG2433; Eukaryota.
DR   HOGENOM; CLU_021066_1_0_1; -.
DR   InParanoid; Q2M1D1; -.
DR   OMA; CGLVKFG; -.
DR   PhylomeDB; Q2M1D1; -.
DR   Proteomes; UP000001819; Chromosome X.
DR   Bgee; FBgn0074281; Expressed in female reproductive system and 3 other tissues.
DR   GO; GO:0071567; F:deUFMylase activity; ISS:UniProtKB.
DR   GO; GO:0016790; F:thiolester hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR012462; Peptidase_C78_UfSP1/2.
DR   Pfam; PF07910; Peptidase_C78; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..608
FT                   /note="Probable Ufm1-specific protease 2"
FT                   /id="PRO_0000280373"
FT   ACT_SITE        441
FT                   /evidence="ECO:0000250|UniProtKB:Q99K23"
FT   ACT_SITE        565
FT                   /evidence="ECO:0000250|UniProtKB:Q99K23"
FT   ACT_SITE        567
FT                   /evidence="ECO:0000250|UniProtKB:Q99K23"
SQ   SEQUENCE   608 AA;  68497 MW;  7F54B6889904CE7D CRC64;
     MLPKLKISAF LLKRLERVKQ QSSGCLYGVF YGDGTLLLLS FNLSNVGQLN YEQIQHRFPA
     ELDLCGLVKF GDCTDAEAHL NEVIKSVDIT DNPILLKCEL GTLVGMRASF FVHGKLEEVP
     YDVMDSEQLY NDFCFTRLQC GFYLQTAATP ECVAKEMHVL RKRVADGNLV FKVPHTNIYI
     HSCGPMDNKL RGESRINDLV QAIPIPSGKE NVVADKKKSK TAAQTQLAKH FGATGCEYDL
     INIDVMRIRT RDLLARDSPP HPALSIAVTT EEQTRAQVPL EIEAMAMLCK NTKLQRLYDV
     LIESICRALR LFEQSLNEHL AESEGGSLAV PRSHHFYPQG FGHFLSCAYL EGLGDDEPIM
     QERRKRLHRQ FSLPVTRPYF RRANQCHFQG EVDDAPWTPL LNTHVGVRPS AVTDGKEYLV
     NGNYHYYHYL QQQVQDKGWG CAYRSLQTIC SWFVLQGYTN APIPTHLEVQ KYLHKINDKP
     SSFVGSSQWI GSTEISMCLQ GFLKVDSKIL HVSSGAELPT IASELAMHFQ TQGTPVMIGG
     GVLAHTIIGV DYCVQSGEVK FLILDPHYTG ADELATIQIK GWCGWKSMDF WSKGSYYNLC
     MPQRPILY
 
 
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