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