ID G0MHR2_CAEBE Unreviewed; 410 AA.
AC G0MHR2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGT59365.1};
GN ORFNames=CAEBREN_22193 {ECO:0000313|EMBL:EGT59365.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; GL379795; EGT59365.1; -; Genomic_DNA.
DR AlphaFoldDB; G0MHR2; -.
DR STRING; 135651.G0MHR2; -.
DR MEROPS; C01.A43; -.
DR EnsemblMetazoa; CBN22193.1; CBN22193.1; WBGene00160918.
DR eggNOG; KOG1542; Eukaryota.
DR HOGENOM; CLU_012184_1_3_1; -.
DR InParanoid; G0MHR2; -.
DR OMA; ACKNEVI; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02248; Peptidase_C1A; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR PANTHER; PTHR12411:SF949; PROTEIN CBG17217; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 58..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..156
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 194..409
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 410 AA; 46209 MW; 89D3D4C7B7238520 CRC64;
MVAISLFKEE DEKAPMAPMA PAYRMEHHPL AMQQCRVPGC QQQESFDTFV MRKALRTFLG
IIVFGFLCVL ALQYAHYLGP QPKAPKLEKG IQNIAQEYIA YTEKYNKSYA TSHESLKRLN
AYYTTEENIA NWNKQSEHGS AVYGHNDLSD WTDAEFIKTL LPKTFYQRLH EDAEFITPIP
ESLAAMKGER NGPLPDFFDW RDRNVVTPVK AQGQCGSCWA FASTATVEAA YAIAHGERRN
LSEQTLLDCD LVDNACDGGD EDKAFRYIHR NGLAYAVDLP YVAHRQNGCA VTDNWNTTRI
KAAYFLHHDE DSIINWLVNF GPVNIGMSVI QPMRAYKGGV FTPSEYACKN EVIGLHALLI
TGYGTSEKGE KYWIVKNSWG NTWGVEHGYI YFARGINACG IEDEPIGILA
//
