ID A0A4U5PBX6_STECR Unreviewed; 473 AA.
AC A0A4U5PBX6;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=Peptidase C1A papain C-terminal domain-containing protein {ECO:0000259|SMART:SM00645};
GN ORFNames=L596_008262 {ECO:0000313|EMBL:TKR93889.1};
OS Steinernema carpocapsae (Entomopathogenic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC Steinernema.
OX NCBI_TaxID=34508 {ECO:0000313|EMBL:TKR93889.1, ECO:0000313|Proteomes:UP000298663};
RN [1] {ECO:0000313|EMBL:TKR93889.1, ECO:0000313|Proteomes:UP000298663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALL {ECO:0000313|EMBL:TKR93889.1,
RC ECO:0000313|Proteomes:UP000298663};
RX PubMed=26392177; DOI=10.1186/s13059-015-0746-6;
RA Dillman A.R., Macchietto M., Porter C.F., Rogers A., Williams B.,
RA Antoshechkin I., Lee M.M., Goodwin Z., Lu X., Lewis E.E.,
RA Goodrich-Blair H., Stock S.P., Adams B.J., Sternberg P.W., Mortazavi A.;
RT "Comparative genomics of Steinernema reveals deeply conserved gene
RT regulatory networks.";
RL Genome Biol. 16:200-200(2015).
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TKR93889.1}.
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DR EMBL; AZBU02000002; TKR93889.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U5PBX6; -.
DR STRING; 34508.A0A4U5PBX6; -.
DR Proteomes; UP000298663; 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; cd02620; Peptidase_C1A_CathepsinB; 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; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR PANTHER; PTHR12411:SF356; PEPT_C1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000298663};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 75..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 188..472
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 53108 MW; DAD31B10E28A594B CRC64;
MSSSPSKSSR RSRPSTTGGY SKLSEEPLAA EDNQPSSAVR SRHRSRHRYS DSVMKKKPES
ESQAELRPRR KHTPLCVLLI VICVVVIAIA LTCVALAVLY HVNEQRKTFR EVQSYLKKMV
ADVNNAENRQ WKAEFNRFGM RKTHYDFAYN KKNASAIQDY VDQLKTYFDS PTMKRHLKEL
EEFPADSLPT HFDARAKWPH CPSIANVPNQ GGCGSCYAVS AVGVASDRAC IASNGTEQGV
LSVEDVLGCC SVCGNCFGGD PLKAMVYWAR EGLVTGGRDG CRPYGVTLEC GTPCTPDAYS
AGEQRRTCIK HCQKTYYRNV YEADKHYGAI AYTMYPRTMM MNEDGVREKI PSVVGHFNDS
SPHPLSEAEI KNIIMKELFL FGPTTLAFPV TEEFLHYAEG IFSPFPQSEI YDRVVYWHVV
KLIGWGHDDN GNQHWLAVNS FGDHWGDNGL FRIDTALLDD AGLEYETGLY RAE
//
