ID Q9UVD1_PNECA Unreviewed; 493 AA.
AC Q9UVD1;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Kexin-like serine endoprotease {ECO:0000313|EMBL:AAF21601.1};
DE Flags: Fragment;
OS Pneumocystis carinii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Pneumocystomycetes; Pneumocystaceae; Pneumocystis.
OX NCBI_TaxID=4754 {ECO:0000313|EMBL:AAF21601.1};
RN [1] {ECO:0000313|EMBL:AAF21601.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Rat {ECO:0000313|EMBL:AAF21601.1};
RA Russian D.A., Andrawis-Sorial V., Kovacs J.A.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; AF009222; AAF21601.1; -; mRNA.
DR MEROPS; S08.011; -.
DR VEuPathDB; FungiDB:T552_01616; -.
DR VEuPathDB; FungiDB:T552_02426; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR003882; Pistil_extensin.
DR PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR01218; PSTLEXTENSIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AAF21601.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 475..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..219
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 216..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..322
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..413
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAF21601.1"
SQ SEQUENCE 493 AA; 54146 MW; 2D896F9D94155C0D CRC64;
CTTKHTGTSA STPIAAGIIA LILSKRSDLT WRDVQALIVY TAVPFNLNYH EWDQLPSGRY
YNNFFGFGKL DAYAMVQQAK TFQKLNPQTI FSTQLIQVNK KFSENNGHIT STFYIHRDYP
THYKFKNLEY ICVSFCYKHQ YRGHLEFSIT SPANVTSQLA HRRPRDKHSG IVYWTFMSVK
HWGEKIVGNW TIDVEDKKDQ NLDGEVFDWQ LHFFGESSES EGVPPPSYPF LSRYPTTTPP
PDPDATSPPD PDANLPPDSN ADPQPPSEPA PPSEPESQPS SEPGSQPPSK PGPQPPSDPQ
PPSDLKPPSK PDARPRPPSD PSSQQDPDTS LSSNPTSTSS SEPPPPSPPP PPPPPPAPAP
APAPPRPELE PEPEPGPEPV PQPPQPQPPQ PQPEPPAXPP KPQPPPPSPP EQKPTSITSS
TSTTSSSKTK ISTTRKASST KASSTTKTST RPSPTEGTFT GSSASHLSFF EKRHLLLQMI
LLLFFFLFLG YSF
//