ID A0A368FDM7_ANCCA Unreviewed; 369 AA.
AC A0A368FDM7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Convertase P-domain protein {ECO:0000313|EMBL:RCN30243.1};
GN ORFNames=ANCCAN_23988 {ECO:0000313|EMBL:RCN30243.1};
OS Ancylostoma caninum (Dog hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN30243.1, ECO:0000313|Proteomes:UP000252519};
RN [1] {ECO:0000313|EMBL:RCN30243.1, ECO:0000313|Proteomes:UP000252519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baltimore {ECO:0000313|EMBL:RCN30243.1,
RC ECO:0000313|Proteomes:UP000252519};
RA Mitreva M.;
RT "Draft genome of the hookworm Ancylostoma caninum.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000256|ARBA:ARBA00005325}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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:RCN30243.1}.
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DR EMBL; JOJR01001617; RCN30243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368FDM7; -.
DR STRING; 29170.A0A368FDM7; -.
DR Proteomes; UP000252519; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR034182; Kexin/furin.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR PANTHER; PTHR42884:SF3; FURIN-LIKE PROTEASE 1, ISOFORMS 1_1-X_2; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
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; PS00137; SUBTILASE_HIS; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000252519};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 234..369
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 40779 MW; CA2438F5950DD114 CRC64;
MENDITFGED EALVSKSRNR KQPDPNDPLW TDMWYLDARA SYDVNDRDDD PMPRYEYSDE
NRHGTRCAGE VAAIFNNSLC IVGIAYNARI GGIRMLDGDV TDAVEAASLG HNSDYVDIYS
ASWGPDDDGR TVDGPAKLTR AAFERGIREG RRGKGSVFVW ASGNGGKDAD SCNCDGYTNR
YGGHCHIVIR AAKPINLRAG DWVTNGVGRN VSHSFGYGLM DAGAMVQLAR NWTTAPEQHK
CRQFYPSRFK TIPHGNRLQL QLYTDGCAGS PDEQVVYLEH VQAIITLKAP KRGDIQIYLT
SPSGTRSTLL TKRARDTSRA GFIEWAFMTT HSWGELAAGL WTLEVDNDGW DGEILPVSLS
ILPSNSVFL
//
