ID A0A016WCN5_9BILA Unreviewed; 787 AA.
AC A0A016WCN5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Peptidase, S9A/B/C family, catalytic domain protein {ECO:0008006|Google:ProtNLM};
GN Name=Acey_s0794.g2388 {ECO:0000313|EMBL:EYC37400.1};
GN Synonyms=Acey-dpf-2 {ECO:0000313|EMBL:EYC37400.1};
GN ORFNames=Y032_0794g2388 {ECO:0000313|EMBL:EYC37400.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC37400.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
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:EYC37400.1}.
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DR EMBL; JARK01000394; EYC37400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016WCN5; -.
DR STRING; 53326.A0A016WCN5; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF200; DIPEPTIDYL PEPTIDASE FAMILY MEMBER 2; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 113..499
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 587..779
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 16..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 787 AA; 88817 MW; 270BB252CD02183D CRC64;
MESCWNSSVY EGSASVNLNG SATQTPSDDS ENRTASRLQF RRRPTYRKFT FEDLFSGKVF
LKDSYTTGWT RNGGLIQTKD EFLGGTTVAT VIHPGTFDAV DYLSDSTLMH SLSSNEKYAF
VSKNIKQIFR HSNEELFEIS RMINGTPSER TFPVGPKGDG LETILTFEWN PNINKNDFVF
VHEYNIYYQL DPEKPGTVRQ LTDDGGYLLR YGVPDWLYEE EILSSGTAIW WSESGQHIAY
IRFDDRSVNR IYIPKYTKGS QYPQYEEIPY PKAGVEENPL VRLYIWTVKT NRTVIAEPPA
DLTRTNQSYY IFSNTWLAMP ANLRHSLGEE RLFTAWATRE QNLVYITLCN EIDCVLTHVQ
SFTVNGRSMW AEPADFKNVF ASKSGFFLLL PHAYNDGNIY NHIAHMQIQK NGSGQITAWH
GGAYDIREIK GYDMTSDTLT FISAGGGLGT MRLYKVSQAT SANKSNIVAL SSFLPDCDYG
THEVSPNGKR AVMSCIKPFQ NTKMYIMDVE KPSSNKLLEG AEEAHIPFDL PELSYEIVKL
PSGYEVHIGI MKPPKFDPTL KYPLLVDVYG GPNSCKVRQS TPNPNMIHFC STLGAVVAWI
DGRGSSNRGW NLKAPVYKAL GQFETIDTID AVKYLTEKYS FIEKEQVAVF GWSYGGFLST
HVAMRDQGET FKCAVAVAPV VDFMLYDSAY TERYLGIPLE NPAGYNASQL LNKASLLENV
KYLLAHGEAD DNVHFQNSAL LAETLQGELV HFTQLVYSNQ DHSMGSRQAH LFMEIGRFLS
EECFSED
//