ID A0A074ZKP6_9TREM Unreviewed; 1538 AA.
AC A0A074ZKP6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=P/Homo B domain-containing protein {ECO:0000259|PROSITE:PS51829};
GN ORFNames=T265_06397 {ECO:0000313|EMBL:KER26352.1};
OS Opisthorchis viverrini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=6198 {ECO:0000313|EMBL:KER26352.1, ECO:0000313|Proteomes:UP000054324};
RN [1] {ECO:0000313|EMBL:KER26352.1, ECO:0000313|Proteomes:UP000054324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT "Opisthorchis viverrini - life in the bile duct.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; KL596750; KER26352.1; -; Genomic_DNA.
DR RefSeq; XP_009169909.1; XM_009171645.1.
DR STRING; 6198.A0A074ZKP6; -.
DR GeneID; 20320576; -.
DR KEGG; ovi:T265_06397; -.
DR CTD; 20320576; -.
DR OrthoDB; 2996957at2759; -.
DR Proteomes; UP000054324; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00064; FU; 3.
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; 1.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_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; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR42884:SF23; FURIN-LIKE PROTEASE 2; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00261; FU; 8.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000054324};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1324..1347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 415..557
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 1354..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 73
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 315
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1538 AA; 168847 MW; BE080120573FC454 CRC64;
MYIFSFKVVW AERQVPLIRE KRSLSPSVRW NDPLYPQMWY IIRNDLNQGY DMNVQEAWML
GYSGKGVVVT IMDDGVDHNH TDLKKNYVYQ FSSGLYKFGV PPTRDPQASY DFNDNDPDPM
PNWRSSTNNS LCVSATVFSK HGTRCAGQVA AEGNNSKCMV GIAFNSRIGG IRMLDGYITD
RLEADTLHFR NDHIHIYSGS WGPEDTGKLY EGPGVLTQSA FQKGIASGRN NFGNIYVWAS
GNGGSQYDSC ACDGYASSPF TLSVSGVGER NLRPWYLEEC SSTLVTTYSS GAHSEKMIAT
VDPNQKCTTT HTGTSASAPI AAGIIALLLE ANPRLSWRDV QYVTLLAANP APFLDGNFTK
NAVGRSYSLL YGYGLMDAGK MVRLGELWRG LPPHHQCTSR VMNYKARLDG IFNLTFPLVF
YGCDSVPRSE NETYSNYTEK SSEEGSPVVY LEHVQLYADI VYQRRGLLQI TLISPSGTKT
VLLPPRRHDE HSGNIGLLTW PLTTVQLWGE SAKGTWYIRV DNLAASKPML GMGSVNMDSV
NGYWRSAWII AYGTDKYPIR LRPPNPERPP PPNFPCNLNF PPYLMFSFPP PSLLSPLCAR
THTQTTALRV KQEWFAPFAK YVVDDSLWKE VYTNGTTISN KAERLDRWAE YFEQQLSWPP
AGTYLEPTGE VEPWTVIVEP PTASEVYDCI CSLKRHRAPG PDDLPPALFK DGGEVLSQRL
SDQFACIWEK ESVPDNWGKS VIVPIFKKGR VCHVECAPGG CTGPGADQCL GGCRHYATQS
RQCVPECPRG TTPYGALRIS VNHADYNAEK THRNRVRPGR IRSSNSFVAN VVCQPCWTLC
GTCVRPHTEY DCMSCSNGRY LLPLITPDDA SDVTMMIVSE VDSDEANKKL PSLVGTCRTE
CPVGYYANKS SSICNRCSAN CMECSGPGTG ECSKCNSGFR LTLGRCVDGN SVDGRCSPGQ
YLKDSHCVDC DQGCDPTGCL PDGDCSRCKS DFPYILNSSC VKACPTGWFA GPPLPDPFTL
ASTSPHDAVS HPRRCEPCPP GCQDCTAFEN CTRCADGLNL QNGTCISTSA SLPCHPQCAT
CFRSPFDCLT CPHDRVLLPN VLIEQVRSKL LFHTASLRSR AQQTESTTPI AMTSSYLCPS
VCPHGTFADR SGDGTICRAC SPSCSRCTAE SHCLECWPSF YLAWGTGRCL PRVLCRQSEY
YDAVDRTCLP CAAGCATCIG PLPTHCTSCS TLPPTPSCLY VTGSEESKSN ADLTDSPWGQ
CVPCCPYRVA LLSRSPKDCM FCVADRASCM SGHEINAGEG LLFEEVTPAP EMIPSWLTKE
PSRLILFVLC GFLMVGVCTF LTIHTIYTWR RRRPRGGEPN TMAVRHRRRR EVDGPNYSEE
EDGAKMSLKL TSSKGGVDIV DGTGNSTMGL DNGFPQNAAV PDSEPIHKTA ADTLVTSSNS
TPPHLDRPRR VLYVHPVYPA PSETGAAQTG PQPCAACTTH LPDEYCSRSV PLPTKQRHDE
ISVSIGGTGA FVNGSASTTV VSSSNLQHTN KPREIKPF
//
