ID A0A158QNK1_HAEPC Unreviewed; 1783 AA.
AC A0A158QNK1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=P/Homo B domain-containing protein {ECO:0000313|WBParaSite:HPLM_0001058601-mRNA-1};
GN ORFNames=HPLM_LOCUS10585 {ECO:0000313|EMBL:VDO40575.1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001058601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0001058601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO40575.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO40575.1,
RC ECO:0000313|Proteomes:UP000268014};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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}.
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DR EMBL; UZAF01017336; VDO40575.1; -; Genomic_DNA.
DR STRING; 6290.A0A158QNK1; -.
DR WBParaSite; HPLM_0001058601-mRNA-1; HPLM_0001058601-mRNA-1; HPLM_0001058601.
DR OMA; ERDSCAY; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; 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; 1.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 3.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.30.70.850; Peptidase S8, pro-domain; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 3.
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 InterPro; IPR032815; S8_pro-domain.
DR InterPro; IPR038466; S8_pro-domain_sf.
DR PANTHER; PTHR42884:SF23; FURIN-LIKE PROTEASE 2; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF01483; P_proprotein; 2.
DR Pfam; PF00082; Peptidase_S8; 3.
DR Pfam; PF16470; S8_pro-domain; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00261; FU; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 3.
DR PROSITE; PS51829; P_HOMO_B; 2.
DR PROSITE; PS51892; SUBTILASE; 3.
DR PROSITE; PS00136; SUBTILASE_ASP; 3.
DR PROSITE; PS00137; SUBTILASE_HIS; 3.
DR PROSITE; PS00138; SUBTILASE_SER; 2.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000268014};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1783
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041122421"
FT TRANSMEM 874..899
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 491..629
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT DOMAIN 1339..1481
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 123..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1576..1600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1085
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 202
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 241
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 415
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 1050
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 1089
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 1263
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1783 AA; 195888 MW; 30027C21F7841CFF CRC64;
MRTGLIVLFS LTCIYAIEHD SICDDDDDTC PEPTHTVIRL AKRDDALARK LAAEHGMRVR
GEPFLDSHYF LYHEDESHSR RRKREAVKRL DSHPAVEWLS EQRARRRTKR DYLHNDFQVV
EGEGKRLSKR NSSSSRRTSS SRDFRKRRRQ AVREIPRLPW PDPLYPDQWY LVGKAVGNYD
MNVREAWLLG YAGRNVSVSI LDDGIQRDHP DLVANYDPLA STDINDHDDD PTPQNNGDNK
HGTRCAGEVA AIAGNNYCGV GVAFKAKIGG VRMLDGAVSD SVEAASLSLN QDHIDIYSAS
WGPEDDGKTF DGPGPLAREA FYRGIKNGRR GKGNIFVWAS GNGGSRQDSC SADGYTTSVY
TLSISSATYD NRRPWYLEEC PSSIATTYSS ANINQPAIVT VDVPSGCTKM HTGTSASAPL
AAGIIALALE ANPDLTWRDM QHIVLRTANP TPLLGNPGWS QNGVGRMISN KFGYGLMDGG
ALVKLAKTWR TVPEQHICTY EYKLAAPNPR PIQGRFQMNF TLEVNGCESG TPVLYLEHVQ
VHATVRYSKR GDLKLTLFSP SRTRSVLLPP RPQDYNSNGF HKWPFLSVQQ WGEDPRGTWV
LMVESVTNNP SASGTFHDWT LLLYGTAEPA QPGDTIHPPT PVPSQTVLGR IQHLTSQIDE
VEPLSFGDLR SVGDCHPECD GGCTESQSAV ACFRCKHFTQ TLRNKAGNGF KCVPHCDDTY
YLDGMNCKMC SSHCHTCSQA EVCETCPGAQ LLVHVANSPQ NGKCVDKCAI GQVPDYETNL
VQARCVLREE RCGDGYFLNS VGKCDQCDQA CALCSGPGTG YWAVQPVRPV TETVLLVTAG
RAALKGKLQR IIDAVQDCSP NAKYPDRDHR SLSLFWSFIW VVLIVALFSF VGFIAYCLLR
DDRNQIDYTP LPHYNSQTGE VHILDSDSEE DDELYEAKHI CDDDRDDSCP EPTHTVIRLA
RRDDALARKI AADHGMEVRE EEEQLSNSNS LDLKKSKGQG QPVPHLPWPD PLYSKQWYLV
GKAAGNYDMN VREAWLLGYA GRNISISILD DGIQRDHPDL AANYDPLAST DINDHDDDPT
PKNNGENKHG TRCAGEVAAV AGNNYCGVGV AFKAKIGGVR MLDGKVSDGV EAASLSLNQD
HIDIYSASWG PNDDGKSLDG PGPLAREAIL RGIRYGRQGK GNIFVWASGN GGGKQDSCSA
DGYTTSVYTL SVSSATYDNR RPWYLEECPS SIAATYSSGK SSEPAIVSTD VPQGCTLRHT
GTSASAPLAA GMIALALEAN PDLTWRDMQH IVLRTANPRP LLGNPGWSRN GVGRMISNLF
GYGLMDGGAI VKLAKVWETV PEQHICTYQN QYKSSRSLRG RFRMNFTLTV NGCGSGTPIL
YLEHVQVHVT VKFDKRGDLK LTLYSPSGTR SVLLPPRPQD SSSHGLNDWP FLSVQQWGED
PYGTWILEVQ SVTNNPTASG NFQILRTFYN WKLVLYGTEE PAQTGDTIHP HYSRRSNRVL
AKKICDDDHD GSCPEATHTV IRLATRNDAL ARKIAADNGM EVRAWLLGYA GRNITVSILD
DGIQLDHPDL AANYDPLAST DINDHDDDPT PQNNGENKHG TRCAGEVAAI AGNNLCGVGV
AFKAKIGGVR MLDGDVSDSG EAASLSLNQD HIDIYSASWG PEDDGKTFDG PGPLTRKALY
TGIKTGRRGK GNIFVWASGN GERLKLENSE LNTPLREDSC SADGYITSIY TLAISSATYN
NLSPWYLEEC PSSIATTYSS SYSTEPAIVS FFPDEEMDIQ IVQ
//
