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Database: UniProt
Entry: A0A0L7QT86_9HYME
LinkDB: A0A0L7QT86_9HYME
Original site: A0A0L7QT86_9HYME 
ID   A0A0L7QT86_9HYME        Unreviewed;      1072 AA.
AC   A0A0L7QT86;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Furin-like protease 2 {ECO:0000313|EMBL:KOC61847.1};
GN   ORFNames=WH47_05574 {ECO:0000313|EMBL:KOC61847.1};
OS   Habropoda laboriosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Habropoda.
OX   NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC61847.1, ECO:0000313|Proteomes:UP000053825};
RN   [1] {ECO:0000313|EMBL:KOC61847.1, ECO:0000313|Proteomes:UP000053825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0110345459 {ECO:0000313|EMBL:KOC61847.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Habropoda laboriosa.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000256|ARBA:ARBA00005325}.
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DR   EMBL; KQ414751; KOC61847.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L7QT86; -.
DR   STRING; 597456.A0A0L7QT86; -.
DR   Proteomes; UP000053825; 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; 9.
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; IPR000742; EGF-like_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR032778; GF_recep_IV.
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; PF14843; GF_recep_IV; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 2.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SMART; SM00181; EGF; 7.
DR   SMART; SM00261; FU; 10.
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:UP000053825};
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};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   TRANSMEM        1009..1036
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          280..437
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          40..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        22
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        61
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        203
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1072 AA;  115939 MW;  38DB4A66C8E0386A CRC64;
     MNLGPAWQKS YTGKGVVVSI LDDGIQTNHP DLALNYDHQA STDINDNDND PMPRDNGDNK
     HGTRCAGEVA AVAFNQYCGV GVAYNASIGG VRMLDGPVND AVEARGLGLN PDHIDIYSAS
     WGPEDDGKTV DGPGPLARRA FIYGVTSGRK GKGSIFVWAS GNGGRHTDSC NCDGYTNSIF
     TLSISSATQG GYKPCTVEHT GTSASAPLAA GIAALALEAN PSLTWRDMQY LVVLTSRSGP
     LEKEPGWILN GVKRKVSHKF GYGLMDAGAM VNLAEQWTNV PPQHICKSDE ISEERRIDPT
     YGYTLSVYMD VTGCAGSLNE VRFLEHVQCK VSLRFFPRGN LRLLLTSPMG TTSTLLFERP
     RDVLSSSFDD WPFLSVHFWG EKADGILKKW QLIFYGTAIN PIRKRTRQFN PGYQGPYVGA
     ASNVQASVAT LDGSSAPILT NRLPGDTSSS FDSPASSSQV GDDSLDTTRK ILHDCDPQCD
     PQGCYGKGPT QCIACKNYRL DNTCVSRCPP RSFPNQGGVC WPCHESCEIC AGAGQDSCLS
     CAPAHLRVTD LAVCLQQCPE GYYENTENST CVPCEANCAS CQDRPDKCTS CEHHLVMYEN
     KCYAACPLYT YETQDYNCAP CHSTCETCNG TAENQCISCR PGLFSLNGTC RASCQVGYSA
     DKKRRECVPC PAGCATCTMS TCTNCNDGWT LNEDGLCAPE YRDRCDTSEY YDSGHCKPCH
     ASCKTCSGST ENHCISCQNS MLLQGKRCLY QCDDGYYSMV QPSRPVCVPC LHTCKTCVSR
     LNCTACHDGL QLQSGECRSS CAQGYYSDRG QCAKCYLSCK TCSGPRRDQC VTCPRGWQLA
     AGECHPECPE GFFKSNFGCQ KCHHYCRTCK GEGPMECTSC PPHSMLEGGL CMECLGAQYY
     DPLTQLCKNC HADCRRCTGP GKFSCAACSP PLHLDKLNNQ CVPCCTGNEK GPQAEECCLC
     DPETGGCRNS SPAGKRRVPG TEFASADTAI SEVYAKYEGT TDKNDSASLA ITATTTIAVA
     ICLVSVALFA TIFIALQAMS GRRETNKGYT QLAVRVEPPD DVDADDTTEL MT
//
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