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Database: UniProt
Entry: A0A484AUH0_DRONA
LinkDB: A0A484AUH0_DRONA
Original site: A0A484AUH0_DRONA 
ID   A0A484AUH0_DRONA        Unreviewed;      1490 AA.
AC   A0A484AUH0;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=P/Homo B domain-containing protein {ECO:0000259|PROSITE:PS51829};
GN   ORFNames=AWZ03_014069 {ECO:0000313|EMBL:TDG39510.1};
OS   Drosophila navojoa (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7232 {ECO:0000313|EMBL:TDG39510.1, ECO:0000313|Proteomes:UP000295192};
RN   [1] {ECO:0000313|EMBL:TDG39510.1, ECO:0000313|Proteomes:UP000295192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Navoj_Jal97 {ECO:0000313|EMBL:TDG39510.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:TDG39510.1};
RX   PubMed=30423125; DOI=.1093/jhered/esy059;
RA   Vanderlinde T., Dupim E.G., Nazario-Yepiz N.O., Carvalho A.B.;
RT   "An Improved Genome Assembly for Drosophila navojoa, the Basal Species in
RT   the mojavensis Cluster.";
RL   J. Hered. 110:118-123(2019).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000256|ARBA:ARBA00005325}.
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:TDG39510.1}.
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DR   EMBL; LSRL02000998; TDG39510.1; -; Genomic_DNA.
DR   STRING; 7232.A0A484AUH0; -.
DR   OMA; TYETQDY; -.
DR   Proteomes; UP000295192; 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; 3.30.70.850; Peptidase S8, pro-domain; 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   InterPro; IPR032815; S8_pro-domain.
DR   InterPro; IPR038466; S8_pro-domain_sf.
DR   PANTHER; PTHR42884:SF13; NEUROENDOCRINE CONVERTASE 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; 1.
DR   Pfam; PF16470; S8_pro-domain; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SMART; SM00181; EGF; 8.
DR   SMART; SM00261; FU; 10.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
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:UP000295192};
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        1332..1355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          555..694
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          16..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        259
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        298
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        479
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1490 AA;  163585 MW;  DAD7BFC56E4722ED CRC64;
     MPSTCCEHPT LIIAETDSEA SNTHNNNSKI YNNNSNIGNN SSKASAGQNA KETEKHHLDD
     IDIFGAYSIP DEPIYTNEFA VHIPAGKSVA DIIANKYGFT NKGQIGALDD YYLFQHHRVS
     KRSLRLSRKH HSALKSESEV KWLQQQHEKI RRKRDGPYQD IPTYSPYHIL RQSNDYVIDQ
     QTNTHFSYSP DPVLSTPLGG AHSPRLEYRD VTSHLIFSDP LFKEQWYLNG GAKDGLDMNI
     GPAWQKGYTG KGVVVSILDD GIQTNHPDLA QNYDPDASFD INGNDSDPTP QDNGDNKHGT
     RCAGEVAAVA FNNYCGVGVA YNASIGGVRM LDGKVNDVVE AQALSLNPGH IDIYSASWGP
     EDDGSTVDGP GPLARRAFIY GVTSGRQGKG SIFVWASGNG GRYTDSCNCD GYTNSIFTLS
     ISSATQAGFK PWYLEECSST LATTYSSGTP GHDKSVATVD MDGRLRPDHI CTVEHTGTSA
     SAPLAAGICA LALEANQNIT WRDMQYLVVY TSRPGPLEKE SGWTLNGVKR KYSHKFGYGL
     MDAGAMVALA EQWNTVPPQH ICKSRENNED RKIEGAYGYS LATHMDVNGC AGTINEVRYL
     EHVQCRITLR FFPRGNLRIL LTSPMGTTST LLFERPRDIV KSNFDDWPFL SVHYWGEKAE
     GRWTLQVING GRRRVNQPGI LSKWQLIFYG TSTQPMRLKS ELLNTQLRNN PIASNPFLFS
     SASNIGQPAN EGGNFNTDSY ASYLNYQNLF SSAGSSPEIA TATLDGQNVS AALAAQSPNG
     PNGDNNLIQY SCDAECDSLG CYGRGPTQCV ACSHYRLDNT CVSRCPPRSF PNQVGICWPC
     HDSCETCAGA GPDSCLTCAP AHLHVTDLAV CLQVCPDGYF EDIKNKTCVP CEPNCASCQD
     RPEFCTSCDH HLVMHENKCF SACPLNTYET DENKCAYCHP SCATCNEASE NNCITCRPSR
     YAYQNKCLNN CPEGFYADKK RLECLPCHEG CKTCSTNGIC SECLPNWTLN KKDSCIVSGS
     ESCSESEYFN LAEGKCNQCH ESCATCNGPL STDCLSCHQN RLLEQSSCVS GCQDGFFMET
     GVCTPCLHTC TQCVSRTNCS NCSKGLELQN GECRTTCADG YYSDRGICAK CYLSCHTCSG
     PRRNQCVQCP AGWQLAAGEC HPECPEGFYK SEFGCQKCHH YCKTCNGAGP LACSSCPTHF
     MLDGGLCMEC LSSQYYDSTT QRCKSCHESC RSCFGPGQYS CKTCAPPFHL DQLNSQCVPC
     CPNQTSADNE TSSENCCHCD KDTGECKTVS TAGKRRTVVG SESIFRNVDR SANGDHGNSG
     TFALRLDSPL TAITAIAVAI CLLIITIFSI IFAVLQRNSN NVSRNSVRYR KIISRSDGRK
     SDPRNEARFI FNVGEDGDET DDNTDDDMDV NVRTVKKVVY EPNGPMYGNE FFIKSTNDID
     AVEFHCKDAD DANQNQFDTH HNANIYTENS SPTYMHQVTS SRMNSKVVHS
//
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