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Database: UniProt
Entry: E4XKE8_OIKDI
LinkDB: E4XKE8_OIKDI
Original site: E4XKE8_OIKDI 
ID   E4XKE8_OIKDI            Unreviewed;       746 AA.
AC   E4XKE8;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=P/Homo B domain-containing protein {ECO:0000259|PROSITE:PS51829};
GN   ORFNames=GSOID_T00013111001 {ECO:0000313|EMBL:CBY24937.1};
OS   Oikopleura dioica (Tunicate).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC   Oikopleuridae; Oikopleura.
OX   NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY24937.1};
RN   [1] {ECO:0000313|EMBL:CBY24937.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21097902; DOI=10.1126/science.1194167;
RA   Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA   Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA   Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA   Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA   Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA   Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA   Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA   Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA   Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA   Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA   Roest Crollius H., Wincker P., Chourrout D.;
RT   "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT   pelagic tunicate.";
RL   Science 330:1381-1385(2010).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR   EMBL; FN653064; CBY24937.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4XKE8; -.
DR   InParanoid; E4XKE8; -.
DR   Proteomes; UP000001307; Unassembled WGS sequence.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016486; P:peptide hormone processing; IEA:UniProt.
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; IPR008979; Galactose-bd-like_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:SF13; NEUROENDOCRINE CONVERTASE 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   SUPFAM; SSF49785; Galactose-binding domain-like; 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};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000001307};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          369..508
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        84
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        125
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        302
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   746 AA;  82112 MW;  22881A893C6BBF70 CRC64;
     MEPLRREKRG LRGETFEPDT RAKGGYHGQV GFNACFLSYD PLWNAEWYIK NTGQDDGTPG
     LDLNVTHVWQ MGYTGRGVTV AILDDGVDYN HPDLYPNYSP ENSWDFSGDD PYPYPRWTSN
     GFNSHGTRCA GEIAAVADNG ICGVGIAFNS KIAAVRMLDQ PYMTDAIEAS SMGFRPQNID
     IYSASWGPTD DGKTVDGPRE LTLQAMRDGV NKGRNGKGSI YVWASGDGGP FDDCNLDGYA
     SSMWTISINS AVNDGETAIY DESCSSIVAS TFSSGKVGAR SNAGVATTDL YGNCTMKHSG
     TSAAAPEAAG VIALALEANP DLTWRDIQTL SDPRHPWQVN GAGFLFNHLF GFGVIDAGSL
     VEESLKWKNA PERKSCIVGE MEIAKKTFTG GEPVELSIDT DSCAGKSNEV NYIEHVQAFI
     TLKTTRRGDL TINMTSPMST NSKLLQPRPR DDDSVVGLNE WPFVSVQFWG ERARGMWKVR
     IALSELTLKQ QYAQVLKWKL VIHGTKDPWN HMPSHIFFLF VLGGISALGR TSAPAEAAGE
     IQRLECYHCT YRENSDGTTF GNKACQDVSD PEASKQFLIS IPNRFYNVTK PTPVVYRYDC
     MTYWRTGKRI EDHFCSETGK CYHCEGTEYM NKSTNAWVHP EAHKEGCASL EGNQPVRPCD
     ATCEVLLMSV MQGNNKDPVA RFVQRGCLPT QMDAQTAAFE TDTKDKFNME TCYDSICNTG
     CTKDGCSSAR VALVSSIFLL TSLFLL
//
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