ID A7RLT1_NEMVE Unreviewed; 614 AA. AC A7RLT1; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 27-MAR-2024, entry version 85. DE RecName: Full=P/Homo B domain-containing protein {ECO:0000259|PROSITE:PS51829}; GN ORFNames=NEMVEDRAFT_v1g160244 {ECO:0000313|EMBL:EDO47748.1}; OS Nematostella vectensis (Starlet sea anemone). OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria; OC Edwardsiidae; Nematostella. OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO47748.1, ECO:0000313|Proteomes:UP000001593}; RN [1] {ECO:0000313|EMBL:EDO47748.1, ECO:0000313|Proteomes:UP000001593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593}; RX PubMed=17615350; DOI=10.1126/science.1139158; RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A., RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J., RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R., RA Technau U., Martindale M.Q., Rokhsar D.S.; RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and RT genomic organization."; RL Science 317:86-94(2007). CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily. CC {ECO:0000256|ARBA:ARBA00005325}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DS469518; EDO47748.1; -; Genomic_DNA. DR RefSeq; XP_001639811.1; XM_001639761.1. DR AlphaFoldDB; A7RLT1; -. DR STRING; 45351.A7RLT1; -. DR EnsemblMetazoa; EDO47748; EDO47748; NEMVEDRAFT_v1g160244. DR GeneID; 5519937; -. DR KEGG; nve:5519937; -. DR eggNOG; KOG3525; Eukaryota. DR HOGENOM; CLU_002976_4_1_1; -. DR InParanoid; A7RLT1; -. DR OMA; VWQKGFT; -. DR OrthoDB; 5474719at2759; -. DR PhylomeDB; A7RLT1; -. DR Proteomes; UP000001593; Unassembled WGS sequence. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central. DR GO; GO:0016485; P:protein processing; IBA:GO_Central. 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; 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 InterPro; IPR032815; S8_pro-domain. DR InterPro; IPR038466; S8_pro-domain_sf. DR PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1. DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 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 SUPFAM; SSF49785; Galactose-binding domain-like; 1. 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 Calcium {ECO:0000256|ARBA:ARBA00022837}; 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:UP000001593}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE- KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..31 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 32..614 FT /note="P/Homo B domain-containing protein" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002711375" FT DOMAIN 472..608 FT /note="P/Homo B" FT /evidence="ECO:0000259|PROSITE:PS51829" FT ACT_SITE 179 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1, FT ECO:0000256|PROSITE-ProRule:PRU01240" FT ACT_SITE 220 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1, FT ECO:0000256|PROSITE-ProRule:PRU01240" FT ACT_SITE 394 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1, FT ECO:0000256|PROSITE-ProRule:PRU01240" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:EDO47748.1" SQ SEQUENCE 614 AA; 68317 MW; 5B0670D4987BAFA0 CRC64; MFERVPPCRL LKSPIVFWIV LGVISWQGVS GADLSAEERV YTNGWAIHVN GGIEEAKEVA KAHGFEKVEP IGTLEGYYHL EHPSHPSRSR RSAEDRTDQL RQHRHVTWVE QQHEKVREKR GFYHDRMVAR GIVPRFKDPL WDAQWYLDDK RKDTDLDIHV IPVWKKGISG KGVVVTILDD GIEHNHTDLI KNYDPNASWD VNDGDNDPFP RYDPTNENKH GTRCAGEVAA EANNTKCGVG VAFNARIGGV RMLDGRVTDK VEAESLSLNP QYIDIYSASW GPSDDGATVE GPGTLATAAF LNGIQKGRGG LGSIFVWASG NGGRHGDSCN CDGYTDSIYT LSISSASDHG ESPWYSESCS STLATTFSSG AHGEKRIVTT DLHNTCTERH TGTSASAPLA AGIFALALEV NPKLTWRDMQ HIVVHTSNHL PLKHDQDWSK NGIDLMVNRK FGFGLLVAEK IVDMANPATY VTVPEKRFCR GQINQDAKVF KWDKPLTIQL PATGCSGTGD EIRYLEHVQL MVSLDYVRRG DLVIYLTSPM GTKSCLLSPR KEDSSNEGFS KWPFMTTHSW GEDPRGTWTL EIKDLGDNKA NHGTLREWQL ILHGTKDKPA HQQK //