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Database: UniProt
Entry: W7IKH6_9PSEU
LinkDB: W7IKH6_9PSEU
Original site: W7IKH6_9PSEU 
ID   W7IKH6_9PSEU            Unreviewed;       518 AA.
AC   W7IKH6;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Alkaline serine exoprotease A {ECO:0000313|EMBL:EWC61365.1};
DE            EC=3.4.21.- {ECO:0000313|EMBL:EWC61365.1};
GN   ORFNames=UO65_3338 {ECO:0000313|EMBL:EWC61365.1};
OS   Actinokineospora spheciospongiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=909613 {ECO:0000313|EMBL:EWC61365.1, ECO:0000313|Proteomes:UP000019277};
RN   [1] {ECO:0000313|EMBL:EWC61365.1, ECO:0000313|Proteomes:UP000019277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EG49 {ECO:0000313|EMBL:EWC61365.1,
RC   ECO:0000313|Proteomes:UP000019277};
RX   PubMed=24604655;
RA   Harjes J., Ryu T., Abdelmohsen U.R., Moitinho-Silva L., Horn H., Ravasi T.,
RA   Hentschel U.;
RT   "Draft Genome Sequence of the Antitrypanosomally Active Sponge-Associated
RT   Bacterium Actinokineospora sp. Strain EG49.";
RL   Genome Announc. 2:e00160-14(2014).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC       ECO:0000256|RuleBase:RU003355}.
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:EWC61365.1}.
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DR   EMBL; AYXG01000115; EWC61365.1; -; Genomic_DNA.
DR   RefSeq; WP_035283404.1; NZ_AYXG01000115.1.
DR   AlphaFoldDB; W7IKH6; -.
DR   STRING; 909613.UO65_3338; -.
DR   PATRIC; fig|909613.9.peg.3339; -.
DR   eggNOG; COG1404; Bacteria.
DR   eggNOG; COG4935; Bacteria.
DR   OrthoDB; 9766923at2; -.
DR   Proteomes; UP000019277; Unassembled WGS sequence.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
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; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43806:SF11; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF05922; Inhibitor_I9; 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; 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.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
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:UP000019277};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..518
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004895875"
FT   DOMAIN          398..518
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   ACT_SITE        156
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        189
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        339
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   518 AA;  52662 MW;  222957FEFB2C96DB CRC64;
     MRHDRLNRRV AAVLLAAGTA ALAVGTPAQA APTSTILGVA NAVPGAYIAV LKDGAMTAAT
     TNGTALDLAK RYGGAVTLTY TATLRGFAVR MDEAAAKRLA ADPAIAYVQQ DGIARISDTQ
     TGATWGLDRV DQRALPLNQT YTYANTAANV NAYILDTGIN KSHPEFEGRA KDGYDFIDND
     SDASDCQGHG THVSGTVGSK TYGLAKKVNL IGVRVLDCQG NGPYSQIIAG VDWVARNAVK
     PAVANMSLGG GADTSVDNAV KAAIASGVTF AVASGNANTN ACSTSPARVP EAITVNATDN
     ADNRSSFSNY GSCTDIFAPG TNITSTRNGG GTTQMSGTSM ATPHVAGAAA LYLSANPNAT
     PAQVRNALVD NATSNAVKSP GTGSPNKLLY TGFIGGGTTP PPSCAGGTNG DGVSIPDTNS
     PVTSSIAVTG CTGKAPATTK VKVDINHTYS ADLALDLVGP SGAVFPLKRA GGVSSSAGVH
     ETYTVNASAE NLNGTWKLRA TDVWSYDTGT IDTWTLTF
//
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