ID A0A2U3A0M9_9ACTN Unreviewed; 790 AA.
AC A0A2U3A0M9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:PWI18068.1};
GN ORFNames=DI272_30905 {ECO:0000313|EMBL:PWI18068.1};
OS Streptomyces sp. Act143.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2200760 {ECO:0000313|EMBL:PWI18068.1, ECO:0000313|Proteomes:UP000245455};
RN [1] {ECO:0000313|EMBL:PWI18068.1, ECO:0000313|Proteomes:UP000245455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Act143 {ECO:0000313|EMBL:PWI18068.1,
RC ECO:0000313|Proteomes:UP000245455};
RA Valanrebinro G., Kumari S., Rameshkumar N.;
RT "Actinomycin D producing novel Streptomyces isolated from the rhizosphere
RT of saline tolerant kaipad rice and its draft genome analysis.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:PWI18068.1}.
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DR EMBL; QFRX01000001; PWI18068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U3A0M9; -.
DR OrthoDB; 9766923at2; -.
DR Proteomes; UP000245455; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
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; 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; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF01483; P_proprotein; 3.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 2.
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 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:UP000245455};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..790
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015569682"
FT DOMAIN 440..572
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT DOMAIN 665..790
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 142
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 202
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 380
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 790 AA; 79633 MW; 25C74F711C23105A CRC64;
MKRQIWTTVA IVLATVSLGA IPAHATEIST TVTESDPIDP PLYDETADGG TVRVNVVTEN
RDDLSGAASA GETLLSYKTL PLVTLEVDKS GLDDLAAQPG VVSVTEDELV APSLDESVPL
IGGDKAVAAG KTGKGSAIAV LDTGVATNHP FLKGRVTAEA CFSPVDANYG ATSLCGNGAA
TQEGTGAANS ASVCADIAEC DHGTHVAGIA AGDGTGLSGA PARGVAPGAD IVAVQVFSRL
DSTKYCGTTT PCIRSFTSAQ IAGLEKVLAL KQAGMPIVAA NLSLGSASYS TACTKDARKT
VIDSLYEAGV ATVVAAGNNG SATAVTAPAC VPGAVSVGAT TDDDEIASFS NHGPLLDVLA
PGNGIVSSVL SGYDSKSGTS MAAPHVAGAF AVLRQAHPDK TLAEREALLK STGTPVTDEA
GVTVPRIDVG KAVGAATPAP DPEPADTTRR TKILNDAPYA IPDLGTVQSP ITVSGVTGNA
PKTLQVSVDV THDWLGEVKI DLVAPDGQTY ALKATNGTDP GGTLSRTYTV DASVSPASGT
WKLQVADKSA GGTGTVDDWA LTFPTPFART APAAIPDAAT LTSEITVDGV TGNASGALQA
SVNVTHQWLG EVKIDLVAPD GQTYALKATN GTDPGGTLSR TYTVDASATA ANGTWKLLVA
DKSSGGTGTL DGWSLTFPSI ESQSTYAVPD AGTLQAPITV TGVSGNAPKT LKVSLRLTHD
WLGEVKIDLI APNGLVYAVK ATNGTDPGGT LDKVYTVDAS ASPIEGTWKL QVADKSTGGT
GTLDDWALTF
//
