GenomeNet

Database: UniProt
Entry: A0A1Y5Y0H0_KIBAR
LinkDB: A0A1Y5Y0H0_KIBAR
Original site: A0A1Y5Y0H0_KIBAR 
ID   A0A1Y5Y0H0_KIBAR        Unreviewed;       647 AA.
AC   A0A1Y5Y0H0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Serine protease, subtilisin family {ECO:0000313|EMBL:SMD21588.1};
GN   ORFNames=SAMN05661093_06901 {ECO:0000313|EMBL:SMD21588.1};
OS   Kibdelosporangium aridum.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Kibdelosporangium.
OX   NCBI_TaxID=2030 {ECO:0000313|EMBL:SMD21588.1, ECO:0000313|Proteomes:UP000192674};
RN   [1] {ECO:0000313|EMBL:SMD21588.1, ECO:0000313|Proteomes:UP000192674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43828 {ECO:0000313|EMBL:SMD21588.1,
RC   ECO:0000313|Proteomes:UP000192674};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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   ---------------------------------------------------------------------------
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; FWXV01000007; SMD21588.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5Y0H0; -.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000192674; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
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; 2.60.40.10; Immunoglobulins; 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; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR013783; Ig-like_fold.
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   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF05345; He_PIG; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49313; Cadherin-like; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 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   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:UP000192674};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..647
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013096886"
FT   DOMAIN          52..122
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          155..383
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          399..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        163
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        194
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        347
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   647 AA;  66376 MW;  7D9CF3442D1AA8F3 CRC64;
     MRTLAVPLRR RAVGLGVVAT TALALTIAVA QPASAAVGQV LGADRAGAIK DSYIVQIKDS
     ASPKARSAQT ARELTAKYGG QVKVAWQHAL NGFAVAMTAD EARRMAADPR IDYVQQDAVV
     SIADTQPNPP SWGLDRIDQR DRPLDNSYTY NTTASNVHVY VLDTGIRISH STFGGRATWG
     FNAIDTNNTD CNGHGTHVAG TIGGSQYGVA KGAQLVAVKV LNCQGSGSFA QVVNGINWVT
     QNAVKPAVAN MSLGAAGSDT ATENAVRNSI ASGVTYAIAS GNSNQNACNF TPAKVAEAIT
     VNASDINDAR ASFSNFGTCT DIFGPGVNIT SAWITNDTAT NTISGTSMAT PHVAGGAALW
     LADHPTDSAA AVQTALINNS SPNKISNPGT GSPNRLLFTN AGDPGPGNPS VSNPGNQTTT
     VGTAVNLQLS ASGGTPPYTW SATGLPPGLA ISSGGLISGT PSTAGTYSVT ATAADTAGKA
     GSATFTWTVN PVGGCTGAGQ KIANPGFESG AASWTATSSV IGQHGTDQPA HSGTWSAWLN
     GYGFIRTDRL SQSVTIPAGC TSYRLSYWLH IDSDETTGSV QYDKLTVQLG SNTLATYSNL
     NEAAGYQQRT FDVGAYAGQT VTLTFTGTED ISLQTSFVVD DVSLDVS
//
DBGET integrated database retrieval system