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Database: UniProt
Entry: A0A1H1ZNC6_9ACTN
LinkDB: A0A1H1ZNC6_9ACTN
Original site: A0A1H1ZNC6_9ACTN 
ID   A0A1H1ZNC6_9ACTN        Unreviewed;       480 AA.
AC   A0A1H1ZNC6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Serine protease, subtilisin family {ECO:0000313|EMBL:SDT35204.1};
GN   ORFNames=SAMN04488543_3893 {ECO:0000313|EMBL:SDT35204.1};
OS   Friedmanniella luteola.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Friedmanniella.
OX   NCBI_TaxID=546871 {ECO:0000313|EMBL:SDT35204.1, ECO:0000313|Proteomes:UP000199092};
RN   [1] {ECO:0000313|EMBL:SDT35204.1, ECO:0000313|Proteomes:UP000199092}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21741 {ECO:0000313|EMBL:SDT35204.1,
RC   ECO:0000313|Proteomes:UP000199092};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; LT629749; SDT35204.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1ZNC6; -.
DR   STRING; 546871.SAMN04488543_3893; -.
DR   OrthoDB; 5165638at2; -.
DR   Proteomes; UP000199092; Chromosome i.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_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; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_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; PF00041; fn3; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00014; FNTYPEIII.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS50853; FN3; 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   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000199092};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..480
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009267907"
FT   DOMAIN          383..480
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   ACT_SITE        141
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        174
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        327
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   480 AA;  49264 MW;  59F90FC8801C9926 CRC64;
     MNRLTGALAA AALVSSVSAG LTLPAHAAPE SGPTARYIVR TDAVGGADDA AQDVRRLGGD
     VEHVYSEVFP GLAATLTADQ ARRLRASDEV AEVVPDRLFH ATGVQTNAPW ALDRLDQRPV
     AGNKTYRYDT TGEGAFAFVL DTGLRFGHQQ FGGRAVSGYD FVDLDDDASD CDGHGTHVAG
     SIGGAGYGVA KGVTLVGVRV LDCEGAGYAS DIIWALDWVA EVAADVPAVV NLSLGGPALD
     ELDEAVERTV RAGIPVVVAA GNENGDACDV SPARVPAAIT VAAVDSADRR ARFSNRGRCV
     DLFAPGVAVR SASNLSNTAT EVMSGTSMAA PHVTGAVARY LGAHPTATPA QAVGALTRTA
     GADAVRDRAG SPDRLLYTGP VTAPGKPTKV AAKKNDRART ATVSWSTPVA DGGRAVTGYR
     VTRNGKDARG QGPVTVTVSA GTRSHTFPRL RKGSAYTFTV RAVNAVGAGA PMSTSVPKLR
//
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