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Database: UniProt
Entry: A0A1Q3JUN7_9SPHI
LinkDB: A0A1Q3JUN7_9SPHI
Original site: A0A1Q3JUN7_9SPHI 
ID   A0A1Q3JUN7_9SPHI        Unreviewed;       389 AA.
AC   A0A1Q3JUN7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Serine protease {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BGN92_14725 {ECO:0000313|EMBL:OJU24528.1};
OS   Sphingobacteriales bacterium 41-5.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895836 {ECO:0000313|EMBL:OJU24528.1, ECO:0000313|Proteomes:UP000187304};
RN   [1] {ECO:0000313|EMBL:OJU24528.1, ECO:0000313|Proteomes:UP000187304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=41-5 {ECO:0000313|EMBL:OJU24528.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S46 family.
CC       {ECO:0000256|ARBA:ARBA00010491}.
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:OJU24528.1}.
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DR   EMBL; MKRO01000171; OJU24528.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3JUN7; -.
DR   Proteomes; UP000187304; Unassembled WGS sequence.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:InterPro.
DR   GO; GO:0070009; F:serine-type aminopeptidase activity; IEA:InterPro.
DR   GO; GO:0043171; P:peptide catabolic process; IEA:UniProt.
DR   InterPro; IPR019500; Pep_S46.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   PANTHER; PTHR38469; -; 1.
DR   PANTHER; PTHR38469:SF1; PERIPLASMIC PEPTIDASE SUBFAMILY S1B; 1.
DR   Pfam; PF10459; Peptidase_S46; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022438};
KW   Protease {ECO:0000256|ARBA:ARBA00022438};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
SQ   SEQUENCE   389 AA;  44914 MW;  0C26D7C3B3C00E0E CRC64;
     MGLTKTNAVQ KKKDYEEIFL QRLNANATLK AKYGNVLQQL NQNYEWIEPF GLARDYYLES
     TSRIELFSII NKMISLMNAK NSKPNAEYQK NLAEQINSLT GLYKDLNANV DKDLFAAMMK
     LYTEKQEAKF VADVAKSQKV KYENDYKKWA DAIYEKNFLL NKDEMLNQLK ANPDAIYRKI
     LESEAFQLVN GLAVYYNENI TPGLNKYQPV IDNLQRKYMQ AQMDVMKDRK FYPDANSTMR
     VTYGQVKGYY PSDGKYYDYQ TYLEGVMEKY IPGDYEFNVP EKLIELYKKK DYGIYGITDK
     SGNKRMPVCF IGSNHTTGGN SGSPALDAYG NLVGLNFDRV WEGTMSDINY DPSICRNIMV
     DARYILFIID KFADAGHLIK ELKIVGLKK
//
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