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Database: UniProt
Entry: A0A1Q3T5F5_9SPHI
LinkDB: A0A1Q3T5F5_9SPHI
Original site: A0A1Q3T5F5_9SPHI 
ID   A0A1Q3T5F5_9SPHI        Unreviewed;       530 AA.
AC   A0A1Q3T5F5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Peptidase C1A papain {ECO:0000313|EMBL:OJV97441.1};
GN   ORFNames=BGO52_09125 {ECO:0000313|EMBL:OJV97441.1};
OS   Sphingobacteriales bacterium 44-61.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895838 {ECO:0000313|EMBL:OJV97441.1, ECO:0000313|Proteomes:UP000186208};
RN   [1] {ECO:0000313|EMBL:OJV97441.1, ECO:0000313|Proteomes:UP000186208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=44-61 {ECO:0000313|EMBL:OJV97441.1};
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 C1 family.
CC       {ECO:0000256|ARBA:ARBA00008455}.
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:OJV97441.1}.
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DR   EMBL; MKTW01000020; OJV97441.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3T5F5; -.
DR   STRING; 1895838.BGO52_09125; -.
DR   Proteomes; UP000186208; Unassembled WGS sequence.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd02619; Peptidase_C1; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR   PANTHER; PTHR12411:SF741; RE20049P; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
PE   3: Inferred from homology;
FT   DOMAIN          113..338
FT                   /note="Peptidase C1A papain C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00645"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   530 AA;  57531 MW;  4A910299A6895367 CRC64;
     MPIRMTDDPK DPNQNDYNDD SGGGGGRSNF PGGGGGLGAL LPLLLGLFKG KGIIVLVVLA
     GAAYFLLGKG GGCNVAQVAQ SLFSQSGYNF NPNEFNKASV YEGLEDDAGK NPLPESVSLL
     KFAPARGNQG QQGSCVAWSS AYGARTVLEA ASTGVDPNQI KFSPSFMYNQ IGLDDCQGSY
     IQRAMEQMSK QGALPLNQFP YSDQDCTTQP NGNQKQEAGQ YKIHGFTRLT NGDNVSSINV
     RAVKEHLAKD APVVIGMMVG QSFMQDMMGR ELWQPQGMDA SQVGMGGHAM CVIGYDDRKF
     GGAFQIMNSW GPEWGKDGVG WVRYGDFKNY VKEAYGIDPL PKRGKVANIP LECSIGLVNN
     ADGKYIQLRS AGTNNFQTVS PIRAGTRFKM SIENATECYI YIFGQEQDGS SYVLFPYLKP
     GETVSKHSPY CGITGYRLFP RDQSMEADTI GTRDYIAIVA SKDELNYNEL NSAISRSRQP
     SYAGKVNEAL QSILIRSASF NNTSDGRIYF KVNANDNKAV ATIVAFDKQK
//
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