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
//