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Database: UniProt
Entry: M6UCU8_9LEPT
LinkDB: M6UCU8_9LEPT
Original site: M6UCU8_9LEPT 
ID   M6UCU8_9LEPT            Unreviewed;       540 AA.
AC   M6UCU8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Caspase domain protein {ECO:0000313|EMBL:EMO40666.1};
GN   ORFNames=LEP1GSC186_4445 {ECO:0000313|EMBL:EMO40666.1};
OS   Leptospira noguchii serovar Autumnalis str. ZUN142.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1085540 {ECO:0000313|EMBL:EMO40666.1, ECO:0000313|Proteomes:UP000012153};
RN   [1] {ECO:0000313|EMBL:EMO40666.1, ECO:0000313|Proteomes:UP000012153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZUN142 {ECO:0000313|EMBL:EMO40666.1,
RC   ECO:0000313|Proteomes:UP000012153};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Matthias M.A., Vinetz J.M., Sutton G.G.,
RA   Nierman W.C., Fouts D.E.;
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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:EMO40666.1}.
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DR   EMBL; AHOP02000030; EMO40666.1; -; Genomic_DNA.
DR   RefSeq; WP_004421829.1; NZ_AHOP02000030.1.
DR   AlphaFoldDB; M6UCU8; -.
DR   Proteomes; UP000012153; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
DR   InterPro; IPR011600; Pept_C14_caspase.
DR   PANTHER; PTHR48104:SF30; METACASPASE-1; 1.
DR   PANTHER; PTHR48104; METACASPASE-4; 1.
DR   Pfam; PF00656; Peptidase_C14; 1.
DR   SUPFAM; SSF52129; Caspase-like; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
PE   4: Predicted;
FT   DOMAIN          25..266
FT                   /note="Peptidase C14 caspase"
FT                   /evidence="ECO:0000259|Pfam:PF00656"
FT   REGION          268..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..316
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   540 AA;  59470 MW;  C1EE5648E308D83D CRC64;
     MKSKLSAIVV CLILFFATDV FAQKRYGLIF GTNYTGNKAG IPELNLCEAD ASYLNDEIRK
     VGNFDEVKIV LGKEVTKDNI EKEIKALAKK AGDNDTVLLY FSGHGAFQRD ASAKNGMRNL
     IICYDRPHLP DDELNKYLEK IKSPKTVFIF DCCFSGGIAK KGKSTRGSAD VPIPEGSNGT
     VKQDAEDFFF QDKTIISSAD DNQTAIEVGG SINHGIFTYN FGKALSSADL NKDNVVTALE
     AFFKSREETV QMAKKFQHEQ IPQISGNASG IFLSGKKSPE PPKPVDPPKP PAPSVEPEPD
     PVKPDPSQPV VTPEEPPVVP TNERGDLVLK TTIIQDRAYG LSDLPPDILI FAKKKRKGNR
     NVKVYIDDQE FSSTITSNSS NFWGAVKRQG QLIPGNIYTI TLNKVPAGVH KITIKADDYP
     EIQETFAVLP NKKNELPINV SMSGFGAIQG KVFYKTLDNP VINQPIFMPT ISSVTGIQKL
     NTDNEGNFWF TNLKPGDYEI KASFAEDLNL NNSMINVREG DVTKVDVILN VKMPSTKTKY
//
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