ID   B6F186_CLOPF            Unreviewed;       700 AA.
AC   B6F186;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=ThiF protein {ECO:0000313|EMBL:BAG75503.1};
OS   Clostridium perfringens.
OG   Plasmid pCP8533etx {ECO:0000313|EMBL:BAG75503.1}.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1502 {ECO:0000313|EMBL:BAG75503.1};
RN   [1] {ECO:0000313|EMBL:BAG75503.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NCTC 8533B4D {ECO:0000313|EMBL:BAG75503.1};
RC   PLASMID=pCP8533etx {ECO:0000313|EMBL:BAG75503.1};
RX   PubMed=18776010; DOI=10.1128/JB.00939-08;
RA   Miyamoto K., Li J., Sayeed S., Akimoto S., McClane B.A.;
RT   "Sequencing and diversity analyses reveal extensive similarities between
RT   some epsilon-toxin-encoding plasmids and the pCPF5603 Clostridium
RT   perfringens enterotoxin plasmid.";
RL   J. Bacteriol. 190:7178-7188(2008).
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DR   EMBL; AB444205; BAG75503.1; -; Genomic_DNA.
DR   RefSeq; YP_002291130.1; NC_011412.1.
DR   AlphaFoldDB; B6F186; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR028090; JAB_dom_prok.
DR   InterPro; IPR032865; Prok-E2_A.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   Pfam; PF14457; Prok-E2_A; 1.
DR   Pfam; PF14464; Prok-JAB; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR   SUPFAM; SSF102712; JAB1/MPN domain; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Plasmid {ECO:0000313|EMBL:BAG75503.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          308..457
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
FT   DOMAIN          574..688
FT                   /note="JAB"
FT                   /evidence="ECO:0000259|Pfam:PF14464"
SQ   SEQUENCE   700 AA;  80832 MW;  14853B50544BAAC6 CRC64;
     MEFDIKEFEP IKLLCSTNEI KYKAPLVFSD RNDFPVEKLP HTLAMGLNYS YICLHRGNID
     DWYIDHSVED FVNRIRFWFS DAACNNLIKP GDDFEPMINY TETGNIVYSY NKLTKFIEEY
     WSNNNEKNGF AYAMCCFNNK EESEHLNINE ESFSVQILEV FEKENLTSLL QKLNRERIKN
     KNVFLGIVGW GQKNSKYNEY FKLINITLEE LYEFNKKIGI DLKRALNILK DKKIPNIIAL
     ISAINRPSKV IGFEKNIEFI NFLFKIKKVN EFNVNKIKED GKALVVKHLE PLTRNLAANI
     STLSCKKNPK ILFVGAGALG SKIIFHLARN GYTDISVVDN DILVPHNLVR HALFADSISK
     NKAKEIINKL NNIYIMDKNK NFKYYSESFI NFAINTDLSI YDVLIDCSAS KSVFSFISEY
     SKKLPALVIR AELANKGKLG LVLKENINRN LKIDDIQVSL FNYALSNTEV AEWLKNYQKL
     KENFEGAQFE DITIGMGCNT NTMKISDNII SYHAAIFSSY IKKHITNDIQ NGEFLISYFD
     ENNLSENYCK IISVQDFISV NTSENNWTTK IYRKAYERIL NELNNSKPNE TGGILLGNIN
     KNNKTIYVTD IYIPKDSKYG PYLFTKGSYG TKEYLEHVLK STGNIINYVG DWHTHPESST
     NMSSKDKKSL LELKEYLKEY SYPAHIMIFN EKDISSYVIS
//