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Database: UniProt
Entry: I0I5Y5_CALAS
LinkDB: I0I5Y5_CALAS
Original site: I0I5Y5_CALAS 
ID   I0I5Y5_CALAS            Unreviewed;      1320 AA.
AC   I0I5Y5;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Gingipain domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=CLDAP_26330 {ECO:0000313|EMBL:BAM00673.1};
OS   Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 /
OS   STL-6-O1).
OC   Bacteria; Chloroflexota; Caldilineae; Caldilineales; Caldilineaceae;
OC   Caldilinea.
OX   NCBI_TaxID=926550 {ECO:0000313|EMBL:BAM00673.1, ECO:0000313|Proteomes:UP000007880};
RN   [1] {ECO:0000313|EMBL:BAM00673.1, ECO:0000313|Proteomes:UP000007880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1
RC   {ECO:0000313|Proteomes:UP000007880};
RA   Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA   Hanada S., Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC
RT   102666).";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AP012337; BAM00673.1; -; Genomic_DNA.
DR   STRING; 926550.CLDAP_26330; -.
DR   KEGG; cap:CLDAP_26330; -.
DR   eggNOG; COG1572; Bacteria.
DR   HOGENOM; CLU_259905_0_0_0; -.
DR   Proteomes; UP000007880; Chromosome.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.380; -; 4.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR011635; CARDB.
DR   InterPro; IPR001769; Gingipain.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR007280; Peptidase_C_arc/bac.
DR   PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR   PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR   Pfam; PF07705; CARDB; 1.
DR   Pfam; PF01364; Peptidase_C25; 1.
DR   Pfam; PF04151; PPC; 2.
DR   SUPFAM; SSF89260; Collagen-binding domain; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007880};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          3..95
FT                   /note="CARDB"
FT                   /evidence="ECO:0000259|Pfam:PF07705"
FT   DOMAIN          384..452
FT                   /note="Peptidase C-terminal archaeal/bacterial"
FT                   /evidence="ECO:0000259|Pfam:PF04151"
FT   DOMAIN          516..585
FT                   /note="Peptidase C-terminal archaeal/bacterial"
FT                   /evidence="ECO:0000259|Pfam:PF04151"
FT   DOMAIN          707..1019
FT                   /note="Gingipain"
FT                   /evidence="ECO:0000259|Pfam:PF01364"
FT   REGION          602..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..631
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1320 AA;  141026 MW;  F2D4EDF19D7A94A4 CRC64;
     MPNPGETATV RMIFRNRGTA TSSPATFYFY VNPAERPPTQ ATAPSFFSGV PSLPPGGSSQ
     FERSVTFASA GCDHIVYTWV DRDNLVADTD RSNNLVGLQV CVGVQCEVDA FESDDNADNA
     GWLQVGVSQQ RSFCRTTPTG LSTLGDQDWV KFTAFRGLTY TLASLSPGIH ADPRITLWSG
     GMQQVLAGPA GTLDWQPPAN GIYFAQVRNS NGKEGSGPLS GYTLSLSAVP AVTDAFEPDD
     QCGQARTIST DGVRQTRLFQ APGDVDWVKF TIAAGETFAM VADNTGQGVN PLITLFSSCA
     QSRSSDRVME GLNRVEDRSA SDQVYFARIA NQNPDRFGAD AHYSISVLAA ACIPDAQEED
     DTRAQAKPLA LNTAQTHNVC PAGDQDWVKI ALTAGEIYVI RTANLGFAAD TVLELFDGQG
     NRIAINDDYD YVRASRIVFE PSVSGNYYVM VRHHDPTAAG PNTNYDLIVE SGFCVPDEAD
     AAGGDNGPGD ARQIATNGSA VARNFCADPL ARNLGDQDWF RFSAVAGARY HIHTEQLGPN
     ADTVLSLYDR NGVTLLASND DSGAGLSAAI VFTPTVAGDY FVQARQYNTR VVGRESSYQL
     RIEENLPPPP PPTPTPPPPT PTPTPPPPDP SEVRTLILVN RARLEAVHGP APASQIMDKL
     FALADHPDVV GAVLQVESAP AVQGAYNAWL ASPTAFVDID LANAVSGAIR NTVLDFAASA
     PNLAYLVIVG DDRIIPFHRV PEANLAKREN EYADALAGAD ALAAALAADM ILTDDFYADR
     EPGTWKNGEL FVPDYAIGRL IQEPDEIIGQ IDVFLAGQTI DTQRALVTGY DFVQDSATQI
     RNLLVNDGIP SISHADFIGP IWPGSLLRAL MLTSTPAGSR HDLVSINGHA THRSFGVPVG
     GDIQASEVLT ATNNFTRTLV YNVGCHGGLN DPATLDLPQA FVRRGAVYVG NTGFGWGGSG
     IVYSESLMRN FTRQLLTNTR ATVGPALMTA KQLYVSRARL IDGYDVKVLM QTTLYGLPMI
     AITSGGTLSD DDPFPSVDDV ITPPGSFGEE TNVGSFRYGL PQSFGAFGAD DADPNYRVNL
     DGNVDFAAGA PIQPGYYRDL TAPNAGALRG VLFLGGVYTE TSATAPIALA YNEYITDTTP
     SAFDAPGWYP STPFAVQSSA FDDAVRDTVV LALGQYNPES GAQRVFDRMA FDTYYSDSPD
     ITPPKILHVD AVLDAARGQG LFKVEASDAS GVTRVVIAHT DGAGVWSSKD LSYDAAALKW
     TGTITATSTT RYFVQVVDGA GNIAIDDDKG RYYPLLPPLP LAPGRALEIR IFLPQVQRGN
//
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