ID B6BHQ4_SULGG Unreviewed; 456 AA.
AC B6BHQ4; H1FTT9;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Putative cysteine-peptidase containing Ankyrin r epeat domain {ECO:0000313|EMBL:EHP30053.1};
GN ORFNames=SMGD1_1529 {ECO:0000313|EMBL:EHP30053.1};
OS Sulfurimonas gotlandica (strain DSM 19862 / JCM 16533 / GD1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurimonadaceae; Sulfurimonas.
OX NCBI_TaxID=929558 {ECO:0000313|EMBL:EHP30053.1, ECO:0000313|Proteomes:UP000006431};
RN [1] {ECO:0000313|EMBL:EHP30053.1, ECO:0000313|Proteomes:UP000006431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD1 {ECO:0000313|EMBL:EHP30053.1,
RC ECO:0000313|Proteomes:UP000006431};
RX PubMed=22203982; DOI=10.1073/pnas.1111262109;
RA Grote J., Schott T., Bruckner C.G., Glockner F.O., Jost G., Teeling H.,
RA Labrenz M., Jurgens K.;
RT "Genome and physiology of a model Epsilonproteobacterium responsible for
RT sulfide detoxification in marine oxygen depletion zones.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:506-510(2012).
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:EHP30053.1}.
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DR EMBL; AFRZ01000001; EHP30053.1; -; Genomic_DNA.
DR RefSeq; WP_008336735.1; NZ_DS995286.1.
DR AlphaFoldDB; B6BHQ4; -.
DR STRING; 929558.SMGD1_1529; -.
DR PATRIC; fig|929558.5.peg.1520; -.
DR eggNOG; COG0666; Bacteria.
DR eggNOG; COG4249; Bacteria.
DR HOGENOM; CLU_599806_0_0_7; -.
DR OrthoDB; 9768004at2; -.
DR Proteomes; UP000006431; Unassembled WGS sequence.
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; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR011600; Pept_C14_caspase.
DR PANTHER; PTHR24180:SF45; ANKYRIN REPEAT FAMILY PROTEIN; 1.
DR PANTHER; PTHR24180; CYCLIN-DEPENDENT KINASE INHIBITOR 2C-RELATED; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00656; Peptidase_C14; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52129; Caspase-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Reference proteome {ECO:0000313|Proteomes:UP000006431};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 83..115
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 116..148
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 221..449
FT /note="Peptidase C14 caspase"
FT /evidence="ECO:0000259|Pfam:PF00656"
SQ SEQUENCE 456 AA; 51271 MW; 5E5E4EBCE6434596 CRC64;
MILKYINIFI ISIFVSLIFT GCVSKFKTLA KDGNIDTIHN ELKSIEDKQE LLAWSAYYGK
FDKVKYLLEN GADINYNKGG TYDLPPAIIM ATAGNNLDMV KYLVKNGADV NKQTGYGRNA
VLAAALQGRL NIVQYLAEQG AELYVADNLF GKNTITQLQE SGYGYFIPVI LNIQKERKAK
LEKQQLPLKT QIASSEDKNS GLDDISSLLK KSEIQKIDNT KWLFIIAIEN YEYTSPVVYS
ANSASQFKTV MQKRLGISEK NTRTLINQGA TSAKIDYNLK DMLRRVKEGD TIYFYYSGHG
IPVASQNNAP YMLAQDMNPA YITDERFKLQ NIYKSLSDSK AAKVVAFMDS CFSGGTDNEH
LIKGVAAARM VPKKVTFDKS KMIVISAGSG TQYSNKYDDK ANRLFSYYLM RGLIKNNNDV
QRLYDYIKSN VQDKSYEMGA SYEQVPVYDG NIGLEF
//
