ID   G2FB90_9GAMM            Unreviewed;       219 AA.
AC   G2FB90;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Ankyrin {ECO:0000313|EMBL:EGW56028.1};
GN   ORFNames=TevJSym_aa01720 {ECO:0000313|EMBL:EGW56028.1};
OS   endosymbiont of Tevnia jerichonana (vent Tica).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW56028.1, ECO:0000313|Proteomes:UP000005167};
RN   [1] {ECO:0000313|EMBL:EGW56028.1, ECO:0000313|Proteomes:UP000005167}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA   Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA   Sievert S.M., Schweder T.;
RT   "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT   jerichonana share an identical physiology as revealed by proteogenomic
RT   analyses.";
RL   ISME J. 0:0-0(2011).
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:EGW56028.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AFZB01000001; EGW56028.1; -; Genomic_DNA.
DR   RefSeq; WP_006473627.1; NZ_AFZB01000001.1.
DR   AlphaFoldDB; G2FB90; -.
DR   eggNOG; COG0666; Bacteria.
DR   Proteomes; UP000005167; Unassembled WGS sequence.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   PANTHER; PTHR24193:SF121; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24193; ANKYRIN REPEAT PROTEIN; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 5.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
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:UP000005167};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..219
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003428788"
FT   REPEAT          58..90
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          119..153
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          154..186
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ   SEQUENCE   219 AA;  23841 MW;  7B3B1883383BD618 CRC64;
     MKLHPILLPS LLALLLMAGC SKPDRPTINL YRAVHVGDID QIERNLYWDA DINATGPDGR
     TPLHVAAERG LLVVVSILLD HGADIDAKNT FGKSPIYTAV MARRPLIARQ LADQGAQFEP
     NEMLIEAVRS NSASRDIIEF LIKRGAKINV TDKDGNTPLH IAVLQNHRVI VKHLIAKGAE
     VNQRNHAGQT ALQLAIANNS EAIIAILHKY GAVAGKPDM
//