RKD2_PYRCJ
ID RKD2_PYRCJ Reviewed; 203 AA.
AC A3MWN6;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Arcadin-2 {ECO:0000303|PubMed:21414041};
GN Name=rkd-2 {ECO:0000303|PubMed:21414041};
GN OrderedLocusNames=Pcal_1636 {ECO:0000312|EMBL:ABO09053.1};
OS Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=410359;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21063 / JCM 11548 / VA1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21414041; DOI=10.1111/j.1365-2958.2011.07635.x;
RA Ettema T.J., Lindaas A.C., Bernander R.;
RT "An actin-based cytoskeleton in archaea.";
RL Mol. Microbiol. 80:1052-1061(2011).
RN [3] {ECO:0007744|PDB:5LY3}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 188-203 IN COMPLEX WITH
RP CRENACTIN, FUNCTION, INTERACTION WITH CRENACTIN, AND DOMAIN.
RX PubMed=27852434; DOI=10.7554/elife.21600;
RA Izore T., Kureisaite-Ciziene D., McLaughlin S.H., Lowe J.;
RT "Crenactin forms actin-like double helical filaments regulated by arcadin-
RT 2.";
RL Elife 5:E21600-E21600(2016).
CC -!- FUNCTION: Part of an actin-like archaeal cytoskeleton
CC (PubMed:21414041). Prevents polymerization of crenactin filaments by
CC binding its C-terminus into crenactin's hydrophobic groove. May act by
CC competing with the D-loop of the following crenactin subunit for the
CC hydrophobic groove (PubMed:27852434). {ECO:0000269|PubMed:21414041,
CC ECO:0000269|PubMed:27852434}.
CC -!- SUBUNIT: Interacts with crenactin. {ECO:0000269|PubMed:27852434}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC Note=Localizes between segregated nucleoids.
CC {ECO:0000269|PubMed:21414041}.
CC -!- DOMAIN: The C-terminal helix is essential for activity.
CC {ECO:0000269|PubMed:27852434}.
CC -!- MISCELLANEOUS: Belongs to a conserved five-gene operon within
CC Thermoproteales denoted Arcade (actin-related cytoskeleton in Archaea
CC involved in shape determination). {ECO:0000305|PubMed:21414041}.
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DR EMBL; CP000561; ABO09053.1; -; Genomic_DNA.
DR PDB; 5LY3; X-ray; 1.60 A; B=188-203.
DR PDBsum; 5LY3; -.
DR AlphaFoldDB; A3MWN6; -.
DR SMR; A3MWN6; -.
DR STRING; 410359.Pcal_1636; -.
DR EnsemblBacteria; ABO09053; ABO09053; Pcal_1636.
DR KEGG; pcl:Pcal_1636; -.
DR eggNOG; arCOG05584; Archaea.
DR HOGENOM; CLU_1340791_0_0_2; -.
DR OMA; LWFEDGL; -.
DR Proteomes; UP000001431; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoskeleton.
FT CHAIN 1..203
FT /note="Arcadin-2"
FT /id="PRO_0000439073"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:5LY3"
SQ SEQUENCE 203 AA; 22555 MW; E10D689E07794C51 CRC64;
MDFPKVLLIR HFTEVLGMKY AGEGGEVLWF EEGLNRVAVG IYFTDLYEEA ELYKRVGALM
GLGASKVFLA VLPDALAFVD PRYFKANGVG LVVVDPAKGV DGVEVKIFAR ARPAAVEPLK
IDAVKAALHE YLASELKRVE ESLFEKVRRY VDQRVEEVKR ALQAVEEAKR AAPPVQRAAA
ESAQEPRGGI GENEWVKILR SKR