ID I2GXC3_TETBL Unreviewed; 539 AA.
AC I2GXC3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=CBS domain-containing protein {ECO:0000259|PROSITE:PS51371};
GN Name=TBLA0A09940 {ECO:0000313|EMBL:CCH58775.1};
GN ORFNames=TBLA_0A09940 {ECO:0000313|EMBL:CCH58775.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH58775.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH58775.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- FUNCTION: Involved in DNA replication and cell separation.
CC {ECO:0000256|PIRNR:PIRNR018148}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR018148}.
CC -!- SIMILARITY: Belongs to the SDS23 family.
CC {ECO:0000256|ARBA:ARBA00006624, ECO:0000256|PIRNR:PIRNR018148}.
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DR EMBL; HE806316; CCH58775.1; -; Genomic_DNA.
DR RefSeq; XP_004178294.1; XM_004178246.1.
DR AlphaFoldDB; I2GXC3; -.
DR STRING; 1071380.I2GXC3; -.
DR GeneID; 14493474; -.
DR KEGG; tbl:TBLA_0A09940; -.
DR eggNOG; KOG1764; Eukaryota.
DR HOGENOM; CLU_024459_1_1_1; -.
DR InParanoid; I2GXC3; -.
DR OMA; MHKERIS; -.
DR OrthoDB; 1449566at2759; -.
DR Proteomes; UP000002866; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042149; P:cellular response to glucose starvation; IEA:UniProtKB-UniRule.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IEA:InterPro.
DR Gene3D; 3.10.580.10; CBS-domain; 2.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR016711; Ssd23.
DR PANTHER; PTHR13780; AMP-ACTIVATED PROTEIN KINASE, GAMMA REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR13780:SF163; PROTEIN SDS23-RELATED; 1.
DR Pfam; PF00571; CBS; 2.
DR PIRSF; PIRSF018148; UCP018148_CBS_YBR214w; 3.
DR SMART; SM00116; CBS; 3.
DR SUPFAM; SSF54631; CBS-domain pair; 2.
DR PROSITE; PS51371; CBS; 2.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR018148};
KW Reference proteome {ECO:0000313|Proteomes:UP000002866}.
FT DOMAIN 219..277
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 309..366
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 539 AA; 60170 MW; 31066F090E6BCE21 CRC64;
MPNSILETGT NLSPNNPTTN NIARHASIVE LLSTPPQLPI PPRNLQSQIN QIHDLKKDTT
HDLKRDNSNS SINSNSTSIS NLSINSITQD NLPIKDNNQN SIHHITSNLN TNELLSSVHN
HKWQFIKLSQ LIEKNKLITI PNNYSIEESF NTLMKYTLTS CPVMSNPNDM NCLTFDYNDL
NSYLLLVLNK FTINDPKKSK LIMDCQSGKP VPVGEIIQLT PKDPFYKLSE NDNLSNVISI
LGSGVHRIAI TNNEMTQLKG ILSQRRLIKY LWDNARSFSD LEPLLNKSLQ SLKIGIINND
HHNSNNNNTT SKVISIQDDQ PLIQALFKMH KERISSIAVV DICNNLIGNI SVTDVKHVTR
TSQYPLLNNT CRHFISIILN FRGLENGKDS FPIFHVYPST SLSRTLAKLV ATQSHRLWIV
QPPESTLELT LSNSSDDSNH LSSFTSENAY KPRGKLIGVV SLTDILNLLA TRQTEHKEID
PQSARRMKAS STESQSTSGT TSQSISHSTS HSTSYSTNST QSISENTTHT KSENANITA
//