ID A0A0S3T6B8_PHAAN Unreviewed; 363 AA.
AC A0A0S3T6B8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 03-MAY-2023, entry version 26.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAU00597.1};
GN Name=Vigan.10G220600 {ECO:0000313|EMBL:BAU00597.1};
GN ORFNames=VIGAN_10220600 {ECO:0000313|EMBL:BAU00597.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAU00597.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAU00597.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
CC -!- SIMILARITY: Belongs to the SGT1 family.
CC {ECO:0000256|ARBA:ARBA00008509}.
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DR EMBL; AP015043; BAU00597.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3T6B8; -.
DR Proteomes; UP000291084; Chromosome 10.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR CDD; cd06466; p23_CS_SGT1_like; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR007699; SGS_dom.
DR InterPro; IPR044563; Sgt1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45862; PROTEIN SGT1 HOMOLOG; 1.
DR PANTHER; PTHR45862:SF2; SGS DOMAIN, HSP20-LIKE CHAPERONE, ACETYLTRANSFERASE A, AUXILIARY SUBUNIT-RELATED; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF05002; SGS; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51203; CS; 1.
DR PROSITE; PS51048; SGS; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000291084};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 2..35
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 162..251
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 272..363
FT /note="SGS"
FT /evidence="ECO:0000259|PROSITE:PS51048"
FT REGION 343..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 363 AA; 40976 MW; 21A6882308BB1951 CRC64;
MAKELERKAK EAFFDDDFAL AVDFYSEAIK LDPKDAHLFA DRAQAHIKLN AFTEAISDAN
NAILLNPSLS KAYLRKGTAC IKLEEYHTAK LALQSGAAFA PDDLRFSKLI QECDRFISEE
PNDFVSTISS NGFHLNNTND GVTKEAEEDS LVSQIKEITI NRPKYRHEYY QKPEEVVVTI
FAKGISAKDL VADFGEQILS VTIDVPGQDV YRFQPRLFGK IIPNNCKVVV LSTKIEIRLA
KAEAINWTSL EYSKDTLPTK ISMPIVQSQR PSYPSSKAKT KDWDKLEALV KKEEKEEKLD
GDAGLNKLFR DIYQNADEDM RRAMSKSFVE SNGTVLSTDW KEVGSKKVEG SPPDGLELKK
WEY
//
