ID I2H684_TETBL Unreviewed; 511 AA.
AC I2H684;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=SH3 domain-containing protein {ECO:0000259|PROSITE:PS50002};
GN Name=TBLA0F03490 {ECO:0000313|EMBL:CCH61886.1};
GN ORFNames=TBLA_0F03490 {ECO:0000313|EMBL:CCH61886.1};
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:CCH61886.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH61886.1, 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 -!- SIMILARITY: Belongs to the SH3YL1 family.
CC {ECO:0000256|ARBA:ARBA00007761}.
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DR EMBL; HE806321; CCH61886.1; -; Genomic_DNA.
DR RefSeq; XP_004181405.1; XM_004181357.1.
DR AlphaFoldDB; I2H684; -.
DR STRING; 1071380.I2H684; -.
DR GeneID; 14496995; -.
DR KEGG; tbl:TBLA_0F03490; -.
DR eggNOG; KOG1843; Eukaryota.
DR HOGENOM; CLU_015320_2_0_1; -.
DR InParanoid; I2H684; -.
DR OMA; NTKGRVA; -.
DR OrthoDB; 37167at2759; -.
DR Proteomes; UP000002866; Chromosome 6.
DR CDD; cd11842; SH3_Ysc84p_like; 1.
DR CDD; cd11525; SYLF_SH3YL1_like; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR033643; SYLF_SH3YL1-like.
DR InterPro; IPR007461; Ysc84_actin-binding.
DR PANTHER; PTHR15629:SF2; SH3 DOMAIN-CONTAINING YSC84-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR15629; SH3YL1 PROTEIN; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF04366; Ysc84; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002866};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 452..511
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 243..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..285
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 55132 MW; B38100189F2141D0 CRC64;
MGLNNPVPRG LKAESKKAAN ILRSFVKPNQ VFGQDQVIPP DVLKRAKGLA VITVLKAGFL
FSGRAGSGVI VARLRDGTWS APSGISMAGA GAGGLVGVEL TDFVFILNTT DAVKSFSEFG
TITLGGNVSV SAGPLGRNAE AAASASTGGL SSVFAYSKSK GLFAGISVEG SVIVERRDAN
AKFYGRNVNA KQILGGKVRP PPAVDPLFRI LESRAFNYKN SYDDYYGEDH DNESFYADIP
DSFVSSDASS ARPNTRSSRW RGDGDDSRSY REDYDDDDYD DDYDDNGYDD RRGGGANRGG
RGGGRGGQYL DDGYDDRRST RRGDDYDDDR AYGHGNRDDY GRGDYGSSNS RNASGDYGRG
DYGSSNRDRD YGKGDYGAND SQRGGSRDYY QNQRNSSYGD DNYRSGNSPR NGNGSRDINR
YSSGGSYDRQ APASPPGPSR MTGIPTRDDA VPGSPKAVAL YSFTGEERGD LSFRKGDVIT
IIKKSESQND WWTGRVSGRE GIFPANYVEL V
//
