ID A0A316VYP9_9BASI Unreviewed; 1138 AA.
AC A0A316VYP9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1 {ECO:0000256|ARBA:ARBA00020357};
GN ORFNames=IE81DRAFT_301880 {ECO:0000313|EMBL:PWN42572.1};
OS Ceraceosorus guamensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=1522189 {ECO:0000313|EMBL:PWN42572.1, ECO:0000313|Proteomes:UP000245783};
RN [1] {ECO:0000313|EMBL:PWN42572.1, ECO:0000313|Proteomes:UP000245783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4658 {ECO:0000313|EMBL:PWN42572.1,
RC ECO:0000313|Proteomes:UP000245783};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC cytoskeleton, actin patch {ECO:0000256|ARBA:ARBA00004134}. Endosome
CC membrane {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004125}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the SLA1 family.
CC {ECO:0000256|ARBA:ARBA00007948}.
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DR EMBL; KZ819378; PWN42572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316VYP9; -.
DR STRING; 1522189.A0A316VYP9; -.
DR InParanoid; A0A316VYP9; -.
DR OrthoDB; 2906837at2759; -.
DR Proteomes; UP000245783; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:InterPro.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd11773; SH3_Sla1p_1; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 3.
DR Gene3D; 2.30.30.700; SLA1 homology domain 1; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR007131; SHD1.
DR InterPro; IPR035800; Sla1_SH3_1.
DR PANTHER; PTHR15735:SF19; ACTIN CYTOSKELETON-REGULATORY COMPLEX PROTEIN SLA1; 1.
DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF03983; SHD1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF50044; SH3-domain; 3.
DR PROSITE; PS50002; SH3; 3.
PE 3: Inferred from homology;
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Reference proteome {ECO:0000313|Proteomes:UP000245783};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 2..67
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 68..130
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 351..411
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 147..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..878
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1138 AA; 121242 MW; 8E2731F782073B4B CRC64;
MAYVSLSKAL YDYAATAEDE LNLKEDDLLY IIDASDTEWW KAKLKTGPED EEKIGLVPAN
YVEEAEPLRQ SRALYDYSPQ TEEELEMKED QLLSVYEDDD DDWLLVRIAD SGAQGKLGFV
PKNYVDEVAA VDGATSLGAP ISAGAAATFD GQAPEEAEEE VEEERQSIPA TFVPPPAGDK
SDEIKMWGVS ALDAKKKKRK GTLGIGNGNL FFASESDKQP VQKFSVLLIE SHALESKGKQ
INLELHEDAG VEDNMIRFVF GSKSEGEEVA QKLEESKSKA IAHGSSATVK SPSPAAGRSL
PPPIASAARP AASPAAAALP PPSRNTSTLP PPARQTASAS PATTPARNGH AAKEACIALY
DFEAQGDDEL SVAENEKLTL VERENEDWWK VRNASGSEGV VPASYIELSD GEDGDEAASS
TQQDEAEREK QEKAAAAMEA TRRTQEAAAR RAREAEERRE EEERRREALK AQPAPAPPRA
APSAVSSASA TRAARDVSVP SGKGAPERPT DSAQAKSRPN PARTRNWVDR TGQFKVEAEF
LGFNQGKIRL HKLNGVIIEV AIEKMSNADI QYLEDVTGKR LTPSSTSRGA DSSTRMDPRS
AGRERDRDRQ REREREQRRR QAQRDGPKRN IDWFEFFLAA GVDVDNCTRY AAAFERDNID
ESILADIESS TLRSLGLREG DIIRVDKFIK RKYKRPDAAP STESKEAAQI RADEEMARKL
QENEQSARRG ASNSPAPNLF SGPDGSLRNN TRRGRPAPKT NGSGSVDPAG IAAAAEGLAR
TVSPPTRAST ASPTVVRKAT HPTGAGGFDD DAWTPRPSST QPSTPGLSAA APKPASVPPT
PPPAPVPAAA PAPTPPTPPA AAPAPAVVSP PPTAAAAPPS DPNSALFDKL AAMKPPSAGL
SPRPGASPAN GSYLSGYNPN APRGPLAPVP GNQGLLSPLV PTSGTGQFVP TSGLGPQATG
YNNGYGGMQP QQTGYMQPQQ TGYMQQQPQQ TGYMQPQQTG YGMGMSMGMS SPGMMSQPTG
YNPQYGISNV SGFGGGMLAP QTTAMPQHQQ QQQHLQPQAT GIQMPMQTGP NDKLGAASIF
GQMKQGTLHQ DSNSNPQSAQ RYDALRPQPT GFAPGGVMGS GFQGNGMYGQ QSGWGGQY
//
