ID G0RD51_HYPJQ Unreviewed; 1115 AA.
AC G0RD51;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1 {ECO:0000256|ARBA:ARBA00020357};
DE Flags: Fragment;
GN ORFNames=TRIREDRAFT_45775 {ECO:0000313|EMBL:EGR50540.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN [1] {ECO:0000313|EMBL:EGR50540.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR50540.1,
RC ECO:0000313|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
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; GL985059; EGR50540.1; -; Genomic_DNA.
DR RefSeq; XP_006963104.1; XM_006963042.1.
DR AlphaFoldDB; G0RD51; -.
DR STRING; 431241.G0RD51; -.
DR EnsemblFungi; EGR50540; EGR50540; TRIREDRAFT_45775.
DR GeneID; 18485060; -.
DR KEGG; tre:TRIREDRAFT_45775; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_45775; -.
DR eggNOG; ENOG502QQC3; Eukaryota.
DR HOGENOM; CLU_003674_0_0_1; -.
DR OrthoDB; 2906837at2759; -.
DR Proteomes; UP000008984; 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 CDD; cd11775; SH3_Sla1p_3; 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; IPR013182; DUF1720.
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 InterPro; IPR035821; Sla1_SH3_3.
DR PANTHER; PTHR15735:SF12; CDC42-INTERACTING PROTEIN 4, ISOFORM B; 1.
DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR Pfam; PF08226; DUF1720; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000008984};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 2..69
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 70..127
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 368..430
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 131..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..807
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1093
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1115
FT /evidence="ECO:0000313|EMBL:EGR50540.1"
SQ SEQUENCE 1115 AA; 119036 MW; 67F04FEF7C214C92 CRC64;
MGFLGIYRAL YDYTPNEDAE LAIKAGDLLY ILEKNDDDGW WKAKKKAGTD DEDEPTGLIP
NNYVEKAETV GHARAIYEYT RQTDEELSFP EDAALEVFDT SDEDWILAGY DGEYGFVPAN
YIELQAAAPA SAPAPPAAPA LPQRPTSQSI TTDDSTPLSE DVPAAASPVA VAPAVAPAAD
PAAAIANVMQ NRQSTKEPMT IRFKEPDLSD EESIRSPALP TRPRPQSQAY SVSSEPPSKP
ERTVESQPKG HLIPGNFHLY NINEMVSVMG KKKKMPTTLG INLQTGTILI APERAENDPP
QEWTADKMTH YSREGKHVFM ELVRPSKSID FHAGAKDTAE EIVASLGELA GAARAEGIRE
IIAAGSQKRQ KKGTILYDFM AQGEDEVTVA AGDEVAIIDD TRSEDWWMVR RLKNGKEGVV
PSSYIEFSGT ITPPSGGQIP ARSMVEQNRL EEIRLTKEAM KASREPQQVG LGTPLPRRGS
SLVATDDGNI SAQQRPRREN GRTDSGSHSA NKSKPDPSKV RVWTDRSKSF SVEAQFLGLK
DGKLHLHKMN GVKIAVPIAK MSHEDLVYVE NLTGISLDDE RPLADVKRSK PPEQKKAPAV
GASVDKPARP EYDWFQFFLS CDVAVGLCER YAQAFTRDSM DESVLPDVDA SVLRNLGLRE
GDIIKVMRTL DAKFGRERGN KVNGDGDGGL FSGPGGALRN NTRKGRPAPA VQTGDVVDAA
VFATKDGNST AETAAKPASP PSPAKSPKRP AGGFDDDAWD VKPTKQEQQT QAQPSAPPAE
APAKNTTPAP AAAPAPAPAP APAPAPPALT GSLQELSLLT TPLEPSKTEP QPQPAAPLVT
DSKAPAPAPQ QPPLGASPAF FSTVPQPNQV QPSLTGVHIS PKTLGRQRPI APSISPPVQG
SLGVPPPPQR PLSAPQTTLP QGMFAAPALV PQVTGLVQGQ VAPPGQSLSD LAQARLQQQY
AAQMQAMQPM QPMQPMLTGY VGPQPQGLGP FPQGAPAPYL QPMMTGAPGY IDPSRMSQYG
GLQPQPTGFQ PGLGQSPFGS GSINNFLPPP LQPQPTGFQS LQPQPTGATN ELKPPMQPLV
PQKTGPPPPV RFGVTPETKK LTPQATGRRA NLAQA
//
