GenomeNet

Database: UniProt
Entry: S0DLB2_GIBF5
LinkDB: S0DLB2_GIBF5
Original site: S0DLB2_GIBF5 
ID   S0DLB2_GIBF5            Unreviewed;      1102 AA.
AC   S0DLB2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1 {ECO:0000256|ARBA:ARBA00020357};
GN   ORFNames=FFUJ_01575 {ECO:0000313|EMBL:CCT63399.1};
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT63399.1, ECO:0000313|Proteomes:UP000016800};
RN   [1] {ECO:0000313|Proteomes:UP000016800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC   {ECO:0000313|Proteomes:UP000016800};
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HF679023; CCT63399.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0DLB2; -.
DR   STRING; 1279085.S0DLB2; -.
DR   EnsemblFungi; CCT63399; CCT63399; FFUJ_01575.
DR   VEuPathDB; FungiDB:FFUJ_01575; -.
DR   HOGENOM; CLU_003674_0_0_1; -.
DR   OrthoDB; 2906837at2759; -.
DR   Proteomes; UP000016800; Chromosome 1.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
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; cd11774; SH3_Sla1p_2; 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; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR   PANTHER; PTHR15735:SF21; PROTEIN NERVOUS WRECK; 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; 2.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016800};
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          365..427
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          125..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          676..922
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1046..1102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..222
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..246
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        721..745
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        823..837
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..875
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        876..903
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1088..1102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1102 AA;  118285 MW;  A3D7275CE9B5F47F CRC64;
     MGFLGVYRAL YDYVPQAEGE LAIKDGDLLF ILDKNGDDGW WKAKKKAGAD DEEEPTGLIP
     GNYVEEAQPV DHARALFDYT RQTDEELSFH EDATLAVYDT SDPDWILTGL DGEYGFVPSN
     YIEMGAPAEL PQSPPPNPEV ASPDLPNDTA PTPSNPAAAI AGVMHGRSVS QQSQQPAAPR
     QPPRASVTFS EPPEVEDEPV RSPTLPARPR VPAPPSPTYD EPPSPIHTRS LQDHRDPDRR
     QDVERTPGGF HMYNINEMIS IMGKKKKMPT TLGINLLTGI ILVAPEHASD GPSQEWTADR
     MTHYSREGKH VFMELVRPSK SVDFHAGAKD TAEEIVSMLG ELAGAVRAEG LREVIMAGTQ
     GSSGGGQKKG QVLYDFMAQG DDEVTVAVGD EVLVIDDTKS EEWWQVRRLK NGKEGVVPSS
     YIEITGSISL PSSSGINSAK SLVEQNRLEE IRLTKEAMKA GKEPQQVGPG MPLPERGSSL
     MARETGNNSG QQRSRRENGR SDGGSQSRSK SKPDASKVRT WTDRSRSFSV EAQFLGLKDG
     KIHLHKMNGV KIAVPITKMS REDLEYVENF TGISLEDDKP LADVKRARSA EKKSPERSTS
     AGATVDKDAK SDYDWFQFFL SCEVAVGLCE RYAQAFIKDS MDESVLPDVD ATTLRALGIR
     EGDIIKVMRT LDAKYGRSRG GKRGTADGVD GEGGLFSGPG GALRNNTRKG RPAPAVQTSD
     VVDASAFSRG ESSKTGENDS RSPPPTSPTN KSPEPRQASS SGFDDDAWDV KPSKQQSPPK
     AQPAVESVQK PAPEPAPVSP PPPALTGSMQ ELSLLSTPLE PTRAEPAPAP APAPVIAAQP
     TSTPVSQPLG GATPSFFTSV AQVRQRPTPP QGTANQGSLV PPPPQRPLSA PQSAQPSGFA
     PPPMMPQMTG ALQGQVAPPG QSLSEITQAR LQQQYTAQMQ QQQAPQQMQP NMTGFPGQQG
     PGLMSFPTGA GQFMQPMMTG MQGPNQFVPM QAQSTGFQPP FPATQSMYGV PTGGINSYLP
     PALEPQRTGM PGLQPQTTGM TNMGGIGSMN NVQVPQPLQP QQTGPPPPVR FGVTNETRKL
     APQATGRRAN LAQATPQNPF GF
//
DBGET integrated database retrieval system