GenomeNet

Database: UniProt
Entry: A0A066XR68_COLSU
LinkDB: A0A066XR68_COLSU
Original site: A0A066XR68_COLSU 
ID   A0A066XR68_COLSU        Unreviewed;      1402 AA.
AC   A0A066XR68;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=SH3 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CSUB01_07075 {ECO:0000313|EMBL:KDN71377.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN71377.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT   of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(2014).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDN71377.1}.
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DR   EMBL; JMSE01000195; KDN71377.1; -; Genomic_DNA.
DR   STRING; 1173701.A0A066XR68; -.
DR   eggNOG; KOG2398; Eukaryota.
DR   eggNOG; KOG4200; Eukaryota.
DR   HOGENOM; CLU_003525_0_0_1; -.
DR   OMA; PMLDRMH; -.
DR   OrthoDB; 2025446at2759; -.
DR   Proteomes; UP000027238; Unassembled WGS sequence.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IEA:UniProt.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:UniProt.
DR   GO; GO:0140042; P:lipid droplet formation; IEA:UniProt.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07651; F-BAR_PombeCdc15_like; 1.
DR   CDD; cd00174; SH3; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR009617; Seipin.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR23065:SF7; CYTOKINESIS PROTEIN 2; 1.
DR   PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF06775; Seipin; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        1027..1049
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1240..1265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          8..261
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          964..1035
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          270..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          753..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          906..959
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1292..1402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..405
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..428
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..474
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..553
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..625
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..784
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        843..879
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1292..1306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1376..1402
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1402 AA;  152342 MW;  31C38625402CC031 CRC64;
     MEAPSVALSF ANNFWGKDDA GVGPLLDRML AAKQTCDELK AFYSARASIE DEYARKLLSL
     CRKSLGSHET GSLKTSLDTV RGEVESMAKQ HQSIAAQMKT ELEEPLAAFA GAMKERRKIV
     QNGIEKILKT KIQQTQHVNK TRDRFEQECL KIKGYLAQGH MVMGQEERKN KAKLEKTQIS
     VATSNTEYEN AVKALEDTTA RWNREWKAAA DKFQDLEEER LDFTKSSLWT FANVSSTVCV
     SDDASCEKIR LSLEKMDVET DIISFIKEQG TGQEIPDPPK YINFCRGDIN DTQSESSDDD
     NYSVAQFPRS INPAFRSSSP QPSTYESHHD PNSSLAQDLG HKESAPVSSR SAAVPDVGRK
     EASSSTPRHQ APDPVRADTS PSSKGFASEQ SHKNAGSSSR SFMLEIEQDD GSPSSRRHFQ
     DMSRREMVPS TAREAPLPTQ RMPPAVDKLR QAVPTTQQHI QQQQQQQSRP HVDASQHGSF
     AAVPHDPYPL DGMTMLCRTG PQSERSSHPP SARPSSRDSQ SDYSNPTSIS SQEPPSGKVS
     PVKQEQASAP PSASDKQVLK KRSGFFQNHS PFRRKSTKDT QGPPANRNTW HPVSAQGSPS
     RRPQLSTQET SNLLGNRSAN SPEPIDANAS LALNVGQNVF SVTTPDLEKR KGSSAQPSQP
     ETDPIALALA ELKGVGVGKQ SSVRVSADRY HGIATPTPSS QPFSRSVPAA ASNGGTTIAG
     LGGTPPPYDQ QVVQRLGVPP QAVTAKAMKE TSQKFADQTR SMFNPVKRPG SGYSGTTQSR
     PMTRGSDVPR AASPAPIRSA SPRAAPAEDI RSAYRSSPRS ASPRTGLAED VHGEYGSASP
     NPRGSVGRDT SQMSSTPRRG SEQPYYRQNS PSSVSRTASP APYLEKMRPG SSHVANDMAI
     QLAPLGDDSY GSMRGRGGNR PGTSSSNRAM GLYEGGGPPG QGDSRQRSKS VADPSRQYTR
     DGRPILHFAR ALYMYQAAIP EELGFSKGDL LAVLRHQDDG WWEAEEVLGK ASRAATSKTA
     QRTLVNVSLL VGASLFLLPF AIVASILFFR NYLPDQVVTA PVHLQYGSGV NPFGTAAIPT
     SALRTQQEYD VTVTLSMPRS PANTHRGNFM IALHLLDAGA LSTGYDKFQP QIPPEPYSHF
     DGKSVLFSSR RPALVPYQDP LVSLASRIFF LAYHILFVDS QTCVLKVPMA ERVELGRGSS
     LPSSAYLEIQ GGQNIETYYA SVTLTAQLRG LRWLMYHYRL ATLTSAVLLF WASEVLFMAM
     AWLVWSVLSG SGSGSGSRTG AGKALEEVSS KAAGRIKKED GSGVDELSDA PRTFPTYGNQ
     APLRYEPEIK EEAQAGPRME DLLPLGGEAD DEEEDDGRGG YKGDSGIGTS YSEDGSSSVR
     RRRIDKGGGL ATKEHCRDAE YD
//
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