GenomeNet

Database: UniProt
Entry: S2JFV6_MUCC1
LinkDB: S2JFV6_MUCC1
Original site: S2JFV6_MUCC1 
ID   S2JFV6_MUCC1            Unreviewed;      1200 AA.
AC   S2JFV6;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=SH3 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF1544_05788 {ECO:0000313|EMBL:EPB87362.1};
OS   Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS   agent) (Calyptromyces circinelloides).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB87362.1, ECO:0000313|Proteomes:UP000014254};
RN   [1] {ECO:0000313|Proteomes:UP000014254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KE123969; EPB87362.1; -; Genomic_DNA.
DR   AlphaFoldDB; S2JFV6; -.
DR   STRING; 1220926.S2JFV6; -.
DR   VEuPathDB; FungiDB:HMPREF1544_05788; -.
DR   eggNOG; KOG2398; Eukaryota.
DR   InParanoid; S2JFV6; -.
DR   OMA; IMMARSI; -.
DR   OrthoDB; 2025446at2759; -.
DR   Proteomes; UP000014254; Unassembled WGS sequence.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IEA:UniProt.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:UniProt.
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; 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; PF14604; SH3_9; 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   Reference proteome {ECO:0000313|Proteomes:UP000014254};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          28..285
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          1130..1194
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          423..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          762..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          913..1122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..446
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..480
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..528
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..708
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..739
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        762..792
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        939..971
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1012..1035
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1047..1121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1200 AA;  133418 MW;  1E7EC8FB01D59FE2 CRC64;
     MASGISHPQQ QHQQHQQQQQ QTSNNTGINF KDAFWDDQNK GVEILSSRLR KSKDTCEELK
     KLYQLRASIE QDYGERLLKL AQTSRIGEFE ENSFAETLSR IPSALETTAR AHIDLAQQLQ
     DHLEVPLDGF LKDQRDVRKM QQQHIENSKQ LKNLHEADVA RAKDYCLSEY NKLRSMEAYR
     SELSNGSTDD IAKIEKEIDE QKRMVAVADQ VYKRSVDNYN AVNDKWVNDW SSTADVYQEM
     EVKRISYLRS TLWSFANMMT ITFSIDEECC DRIRTALEIT DVQKDVTAFV QRYGTGNRIP
     APMQYEALYD ASHVQTTMPT SAVNKSSAPV MATAVGVAAA APATIGTMAA VSNLSNSDQP
     LSAPLPKTSS SANSLSDATP RGASESAAAA KKLPPHPPVT ILTNPDEELK SVDRQLRQLE
     VQNTTPQSEN ENHQFNIMTS PQQLTSADVD EKREIVDKEQ QQPPLSGVTN TTDQSNGPVS
     TAMKEVEQIL NQKNNSQDAV ATTATAETAT SKNRESYASS SHTDNGPKQS LPPIMMARSI
     PPSAAAGKTA SPTASNRPVS DDFSGSIYNA LGMKEEPATS QYDLHKEQSD SVTKSNSAVE
     LAPLSSETHI LMPFDTLATR NESTISNGSG KDMNQKYKPM PNPIYNSNGA MIAAKDIPPS
     KNEMNYAAPE TVPNMKPVVG VRTSSLLLSQ KPSSPQNGSR TSSLNREMIN NKNDEDDYED
     NEDEKEYHNR MPRPPPKDER WVISSIRRPQ QLPVRTMNAK MFDGTTSSRN SMASPTPPPI
     VSASSAEHSP AADLNTSPAA GADNVEDDIH RHPKPHRPAI PLTIDIPNSV KPASDVAQNA
     AQQVIAEGKR RSQMSPVQQN MDLHQQPQSQ PQTMDRNVIR GYINNQQNGM EEGGIRPAPW
     QEEFNNDDHR VMRAPMPNNG SGYYSNGHAG YQPGMPGPRS SSIKLSEQQQ QQQQQQQQML
     MQQQQQQQQQ QHFEEETKKR FGKNAKQFSG ESSVKSKEKE NKTGRFSLGF FGGGKKEKKK
     EKEKEKEKEK EKESAAAAAA AAAAMYTQQP PDSSYMQQQQ QQPYMQQQPR PLSQQQMYQK
     QPSLHELSQS DLKSNHSGQQ QQHTPQAQQQ ATQQQLPQPQ LVKAPLSADR FIGFAKAQWP
     FEATIDGEMS FQADEVVGII HKQMDGWWEA ERLGPVGAGQ RGLVPGNYML DNQPPPPSLQ
//
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