ID A0A0D0BAM8_9AGAR Unreviewed; 563 AA.
AC A0A0D0BAM8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Septation protein imp2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=GYMLUDRAFT_43373 {ECO:0000313|EMBL:KIK60765.1};
OS Collybiopsis luxurians FD-317 M1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC Collybiopsis luxurians.
OX NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK60765.1, ECO:0000313|Proteomes:UP000053593};
RN [1] {ECO:0000313|EMBL:KIK60765.1, ECO:0000313|Proteomes:UP000053593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK60765.1,
RC ECO:0000313|Proteomes:UP000053593};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN834773; KIK60765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0BAM8; -.
DR HOGENOM; CLU_003525_1_1_1; -.
DR OrthoDB; 2025446at2759; -.
DR Proteomes; UP000053593; 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; PF00018; SH3_1; 1.
DR PRINTS; PR00499; P67PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
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, ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000053593};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 32..286
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 500..563
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 295..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 87..114
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 301..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..425
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 62232 MW; 74FA0831F55E8C25 CRC64;
MSVRTQGSVS SLSKYATAKS PGIDLYNGST SRDFCNSFWG EGDAGVNVLF ARMRGAMRTT
DSLRNFWKER AAIEEEYARK LIQLAQNAMG KDEIAELRNA LDTLQLETEK LANTHLQLAS
QIRTEMEEPT AALLNKQNDH RRTIQASVEK KYKSKLSSET HVSKAREKYQ TDVVRIANYN
AQLENQPQSP EADKIRLKLK HAMQTVNANE KDYKAFTKAL ADMIPGWEND WKLYCDLSQD
LEEERLDFMK DNLWAYANAV STVCVADDES CETIRTVLDQ LETDRDIEVF VHEYGTGNSI
PNPPEFITGP VNADGSSSRT SLVGNLSSPA VSTRPANFNR TTRRPSTNAP PYNHNAGGSG
AQSPPPSQTT LQRDNSAAAS TTGGGRTHRT PSPTRSTNVA SPPRMTPNNS VNVPPPPPAV
PSSPPQMHSQ PSSQQMRNGM NGGYGEREMA EARANNVSTA SGDSQPNTRR MTLPPQPTDV
EVAAPIPPIP PSGERGNTNK ILFYVEAMYD YTATIEEEFN FQAGDIIAVT DIPDDGWWSG
ELLDEARREE GRHVFPSNFV RLF
//