ID A0A2G4STJ0_RHIZD Unreviewed; 833 AA.
AC A0A2G4STJ0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=FCH-domain-containing protein {ECO:0000313|EMBL:PHZ12071.1};
GN ORFNames=RHIMIDRAFT_313598 {ECO:0000313|EMBL:PHZ12071.1};
OS Rhizopus microsporus ATCC 52813.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=1340429 {ECO:0000313|EMBL:PHZ12071.1, ECO:0000313|Proteomes:UP000242254};
RN [1] {ECO:0000313|EMBL:PHZ12071.1, ECO:0000313|Proteomes:UP000242254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 52813 {ECO:0000313|EMBL:PHZ12071.1,
RC ECO:0000313|Proteomes:UP000242254};
RX PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT "Lipid metabolic changes in an early divergent fungus govern the
RT establishment of a mutualistic symbiosis with endobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
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DR EMBL; KZ303850; PHZ12071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G4STJ0; -.
DR STRING; 1340429.A0A2G4STJ0; -.
DR OrthoDB; 2025446at2759; -.
DR Proteomes; UP000242254; 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:UP000242254};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 8..261
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 769..833
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 403..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 833 AA; 95243 MW; 44A5032BF41822DB CRC64;
MTTNALHMQI SPGSNFADAF WDDNFKGVDI IFNRLKRSKE TCEEIKRLYE SRAQIEQEYG
ERLLKLAATS RVGEHEEGSF AETLSRIPST LETTGRAHID LAQQLRDHLE IPLDGFLKEQ
RDIRKSQHTQ IENLRQLKNL HEAEVARARE YYSNESIKLM SLEKHFTVEM EKEIEEQRKL
VTIAEQVYRR AVDNLNAVNE RWICDWKHSA DIHQEMEVKR ITYLRSTLWT FANMLTSTFN
IDEECCDRIR AALEITDVQK DITDFVQCHR TGSKLPSPIP YESFYKPVKR ELYSQQPSKE
SLTHSVTVLT NPDEELKSVD HQLQQLEQLQ TPRLEPANDL PLTGATVSTH SHVSSAMKEV
EQMLNQTNDS SSTHLDNYNL AVHESTDRFS ADICNALGIK ETQDATSKND TVSPSPSQRS
KENGIKYKPM PNPSFTSIQS EHIETEERPV SETQSESNKP EIQPEPKKED DDDDDKEIEE
YQSRMPRPPP KDEKWVISSI RRPQQVPIKT PNHEEIPRSN TENLSHQASP AEDKKGHQPK
VHKPVVPLTI EIPNPVNPTK LPQLAAHQVI EDARRHSQMS PATIEMNRQQ NRDDNGGIRP
APWQDSGIMH PDDKKGYMPN MNGQYPPPNG YHAYHPPEHI NSHPRGSSLA ILPNHQDFLP
PQHAAYPEEE ANKKRSSKSK AEATGKSGKE SKGAGRFSLF FTGNKKDKKK EKENQQQQQQ
QIQPYMLDHQ QRPQSHYQTL TKEPVEKDVF YNPPVSAPMP PTAINGSHKF ICYVKAQWPF
EATIEGEMSF SQDEVLGILH KQSDGWWQAE RLTGEAAGQR GLVPGNYMVD APH
//