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Database: UniProt
Entry: A0A2G4STJ0_RHIZD
LinkDB: A0A2G4STJ0_RHIZD
Original site: A0A2G4STJ0_RHIZD 
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
//
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