ID A0A2H3J1G6_9EURO Unreviewed; 737 AA.
AC A0A2H3J1G6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Fps/Fes/Fer/CIP4 homology {ECO:0000313|EMBL:PCH09052.1};
GN ORFNames=PENO1_003280 {ECO:0000313|EMBL:PCH09052.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH09052.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH09052.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH09052.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
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:PCH09052.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NPFK01000004; PCH09052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3J1G6; -.
DR STRING; 290292.A0A2H3J1G6; -.
DR OrthoDB; 4260488at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:UniProt.
DR CDD; cd20824; C1_SpBZZ1-like; 1.
DR CDD; cd11912; SH3_Bzz1_1; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR035459; Bzz1_SH3_1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15735:SF12; CDC42-INTERACTING PROTEIN 4, ISOFORM B; 1.
DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF14604; SH3_9; 2.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 8..277
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 407..457
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 579..639
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 679..737
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 457..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 316..390
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 458..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 81652 MW; 7C30E3E8CC14FE2C CRC64;
MAEVNVNPQF GAELKDAFKP VNSWVSNGIA WLDDIQQFYR ERSAIEREYA AKLSALCKKY
SDRKAKKISS LSVGDTPTMT PGSLESASLT TWSTQLTTVE SHAAVRDKFG LDLISHVADP
LKNISARYEE LRKSHVEYHG RLEKERESQL SELKKVKGKY DGVCQEVENR RKKTESSFDY
NKTKAQTAYQ QQLLEMSNSK NTYIINIHVA NKLKNQFYHE YVPEVLDSLG DLNETRVEKL
NSFWSLAAQL EKGASTQSTE LMTHLGNEIP RNNPKLDSLM FLQHNASQSQ EPPNLTFEPS
PVWHDDDQMI TDESAKVFLR NMLMKSKSQV RELKAEAEKQ QREVEAAKRI RDNIRQGKDK
RDEVDVVKAI FNLQEKLHET ERKKMTAEVE TLTILAVVGD LSLGAKNHNF RSQTFKIPTN
CDLCGERIWG LSAKGFDCVD CGYTCHSKCQ MKVPAECPGE QTKEEKKKLK AERQEQAQSA
PAVSEHAPSN GNNGTVADMP ALTRNDTMNS LSSGYAHSAH RSVSGSISSS KPSGEEPAEL
SAAPPRSSTS TTKRNRILAP PPTQYVSSPT AAELPASKKN EQRGKMVYAY QATGDGEVTV
NEGQEIVVLE PDDGSGWMRV KAGSQEGLVP SAYAELTPAP SPALTERPAS TYSNSSASLP
GSTTTKKVGP AVAPRRGAKK LQYVEALYDY EARSEAEHSM SEGDRFVLVT KDSGDGWAEV
EKGGQVKSVP ANYIQEV
//
