ID A0A2J6Q9R3_9HELO Unreviewed; 910 AA.
AC A0A2J6Q9R3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Cell division control protein {ECO:0000313|EMBL:PMD23017.1};
GN ORFNames=NA56DRAFT_597888 {ECO:0000313|EMBL:PMD23017.1};
OS Hyaloscypha hepaticicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD23017.1, ECO:0000313|Proteomes:UP000235672};
RN [1] {ECO:0000313|EMBL:PMD23017.1, ECO:0000313|Proteomes:UP000235672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD23017.1,
RC ECO:0000313|Proteomes:UP000235672};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KZ613476; PMD23017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6Q9R3; -.
DR STRING; 1745343.A0A2J6Q9R3; -.
DR OrthoDB; 2025446at2759; -.
DR Proteomes; UP000235672; Unassembled WGS sequence.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:UniProt.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:UniProt.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd07651; F-BAR_PombeCdc15_like; 1.
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 Cell cycle {ECO:0000313|EMBL:PMD23017.1};
KW Cell division {ECO:0000313|EMBL:PMD23017.1};
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077};
KW Reference proteome {ECO:0000313|Proteomes:UP000235672};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 13..266
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 850..910
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 281..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 910 AA; 99977 MW; 11EE64043CE08AFB CRC64;
MPGTVSDGPS VALSFANNFW GKDDAGVEPL LQRMLNAKQT SDELKSFYTA RAAIEEEYAR
KLLSLSRKPL GSQETGTLRA SLDVLRGEVE QMGKSHQNIA GQMKTELEEP LAAFAGAMKE
RRKIVQNGIE KLLKVKVAQT QLVNKTRDKY EQECLKIKGY LAQGHMVMGQ EERKNKAKLE
KTQINLATSN TEYENAVKAL EETTGRWNRD WKAAADKFQD LEEERLDFMK SSLWSFANIA
STVCVSDDAS CEKVRLSLEN CEVEKDIVAF IRERGTGQEI PDPPKYINFC RGDVSDSQSE
ASEDDSYSVA QFQRTINPAY RSSSPQPSTY ESHHDPQVSL VRDLGRDPAT PPSREATLTP
QKLVMDRSKP PQLDYQAQPS RLSYEQSHHG PLAAVPHDPY PMDGMTMLCR TGPPSERSSA
HSPARPASRD SQSEYSNPTS FSSQEPPSGK TSPVKQSAPP PERTVLKKKS GFFQSHSPFR
RKSIKEKDNS TVMTPSNRNT WSASRTNNNQ NTPSRYGQES RNMITDRATG SPEPIDPNAS
FQLNVGNNVF DVATPDRKSK AAQNKTAQQE DDADPIAQAL AELKGVTKAS SSRMSADNYH
GIPTPAPGAT PNSRPGGAQM ANGALMAGMR GTPPPSYDQP MQRLGLPQPA FTSKAMQQTR
QKYVDQTQNM FNSQGRPESR GGYGSGPQSR PGTRGNDMPR ATSPAPPRSA SPRPGMQVDT
RQAYRSASPN PYGGSQRRPQ SESPQKRGSD LGYYRQPSQN SANDVARAAS PAPFRDQDRP
GSSHVNNDMS IQLAPGPDEG YGSKGRASSR AGNARPMSYY GGGQDGSIGS SRQRSKSVAD
VRQYNREGRP ILHFARALYM YQAAIPEELS FAKGDILAVL RHQDDGWWEA EVAGKNGRPG
LVPSNYLQNC
//
