GenomeNet

Database: UniProt
Entry: A0A2J6Q7D0_9HELO
LinkDB: A0A2J6Q7D0_9HELO
Original site: A0A2J6Q7D0_9HELO 
ID   A0A2J6Q7D0_9HELO        Unreviewed;       853 AA.
AC   A0A2J6Q7D0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Formin GTPase-binding domain-containing protein {ECO:0000259|SMART:SM01140};
GN   ORFNames=NA56DRAFT_645344 {ECO:0000313|EMBL:PMD22151.1};
OS   Hyaloscypha hepaticicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX   NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD22151.1, ECO:0000313|Proteomes:UP000235672};
RN   [1] {ECO:0000313|EMBL:PMD22151.1, ECO:0000313|Proteomes:UP000235672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD22151.1,
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; KZ613479; PMD22151.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6Q7D0; -.
DR   STRING; 1745343.A0A2J6Q7D0; -.
DR   OrthoDB; 2722688at2759; -.
DR   Proteomes; UP000235672; Unassembled WGS sequence.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR010473; GTPase-bd.
DR   Pfam; PF06371; Drf_GBD; 1.
DR   SMART; SM01140; Drf_GBD; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000235672}.
FT   DOMAIN          321..596
FT                   /note="Formin GTPase-binding"
FT                   /evidence="ECO:0000259|SMART:SM01140"
FT   REGION          1..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          804..827
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..128
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..144
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..307
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..351
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..442
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..827
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   853 AA;  94862 MW;  131E907FE76316A6 CRC64;
     MASQYPVPDS HNHRRTKSSV LSFMHKRTPS GGAGLSSNLP KDFVNLPAYQ SVSHLPHDHQ
     YTRALGELQQ NQQSQPPLSP KKSREAQRPN TSEDGSKSLH KKTMSAISLK SLGKDAERKS
     KEPKPNKKKS TTNLANLLSR PKSSKNLRKQ AEEDTRAQKD KENRTPTSTS SIEATRPPPI
     YAQFSSEYFA KQPLGGKFLE GQIDLYTPQD DGRQRDFHAG PDGPPSLGMP AGGSQRPKST
     YLPSSFSIQD ITRKVSGGSR HSAEIIRRVS GAKRPSFERT ATASSAKSDN IEKPLPQKGH
     RVKPSTSSTD KKSPPRPIES GPVVPDKDVD REFEAMLDRR NIPEHQRGKM RSLAMSMKKD
     FIRQDWAELA AAKDGTPGTS RSNSSAEATS STQDVPEVKT KRPRSRTFTL SRASSKEPPS
     PSKKSKDEKS LTKSKKSLES LKDGNKSLTA SGAAVAQTLI AKAKGQLTDD FVSYLRKVRK
     PELVEVGKLH KLRLLLRNET VAWTDGFIGQ GGMDEIVGLL HRTMEVEWRE EHEDALLHEV
     LLCLKALSTT ALALQHLDRI QVTLFPALLH MLFDEEKKGP SEFTTRNIIT SLLFTYLKSA
     PMSERTHRAK VLLSYLRDPE PSESQRPVGF VLEMRRPRPY RVWCKEVVNV TKEVFWIFLH
     NLNVVALPKA TTNHDGHSHP QGTPATSDST FNSANPHHVY MNQHFPKERP PVPAAPYVGG
     VEWDATNYLA SHLDIINGII ASLPTQAERN TLREQMLVSG WEKCLGGTLR LCKEKFYGGV
     HDGLRCWVAA ACDDGWDTRD VRCGPSVEST KTSPKKSPKK NAPVEDAPKI EMKLDFLSGA
     QQINSPLNDD VWL
//
DBGET integrated database retrieval system