ID A0A2T9Z160_9FUNG Unreviewed; 1613 AA.
AC A0A2T9Z160;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=FH2 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BB559_001636 {ECO:0000313|EMBL:PVU98345.1};
OS Furculomyces boomerangus.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Harpellaceae; Furculomyces.
OX NCBI_TaxID=61424 {ECO:0000313|EMBL:PVU98345.1, ECO:0000313|Proteomes:UP000245699};
RN [1] {ECO:0000313|EMBL:PVU98345.1, ECO:0000313|Proteomes:UP000245699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AUS-77-4 {ECO:0000313|EMBL:PVU98345.1,
RC ECO:0000313|Proteomes:UP000245699};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(2018).
CC -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC {ECO:0000256|ARBA:ARBA00037935}.
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:PVU98345.1}.
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DR EMBL; MBFT01000082; PVU98345.1; -; Genomic_DNA.
DR STRING; 61424.A0A2T9Z160; -.
DR Proteomes; UP000245699; Unassembled WGS sequence.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:UniProt.
DR GO; GO:0005938; C:cell cortex; IEA:UniProt.
DR GO; GO:0032153; C:cell division site; IEA:UniProt.
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 GO; GO:0051301; P:cell division; IEA:UniProt.
DR Gene3D; 1.20.58.630; -; 1.
DR Gene3D; 6.10.30.50; -; 1.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 1.10.238.150; Formin, FH3 diaphanous domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR47102; PROTEIN BNI1; 1.
DR PANTHER; PTHR47102:SF2; PROTEIN BNI1; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 2.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000245699}.
FT DOMAIN 95..497
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 921..1398
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1399..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1533..1564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1576..1613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 522..592
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1226..1253
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 13..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1613 AA; 181782 MW; 3D496B7EE2CC83AA CRC64;
MSSSSRGSRK NSDYSPNRSH SHGKETNKAF QDDRFSPTTI PSNPQSNTFR NVVSATFSAR
SSSSTNRTFS SGTPRSNSIT TWADEPEGDN PRYKIDYSNP DEVDEEFEQM MHDMDLKEEQ
KDQMRNMTIE KKITLLHSKS QYREFRGDKS KPGAFCRVLK DAEVNTIEHK KLIHLKVCLT
TQPIAWVREF VNREGLKWLT ILLKKITSGR HRFNLYCTRV ELEILRCMKV ILNIEWGAQE
AIQVPDCITA LCFSLDSQVL MTRKIAAELL TFVCYCGNQV GHFQVIKGIE ELQQIRGENT
FFGAWLQAFE DLLNLDPKQI SPSRLGLVAP QDKELIDIGI ANMILVNSIV SVCEDAETRT
EYRAQLSEAG IERIMKKLSK FENPLISLQI DKYMTELEQD YNNLLESYNM DGIEDDSDIN
ILLNIIKENL VSDPKTSEYF TAVIQRLLLL KDPSYGSQQP QFLDSMKPED DNSLFIKRLQ
LVDSLIEKVI VENKKPEMLE IPNNSRINVG SIINSFSNED SLEEIIRESI DLKEQLEKVT
REKTHLEQEV ANKSEGLVGN LKNKIFALED LLRMSRHTIE GLQTQNKELR KQFAERLHKQ
ENHLKQILQT VESVANDADA VSVQRNQFQL ENVALRTGTA WDYAEKDGKI VPILNQTRLE
KEVEKLKHLP SINTSSSLTK SKIEQVLMDG KDRSNSDTAL KPSPLSLTQS PDQTKETGSF
NEISRNSSRK RTISNKRYTM GIFPKDVAES LSSDHPLPSR YEQNQTYSKQ GDINIKTNSF
GMIQGPKSSG DDSIEKENDD VTSASQLGLS SKNLIGSDQE IMTQVRSTSD NKQDKPLPEI
ETDLNNQKDH NINAHPKPMP ISGNSSMESM INQRATNLEA EGQLISDIFG SSSNSLNKLG
KSSPESIIMS NSMIFGPVPR KELRFIPRKK LKMLQWDKMS DHDQLNQTFW IKYDKYSKKS
EDEIELTLHK NGTFERLENM FSAKEGVDLN LLRERKRLER ERNGKKEDSR DTKASDIFHV
PSILSSKRSN NINIMLGRLK KFKLNELKDA VMTLNDTILT ENILKQFLAY LPTPEEKALI
TVQHQTNGGK LARADQFLFE MMSVFRYEKR LSVMLTRISW KEHYDGLMED IGAVSVASKA
VSSSSNLSTI LGVVLTIGNF MNGAGFRGGA FGFKISSLTK LMDTKALDNK TTLLHFLAST
LEEHFPETLE VLVELKPVDS ACRVSYQEMR TELNEMTERL EEAKIELQLH IDREDAKRTL
LEVDGPDDST LGLNREKIRD DGGSRSDLNV EKETKLEQGG NNDNESNNND DRFISFISAF
IQKASTQLKI VTNQISEMDV LYSYCIRLYG EDPNTMAPDE FFGIFRTFIF SLEKTIKDNK
MEKNRKLATE KRRQQIEASL EVRKRNAAMN TQKTRGKLGS PENDTKGASS GVPSGESTSL
EGVQGSNEKG TMDDLINSLR QGNALGRSSV GGNGLGGGPG QQTGVANAAT QILEHRRPRR
REINSIRQST LRRSLHRTSI SLKAMQMLKE IDEDSHQADK GMAPPVPKIP TALRKSNRAG
MSGSISSIDV GLEISSDEVM SDSDGGVGSV GGPSGVGRMD LSRASSIDSD EMF
//
