ID A0A1A9VAS0_GLOAU Unreviewed; 1652 AA.
AC A0A1A9VAS0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=FH2 domain-containing protein {ECO:0000259|PROSITE:PS51444};
OS Glossina austeni (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7395 {ECO:0000313|EnsemblMetazoa:GAUT031298-PA, ECO:0000313|Proteomes:UP000078200};
RN [1] {ECO:0000313|Proteomes:UP000078200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTRI {ECO:0000313|Proteomes:UP000078200};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GAUT031298-PA}
RP IDENTIFICATION.
RC STRAIN=TTRI {ECO:0000313|EnsemblMetazoa:GAUT031298-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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DR STRING; 7395.A0A1A9VAS0; -.
DR EnsemblMetazoa; GAUT031298-RA; GAUT031298-PA; GAUT031298.
DR VEuPathDB; VectorBase:GAUT031298; -.
DR OrthoDB; 623207at2759; -.
DR Proteomes; UP000078200; Unassembled WGS sequence.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:InterPro.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 1.10.238.150; Formin, FH3 diaphanous domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR027649; Inf2.
DR PANTHER; PTHR46345:SF8; FORMIN 3, ISOFORM B; 1.
DR PANTHER; PTHR46345; INVERTED FORMIN-2; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM01139; Drf_FH3; 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.
PE 4: Predicted;
FT DOMAIN 252..668
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 128..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1305..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1353..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1477..1500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1569..1652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..200
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1652 AA; 183227 MW; E45C6C80B373A869 CRC64;
MIVYIFSVSF RFHRKVAQSV GDIIVQLDVF DEQRECDEAQ SLQGPNGINL SSHLDVFYAI
LRQVADTPQE VPFLSILQHL LRIDPKEPVS DIIWDTAEKL VHRATLLENH EDSVRLLRTS
SGQKFTCPNC RSDATSPSRK PSGVPISLQS ASATTLTPLN NNGHLQSVST GVNKPPPPPP
PAPPIPTHLA NKGVPPPPPP PMNRAPVLQP IAGAPPIPPP LAPTNLLAPH STLTPSRPLT
PEPRLNDILL PQQDTPAPKT KMKTLNWGKI PPNKVLGKQN IWTIVASNHQ GSSMTDMDWS
EMEGLFCIQS TSAQCSPKLG RADGFAGGSV SMGHDTLDRK SKKENTEITL LDGKRSLNVN
IYLKQFKGYN SNDEIIQLIR NGDHEAIGAE KLKGLLKILP EVDELDMLKS FNGDRQRLGS
AEKFLLQLTE VPNYKLRIES MVLKEEFAAN ITYLDPCINA MIYAGDDLMN NKHLQEVLYM
VVVAGNFLNS GGYAGNAAGV KLISLQKLTD IRANKPGMNL IHFVAMQAEK RNPALLNFTH
ELSVLENASK TTPEQINNEI NTLDNHIRRI KRQIELPATD EDIKEQMTEF LQSAERELSV
LKSGMRDVEA MRLKLADFFC EDPATFKLEE CLKIFHIFCD KFKQAIKENE RRQQQEEQAT
LRRKQREEQL ARKTKYANQC GTPVSDNETT QYNVDTIFDP KSSPAFSRKR MSSFNNGSDV
NNGCIRIEAS NGGGSEGISP DITPNGSMRR RRSRVLNEED DLMEFLRSSG HDHQGRERKV
AYGSLDRSWA RRARSGSSNR KRPDLLNVDF GTDRERAASP APILSQDKAS PVSSSGGEII
KEEVKPRIPR EWRQKIETWL QSNENDEKHE EYKRKRRLVN INRRSLENDS ESERKLDTLP
EEKCIPTTPN LYTNDSNQMK INKNSKGNIN TTDALNLLSE NYKRPYTDWK PSATLDTDVV
GTLQAIADVS NTRKKPKSKE KTVETEVEVP DSAISLSPTL LTDDIQNYQK PNDLVVCRKQ
KSTENNSTLE SIAEEDRRKT LTQQLGERDA PDRLHTYVME KETAPTKSHV SILSTPSFVD
SHKPSIKSSI NAKVHMESEV KTKADASARF SENSSKTQSH NEITQAYNRQ EIDADNIETP
PAERKFISSP PTTVVMVNGR VENLTTTIAN QKNMGTEPTC IENQLDNAAP GHFDRYSLAR
RTRRFKRPTD YSSGNEELSS NKISIENKSS AQPANTIEIR KGQGTKVVDK PTPLPSNNQN
TEVIPKRPAL NSKTITKLEK VGRHISSINQ KDVQEAIRNL KSPTDIPERL WSPSRNAAKN
KSNLPTGHVP ATTINSGSAI IKISNHELND EGFEETQSLV SDTPSHGKES TNSSCNEVNE
TPGELHKTIT QKTPAPIQKI SSKLADRLHL SKLRNAQTTR PLPSSSHSAP RKIVVSVDKT
RNARVANGQL VTGSGTYANN PQQRRTNGPI AANIRNVERS GSRNSLRSSR SSINSAASTQ
TVKRMPVMLN KAPLQTVSVE SSPSKRPLAA QNTKITLNGV RISGVPASRS SSSGSSIGHN
IVVVRKTSSN ALQRHHPANN NLGSTSFKEN QTNVGSARPQ AARNTILVKT SLTNAPAMSS
MQRNNPRSNS STSRGISSFM RPTTASTTKR QK
//
