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Database: UniProt
Entry: T1K2H3_TETUR
LinkDB: T1K2H3_TETUR
Original site: T1K2H3_TETUR 
ID   T1K2H3_TETUR            Unreviewed;      1119 AA.
AC   T1K2H3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=FH2 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=107359819 {ECO:0000313|EnsemblMetazoa:tetur04g05020.1};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur04g05020.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur04g05020.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the formin homology family.
CC       {ECO:0000256|ARBA:ARBA00023449}.
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DR   EMBL; CAEY01001362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015781881.1; XM_015926395.1.
DR   AlphaFoldDB; T1K2H3; -.
DR   STRING; 32264.T1K2H3; -.
DR   EnsemblMetazoa; tetur04g05020.1; tetur04g05020.1; tetur04g05020.
DR   GeneID; 107359819; -.
DR   KEGG; tut:107359819; -.
DR   eggNOG; KOG1923; Eukaryota.
DR   HOGENOM; CLU_003597_0_0_1; -.
DR   OMA; MMPGFSP; -.
DR   OrthoDB; 471257at2759; -.
DR   Proteomes; UP000015104; 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   GO; GO:0022604; P:regulation of cell morphogenesis; IEA:InterPro.
DR   Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014767; DAD_dom.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR010472; FH3_dom.
DR   InterPro; IPR043592; FMNL_animal.
DR   InterPro; IPR014768; GBD/FH3_dom.
DR   InterPro; IPR010473; GTPase-bd.
DR   PANTHER; PTHR45857; FORMIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR45857:SF4; FORMIN-LIKE PROTEIN; 1.
DR   Pfam; PF06367; Drf_FH3; 1.
DR   Pfam; PF06371; Drf_GBD; 2.
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; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000015104}.
FT   DOMAIN          36..493
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          573..1044
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          1072..1105
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          167..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1044..1064
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1093..1119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..479
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..498
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..566
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1047..1064
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1119 AA;  127256 MW;  C716095F0EFBF9A4 CRC64;
     MGQTLSADGA DTRDNAHKTI SIEIPPNETA SDDKSDQMPD RDEVNARFNE VIALMDLPPD
     KAKALRSYDI ERKWEMIRDQ EKVTAKESPE FYLRKLRAYL DPKASRSSKK RRIVGDSTST
     QVLRDLEISL RTNNIEWVRE FLSERNRGLD VLIDYLTFRL TTQQQQQKLA QSANNRSPDG
     GNGDNLSESN LKNLTSTLNS SQTIRPTQNL FRRPSLFRSF NKSKLGNVDG DVHVSIMCMR
     AIMNNKNGFN MIMEHPYAIN SIALSLNHQS LRTKSLVLEL LAAICLVNGG HQLILNAFDN
     FKEVMGESRR FQTLMNYFTK PEVFNIDFMV ACMQFINIIV HSVEDMNFRV HLQFEFTQLG
     LDDYLENKLR NTESEDLSVQ IQAYLDNFFD VGALMEDAEQ KNLATDRAQT LALQLSHSNE
     IAKELETKYN ELVLQYSVLE QDYKSASEEN HHLSEELSTL RKTIQMREEE SRRRQSLLES
     KIMQLESRTM NGQTSPKDDS EKAPMKTTAT SPMTPPESGV KTPAAVAAPP PPPPPPPPPP
     PPPPPPPPPS RSVAPPPPPP PPMNAQNPGM MTIKQSFATR YKLPTLNWNA LKPAQVKGTI
     FQEFHAEDRI INSINFEEFE EQFKLGPKPE LARKGSNPQV AAQKKFKTNE KTSLLEHNRL
     RNMAISLRKV NIDTETVIKA INSFDIDTLT LEYIEILLRM IPNPQEIQAY REFERSGRSI
     DEMTDEDKFL FKISKIERLE QKLKIMSYME TLMKPEPTPG ISGKPSFGVT LNVIKVWRTR
     IIAITEAARA LRTSTGIRTV LEYILVFGNY LNSATRAMAA AGQAYGFKLQ NLELIVETKS
     SADRSRCLLH YVAECIQRNV EGESGLSEEE RLYKTLATLS PTTATKKFAG PNSLLSGLDV
     SIESIKLPFD LETLLNLLES VATNATLETC ASEVFELEKG MELVKRELQL RSSQKDPATQ
     RLQNFVASKS TELSNLKEDL RRSQSEYSNC VEYFGENSKL LESSSAFFNI FAKFLKHYKQ
     CLRDIKINQK KKLEALIQAK IQEHQNQNKT SPEKEVSSQE TKVRDKRLLK QDEVYNGALE
     DILLSLKNEP YRREDAVRRS QRKKQANARP QSHISEMDV
//
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