ID A0A371HBV4_MUCPR Unreviewed; 1499 AA.
AC A0A371HBV4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
DE Flags: Fragment;
GN Name=FH6 {ECO:0000313|EMBL:RDY00268.1};
GN ORFNames=CR513_16572 {ECO:0000313|EMBL:RDY00268.1};
OS Mucuna pruriens (Velvet bean) (Dolichos pruriens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Mucuna.
OX NCBI_TaxID=157652 {ECO:0000313|EMBL:RDY00268.1, ECO:0000313|Proteomes:UP000257109};
RN [1] {ECO:0000313|EMBL:RDY00268.1, ECO:0000313|Proteomes:UP000257109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jos {ECO:0000313|Proteomes:UP000257109};
RC TISSUE=Seed {ECO:0000313|EMBL:RDY00268.1};
RA Nnadi N.E., Vos R., Hasami M.H., Devisetty U.K., Aguiy J.C.;
RT "Draft genome of Mucuna pruriens seed.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the formin-like family. Class-II subfamily.
CC {ECO:0000256|ARBA:ARBA00006468}.
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:RDY00268.1}.
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DR EMBL; QJKJ01003036; RDY00268.1; -; Genomic_DNA.
DR STRING; 157652.A0A371HBV4; -.
DR Proteomes; UP000257109; Unassembled WGS sequence.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR014020; Tensin_C2-dom.
DR PANTHER; PTHR45733; FORMIN-J; 1.
DR PANTHER; PTHR45733:SF8; FORMIN-J; 1.
DR Pfam; PF02181; FH2; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00498; FH2; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51444; FH2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}.
FT DOMAIN 199..339
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1044..1442
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 487..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1417..1458
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 602..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..875
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..920
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..971
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1030
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RDY00268.1"
FT NON_TER 1499
FT /evidence="ECO:0000313|EMBL:RDY00268.1"
SQ SEQUENCE 1499 AA; 165674 MW; DF55FEEDEA49A1F4 CRC64;
MALFRKFFYK KPPDGLLEIT ERVYVFDYCF TTDIMEDEEY KVYIGGIIGQ LRGHFPDASF
MVFNMREGDS QSQISNILCD YDMTVIDYPR QYEGCPLLTM EMIHHFLRSG ENWLQLGQQN
VVLMHCERGG WPLLAFMLAA LLIYRKMFTG EQKTLDMIYK QAPRELLQLM SPLNPLPSQL
RYLQYISRRN VGSEWPPLDR ALTLDCVIIR FIPNMSGEGG CRPIFRIYGQ DPFIPADRTP
KVLFSTPKRS KLVRYYKQVS DCELVKIDIH CHVQGDVVLE CINLDSDLER EQMMFRVMFN
TAFIRSNILM LNRDEIDILW NAKDYFPKNF RVEALFSDMD ASSSVISIDL PRVEEKEGLP
VEAFAKVKEI FSNVDWLDSK TEVVNVLQQI TSSSILRERL DSGVSAVTTE MLKESFSGIL
ELDLKEQSDI KNLTAAVQGK HSTSPLASPV KAAVGNKTEL LQSKASLKNN VETLECLGQG
NQSIPSFGLS ADSDSTKNEA ESLETKQSLE NKTDLLESKG KAVESEALLE NVSRFKFEPK
PVPEIDTTSP ISISTEMPIE SLESKASVEK DTKFPTSMAH GEQSMPLIEP SKDANSMKQK
MGPLESKEKD TESLESKSLL ENDTGFPPSM ALGKQSIPLI QPSRDANSMK KIGQLEQMAL
SENDMKSVTS TVQRKQYSPL LEPPVDENSI KKKIEPQELQ VALQLPTQTK IISPRVRPAV
RSASASYCNS LQGSPVAISR YHSAPSALGI TSVLQDHAPM DIKEVTRAAT ISPLPSTLPP
SDSKVPTSIG PSSTSVPPAS LPPLLPSLPL KTSVDALTAM EKTFGSLAPA AVTPPPPSAP
PPQYEHTSKL MQPNEGKKSL VSPPPSPPSD SMLAPPPSSL PETSLSTPKD SFKGPPAPPP
PPTPSSPSSI PPPPPLSEIP SSASHPLSSP SSMNKSVAIS GPPPPPPPPN LSGSTPSPLV
PPPPPPPASP SQSSLSNNFT NVPPIPPPPS PSANGLSKSA VPGPPSVPGP PSVPRAPSVP
GAPSVPGPPS APFGAKERGL LRANPRGQTK RSNLKPYHWL KLTRAMQGSL WAETQKLDEF
CRAPEFDMSE LEVLFSAAAP ASDGKGGKSN RRSGQKVDKV QLIELRRAYN CEIMLTKVKI
PLPDLMCAVL ALDDSVLDVD QVENLIKFSP TKEEMEQLKN YSGDKDNLGK CEQFFLELMK
VPRVENKLRV FSFKMQFCSQ VSELKRDLHI VNCASEDIRN SVKLKRIMQT ILSLGNALNH
GTARGSAVGF RLDSLLKLTD TRARNNKMTL MHYLCKVLAE KLPELLDFPK DLLSLEASTK
VQLKYLAEEM QAISKGLEKV VQELTASEND GPVSEYFCQI LKEFLSYAEA EVRSVAQLYA
SVGRNADALA LYFGEDPARC TFEQVVTTLL NFVKMFIKAH EENCKQIELE KKRAEKEADN
EKSKLQAAKK EAEQMMRTTI KTFSKLVYVE IHMRHSHEFL VNIHFILNLF HVQQKSSFM
//
