ID F1A1R9_DICPU Unreviewed; 1657 AA.
AC F1A1R9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=HP domain-containing protein {ECO:0000259|PROSITE:PS51089};
GN ORFNames=DICPUDRAFT_51061 {ECO:0000313|EMBL:EGC29857.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC29857.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
CC -!- SIMILARITY: Belongs to the villin/gelsolin family.
CC {ECO:0000256|ARBA:ARBA00008418}.
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DR EMBL; GL871384; EGC29857.1; -; Genomic_DNA.
DR RefSeq; XP_003293612.1; XM_003293564.1.
DR STRING; 5786.F1A1R9; -.
DR EnsemblProtists; EGC29857; EGC29857; DICPUDRAFT_51061.
DR GeneID; 10504930; -.
DR KEGG; dpp:DICPUDRAFT_51061; -.
DR eggNOG; KOG0443; Eukaryota.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; F1A1R9; -.
DR OMA; HREFPGS; -.
DR OrthoDB; 25995at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR CDD; cd11289; gelsolin_S2_like; 1.
DR CDD; cd11293; gelsolin_S4_like; 1.
DR CDD; cd11291; gelsolin_S6_like; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 3.40.20.10; Severin; 7.
DR Gene3D; 1.10.950.10; Villin headpiece domain; 1.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR007122; Villin/Gelsolin.
DR InterPro; IPR003128; Villin_headpiece.
DR InterPro; IPR036886; Villin_headpiece_dom_sf.
DR PANTHER; PTHR11977:SF138; HP DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11977; VILLIN; 1.
DR Pfam; PF00626; Gelsolin; 5.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF02209; VHP; 1.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 7.
DR SMART; SM00364; LRR_BAC; 7.
DR SMART; SM00365; LRR_SD22; 5.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00153; VHP; 1.
DR SUPFAM; SSF55753; Actin depolymerizing proteins; 6.
DR SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF47050; VHP, Villin headpiece domain; 1.
DR PROSITE; PS51089; HP; 1.
DR PROSITE; PS51450; LRR; 5.
PE 3: Inferred from homology;
KW Actin capping {ECO:0000256|ARBA:ARBA00022467};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1593..1657
FT /note="HP"
FT /evidence="ECO:0000259|PROSITE:PS51089"
FT REGION 558..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 894..921
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 558..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..791
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1657 AA; 189351 MW; 6661E97521C3A0AD CRC64;
MGNQQSGLQQ TDTQAVTFSK DTESVEISDR YLVTFPLELR QLPNLKYLNL SRNKITRVDG
VSGILNLEEL DISYNALTIL SDDLFLCNKL NKLNLSFNQI SQIQSLIQQL KQIKQINLSN
NIISQLPNEI GFLKNLTVLN ISFNKLQNLP KTIGQLDNLT KLIANNNKLQ LLPIEIGALS
QLTLLDLAEN ELRILPTQVS QLGCLTKLYL DNNDFLEMIP EISKLTQLKE LNLRSNQLVD
LPSSYHKLVN LQILDLDDNQ WDHIDYTVND IKRLLDYLKT KKDIVNKSRK STSKEYRRTI
TRQKLEDKKR LSLNNLFENN FQVIEFKKKL LQLKGKSIVF VKKVPLLVDS LNTEDIFIFD
IGKKIYIING NPNLNQRERQ KAVHLSKLMK EERGAADIIL LDFKNSRKEE INEFWKDFGV
TGRVNLKNKS SNNDDDDIVQ EEHILETKLF KFFEPEEGRL DIQVYAAQIL YRNMLDSNSC
SILDTGTDIY VWSGLYSSAN EKSWSMLKAE ELISRRSDNA EIHWLIEGME TLLFIEYFVD
WVDNSWDQEY IKTQNQIKER EEQEKLEAER ERRRMEKEEE EEMEKMKRRS FEQQQLQQQQ
QQQQEFEQQI KQQKQQTLEQ QKQELSFAAS TSINNSPYTF TPIISPTQTT TANNNFIKPL
PSIVNLPSIP SSNYNNNNNN LSEREKIKER EKEKIRERLK QRESGASTSQ TNLLQPQKIS
PEASPILPSI PKSIPSIQLE KESSVILPSI TKPLPKEPDV VTLPQTKQPS PVITPSQPTK
QPSPVLSPVK PLPKEPTVVA LPKVEPVKPL PKEPTNAVPL PKVEPAKPLP KEPTVVALPK
VEPVSIKKET ITPTVTVNEQ SIFDDKNGSQ TLAPLPEKAE TAKRQAASRN PIRARQERAA
LEEAEAKKRL AEQEQMKLNN TLSVPANTST NKASSVASAL GGFGLLYSVG ADETMFKKRA
ERAAAAAVNP EPFSINIQPK DQPKLLHVKG RRSPFVRQVE LSYQSLNKGD VFILDCGKEK
NLLYQWNGSE ANRIEKGKGM DIGKSIKDKE RVGCRVVIID EGKEPEDFWK VLGGKGEIAS
ADTAGDDREA ELNIRKYINL FRAQPINGDK ELDLVPLDGR LSKTLLEGGE CYILDCISEM
FVWTGSNSKL KVRNMTLKLA NDMFASRSAN CWTSGAVHRE FPGSEQVLFK ERFSDWGGSL
PIAMQQAPVG VNTASAKKQE KIDVATMHKP KPEKEEVMID DGSGKLTIWR VEEFQKVAID
PKNYGQFYSG DSYLILYTYF FKNKDNYLIY FWQGKNSSIN EKGTSALLTV ELDDQLKGMA
KEVRVVQNKE PKHFLTIFKG RFIIHQGKDP LSKNYKPQAN IKDPRLYHVR GTTDFNTRVI
QSKLSTLTLN SYNSFILNNQ INNGTIYIWY GKLSNSIERA LAKKIVQSTS PNQNDGAGCK
VVEFEENKES EEFFKLLGGR SNYPLSKITS RVEPRLYLCT VGTGVFVVEE VNSFAQDDLL
QEDVFIVDGI DNIFVWIGTE TTEVERKSSM EVAMEYSATL PAPRKQNVPV YLTYHGKEPF
IFTSLFHGWD FSKRILPTFS YDGELTLAKD VLNLYTKKYT YEEIVNKKYP KGIDGSRLEE
YLEEDDFKKI FQGLTLEEFQ KLPLWKKQTW KKELRLY
//