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Database: UniProt
Entry: T1DQH1_ANOAQ
LinkDB: T1DQH1_ANOAQ
Original site: T1DQH1_ANOAQ 
ID   T1DQH1_ANOAQ            Unreviewed;       420 AA.
AC   T1DQH1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   13-SEP-2023, entry version 32.
DE   SubName: Full=Putative ca2+-binding actin-bundling protein {ECO:0000313|EMBL:JAB00431.1};
DE   Flags: Fragment;
OS   Anopheles aquasalis (Malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=42839 {ECO:0000313|EMBL:JAB00431.1};
RN   [1] {ECO:0000313|EMBL:JAB00431.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Whole body {ECO:0000313|EMBL:JAB00431.1};
RG   Brazilian Malaria Network (MCT/CNPq/MS/SCTIE/DECIT/PRONEX 555648/2009-5) and Research Network on Bioactive Molecules from Arthropod Vectors (NAP-MOBIARVE;
RG   University of Sao Paulo);
RA   Marinotti O., Ribeiro J.M.C., Costa-da-Silva A.L., Silva M.C.P.,
RA   Lopes A.R., Barros M.S., Sa-Nunes A., Konjin B.B., Carvalho E., Suesdek L.,
RA   Silva-Neto M.A.C., Capurro M.L.;
RT   "Transcriptome sequencing and developmental regulation of gene expression
RT   in Anopheles aquasalis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GAMD01001160; JAB00431.1; -; mRNA.
DR   AlphaFoldDB; T1DQH1; -.
DR   VEuPathDB; VectorBase:AAQUA_002999; -.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0051017; P:actin filament bundle assembly; IEA:InterPro.
DR   CDD; cd21298; CH_PLS_rpt3; 1.
DR   CDD; cd21301; CH_PLS_rpt4; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 3.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR039959; Fimbrin/Plastin.
DR   PANTHER; PTHR19961:SF18; FI19014P1; 1.
DR   PANTHER; PTHR19961; FIMBRIN/PLASTIN; 1.
DR   Pfam; PF00307; CH; 3.
DR   SMART; SM00033; CH; 2.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
PE   2: Evidence at transcript level;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          74..182
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          195..303
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   REGION          315..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          363..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:JAB00431.1"
SQ   SEQUENCE   420 AA;  45748 MW;  ED95CC76E1766776 CRC64;
     GVNLEALRET NALNRAEVML QQAAKLNCRS FVTPQDVVNG VYKLNLAFVA NLFNNHPGLD
     QPEEIEGLES IEETREEKTY RNWMNSMGVK PHVNWLYSDL ADGLIIFQLC DIIQPGIVQW
     KRVHQKFTPL RKFMEKLENC NYAVELGKQL KFSLVGIAGQ DLSDGNATLT LALIWQLMRA
     YTLSILSRLA NTGNPIIEKE IVQWVNSKLQ SAGKRTSLKN FQDSAIADGK IVIDLIDAIK
     PGSINYENVR EGGNPEENLE NAKYAVSMAR KIGARVYALP EDITEVKAKM IMTVFACLMA
     MDYVPNMDSA AKPVASVQSS TPSPVASANS NGLAAAAAAS PEPKQQEPKE VVQIVEAPVA
     APVITNGNGT LEESHDSEWN DQETTNTTTT TTTGETISEA ATAATTAAAS SEAVVDEFAD
//
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