ID A0A182RVT9_ANOFN Unreviewed; 241 AA.
AC A0A182RVT9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=CAP-Gly domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN010399-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN010399-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN010399-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TBCB family.
CC {ECO:0000256|ARBA:ARBA00025779}.
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DR AlphaFoldDB; A0A182RVT9; -.
DR STRING; 62324.A0A182RVT9; -.
DR EnsemblMetazoa; AFUN010399-RA; AFUN010399-PA; AFUN010399.
DR VEuPathDB; VectorBase:AFUN010399; -.
DR VEuPathDB; VectorBase:AFUN2_014107; -.
DR OrthoDB; 5485090at2759; -.
DR Proteomes; UP000075900; Unassembled WGS sequence.
DR GO; GO:0043014; F:alpha-tubulin binding; IEA:InterPro.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:InterPro.
DR GO; GO:0007021; P:tubulin complex assembly; IEA:InterPro.
DR CDD; cd01789; Ubl_TBCB; 1.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR045172; TBCB_Ubl.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR18916; DYNACTIN 1-RELATED MICROTUBULE-BINDING; 1.
DR PANTHER; PTHR18916:SF6; DYNACTIN SUBUNIT 1; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF14560; Ubiquitin_2; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186}.
FT DOMAIN 13..90
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 179..221
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 132..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 241 AA; 27280 MW; B818C48F5392D242 CRC64;
MSPTSNFELS DIVTINISNS QNDTVSFERK YSRSLKIYEF KAKLEPITGG NAGTMRLELY
SGDRLVSKLD DDNQPLGSYS IEDGMRVHVV DQFQCIQENV PKFELSQEEY DKKADSVRNF
LKKNKLGKYN EEEMAKQEEE RKRQEEEDRQ KLDATTIGAR CRVTAKNNPV RLGTVMYKGL
LDGKPGVFIG VKFDEPLGVN DGSVNGKRYF DCGPKYGSFV APKAVEVGDF PPEEYSLDDE
L
//
