ID D2VE47_NAEGR Unreviewed; 437 AA.
AC D2VE47;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Tubulin tyrosine ligase {ECO:0000313|EMBL:EFC44819.1};
GN ORFNames=NAEGRDRAFT_67150 {ECO:0000313|EMBL:EFC44819.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC44819.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC44819.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG738866; EFC44819.1; -; Genomic_DNA.
DR RefSeq; XP_002677563.1; XM_002677517.1.
DR AlphaFoldDB; D2VE47; -.
DR STRING; 5762.D2VE47; -.
DR EnsemblProtists; EFC44819; EFC44819; NAEGRDRAFT_67150.
DR GeneID; 8848267; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_67150; -.
DR eggNOG; KOG2157; Eukaryota.
DR InParanoid; D2VE47; -.
DR OrthoDB; 100598at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:EFC44819.1};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT DOMAIN 32..59
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 32..59
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 437 AA; 50267 MW; AFF765E8B10EE69C CRC64;
MSCCSSTELH RDEEASKQHQ PEGKFIHFST VETVQGICWF YRSNGFCKHD DCPYQHIIPS
NDDLYKKKST TTLNNINSST TSTTLVSSSS PSLESSSNNN NTTSFSSPIS NNNKTYCWIS
MAKELKFAAS VLRRTFEENG FNLLINKEDF AQFNKNNKSN LEDDNYRGLP LFWGHVFPRN
NIVKWFELPS HTLINHFVNS HELCNKSLMA LNFQDLSEKK VKSKSQYVPV SFYLPDQLNL
FINHCENQEE TEKSIWIVKP GRSGEGRGIQ IYQSYQQVIV GEFPQIPTCE IESGIISEKS
LKLGKHKMVV SKYIDNPLLI ENKKFDMRMY VLLIGGGSQE RFGSNTEEFH TYFYRDAIVR
FASEDYTTDL DTLKNPFIHI TNNSVNDKKN KIQNETITQK FGFFSNMYLP ELIPCLEKMD
IDWNQFATSL VGSKLNA
//
