ID V6TTC1_GIAIN Unreviewed; 1392 AA.
AC V6TTC1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Serine/threonine-protein kinase NEK {ECO:0000313|EMBL:ESU41834.1};
GN ORFNames=GSB_153764 {ECO:0000313|EMBL:ESU41834.1};
OS Giardia intestinalis (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=5741 {ECO:0000313|EMBL:ESU41834.1, ECO:0000313|Proteomes:UP000018040};
RN [1] {ECO:0000313|Proteomes:UP000018040}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GS {ECO:0000313|Proteomes:UP000018040};
RA Adam R., Dahlstrom E., Martens C., Bruno D., Barbian K., Porcella S.F.,
RA Nash T.;
RT "Genome sequencing of Giardia lamblia Genotypes A2 and B isolates (DH and
RT GS) and comparative analysis with the genomes of Genotypes A1 and E (WB and
RT Pig).";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESU41834.1, ECO:0000313|Proteomes:UP000018040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS {ECO:0000313|EMBL:ESU41834.1,
RC ECO:0000313|Proteomes:UP000018040};
RX PubMed=24307482; DOI=10.1093/gbe/evt197;
RA Adam R.D., Dahlstrom E.W., Martens C.A., Bruno D.P., Barbian K.D.,
RA Ricklefs S.M., Hernandez M.M., Narla N.P., Patel R.B., Porcella S.F.,
RA Nash T.E.;
RT "Genome sequencing of Giardia lamblia genotypes A2 and B isolates (DH and
RT GS) and comparative analysis with the genomes of genotypes A1 and E (WB and
RT Pig).";
RL Genome Biol. Evol. 5:2498-2511(2013).
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:ESU41834.1}.
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DR EMBL; AHHH01000108; ESU41834.1; -; Genomic_DNA.
DR EnsemblProtists; ESU41834; ESU41834; GSB_153764.
DR VEuPathDB; GiardiaDB:DHA2_153443; -.
DR VEuPathDB; GiardiaDB:GL50581_1610; -.
DR VEuPathDB; GiardiaDB:GL50803_009354; -.
DR VEuPathDB; GiardiaDB:QR46_3273; -.
DR Proteomes; UP000018040; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 7.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR24120:SF4; ANKYRIN REPEAT AND SOCS BOX PROTEIN 12; 1.
DR PANTHER; PTHR24120; GH07239P; 1.
DR Pfam; PF12796; Ank_2; 7.
DR SMART; SM00248; ANK; 22.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Kinase {ECO:0000313|EMBL:ESU41834.1};
KW Transferase {ECO:0000313|EMBL:ESU41834.1}.
FT DOMAIN 1..402
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 542..574
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 607..639
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 828..860
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1170..1202
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ SEQUENCE 1392 AA; 151700 MW; 71E3B65AC5E673E0 CRC64;
MESTGLVQSI SDSYDVESII KNQLGPNFYI VKDKVTGTRL KLIPIEFTNS WIPGLPNEMA
FINYCTSLTN PNLAKYQGWF KEQTSQILYV KVVNPSDPTI LTLLARNHAF LEDTIWDIAT
NLVELLVYLH KHHMLVWSGL SPSLVHLTSQ NNLIVDNYFA SFRFKTFLSG AIDPFLAPEI
LNMFPSTPNH GLDASYTSRE CRSSAETDVQ LSTSGTVSPE LSKTNPMSLN IESISISFSG
NHDDISTPRN EKNNFTIEQG LGSFKALVTP RLASQNSSSY RSPEHQISHA TSSFYSEGVS
EEVAEVQHMV ELAGLSSSKK TKVDVWSMGA LLLCLCLGRP LTARDNCVQL AKDLCESSKT
GSCLYSYSLC SFIRNCLHPD PAKRPGISVI RERLQVHMKP RLSLPESLRG SFCCHLGESA
DSTGQILLTT PRGGAFNNDK FHQRQQLKSE QTDNLLIKAA EVGDYNAVKK NIGYLGSTGS
AGRTALMFAA ANGHTKCIKL LAKETRLKDQ QGLTALIYAV KNRNRDAIPL LVKDEAGMQD
NQGFTALMYA TADNDIETVS ILIKKAAGKE LKKQNNKGET ALMIATQYWN NEIADHLIKE
ARIVNTDGST ALMYAAKNGN VSYVKLLAPK EAGMKALNGD RALELALINS HSDCADILSR
YELKLSAGET PLLYALKSGN NRLATISTPV YSQSQEFSKA GHLAYAIKSN NAQAVKELLL
FETPPAHSPD GSYLDLAIRS GHSQILSIIY SYALLHSLDV YVSPRHGTTV TKLMECAISN
DIAGIANYLF QLGLTDRHGN TALMYAVRHR NHDATIALVC EATIQNLAGW TPLMVAAANG
DADLVRELVE HSHGFSTRRK ETALMMAVKS GSILCVRLLT KAEARKQDTN GTTALMLAVM
LGNYPLAEIL MPFEAGIQDI NGVTALMIAA QLGDSGMAHL LADRESMLQT NSSCIDGAGW
TAMMYAAREG YSEIVSILAS HESSMQMAAG RTALMISAYS HNDSCVELLC ASEGEAQDEN
GFTALMYAIN SKYNGSDTVA KAQIQRCIHL LLHEAHLSDY GELTPLSLAA SVNNLDVMKL
ICSNLILRRQ LTKVDSQGMT VLMHAALQGH TECVEELLRY DKTMLDNKPI HLSRAQDAAG
MTALMYASCN NRLSCVNVLL PVECNIEATD GSTALMLAAR EGYIDIVRAI VAESDELGKI
NHEGSTALAL AAAGGYTECL KFLYSSYLSK GISPANQGFS RLMLDASLNN VDAVQLGINK
GEARNVSSTG LTALMYATIN NSVESVLLLA PYEIKMTTGS GITALMLASK MGHALCAKAL
VNEELGMQSI QGWSALMFAA FSNKPECIEL LIEAEFKLKN KDGDTALDIS RIYRTKEANE
LLHAYHVSLR LL
//
