ID A0A1I8FX53_9PLAT Unreviewed; 1472 AA.
AC A0A1I8FX53;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=ANK_REP_REGION domain-containing protein {ECO:0000313|WBParaSite:maker-uti_cns_0000259-snap-gene-1.8-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0000259-snap-gene-1.8-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0000259-snap-gene-1.8-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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DR WBParaSite; maker-uti_cns_0000259-snap-gene-1.8-mRNA-1; maker-uti_cns_0000259-snap-gene-1.8-mRNA-1; maker-uti_cns_0000259-snap-gene-1.8.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd21180; GH2_GIPC; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
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; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR PANTHER; PTHR48016:SF29; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 1A; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}.
FT REPEAT 72..104
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 295..327
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 940..1204
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1259..1339
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1437..1472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 968
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1472 AA; 153732 MW; F5746DCC32CD4F40 CRC64;
MACAVEKWRP PPSPPPQQQQ QPCEPEQQQQ QQQQSRVLQD MMFSYTADGS VEKLKALMTR
PGAGFGCARP ATGDTPLLMA ARRGHLATVR LLLQHGVDAT VLSRDGESVL DIGNSHVRKA
VLDRQLTPDA QFAQACWQGC LFGVRHHLRH LTDEELRSAR NRDGCPAGIL LVRDLERIGR
LAEQFRIDYR PAEVLRLLQD RGLDVNAAVD VPTGRSPLHF VAAAAGGSGG SGGSWLGAAR
HARPLLTALA QAGANLEAAD SRQYTPLHCA CLAKATSAVK ELLRLGASHR AIGLMGSTPL
HLSAMQGDAE SAALLLHAGA DPGAADAGGQ TPVDLANSAR IRCLLEGRPA PPDRPQPDRP
RRVGRSRTEV SPASAAAASA ESQPLRLPSI FGESGGQQQR AAEAAAAARA RGRSASPPML
AAAAVVFHRH PSARSSDSPA PSNFLHHRRL PWQSGGPAAP SRQDSAASSM DSSRGRNSSR
TCLEDMEDSA AATPRSLTLS SSVSAPSLMS AALSASATSP AATAASTAGP LNPIAETIDE
AAEATSPPSS ARRSDASQLP RQSVVLGRRV PIAKAPLRMS TPATVVKRSG GGGGASSVVA
MTTRSKTEAQ IELSNSVEIL EDPQSVGLND AVTAAPTATS PAASTASAPA ASPASAPAAS
PAASPASAPA SAQDADAQPS APAVSASSKA AAKATKAKPS PSASSAAVGE GQSAVGKSAS
QPGKQQQQRQ PISAPKRLTA APVRKRGAGG AVNQRKKQQQ PQQKQQSSGA KKPSAAKSVA
LTKNPSVIQS DEAASEEAVA PSLVELSGVE PGPGWLVSAT AVDGGGGVQL LAAAAPTGAA
GLSRYPVLSS IGSNLSAADD RTLLSEIPEM LDVEPTDADE CDEPLQQPPD SVFVSHAGAE
NGTAGAVGGS DPLNDTISSL SSTASGRDGD DAAYSDGIYW RQGPKIGSGS FGVVRQGLTE
AGRIIAVKQV SIEREDSSVE TELRRIRQEV EILRNLRHRN IVQLLGTRCD GDMFYIIMEF
VPGGSIRGLL DRYGSLSERV CRRYLRQVVS GVAFLHANGV VHRDIKGHNI MVTDAGVIKL
IDFGCAKRLH ATQMSLSGKR AQQQMSLEGT PYWMAPEVVL EAGHGAKSDC WSVGCTLLEM
ATTRPPFADM PPMAAIFAIG NGEPKPPTLP QEFSADAHSF YAGCLVRDPA LRPAAEDLAK
HRFLRARSRA ESSGGTGSVS SADHLLHAEH AQDRDGAPTG WPNWLDDFLF AHIKGQKKEI
EVEKSEDALG LTITDNGAGY AFIKRIKAGS IIDRIDHIQP GDHIEKIDGE NFVGKRHFDV
AKRLKEIPRG TTFVLRLVSP EKSPYANLNP RSGSRGHPAG GGGGGGGLGS GKKTIRLKAR
GLLGISDAEL AQSIWEIGQV AGNPHEFALM VDRDLGEFAF PDGLVFDFWG AVSDAKAGRI
RPGSGGGGGR APADSRKAEP EEEGAVEFTE EF
//
