ID J9INH4_9SPIT Unreviewed; 1139 AA.
AC J9INH4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Protein kinase domain containing protein {ECO:0000313|EMBL:EJY80844.1};
GN ORFNames=OXYTRI_21765 {ECO:0000313|EMBL:EJY80844.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY80844.1};
RN [1] {ECO:0000313|EMBL:EJY80844.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY80844.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(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:EJY80844.1}.
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DR EMBL; AMCR01007386; EJY80844.1; -; Genomic_DNA.
DR AlphaFoldDB; J9INH4; -.
DR EnsemblProtists; EJY80844; EJY80844; OXYTRI_21765.
DR OrthoDB; 167568at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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; cd06606; STKc_MAPKKK; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR46492; DYNEIN ASSEMBLY FACTOR 4, AXONEMAL; 1.
DR PANTHER; PTHR46492:SF1; DYNEIN AXONEMAL ASSEMBLY FACTOR 4; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13414; TPR_11; 2.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 3.
DR PROSITE; PS51203; CS; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000313|EMBL:EJY80844.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:EJY80844.1}.
FT DOMAIN 90..451
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 375..465
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT REPEAT 865..898
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 947..980
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 1092..1125
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 13..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 534..561
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 625..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1139 AA; 132134 MW; CED815C62980A708 CRC64;
MDSLTLIQLE PIDQSNNNSV DNKANQTSNN LQNPGQSKLA QNFIGYTGFT QQNGLDLNLN
DEDVDQDLKE RIRRDSQKTI KRNCQLTEFI RIGDLLGEGA YGKVYKAFNM QDGKTIAVKV
MKIQPQDQNE QKLIKLTSNL QKEITLLQNL KHQNIVKYLD SCIIDDSDVN IYMEYLPGGS
ISSIIKEYGP MDESAIRHFT KQLLEGLNYL HQNHIIHADL KGGNILFDGL DNIKLSDFGA
AKFIENISAL SASQSDICQS IKGSLYWMAP EMIMQQGYGR KIDIWSLGCT IIEMASGTHP
WPDVKNYPQL VLEIVNKRIP LIPDHLSENA QDFIPPIHIR YIRMKCHRVT MEKPVVQIKS
PLDMNSMTTK TIIKKREEAF TWSQTDDSIT LTFPIRNVTL KGIDVIYTPE FIKINVTSQK
FVSIVDFAQL IDNENPQNRI QLQDEGLEVY LMKASSSKGH WNEIQLRGQS KSELIARREQ
SLQQYYTHQE KKFKEAADLK VKMDKMSIDQ QMKVEDFQRS QLKKIKQEQK QLAEQQLYND
LDNLEQINRK LLEQKHQKDQ DSNYQDQSAD QIKINKDDKE NVQSQGNRGN HTVIPEFRGD
TGFSFKNKQD KDIFGDEDDI ETIPTQQQRT KNQHSNAQTN KSKDNETYVE EITEEQAQLI
NSQFETQLEV EVPVPQVRGK QDVTVPFTEK KFPNLPARES HNKEPPYPKS KKIDKKKDDV
FIDIEDKDPV WLKDKGDHFF KRNDFYSALN AYSKALEIDK EFMMCRLNRA TAWLKMRAFQ
NCIDDCTDIE VQVQNIKDSE REDEFYQKLL ARVYVKRGAS YSWLSMFDKS VDEFKKALEY
KGIFSELELN EIEKDIEKII SRKQSQQLKQ EGDMKFAQSD LEGALEMYTK ALQLDDKNEY
AHANIGLIHM KRQDYQKCIE FSTRALEILD HFMNDTKSFQ RDNKLEVKIL LRRGKSFENV
GEYEKAKEDL DKAIGLEPQN GEARTLLKKV QEKLDAILFD KYNKQAIEYQ KQQNFAGALE
FYEKCLRITK KGTSLDNIAV YVNKIACLLQ LEKHDRVVTE CNDALRLIKN FKNKNDDKQT
PEDKKRLSQM EIRVSVRRGN ALAKLNRVSD AIQEYERAIK LDPENETIKR DLDTLRKGA
//
