ID A0E8G3_PARTE Unreviewed; 1050 AA.
AC A0E8G3;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE SubName: Full=Chromosome undetermined scaffold_82, whole genome shotgun sequence {ECO:0000313|EMBL:CAK91580.1};
GN ORFNames=GSPATT00024309001 {ECO:0000313|EMBL:CAK91580.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK91580.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK91580.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK91580.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
CC -!- SIMILARITY: Belongs to the DRC1 family.
CC {ECO:0000256|ARBA:ARBA00009688}.
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; CT868663; CAK91580.1; -; Genomic_DNA.
DR RefSeq; XP_001458977.1; XM_001458940.1.
DR AlphaFoldDB; A0E8G3; -.
DR STRING; 5888.A0E8G3; -.
DR EnsemblProtists; CAK91580; CAK91580; GSPATT00024309001.
DR GeneID; 5044762; -.
DR KEGG; ptm:GSPATT00024309001; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_291107_0_0_1; -.
DR InParanoid; A0E8G3; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005858; C:axonemal dynein complex; IEA:InterPro.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0070286; P:axonemal dynein complex assembly; IBA:GO_Central.
DR GO; GO:0060285; P:cilium-dependent cell motility; IBA:GO_Central.
DR GO; GO:0003352; P:regulation of cilium movement; IBA:GO_Central.
DR CDD; cd13999; STKc_MAP3K-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR039505; DRC1/2_N.
DR InterPro; IPR039750; DRC1/DRC2.
DR InterPro; IPR029440; DRC1_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR21625:SF1; DYNEIN REGULATORY COMPLEX PROTEIN 1; 1.
DR PANTHER; PTHR21625; NYD-SP28 PROTEIN; 1.
DR Pfam; PF14772; NYD-SP28; 1.
DR Pfam; PF14775; NYD-SP28_assoc; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022527};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 132..378
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 564..624
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 679..731
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 999..1026
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1050 AA; 123842 MW; ADF3CB93608161B3 CRC64;
MEVLKQKKSK NKRSSGGSED KLIPPDKQDQ QQETANFSPK QGNQGSNLNV ESNKVVSNYN
INNATGSEFS DVSSCCSNES KDQQLESSQS NSPKKHNMFK EKNLYQKHQE ILMSLLKNLG
INEKLLINYK EIKQGPQIGK GSYGIVFKGN WLGQGVAIKS YCQRKDQQMH KQLMADFLKE
VQVISNLRHP NIVLYMGVCI KQDNFYLITE YMENGSLKTK NLNFIQIIED ITLGMNNLHG
RKIMHCDLKS SNVLIDSNWN VKLCDFGLSK IKSKKTKIMI GTPHWMAPEI MRGEPYTEKS
DVYSFGLILW EIITGKMPYE NLSVTQILGT VGRGHTQVEI PQSSNPPILA IIAKDCLKRD
PSQRPIFAKN PERIQESQKQ KCKTRRKLRN TQLIFYLIDI NINIFIQLMD SKKQAKGSEQ
VQKSRGNIDM LIRTKKEELY TIKQKNDQKQ KETRAQEEFK RAERANKIED ESKKANSKNA
ELEQEWCNLQ EKDECEELNK LINQQKDKFA QIMHAKDELI KQFLDELNKK DDDFGKMIKE
QAIDIQTLIQ KMRSQFFQLR ECIHEDLESI ENEYIEERAN LLNNYQTEIR NLFDKRTEKE
KSFVDERERK EEEYTKDIEK LRIQGLKSYA ELKISMETEI QNLEKCYEDM KALYQLNTEK
LDYNLKVLKE KQISHTHTHD DLKRKDQNLN NRLRSLIKDY NEFDTKFKQT NKELTQEYKR
ITRQFKELQR KFKHFDKADQ KAYADIHSMN ELEVRKLKAK ILKCDKTIHI QQLGVDWEEP
QDQKETEEKS QIMAEEEVQL PLSEEKLQEI VEILIEEVDF LIDDKMRETL EKAEQQEISN
VKLGVIKKCL NIDSIDEMLI FIDELIKNCE LKVQEEQPQQ EAVTEAIKKV QIEQPQTVPD
EAPKINYDTF IINQNSIINF LMHWMKTNEQ RKKQIEKMSS RRAAKQETER QKKERIAKEG
KKYWEKLTQV LPEKTFRVWR ILDKQLSKYY ELLLKRSKLV EETGQIHNHN EELKNLLNQY
LQINHELKIP PTRFLKLEQQ QDNVKLQNSK
//
