ID A0A0V0QX20_PSEPJ Unreviewed; 1393 AA.
AC A0A0V0QX20;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Protein kinase-like domain {ECO:0000313|EMBL:KRX06637.1};
GN ORFNames=PPERSA_13116 {ECO:0000313|EMBL:KRX06637.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX06637.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX06637.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX06637.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
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:KRX06637.1}.
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DR EMBL; LDAU01000094; KRX06637.1; -; Genomic_DNA.
DR EnsemblProtists; KRX06637; KRX06637; PPERSA_13116.
DR InParanoid; A0A0V0QX20; -.
DR OMA; TRICICY; -.
DR OrthoDB; 195880at2759; -.
DR Proteomes; UP000054937; 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; 1.25.40.10; Tetratricopeptide repeat domain; 5.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45641:SF20; PUB DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45641; TETRATRICOPEPTIDE REPEAT PROTEIN (AFU_ORTHOLOGUE AFUA_6G03870); 1.
DR Pfam; PF13181; TPR_8; 4.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 13.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 5.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50005; TPR; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KRX06637.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}; Transferase {ECO:0000313|EMBL:KRX06637.1}.
FT DOMAIN 58..329
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 553..586
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 1155..1188
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 1241..1274
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 1346..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 605..676
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1168..1198
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1355..1375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1377..1393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1393 AA; 166040 MW; D643E3CCB53304ED CRC64;
MQNNIQSVFK QYIEGQECQI NQKIVENAPD SQILDFDTQN QLINNSKLLE LSENETYKNN
LIQLQQICSG KVYIFFDKEI EKAECQTQFA IKAFQSKQIY LQEKNIFKKI YEKNGNQFID
EMVQLVNFDD YSLSLFMQLG VMDLQKFFEI KQKLNLQAEE KEIWYAINQL VNLVEKLKEF
DIYHCDIKPG NIYLYHSDEE DFQYKLKLGD FGAFLDLSDQ KQKEQQIQLK AYSPPYMPLK
TDLKNSDDLL KFNYFQIGRI IYEIMLRNIK LENYFTSRDP NIMRQVIEQK LVPKFSEDLI
EFLNQTLFLK DFSYKSVIEQ KIQSQKEKIG ILDPNYQILN YKMNQRKNQL QKNEEANKAI
YFQQQFAEIS ICAQFQLGKT VSDVLKNFKL EELKKYDNLM KIEEAQIFYK NCLLSFQMVS
DDQKCEECIN NYIIQKIDTL QDKNLKFDIE NQVFSVRNIF LIKSGKLDKA LSLIDQQIEK
LEQLKNNVDM FLYYKYLVDI KQNKGEILRM QNKNQNSLQE FLKIAEYKNE QDKISKECGN
DFLQPNQQQI KLVTYYEKIA IIYADLQQEE NAKEYYQKAL EIRLQNKDQK WLYQVKKCYE
NLVLLEKNMQ QKLQYEQKKQ QIQKMIESRE QKNVLQHRKY HNQAQELLKK SEIAKAKELE
RKAIEILENL GEKDSQEAAH YWVSLGNMQK QTDESEESLI SFKNAQEIYE SHFPDKLESS
QYANILNCVA SFYLMYQEYE ISEKYFQLAI DISEKLGKQD EENYVLYAYN LALIYKYQGE
LQKCVDAAGL AYKINLKMEK LCYKNLSKNC YTMGTCLLKL EKFQEGKEYL SKSIDYLDLD
ERSEEEKQDE YMNLYNELGY VFFDIKCYDL AIKYMLKSVD LQQKVIDKEQ QETNKNYFRE
KLVNSLRILS FSCRADKDLE KYAQYYEQAI DINKLLVLDK YEEIEFISDY NQIAQAFFDA
DDYNSSEKYF KKALEYSNTL KTQFDEDSVE LKDLNYLIMV LYKGMIKLYE KSGQKEEQGE
IQEQLIKFRE NLKQDDSLLL NESQMSQKSN NNNINITKTE ENKEEDNQLI MEYINFGIYQ
QNDKKNLKSA EEMYLKALNL AEEILEEKKI KMCYIKLSQM FAGVDLEKQE KYSQQYVKFL
RQSKEDKLNS QEEIPSIFVN LGNNYYKEEK YEEAIRCLES AYQEISQQQS EKENLKMVIA
IHEILNLCFE KSQQPQKAID VQLKIMEFYE IFEMKNDEKL TQLVFNLGYT YNENEKFDFA
YQYMEKAGNM AEETLDKEGQ FSLYYQIGTI YAQRSKFEES LIYLEKCLVI LEELGKGATI
YEENYKDLKD FYENIKVMNG GFGEDQQAEQ KQNDQFSSKL EENEEKIDYK SGNKYPEDSK
NYGNEMNDLL ENL
//
