ID A0A1D1V189_RAMVA Unreviewed; 1277 AA.
AC A0A1D1V189;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=RvY_06193-1 {ECO:0000313|EMBL:GAU94415.1};
GN Synonyms=RvY_06193.1 {ECO:0000313|EMBL:GAU94415.1};
GN ORFNames=RvY_06193 {ECO:0000313|EMBL:GAU94415.1};
OS Ramazzottius varieornatus (Water bear) (Tardigrade).
OC Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC Hypsibioidea; Ramazzottiidae; Ramazzottius.
OX NCBI_TaxID=947166 {ECO:0000313|EMBL:GAU94415.1, ECO:0000313|Proteomes:UP000186922};
RN [1] {ECO:0000313|EMBL:GAU94415.1, ECO:0000313|Proteomes:UP000186922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YOKOZUNA-1 {ECO:0000313|EMBL:GAU94415.1,
RC ECO:0000313|Proteomes:UP000186922};
RX PubMed=27649274; DOI=10.1038/ncomms12808;
RA Hashimoto T., Horikawa D.D., Saito Y., Kuwahara H., Kozuka-Hata H.,
RA Shin-I T., Minakuchi Y., Ohishi K., Motoyama A., Aizu T., Enomoto A.,
RA Kondo K., Tanaka S., Hara Y., Koshikawa S., Sagara H., Miura T.,
RA Yokobori S., Miyagawa K., Suzuki Y., Kubo T., Oyama M., Kohara Y.,
RA Fujiyama A., Arakawa K., Katayama T., Toyoda A., Kunieda T.;
RT "Extremotolerant tardigrade genome and improved radiotolerance of human
RT cultured cells by tardigrade-unique protein.";
RL Nat. Commun. 7:12808-12808(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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:GAU94415.1}.
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DR EMBL; BDGG01000002; GAU94415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D1V189; -.
DR STRING; 947166.A0A1D1V189; -.
DR Proteomes; UP000186922; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd06608; STKc_myosinIII_N_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
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 PANTHER; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50219; CNH; 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000186922};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 39..303
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 949..1250
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 343..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..642
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..799
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1277 AA; 140047 MW; CB7CCE6BBB8A72D5 CRC64;
MALQMVPQYN QSNNSATVNN NLLLDDIDLS ALKDPKGIFE LIEVVGTGTY GQVYKGRHTR
TGQLAAIKVM EVSEDEIEEI KLEINVLRKY SHHKNIATYY GAFIQKSPPG KDDQLWLVME
YCGAGSVTDL VKNTKGGSLK EEWIAYVCRE ILKGLAHLHN NKIIHRDIKG QNVLLTDQAE
VKLVDFGVSA QLDRTIGRRN TFIGTPYWMA PEVIACDDNP GATYDNRSDL WSLGITSIEM
AESSPPHCDL HPMRALFLIP RHPPPRLKSK KWTKKFTGFL EKVLVKDYHK RPFTEDLLQH
TFIRDQPTER QVKIQLKDHI DRCKRLRGRS TDAAWELQGE FHQFSGSDED ESGRSDNAEN
VQEGNADDGP QSSRHGQRLV MPGESTLRKS FLQLQQKHLS TPQSSTADLN LLNGKNSSGG
PPALVREHRE GPIVHHPQRH SVASNNNSSS SNADGPPQLP EKTRQINLRR VEPQPVAASS
GPPLPARTGA LSQAPAHKVE DLDAVAAQLA RLGAPSVRGD SDDESVAKQP LKMRRVVISS
EEEDETEVSE SSNGKRRQRR VVSSSESSSD ESGASSDDHS SDDDEDLDDE IMIKQNALNA
TLAGELDKSL SPPGSAPPPV KPPPLPPQTS MQNRPLPPLP AEALPAKRAI TKNESFSSQR
VSGGSDHEDD EGTMRKPKRT SSERSAVRPE PPQAQAANSF RERPISQINA QPAIARGPMQ
REAFAKLRQT SAASSSSPNF AGSNGGGAAN LAKSRSSYHF PGQGQNGGQG SASPPTAAGG
RRVSSPPPHR REEGHNYPRD RNGAVMPDLL PIGVADGNWS PQMPQDKRTS EEYRMAVGKA
AAGSHGSSRD LVAAGQNGSQ PQLQSASGQK KSPTVYPFAL QQGALTPANK RESMAVNVNV
VPGSEAVGNL AQITRSGNPA SVSVSVANSS IVGGVGDTPE IRKYKKKFNS EVLCAALWGV
NLLIGTDSGL MLLDRSGQGK VYQLIHRRRF QQMEVLENQN ILVTISGKKN RLRVYYLSWL
KNKILRTENS LSGMDSKRNG WLNQGDIQGA VHFKIVKYER IKFLVIALKD SVEIHAWAPK
PYHKFMQYKS FNEQLQHKPL LVDLTVEEGT RLKVVYGSTV GFHAVDVDAG TVYDIYTVPH
EQSPVTPHAI VPLPNSHGMQ LLLCYDNEGV YVDTYGKQLK NSKLQWGEMP TSVAYIGGTS
SNGGPVHAQI MGWGNKAIEI RNVETGHLDG VFMHKKAQKL KFLCERNDKV FFSSAKSGGA
ACQIYFMTLS KNAIPNW
//
