ID T2M4T1_HYDVU Unreviewed; 512 AA.
AC T2M4T1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Mitogen-activated protein kinase kinase kinase MLT {ECO:0000313|EMBL:CDG66930.1};
DE Flags: Fragment;
GN Name=MLTK {ECO:0000313|EMBL:CDG66930.1};
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087 {ECO:0000313|EMBL:CDG66930.1};
RN [1] {ECO:0000313|EMBL:CDG66930.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole animals {ECO:0000313|EMBL:CDG66930.1};
RX PubMed=24065732; DOI=10.1093/gbe/evt142;
RA Wenger Y., Galliot B.;
RT "Punctuated emergences of genetic and phenotypic innovations in eumetazoan,
RT bilaterian, euteleostome, and hominidae ancestors.";
RL Genome Biol. Evol. 5:1949-1968(2013).
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DR EMBL; HAAD01000698; CDG66930.1; -; mRNA.
DR AlphaFoldDB; T2M4T1; -.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR23257:SF937; SAM DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|EMBL:CDG66930.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|EMBL:CDG66930.1}.
FT DOMAIN 6..251
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 323..391
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT COILED 267..308
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CDG66930.1"
FT NON_TER 512
FT /evidence="ECO:0000313|EMBL:CDG66930.1"
SQ SEQUENCE 512 AA; 59530 MW; 852B961E46213F2C CRC64;
LQIEDFEFFE KLGSGSFGSV YRARWISQNK EVAIKKVLSL DKEAEILGVL SHRNIIHFYG
AIIMHLNFCL ITEYAKHGSL HDYLVNHELD FLQILTWSEQ IALGISYLHN EAPFTIIHRD
LKSKNVVITG DMVVKLCDFG SSRYLDQTTK MSLAGTFPWM APEVIQSMPI SEACDTYSYG
ILLWEMLTRE VPFKGMEGVQ VAWLVVVKEE RLTIPSSCPP EFSNLLVSCW KTDPKLRPNF
KQIQAIINKM LDNNALAEET NSFIRNKKDW QAEIEQTVLR LKKMEKNLSS KEQELHEREL
RLLKKEQKIN LVKMLNKTKL VDWDESDVYC WIEQLGNEAI DLYPYSQIFF DNHINGRRLS
LLTNEDLKYM GILSHGHRLD LLDQISKLVE ELEHLHHFPP LHQVPSIESQ IRNQKVQNLT
LIFGNHCRLG PTPMDHKWKL FIEVDGDDEA ILAIKEVHLI WPEDQLTIQE PPYVMHRWIT
VPGNNSPIFV DCIVSYKNSI KKPHSTKHRH EV
//
