ID A0A091MRT6_9PASS Unreviewed; 1333 AA.
AC A0A091MRT6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Mitogen-activated protein kinase kinase kinase 1 {ECO:0000313|EMBL:KFP80173.1};
DE Flags: Fragment;
GN ORFNames=N310_12074 {ECO:0000313|EMBL:KFP80173.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP80173.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP80173.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP80173.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KK836499; KFP80173.1; -; Genomic_DNA.
DR Proteomes; UP000053537; Unassembled WGS sequence.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16494; RING-CH-C4HC3_ZSWM2; 1.
DR CDD; cd06630; STKc_MEKK1; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011989; ARM-like.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR007527; Znf_SWIM.
DR PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR PANTHER; PTHR48016:SF29; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 1A; 1.
DR Pfam; PF21040; CEP104-like_TOG; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF04434; SWIM; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50966; ZF_SWIM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFP80173.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000053537};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFP80173.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 179..207
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DOMAIN 284..333
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1064..1329
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1093
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:KFP80173.1"
FT NON_TER 1333
FT /evidence="ECO:0000313|EMBL:KFP80173.1"
SQ SEQUENCE 1333 AA; 147263 MW; 6FDB9FB9E4A0BE40 CRC64;
RDMENKETLR GLQKMDDRPE ERMIREKLKA TCMPAWKHEW LERRSRRGPV VVKPIPGKVD
GSEMNKLCLE PQAEGQSTAS SPTQKGRRSP SPSSSSSSSA RTVKSESPGV RRKRVSPVPF
QSGRITPPRR APSPDGFSPY SPEETNRRVN KVMRARLYLL QQIGPNSFLI GGDSPDNKYR
VFIGPQTCSC GRGTFCIHLL FVMLRVFQLE PSDPMLWRKT LKNFEVESLF QKYHSRRSSR
IKAPSRNTIQ KFVSRMSNSH TLSSSSTSTS SSENSMKDEE EQMCPICLLG MLDEESLTVC
EDGCRNKLHH HCMSIWAEEC RRNREPLICP LCRSKWRSHD FYSHELPSPV DSSGTQRRTQ
DSNFNLTHYG VQQIPSTYKD LAEPWIQVFG MELVGCLFSR NWNIREMALR RLSHDVSGAL
LLANGESTGN SGSSNGNNTS AGALGAASGS SQTSISGDVV VESCCSVLSM VCADPVYKVY
VAALKTLRAM LVYTPCHTLA ERTKLQRLLK PVVETILVKC ADANSRTSQL SVSTLLEMCK
GQAGELAVGR EILKSGSIGI GGVDYVLNCI LGTQTESSNW QALLGRLCLI DRLLLEFPGE
FYPHIVCGDV LQADSVLDRY KKLLSLLNFA LQSIDNSHSM VGKLSRRVFL SAARMVARVP
HVFVKLLEML SVTSSTHYAR MRRRLMAIAD EMEIAEAIQL GMEEMHSGDC RHEDFLQLPV
PDNSPEATES NTPNNTVQLS GKSGKGLSDK KPSASPEDIS ETLAGLAVGL PVSSAEQPKP
AIQTKGKPHS QCLNSSPSSS HSQSLFPALL SPSNPSVPAG TVTDVSKLRP QGFVPCKIPS
PSPQTQRKLS LQFQRNCSEN KESEKLSPVF TQARPLPSSH VHRPKPSRPT PSDVNKQGEN
LKSSMTLDLN DISQCDGNSS SSAVIPSEET VFTPVDEKCR LDANAELNSS IEDLLEASMP
TSDGTVTFKS EVAVLSPERA ENDDTYKDDV NHNQKCKEKM EAEEEEALAI AMAMSASQDA
LPIIPQLQVE NGEDIIDFEF RLQTPETLPG HTKAKHHYRE DAEWLKGQQI GLGAFSSCYQ
AQDVGTGTLM AVKQVTYVRN TSSEQEEVVE ALREEIRMMS HLNHPNIIRM LGATCEKSNY
NLFIEWMAGG SVAHLLSKYG AFKESVIINY TEQLLRGLSY LHENQIIHRD VKGANLLIDS
TGHRLRIADF GAAARLASKG TGAGEFQGQL LGTIAFMAPE VLRGQQYGRS CDVWSVGCVV
IEMACAKPPW NAEKHSNHLA LIFKIASATT APSIPTHLSP GLKDVTLRCL ELQPQDRPPS
RELLKHPVFR TTW
//
