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Database: UniProt
Entry: A0A151NDJ1_ALLMI
LinkDB: A0A151NDJ1_ALLMI
Original site: A0A151NDJ1_ALLMI 
ID   A0A151NDJ1_ALLMI        Unreviewed;       918 AA.
AC   A0A151NDJ1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Interleukin-1 receptor-associated kinase 1 {ECO:0000313|EMBL:KYO34868.1};
GN   Name=IRAK1 {ECO:0000313|EMBL:KYO34868.1};
GN   ORFNames=Y1Q_0017056 {ECO:0000313|EMBL:KYO34868.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO34868.1};
RN   [1] {ECO:0000313|EMBL:KYO34868.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO34868.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA   Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA   Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA   Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA   Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA   McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA   Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA   Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA   Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA   Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(2012).
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:KYO34868.1}.
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DR   EMBL; AKHW03003281; KYO34868.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151NDJ1; -.
DR   STRING; 8496.A0A151NDJ1; -.
DR   eggNOG; KOG1187; Eukaryota.
DR   Proteomes; UP000050525; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProt.
DR   GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR   GO; GO:0010033; P:response to organic substance; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd01396; MeCP2_MBD; 1.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR000488; Death_domain.
DR   InterPro; IPR016177; DNA-bd_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR27001; OS01G0253100 PROTEIN; 1.
DR   PANTHER; PTHR27001:SF489; PROLINE-RICH RECEPTOR-LIKE PROTEIN KINASE PERK8; 1.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF01429; MBD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00391; MBD; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF54171; DNA-binding domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50982; MBD; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 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:KYO34868.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Receptor {ECO:0000313|EMBL:KYO34868.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          93..165
FT                   /note="MBD"
FT                   /evidence="ECO:0000259|PROSITE:PS50982"
FT   DOMAIN          583..874
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          886..918
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..390
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..918
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         610
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   918 AA;  98312 MW;  C439F09E46C257EB CRC64;
     MHVSRSGCSH GRHGKGEEKV EDQHTQGKPG KAKKTKKERQ QHETVAAAGG QPSAEPAEAG
     KAETSEGEGG AGAAPAAPEP SASPKQRRSI IRDRGPMYDD PTLPEGWTRK LKQRKSGRSA
     GKYDVYLINP QGKAFRSKVE LIAYFEKVGD TSLDPNDFDF TVTGRGSPSR REHKPPKKPK
     APKGPGTGRG RGRPKGSGAA AKARAGPVEG VQVKRVVEKS PGKLLVKMPF QPGPAGAKEG
     GGVATASAPV LALRRPGRKR KAEPDLQATP KKRGRKPGGG AGVGTPVAAA EVRKKAAKEA
     VVSATAPAAA HETLLPIKKR KTREAVALEP RPLPPAPERG GPKGPKAGRR SKEGSPKGRG
     GAGGSLPAKK EPPLPPLLQP PHPEPPASPP DSVFCRLMDA LGRADWERFA SRVVRDQVEL
     RLAGTSEGRT QRVLWSWGHR NARVGDLLAL LGELELDWAH DLIASWQPPP EPWTRLPHST
     SLAPPLPSVP LPSVPPAPCS TARTLPWDPP KALPVPVPPL PEPSCLSLPL PGPPPRSLLS
     TSSHDTVTSP DPVTLLSQVL PPPGFPRLLA WPLAELVEAT GGFSEQHKVG EGGFGCVYRA
     RLRHTDCAVK RLKEDAELNW NLVHNSFITE LEKLSRYRHP NIVELAGFCA EKGHFCLVYV
     FMPNGSLDDR LRPQDGRPPL TWPQRLSVLV GAARAIQFLH QDVPSLIHGD VKSSNILLDQ
     ALTPRLSDFG LARVGVGGGR GGRSGTLGRT GTVRGTLAYL PPEYVQTGAL SPAIDTYSFG
     VVLLEALTGR RALETDERGQ TKYLKDLVAA EEEESGVGDR DVGTRLGQAY ADSQAGPCPP
     LLSTSLGHLA AQCLHRRSKQ RPHMDQVYEE LERLQQALCW EPALPPCRSP VDPQNQPEES
     DDSLPGVGDS FSSESCWV
//
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