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Database: UniProt
Entry: A0A1V4KVY9_PATFA
LinkDB: A0A1V4KVY9_PATFA
Original site: A0A1V4KVY9_PATFA 
ID   A0A1V4KVY9_PATFA        Unreviewed;      2496 AA.
AC   A0A1V4KVY9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=TEX2 {ECO:0000313|EMBL:OPJ88545.1};
GN   ORFNames=AV530_003071 {ECO:0000313|EMBL:OPJ88545.1};
OS   Patagioenas fasciata monilis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX   NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ88545.1, ECO:0000313|Proteomes:UP000190648};
RN   [1] {ECO:0000313|EMBL:OPJ88545.1, ECO:0000313|Proteomes:UP000190648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ88545.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OPJ88545.1};
RA   Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA   Shapiro B.;
RT   "Band-tailed pigeon sequencing and assembly.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:OPJ88545.1}.
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DR   EMBL; LSYS01001520; OPJ88545.1; -; Genomic_DNA.
DR   Proteomes; UP000190648; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR   GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:UniProt.
DR   CDD; cd09769; Luminal_IRE1; 1.
DR   CDD; cd10422; RNase_Ire1; 1.
DR   CDD; cd13982; STKc_IRE1; 1.
DR   Gene3D; 1.20.1440.180; KEN domain; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR010513; KEN_dom.
DR   InterPro; IPR038357; KEN_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR16155; DED DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR16155:SF3; ZMP:0000000735; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF06479; Ribonuc_2-5A; 1.
DR   SMART; SM00564; PQQ; 5.
DR   SMART; SM00580; PUG; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS51392; KEN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          559..820
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          823..952
FT                   /note="KEN"
FT                   /evidence="ECO:0000259|PROSITE:PS51392"
FT   DOMAIN          949..994
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   REGION          404..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1011..1080
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..531
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2496 AA;  285341 MW;  3318EEF43EB9F7CF CRC64;
     MQPRLSSYFI NYKASQNTSS VTVPETLLFV STLDGSLHAV SKRTGAIKWT LKEDPVLQVP
     IHVEEPAFLP DPNDGSLYTL GGKNNEGLTK LPFTIPELVQ ASPCRSSDGI LYMGKKQDIW
     YVIDLLTGEK QQTLTSSFAE SLCPSASLLY LGRTEYTITM YDTKKKELRW NATYFDYAAS
     LPDKDIKYKM SHFVSNGDGL VVTVDSESGD VLWIQNYASP VVAFYIWQRE GLRKVMHTNV
     GIETLRYLTF MSGEVGHITK WKYPFPKETE TKSKLTPTLY VGKYSTSLYA SPSMVHEGVT
     VVPRGSAIPL LEGPKTEGVT IEDNGECVIT PSTDVKFSGR LKEKNKLSYW NDWLLIGHHE
     TPLSAPTKIL EKFPSNLPKR PENVIPADSD KAAIEEVIDI VEGSSTDVPP AAPKDIEEKP
     ARPVPRPEAP VDSMLKDMAT IILSTFLLVG WVAFIIAYPM SVHQQQQRQH QLEEKIQLLQ
     QQQLPFGAPS DLPPEADFLD PSCGRPENSA ASTPNLSPRA SNHSAYSSVS TSDVGSCIST
     EQEEGDEDAN RVMVGKISFN PKDVLGHGAE GTIVYRGTFD NRDVAVKRIL PECFSFADRE
     VQLLRESDEH PNVIRYFCTE KDRQFQYIAI ELCAATLQEY VEQKAFSHHG LQPITLLQQT
     TSGLAYLHSL SIVHRDLKPH NILISMPNAH GKVKAMISDF GLCKKLAVGR HSFSRRSGVP
     GTEGWIAPEM LSEDCKENPT YTVDIFSAGC VFYYVVSDGS HPFGKSLQRQ ANILLGAYSL
     ESFSAGRHED IVARDLIEQM INMDPQKRPS ASCVLKHPFF WSLEKQLQFF QDVSDRIEKE
     SLDGPIVKQL ERGGREVVKM DWRQHITVPL QTDLRKFRSY KGGSVRDLLR AMRNKKHHYR
     ELPPEVQETL GSIPDEFQQH RTFRGFCSLT AGFPSSKAMD YKTLPVDKWD ENHVQCWLQS
     TGIKKEYVEK LHAEEVTGPV LMELDEPFLK GIGMKKGQIH MLIRKRNELL QPQENAQPAK
     HLNSKTSDRT DPQTDPGIPR NASAQKTSNG DSCGPADKPS GDNTASTSGK RRQSNNTQLQ
     STAEVLELSN CRPFRSQNTD FKYVKDRVLA PESGVNGLIT PCHEYKSFAT AAELNKNQLQ
     SKFACEVIRF ASACMNIRTN GTIHFGIMDS VEDRGWKHGQ IVGIKVKERE YYVDALDYIE
     KCFFKHVQET ARKCIHPPVF VEVISKDSEE QRFVVEVDIE PTSSLVKNKF FQVCLPKYNE
     DKKRVDLTET SVPYQRLGAK SEPVKHNDLA TFLQGLQDRD AEREKAELSS AEVHTEIPQN
     LGRKLSILLN DGKSYMDDSL RYILVTNRCE KNDLNYINFL MHLNIFCVFD FDEDSNVSGL
     CSKYKEHHAV RLYFLQDFSN ESKTGNPPAQ KHLCLFDQTS WIFCNGRSDF LGNEEPCDEN
     TWIRTKKKYL KKAITRICDE ILPKRSFIVL FLLLSPVQKP LVDTFQEFYT EMNGMEYIVC
     IAESRENYNK WANLAQTSCS IETLEQCSVV GMKLSHVDAT IETMLPSTAQ PRHLPVSSRG
     LCTLPSREEE KLFSLEILCV DQCNDIKLDC LTEKEIQEME QNFYRGRKII WENFWLADTR
     RCGEIIEREA CKDASKLLDD ILQGSGLNYS VAKLKIFHHP GSGGSTIARQ VLWKRRKDLR
     CAVIKTSYPP ATVCEHALAF RDYEEKEFSH CLPVLLLIED YDEDYLEELR NELMDAVSTR
     KINSPRPYFI LMCCRRSNDP ERLCKASPLD TVAVTHKLTD TEKSLFKTKL EKLKQKDVKP
     EFILTFVLMC EEFNETYVRD FVGHILQGID RSSRDTLLMR YVALLSFYVP HSYVSLSHCE
     AFLGLGVYTE SRSRAYDFKS HLSEQARMIF IELRDSTTYI SSVRIIHYLV AKEILHQLSG
     DEPQSQLAMT LLQEKTLFEN RFGREEFIKF IRDLFIRRDK RSRGDNTDTL FSPFIEHVCK
     VEDCEKAIHV LKAAYELLGK DPFFAQQLAR LHYSNEKFED AEHWARIAKF HLPNDSYILD
     TEGQVYRKWF SFMVDKRTQE DSPEHIIQRI EMALKAMKCF RAAQQAAKAE RDSMNNAGYF
     GEVEVGCRLL RFLSTVHVFR RSPEGEHSEL VKYLITDYVP KDIEKTWGCF HSCLKGLRQN
     LYNALEWISE DLSYFQTDKH HQREEEDEKD EKEEQIYNPR KWLKRQSEVY AKFFVSASLL
     EESNSGPESQ LIRRMNIYKN GGGSVTNILS FLTDKKESRS ADKLENILSF YTENPLRDRL
     EDNDLINYIL CHITLACLSP GSAKLLPAQT LRDLSARFFK GKRPFPASAY FLLTLLYWPD
     EALDKEPNPD KDEILNSALQ TLKRLYDIKM KDVPTRKKRI YTHFFLGKGY GLSKIVHKTK
     IDKLITGSLD EKRMKWLHGT VWNIAKIRDI LKRVSGWTKD RNLFIRGHVK EFPILPLHRD
     SVPPGNENVT FYLGFSFNGL VAFNIEVENN PTVSRT
//
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