ID A0A851NNJ9_9GALL Unreviewed; 1283 AA.
AC A0A851NNJ9;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=Tyrosine-protein kinase BAZ1B {ECO:0000256|ARBA:ARBA00069894};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
DE AltName: Full=Bromodomain adjacent to zinc finger domain protein 1B {ECO:0000256|ARBA:ARBA00076449};
DE Flags: Fragment;
GN Name=Baz1b {ECO:0000313|EMBL:NXC41737.1};
GN ORFNames=PENPIL_R14585 {ECO:0000313|EMBL:NXC41737.1};
OS Penelope pileata.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Cracidae;
OC Penelope.
OX NCBI_TaxID=1118817 {ECO:0000313|EMBL:NXC41737.1, ECO:0000313|Proteomes:UP000613066};
RN [1] {ECO:0000313|EMBL:NXC41737.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B10K-DU-001-08 {ECO:0000313|EMBL:NXC41737.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXC41737.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000256|ARBA:ARBA00051245};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the WAL family. BAZ1B subfamily.
CC {ECO:0000256|ARBA:ARBA00061696}.
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:NXC41737.1}.
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DR EMBL; WBMW01001952; NXC41737.1; -; Genomic_DNA.
DR OrthoDB; 787137at2759; -.
DR Proteomes; UP000613066; Unassembled WGS sequence.
DR GO; GO:0090535; C:WICH complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:TreeGrafter.
DR GO; GO:0140801; F:histone H2AXY142 kinase activity; IEA:InterPro.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:DNA damage response; IEA:UniProtKB-KW.
DR CDD; cd15628; PHD_BAZ1B; 1.
DR FunFam; 1.20.920.10:FF:000031; Bromodomain adjacent to zinc finger domain, 1B; 1.
DR FunFam; 3.30.40.10:FF:000131; tyrosine-protein kinase BAZ1B isoform X1; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR047174; BAZ1B.
DR InterPro; IPR047256; BAZ1B_PHD.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46802; TYROSINE-PROTEIN KINASE BAZ1B; 1.
DR PANTHER; PTHR46802:SF1; TYROSINE-PROTEIN KINASE BAZ1B; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF15612; WHIM1; 1.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:NXC41737.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000613066};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 394..458
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 978..1028
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 981..1026
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1153..1223
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 100..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 330..373
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 642..681
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 216..229
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..259
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1071
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1113
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1271
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXC41737.1"
FT NON_TER 1283
FT /evidence="ECO:0000313|EMBL:NXC41737.1"
SQ SEQUENCE 1283 AA; 147413 MW; 7309EB9E712628F1 CRC64;
TSLKKEERKW VPPKFLPHKY DVKLKNEDKI ISNVPADSLV RTERPPNKEI LRYFIRHNAL
RAGTGENAPW VVEDELVKKY SLPSKFSDFL LDPHKYLTLN PSTKRKSSGS PDRKPSKKSK
TDGSSLSQPL SPTLWCHVHL EKSIIGSPLK VKNSKNSKSP KEELEEMMKI MSPGKLGSNF
NIPKRSRLGK GSNKSLDKKQ KGKRVLNGQK TSGKSKSPRK GLKTPKMKMK QMTLLDMAKG
TTKVSRAPRS SGGTPRSSSK PQKHLPPAAL HLIAYYKENK DREDKKSALS CIISKTARLL
SNEDRARLPE DLRGLVQKRY ELLEHRKKWA AMTEEQRKEY LKKKREKLKE KLKERAKERK
EKEMEKNKRF EDQDLKGKNL PTFKLVDTPE GLPNTLFGDV AMVVEFLSCY SGLLMPDAQY
PITAVSLMEA LCAEKGGFLY LNRVLVILLQ TLLQDEIAED YAELGMKLSE IPLTLHSASE
LVRLCLRKSD VQEESEVSDN VDESKDSATF EDNEVQDEFL EKLETSEFFE LTPEEKLQIL
GALCHRILMT YSVQDHVEAK QQTSAELWKE RLAILKEEND KKRAEKQKRK EMVAKNKENG
KDEHTMGRNE KKKNEMVKIE HRVEIEADDM ISAVKSRRLL AIQAKKEREQ QERQMRVRME
KEAEEERIRK HKAAAEKMFQ DGIAKAKLVM RRTPVGTDRN HNRYWLFSDE VPGLFIEKGW
VHDSIDYRFI LPHQKKEEAK KDYSPGEKRK GAASDGRTSA LHRSGHTADL PAETTTPKQG
QNLWFLCDSQ KDLDELIDCL HPQGARESQL KERLEKKYQD ITHSMHLARK QNLGLKSCDG
NQELLTYLRS DLIEVATRLQ KGGLGYVDVT PEFEARVHSL ESLKDFGECV IALQAGVIKK
FLQGFMAPKQ KRRKHQGEDY AAKAEEIDEE KKIAEEAKVA SAMEKWKTAI REAQTFSRMH
VLLGMLDACI KWDMSAENAR CKVCRKKGED DKLILCDECN KAFHLFCLRP ALYEIPDGEW
QCPACQPSTA RRSSRGRNYT EDSAEDEGEE GEEASDEQEA EEEEEEEEDY EVAGLKLRPR
KAARGKQSTA MYSSRQGRHQ RKKQSLHPAR GPRQRAAPVN SADIDELVLQ TKKMTRRQSL
ELQKCEEILG KLVKYRFSWP FREPVTAEEA EDYLEVISNP MDFQTMQSKC SCGHYRSVQE
FLSDIKQVFS NAEHYNQNGS HVLSCLEKTE QCLIDMVHKH LPGHTYARRK RKKLSARCQG
LEEQEGDSES EPLEHSRGRK RKK
//
