ID A0A093FS56_TYTAL Unreviewed; 1453 AA.
AC A0A093FS56;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Tyrosine-protein kinase BAZ1B {ECO:0000313|EMBL:KFV57144.1};
DE Flags: Fragment;
GN ORFNames=N341_06216 {ECO:0000313|EMBL:KFV57144.1};
OS Tyto alba (Barn owl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV57144.1, ECO:0000313|Proteomes:UP000054190};
RN [1] {ECO:0000313|EMBL:KFV57144.1, ECO:0000313|Proteomes:UP000054190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV57144.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00475}.
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DR EMBL; KK395644; KFV57144.1; -; Genomic_DNA.
DR Proteomes; UP000054190; Unassembled WGS sequence.
DR GO; GO:0090535; C:WICH complex; IEA:InterPro.
DR GO; GO:0140801; F:histone H2AXY142 kinase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd15628; PHD_BAZ1B; 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; IPR013136; WSTF_Acf1_Cbp146.
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; PF10537; WAC_Acf1_DNA_bd; 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; PS51136; WAC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|EMBL:KFV57144.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00475}; Reference proteome {ECO:0000313|Proteomes:UP000054190};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:KFV57144.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1..90
FT /note="WAC"
FT /evidence="ECO:0000259|PROSITE:PS51136"
FT DOMAIN 563..627
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1147..1197
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1150..1195
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1323..1393
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 107..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 503..542
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 734..764
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 107..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1239
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV57144.1"
FT NON_TER 1453
FT /evidence="ECO:0000313|EMBL:KFV57144.1"
SQ SEQUENCE 1453 AA; 167352 MW; 80EE3435046B2FE3 CRC64;
EYEARLARYG ERIWTCKSTG SSQLTHKEAW EEEQEVAELL KEEFPIWYEK PVLEIVHHNT
VSLEKLVDAA WLEIMTKFAV GEECDFEVGK EKTLPVKVMR IHPLEKVDEE ASEKKSDGAC
DSPSSDKENS SQAVQDNQKE AILKEDDNRR ESMNDRARRS PRKLPTSLKK EERKWAPPKF
LPHKYDVKLK NEDKIISNVP ADSLVRTERP PNKEILRYFI RHNALRAGTC ENAPWVVEDE
LVKKYSLPSK FSDFLLDPHK YMTLNPSTKR KSSRSPDRKP PKKSKADGSS LGQPLSPTLW
CHVHLEKTII DSPLKVKNSK NSKCPKEELE EVMKIVSPAK LGTNFHIPKK SRLGKGSNKS
LDKKQRGKRV LNGQKSSGKS KSPRTGLKTP KMKMKQITLL DMAKGTTKVS RAPRNSGGTP
RSSSKPQKHL PPAALHLIAY YKENKDREDK KSALSCIISK TARLLSNEDR ARLPEDLRGL
VQKRYELLEH KKKWATMTEE QRKEYMKKKR EKLKEKLKER AKERKEKEMK EKLEKQKRYE
DQDLKGKTLP TFKLVDTPEG LPNTLFGDVA MVVEFLSCYS GLLMPDAQYP ITAVSLMEAL
CAEKGGFLYL NRVLVILLQT LLQDEIAEDY AELGMKLSEI PLTLHSASEL VRLCLRKSDV
QEESEVSDNV DESKDSAAFE DNEVQDEFLE KLETSEFFEL TPEEKLQILG ALCHRILMTY
SVQDHVEAKQ QTSAELWKER LAILKEENDK KRAEKQKRKE MVAKNKENGK DENMMGRNEK
KKNEIMKIEH RVEIEADDMV SAVKSRRLLA IQAKKEREQQ EIQMRVRMEK EAEEERIRKH
KAAAEKTFQD GIAKAKLVMR RTPVGTDRNH NRYWLFSDEV PGLFIEKGWV HDSIDYRFIL
PHQKKEDFKK DYSPGDKRKS AATDGRVSKL HRSVHATDLP TETTAPKQGQ NLWFLCDNQK
DFDELLDCLH PQGVRESQLK ERLEKRYQDI THSIHLARKQ NLGLKSCDGN QELLNYLRSD
LIEVATRLQK GGLGYVDVTP EYEARVYSLE SLKDFGECVI ALQAGVVKKF LQGFMAPKQK
RRKHQGEDYI AKAEEVDEDK KMAEEAKVAS AMEKWKTAIR EAQTFSRMHV LLGMLDACIK
WDMSAENARC KVCRKKGEDD KLILCDECNK AFHLFCLRPA LYEIPDGEWQ CPACQPSTAR
RSSRGRNYAE DSAEDEGGEG EEASDEPDAE EEEEEEEDYE VAGLKLRPRK AARGKQSTAV
YSLRQGRHQR KKQSLQPARG GPRQRAAPVN GADIDELVLQ TKKTTRRQSL ELQKCEEILS
KLIKYRFSWP FREPVTTEEA EDYFEVISNP MDFQTMQSKC SCGNYRSVQE FLSDIKQVFS
NAEHYNQNGS HVLSCLEKTE QCLIDMVHKH LPGHTYARRK RRMLSARCQG LEEQDGDSES
EPLEHSRGRK RKK
//
