ID A0A091V0F0_NIPNI Unreviewed; 1538 AA.
AC A0A091V0F0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Bromodomain adjacent to zinc finger domain protein 1A {ECO:0000313|EMBL:KFQ96187.1};
DE Flags: Fragment;
GN ORFNames=Y956_04747 {ECO:0000313|EMBL:KFQ96187.1};
OS Nipponia nippon (Crested ibis) (Ibis nippon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC Nipponia.
OX NCBI_TaxID=128390 {ECO:0000313|EMBL:KFQ96187.1, ECO:0000313|Proteomes:UP000053283};
RN [1] {ECO:0000313|EMBL:KFQ96187.1, ECO:0000313|Proteomes:UP000053283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFQ96187.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL410344; KFQ96187.1; -; Genomic_DNA.
DR STRING; 128390.A0A091V0F0; -.
DR eggNOG; KOG1245; Eukaryota.
DR Proteomes; UP000053283; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR CDD; cd05504; Bromo_Acf1_like; 1.
DR CDD; cd15627; PHD_BAZ1A; 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; IPR037325; Acf1_Bromo.
DR InterPro; IPR047171; BAZ1A.
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; PTHR46510; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 1A; 1.
DR PANTHER; PTHR46510:SF1; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 1A; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF02791; DDT; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00475}; Reference proteome {ECO:0000313|Proteomes:UP000053283};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1..92
FT /note="WAC"
FT /evidence="ECO:0000259|PROSITE:PS51136"
FT DOMAIN 387..460
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1125..1175
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1128..1173
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1430..1500
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 111..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 275..359
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 113..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1233
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ96187.1"
FT NON_TER 1538
FT /evidence="ECO:0000313|EMBL:KFQ96187.1"
SQ SEQUENCE 1538 AA; 176091 MW; B9B02DF5565E190F CRC64;
FSDFFERTIL CNSLVWSCAV TGKPGLTYQE ALESEKKARH NLQSFPEALI IPVLYLATLT
HRSRLHEICD EIFAYVKDRY FVGETVEVVR NNGARLQCKI LEVIAPAHHN GMANGHASST
DGDTIVISDS DDSETHNSSA QNGEKRAIID PSLFKYKVQP IKKELYEAVI VKASQLSRRK
HLFSRDRLKL FLKQHCEPHD GVIKMKATSI AKYKLAEQNF SYFFPDAPPT FIFSPASRRR
GRPPKRASTS LDDKITAKQN TQGNKSKVAR EKTRFQKQKE DMQAMAFEKA KLKREKANAI
EAKKKEKEDK EKKREELKKI VEEERMKKKE EKERLKIEKE KEREKLREEK RKYVEYLKQW
SKPREDMECD DLKELPVPVP VKTRLPPEIF GDALMVLEFL YAFGELFDLQ DEFPEGVTLG
KLSFMWQEVL EEALVGNDTE GPLCELLFFF LTAIFQAMAE EEEEVAKDQI ADAETKDLTE
ALDEDADPTK SALSAVATLA AAWPQLHQGC NLKNLDLDSC TLSEILRLHI LASGADVTSA
NAKYRYQKRG GFDATDDACM ELRLSNPGLL KKLSSTSVYD LLPGEKMKIL HALCGKLLTL
VSTRDFIEDS VDVLRQAKQE FRELKAEQHR KEREAAAARI RKRKEERLKE QELKMKEKQE
KLKEEEQRNP AAEVSVGEEE REDLDTSTES KEIERKEQDM DTVTEDEEEL GPNKKRGRGR
RGQNGYKEFT RPEETTCEKS EPLTAEDEEA LKQEQQKKEK ELLEKIQNAT ACTNITPLGR
DRLYRRYWIF PSVPGLFIEE DYSGLTEDML LPRTSSFQNS VQSCTSEPQV FSKTGESLKS
SESTSNIDQD SHTSVVVEVP RPVYKPNRWC FYNSREQLDQ LLEALNSRGH RESALKETLL
QEKSRIYEQL SSFPVEKFHI PDKPQSDIRP PSGRGRMQNA HDGSHVSAEK QLELRLRDFL
LDIEDRIYQG TLGAIKVTDR QSWRAALEHG RYEFLNDENK ENGIIKTVNE ESEEMETDDQ
DKFIVKDRLV GLKTEAPSAA STSTSTPQPV NNVVHYLASA LLQIEQGIER RFLKAPLDAS
DGGRSYKTVL DRWRESLLSS TSLSQVFLHL STLDRSVIWS KSILNARCKV CRKKGDAESM
VLCDGCDRGY HTYCIRPKLK VIPEGDWFCP ECRPKQRSRR LSSRQRPSVE SDEETAEQLG
EGEEEANYDE MGQSEEEHYE EEQDEEDESQ EEEEISPSKQ GRPQVKFPLK MRAAKLNNPF
SSRNSQRQAR YASRSQQNTP KQTEPLSKVT RRGIRKVKSA PPSVTKPCLR LNSRTTRQSQ
SSLQADVFVE LLGPRRRRRG RKNADDTLEN SPSNSLGFRI VDTADSNERL RKYPVSASKL
SLPVTEPKRR GRKRQSTESS PQTSLNRRSS GRQGGVHELS AFEQLVVELV RHDDSWPFMK
LVSKIQVPDY YDIIKKPIAL NIIREKVNKC EYKLASEFIE DIELMFSNCF EYNPRNTSEA
KAGTRLQAFF HIQAQKLGLP ITSGNVDHAA PAAKKSRI
//
