ID A0A0V1M594_9BILA Unreviewed; 1373 AA.
AC A0A0V1M594;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Bromodomain adjacent to zinc finger domain protein 1A {ECO:0000313|EMBL:KRZ67028.1};
DE Flags: Fragment;
GN Name=Baz1a {ECO:0000313|EMBL:KRZ67028.1};
GN ORFNames=T10_834 {ECO:0000313|EMBL:KRZ67028.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ67028.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ67028.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ67028.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00475}.
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:KRZ67028.1}.
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; JYDO01000213; KRZ67026.1; -; Genomic_DNA.
DR EMBL; JYDO01000213; KRZ67028.1; -; Genomic_DNA.
DR Proteomes; UP000054843; 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; cd15489; PHD_SF; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
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; 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; 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; PF10537; WAC_Acf1_DNA_bd; 1.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
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; 2.
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:UP000054843};
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:PRU00146}.
FT DOMAIN 25..133
FT /note="WAC"
FT /evidence="ECO:0000259|PROSITE:PS51136"
FT DOMAIN 401..466
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1025..1077
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1127..1178
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1268..1338
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 149..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 338..365
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1103..1118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ67028.1"
SQ SEQUENCE 1373 AA; 157460 MW; ADA38060D4B44F5A CRC64;
LLSMPLLQGE PLRFVPRPAD LHPDEKVFYC PCTKEVFREF EQYFKRTMIL NSLVWTCAAT
GDEGLTYEAA LKSEHAVCAP PDNIAEELVK AILFLVKLTA KVRLCDVVGM IHSFISTHVF
VGETAHFVDN AGNRRTGVVR SVTVPETVNK SDDNLETPSS PSENANKLNG SKNLIGAKGS
AAVYVVEFSI DDAANESLTG NTLLCCVDES KVFRKRPLSK EECYALLRAY CCTSQENIWV
VKDDIAERHE VSKLEWDKIY GGPLPDLSIY KSCNEQAPSE SDESEDDAED LGEEFAHGGK
HNKALTLMWT EVEKYQVDIG AELKERISKG FAVTEMDIRN IRALIKKAKQ QCRIQKRENR
KRQRKNNPKC RKVRDDLLFN DDDQAEFPTL AAVNFPKHVS PARFGDYLSL LDFLHQHGNR
IQLRDYFPDG VTLSMLYKAT LDCSPEGIFA ELLCYLLTVL FERQCEEDGD DVKILKSEEI
AMLDSAEIEY KFYLPKMEKA TEMFKEMRNT HGVSVYRLPV DGYTLSEVVR IYFQSSGHFT
GCRNGRFRNL HRGSFKSYDD QAFNFSIKRP ELIESLRRVS VYELKPDDRL DLLLVLRDQL
LTFQLFRDLL DTSSERVRSI RLDLLRQKVP NGSVEREMIC FLKSTLRCGE RSRAGSKQQQ
QQQIDGVDEQ QHQLNSLLRK FQSFVDRPLS DDLDLSDFVE PLTSVRLDEL ESVEQIELVR
KLRRHLFNQL YRSALFDLFE LQSTIGMTLL GQDRSYRRYY FVRSVGAVLV ENVFELDFDN
AERCSDRVVV VAAAASFEQQ PLVPRWQMLR DLDTLNALLN SLNRRGEREA ELAANLLLFK
GQLVQMFASF DDTLNNAEAE PLLELELEPV DSKLLIERSF RLSLLDFENR LFYSRMQTAP
IADRQRWREQ LEGEQQRLEV KHLAQILIDL VNTIDCKFME NFSTRPVKKF HCTTAATTTS
SSSSASADDS VQCNSVVDGQ STDSEKTTCL NLWKQSLDSC FSYSSLHLHL LTLDKQLTWQ
KSILNMRCRK CRRKGDMNNL AICSDCGRAV HLGCSKPCLQ TLPTEDDGWI CFLCKKQQNW
NAKKAAIVEE EAFDEEEEEA TTAEAEERSH QKQEQEKLKV QQKSETYSIC SNCTTVIRHI
KQRIHCSSCT LSFHTRCVGV KKSEIAVASW LCKNCNPKIS NGINGKNLQM KLSRSGRPLR
GYISPVASSF IGSPNGIIAQ PDSCDSNGLT QKRKAKNNGR LKKRTINKRR AEQSDVETRC
NTCISRLVEH PDAWPFLKPV SRREAPDYYD IIEQPMDLRT IQMRLLRHEY SSVSEMVRDA
QLMFSNCRQY NEAETEVYAC GERLSKFCQQ QLEHLKLRDH EKLNVRKRRR AAF
//
