GenomeNet

Database: UniProt
Entry: A0A016WGY8_9BILA
LinkDB: A0A016WGY8_9BILA
Original site: A0A016WGY8_9BILA 
ID   A0A016WGY8_9BILA        Unreviewed;      1198 AA.
AC   A0A016WGY8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Bromo domain-containing protein {ECO:0000259|PROSITE:PS50014};
GN   Name=Acey_s0727.g1881 {ECO:0000313|EMBL:EYC38293.1};
GN   Synonyms=Acey-lex-1 {ECO:0000313|EMBL:EYC38293.1};
GN   ORFNames=Y032_0727g1881 {ECO:0000313|EMBL:EYC38293.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC38293.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914}.
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:EYC38293.1}.
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; JARK01000327; EYC38293.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016WGY8; -.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR045199; ATAD2-like.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23069; AAA DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR23069:SF0; TAT-BINDING HOMOLOG 7; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00297; BROMO; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00674; AAA; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
PE   3: Inferred from homology;
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Reference proteome {ECO:0000313|Proteomes:UP000024635}.
FT   DOMAIN          880..950
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          85..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1084..1108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..140
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..255
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1084..1103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1198 AA;  135929 MW;  0ACBF66D8D7BBE58 CRC64;
     MVYRSLAEND LAEHHLRGSF MKSIIRSATE QLHKELISGQ PVAGYTRSGR RIAGGIHYEE
     SDSTDEDDYE KRRRRRRFAK ERYNDENVDI RSPSPKRCSV KRRGAVEDEE DHEKEQKQED
     SEQHEDPHSN MYDNIKRERK TVTTSLPNSP RLTNGTESSR SLRQANRERL SNGVAKEEPV
     VEVEGSRSSE ETEEDDEKTP EPRQYSLRKI RQPVDRFAST VTPRERHRED RERRSRGRST
     DRRDRKAKRA AKRRRRELRS DSSSTSSSDS DDIIRTRNDD LRFERRKERS LAKARNRYLP
     INLSDKDLSA SQAVIRERLR QTGGSCTDID PMSIDSGIGF EQVGGLGSHI QSLKEVVLFP
     MLYPEIFKQF NIMPPKGVVF YGPPGTGKTL MARALANECS KGGKKVAFFM RKGADCLSKW
     VGEAERQLRV LFDQAYAMRP SIIFFDEIDG LAPVRSSKQD QIHSSIVSTL LALMDGLDNR
     GEVVVIGATN RLDTLDPALR RPGRFDRELK FSLPDANARM QILTIHTSKW GDSQPDEETL
     RWLADGTSGY CGADLQYLCT EAVLVALRSR FPHIYMSKER LKLDPSDLVI DKNCFTTAMR
     RITPASRRDL SIPSRQLDER TSILLLSTVT SILNIRIPTG YRSSQSVQNT AATELEKVVR
     ALEQPPCVPA VRLMLCGSEE HPDLGQTSYV LPAVLGKLDH LPVFSIAVAR LFADGRPEET
     LAQTVQSALR AAASGPCILL LPSIDQWYEV VPPSVAHMLA TALDSLHGFT SILFLASCDC
     AYDSCCNEVK DLFGPSQCLS LRPPKEQHRR RYFEHILASA RIPPKVFDPS LYQEPEKAGD
     EVATTSRKLN EKEARELVKI YESQLRRFRI WARDKLSALR RDRRFTIFVK PVDSEDVEDY
     YDVIKNPMCI SEMEEKIDRQ EYLHPDHLLS DIRLIRDNAI EYNPVNTEEG RVIRHNAHAL
     WETVVDLFDV DLDVDFVESL ENNAKMLADA GVQPTNEKLL ELPPGFKRTV PWSVNAGYMT
     QLVKESAKEA NGEKREAQTS AVTNNVQRVK FRNHRRNRGG YAFPNSAKKK KTAAIVKSLK
     RSLANSVDES SGSQTSQAGS EEESVENGDC MEIEAEKQKS PQTKKKLILP EDKINELVNT
     CVHRSNGWSV SELERLAAVL AHDIEEFRDK WDRSSLPSKL LATVNSWQVN SGRVFASV
//
DBGET integrated database retrieval system