ID G1KL88_ANOCA Unreviewed; 1089 AA.
AC G1KL88;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=ATPase family AAA domain containing 2B {ECO:0000313|Ensembl:ENSACAP00000011317.4};
GN Name=ATAD2B {ECO:0000313|Ensembl:ENSACAP00000011317.4};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000011317.4, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000011317.4, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000011317.4,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000011317.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; G1KL88; -.
DR STRING; 28377.ENSACAP00000011317; -.
DR Ensembl; ENSACAT00000011555.4; ENSACAP00000011317.4; ENSACAG00000011448.4.
DR eggNOG; KOG0732; Eukaryota.
DR GeneTree; ENSGT00550000074694; -.
DR HOGENOM; CLU_001448_3_0_1; -.
DR TreeFam; TF314783; -.
DR Proteomes; UP000001646; Chromosome 1.
DR Bgee; ENSACAG00000011448; Expressed in forelimb bud and 12 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd05528; Bromo_AAA; 1.
DR CDD; cd19517; RecA-like_Yta7-like; 1.
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; 2.
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:SF5; ATPASE FAMILY AAA DOMAIN-CONTAINING PROTEIN 2B; 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 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646}.
FT DOMAIN 969..1032
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 936..963
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 80..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..272
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1089 AA; 123259 MW; 34F962672D79B639 CRC64;
MVNTRKSAQS QRLLGKAAGS GPGSHFISSR TRLSRTSAKA AAAAAEAALA AGAAAGQEDD
SARRDDGSDG SLSDSHISPP AKRTLKHADS VCKDKSKSRS TGQREEWSVS TGQSRLNSQS
GATLPNGRSL SLKSCSLRGE KKGDGDHACI NGGREIRKSC RSRKNRFESL NQSLLFDQLV
NSTAEAVLQE MDNINIRRNR RSGEVERLRM WTDTEFENMD MYSRVKRRRK SLRRNSYGIQ
NHHEVSTEGE EEGNDESQEE DGDIEAEEAE GEENDRPYNL RQRKTVERYQ APPIVPAHQK
KRENTLFDIH RSPARRSHIR RKKHAIHSSD TTSSDEERFE RRKSKSMARA RNRCLPMNFR
AEDLASGILR ERVKVGASLA DVDPMILDKS VRFDSIGGLS NHIHALKEMV IFPLLYPEIF
EKFKIQPPRG CLFYGPPGTG KTLVARALAN ECTEGERKVA FFMRKGADCL SKWVGESERQ
LRLLFDQAYL MRPSIIFFDE IDGLAPVRSS RQDQIHSSIV STLLALMDGL DNRGEIVVIG
ATNRLDSIDP ALRRPGRFDR EFLFSLPDQK ARKHILQIHT RSWNPRLSDH FLEELAEKCV
GYCGADIKAL CTEAALIALR RRYPQIYASS QKLQLDVASI VLSAQDFYHA MQNIVPASQR
AVMSSGHALS PIVRPLLERT FNDILAVLRR VFPHAEISQS DKKEDATNLI LDDSEDENAS
SIFEISCPLG SPKKQLSAAI NNKPYLHFTM SAYHQSTSYR PRLLLSGERD SGQTSHLAPA
VLHSLEKIAV HRLDLPALYS VSAKTPEESC AQIFREARRT LPSIVYMPHI GDWWEAVSET
VKATFLTLLQ DIPSFSPIFL LSTSETMYSE LPEEVKCIFK IQYEEVFYIQ RPSEEDRRKF
FEELVLNQAS MPPPRRKQTA LSDLEVLPLA LPSPTHQLSE AEKQRLEDQE ENTLRELRLF
LRDVTKRLAT DKRFNIFSKP VDIEEVSDYL EVIKEPMDLS TIITKIDKHN YLTTKDFLID
IDLICSNALE YNPDKEPGDK IIRHRACTLK DTAHAIIAAE LDPEFNKMCE EIKEARKKRG
IMIYVTDLL
//