ID A0A452HW23_9SAUR Unreviewed; 1658 AA.
AC A0A452HW23;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000019317.1};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000019317.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000019317.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR Ensembl; ENSGAGT00000022001.1; ENSGAGP00000019317.1; ENSGAGG00000014257.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0016586; C:RSC-type complex; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR CDD; cd04717; BAH_polybromo; 2.
DR CDD; cd05524; Bromo_polybromo_I; 1.
DR CDD; cd05517; Bromo_polybromo_II; 1.
DR CDD; cd05520; Bromo_polybromo_III; 1.
DR CDD; cd05515; Bromo_polybromo_V; 1.
DR CDD; cd05526; Bromo_polybromo_VI; 1.
DR CDD; cd21984; HMG-box_PB1; 1.
DR Gene3D; 2.30.30.490; -; 2.
DR Gene3D; 1.20.920.10; Bromodomain-like; 6.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR037968; PBRM1_BD5.
DR InterPro; IPR037382; Rsc/polybromo.
DR PANTHER; PTHR16062:SF19; PROTEIN POLYBROMO-1; 1.
DR PANTHER; PTHR16062; SWI/SNF-RELATED; 1.
DR Pfam; PF01426; BAH; 2.
DR Pfam; PF00439; Bromodomain; 6.
DR Pfam; PF00505; HMG_box; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00439; BAH; 2.
DR SMART; SM00297; BROMO; 6.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47370; Bromodomain; 6.
DR SUPFAM; SSF47095; HMG-box; 1.
DR PROSITE; PS51038; BAH; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 5.
DR PROSITE; PS50014; BROMODOMAIN_2; 6.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020}.
FT DOMAIN 82..152
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 218..288
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 420..490
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 558..628
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 696..766
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 837..882
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 976..1094
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1177..1293
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1400..1468
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 1400..1468
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 17..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1452..1482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1518..1570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1544..1560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1658 AA; 190337 MW; FE9A8734BABCE00A CRC64;
MRRLAFRGAG CTLKLDSMGS KRRRATSPSS SISGGDFDDG HHSTNIPGPS RKRRRLSNLP
TVDPIAVCHE LYNTIRDYKD EQGRLLCELF IRAPKRRNQP DYYEVVSQPI DLMKIQQKLK
MEEYDDVNLL TADFQLLFNN AKAYYKPDSP EYKAACKLWD LYMRTKNEFV QKGDAEEEEE
EDEGHDNQGA ISEVSSPSYL KEILEQLLEA VAIATNPSGR LISELFQKLP SKVQYPDYYA
IIKEPIDLKT IAQRIQNGSY KSIHAMAKDI DLLAKNAKTY NEPGSQVFKD ANAIKKTFNM
KKAEIEHNEL AKSSLRIRTP SNLAASKLTG PSSQGKGSVG DERNSTNKYY RNKRSVQGDR
LSAITMALQY GSESDEDAAL AAAARYEEGE SEAESITSFM DTSNPLYQLY DTVRNCRNNQ
GQLISEPFFH LPSKKKYPDY YQQIKMPVSL KQIRTKLKNH EYETLDHLEC DLNLMFENAK
RYNVPNSAIY KRVLKMQQVM QAKKKELARR DDIEDGDSMI SSATSDTGSS KRKSKKNIKK
QRMKILYNVV LEAREPGTGR RLCDLFMVKP SKKDYPDYYK IILEPMDLKI IEHNIRSDKY
SGEEAMIEDM RLMFRNARHY NEEGSQVYND AHILEKILKE KKKELGPLPE DDDIASPKLK
LSRKSGISPK KSKYMTPMQQ KLNEVYEAVK NYTDKRGRRL SAIFLRLPSR SELPDYYVTI
KKPVDMEKIR SHMMANKYQD IDSMVEDFVM MFNNACTYNE PESLIYKDAL VLHKVLLETR
RDIEGDEDSH VPNVTLLIQE LIHNLFVSVM SHQDDEGRCY SDSLAEIPAV DPNFPNKPPL
TFDIIRKNVE NNRYRRLDLF QEQMFEMLER ARRMNRTDSE IYEDAVELQQ FFIKIRDELC
KNGEILLSPA LSYTTKHLHN DVEKEKKEKL PKEFEEDKLK REEEKREAEK SEDSAGGAGL
SSLHRTYSQD CSFKNSMYHV GDYVYVEPAE ANLQPHIVCI ERLWEDSAGE KWLYGCWFYR
PNETFHLATR KFLEKEVFKS DYYNKVPVSK ILGKCVVMFV KEYFKLCPEN FRDEDVYVCE
SRYSAKTKSF KKIKLWTMPI SSVRFVPRDV PLPVVRVASV FAKTDKVEDE KHTETLEDNK
VGDSILNLEK EKEDVPVEMS NGEPGCHYFE QLRYNDMWLK VGDCVFIKSH GLVRPRVGRI
EKMWVRDGAA YFFGPIFIHP EETEHEPTKM FYKKEVFLSN LEETCPMTCI LGKCAVLSFK
DFLSCRPTEI SENDVLLCES RYIESDKQMK KFKGLKRFSL SAKVVDDEIY YFRKPIVPQK
EPSPLLEKKI QQLEAKFAEL EGGDEDIEEM AEEEGEIIEA PSMPQLQTPL ASELDIMPYT
PPQSTPKSAK GSTKKEGSKR KINMSGYILF SSEMRAVIKA QHPDYSFGEL SRLVGTEWRN
LEATKKAEYE ERAAKVAEQQ ERERAAQQQQ QNSSPRAGTP VGALMGVVPP PTPMGMLNQQ
LTPVAGVIGQ SVSSMVGTPA PGGSPFGQPM GLLGPPGQQA PPPYPGQSQA SQQVIQQPTT
PMFVSPPPKT QRLLHSDAYL KYIEGLSAES NSISKWDQTL SARRRDVHLS KEQESRLPSH
WLKSKGAHTT MADALWRLRD LMLRDTLNIR QAYNIENV
//
