ID A0A1D1VRG2_RAMVA Unreviewed; 1049 AA.
AC A0A1D1VRG2;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=RvY_13962 {ECO:0000313|EMBL:GAV03561.1};
GN Synonyms=RvY_13962.2 {ECO:0000313|EMBL:GAV03561.1};
GN ORFNames=RvY_13962-2 {ECO:0000313|EMBL:GAV03561.1};
OS Ramazzottius varieornatus (Water bear) (Tardigrade).
OC Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC Hypsibioidea; Ramazzottiidae; Ramazzottius.
OX NCBI_TaxID=947166 {ECO:0000313|EMBL:GAV03561.1, ECO:0000313|Proteomes:UP000186922};
RN [1] {ECO:0000313|EMBL:GAV03561.1, ECO:0000313|Proteomes:UP000186922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YOKOZUNA-1 {ECO:0000313|EMBL:GAV03561.1,
RC ECO:0000313|Proteomes:UP000186922};
RX PubMed=27649274; DOI=10.1038/ncomms12808;
RA Hashimoto T., Horikawa D.D., Saito Y., Kuwahara H., Kozuka-Hata H.,
RA Shin-I T., Minakuchi Y., Ohishi K., Motoyama A., Aizu T., Enomoto A.,
RA Kondo K., Tanaka S., Hara Y., Koshikawa S., Sagara H., Miura T.,
RA Yokobori S., Miyagawa K., Suzuki Y., Kubo T., Oyama M., Kohara Y.,
RA Fujiyama A., Arakawa K., Katayama T., Toyoda A., Kunieda T.;
RT "Extremotolerant tardigrade genome and improved radiotolerance of human
RT cultured cells by tardigrade-unique protein.";
RL Nat. Commun. 7:12808-12808(2016).
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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:GAV03561.1}.
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DR EMBL; BDGG01000009; GAV03561.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D1VRG2; -.
DR STRING; 947166.A0A1D1VRG2; -.
DR Proteomes; UP000186922; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR048589; SAMD1-like_WH.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF102; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF21524; SAMD1_WH; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000186922};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 708..998
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1039
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 895
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1049 AA; 116718 MW; D86596A8F1FEFF69 CRC64;
MTLTDRESSS SPSEASSEAG SSTSSETSNP SNPAVSDSDQ DDVVDPVCLE WFKDVIKKIK
GQKQRPGLDR MTQALKPYIT GTKYDSQSIK KQLALAIRDG HLFKVYSNGE PSYKDTQNLR
SLRKLVIKKE ADLKRAAKAA VREIGEKDGT DPETIERYIK YTFEVKLEAE TLKSGIAKAL
HHLTTSKSKD LIEQDGRYKH NPKSDTKADE EEDDAEGSRP RSSLSATPRL KDNSEEIPLP
TAIAKTKSKS KMTKSAEAAD LPAKQLSTPA ALSGSKRSSA SASPSKTTTP DTPLKRADLL
PAERHKSSTP KLDNSLKRKK SQSPEKKSDK LLTPSSSKPP KISPEVKEKA KASQPTLPLK
SQEATAVPVV EKKKRGRPPL KKKAELAALE ASAAGAKSKS AEKAKEEVKG KSQEESSGDS
QADEKTAAIF PDADFDDRVP KELRDGLSSY FSLSTVKRKS RVAYNSLVTA VVPPTKDGDI
SQDNEPKPST SRQKSPPASR QSLPSTSKSP SAPTVWRKKL PSISGQRAPP DGRAKSPEDK
PSTSREKADW DTLTDSGSDA RVKSESQEGA ADGIKKKKGK KPGSYQLKGL SDQLSKYFTA
PPGARQRKPP AHYTPIADKY PKQKVRKAAE STTASDRSES RSGKVSDDGR TSKSTSKTKD
MSERSIRVDS PGKEGFRIPD VVPKHFEDLF RQARMKALEK IPTVSADYEG SLPPKIQLGN
KKIVTWYTSP FPEEYIRCQC LYLCEFCLQY MKTVKVLKSH YEKCPWHRPP GTEIYHDVVE
GEDGEGRRQE LVLYETDGNE WKEYCQNLCL LAKLYLDHKT LYYDVEPFLF YVLTSRDKFG
DHLIGYFSKE KNCPQRYNVS CIMVLPPYQG GGYGRFLIDF SYLLSRVEGQ HGTPEKPLSE
LGQISYHAYW RSAILDFFLE QRQKSSTKTS IKAICDATGM WPQDVADILQ QLNFLVKKED
SNAWEFSLVP DVLDAYFERK NSAKKRLPLH ADKLNWDPWR GEGMGLTSGE SDHGESQTDM
QLDTHDEAKD GHRSRDTSQS DTSQGRWLT
//
