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Protein

Histone acetyltransferase type B catalytic subunit

Gene

hat-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.By similarity

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei178 – 1781Interaction with histone H4 N-terminusBy similarity
Active sitei284 – 2841Proton donor/acceptorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Chromatin regulator, Transferase

Keywords - Biological processi

DNA damage, DNA repair

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase type B catalytic subunit (EC:2.3.1.48By similarity)
Gene namesi
Name:hat-1
ORF Names:NCU06472
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805 Componenti: Chromosome 3, Linkage Group III

Organism-specific databases

EuPathDBiFungiDB:NCU06472.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 508508Histone acetyltransferase type B catalytic subunitPRO_0000227726Add
BLAST

Interactioni

Subunit structurei

Component of the HAT-B complex composed of at least hat-1 and hat-2. The HAT-B complex binds to histone H4 tail.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ7RYU8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni44 – 463Interaction with histone H4 N-terminusBy similarity
Regioni207 – 2093Interaction with histone H4 N-terminusBy similarity
Regioni249 – 2513Acetyl-CoA bindingBy similarity
Regioni256 – 2627Acetyl-CoA bindingBy similarity

Sequence similaritiesi

Belongs to the HAT1 family.Curated

Phylogenomic databases

eggNOGiNOG326277.
HOGENOMiHOG000164382.
InParanoidiQ7RYU8.
KOiK11303.
OMAiHISYDEK.
OrthoDBiEOG7HTHSD.

Family and domain databases

Gene3Di1.10.10.390. 1 hit.
3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
IPR013523. Hist_AcTrfase_HAT1_C.
[Graphical view]
PANTHERiPTHR12046. PTHR12046. 1 hit.
PfamiPF10394. Hat1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF038084. HAT-B_cat. 1 hit.
SUPFAMiSSF55729. SSF55729. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7RYU8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGDDDWWTS SNEALLVSLV TPSDTGVKTL DTFHPEYTNN IFGEKEQIFG
60 70 80 90 100
YKGLRINLQY NASDMLPNLK VSYKKKYQPT ADEEALDINE VLSEFLPEIA
110 120 130 140 150
FQKQSDFETR LKSIPDNWTP PGTLVTSFTN KDGEYEVYSG KITDPAVKQL
160 170 180 190 200
LNRIQILVPF FVDGGTPIDM EDPDVDRWTI YFLYNKRPLL NQPDKFSYHF
210 220 230 240 250
AGYSTLYRYY AFQPPAESES KTPTDTPTFS VDGDFDLDTL PCRTRISQFI
260 270 280 290 300
IIPPFQQKGL GSRLYSIIYQ QYLKHEPTIE LTVEDPNEAF DDMRDLADLA
310 320 330 340 350
FLSKQPEFQA LKIDTSVEIP EEGKAPSNIV DQAAWEACRK KFKIVPRQFA
360 370 380 390 400
RVLEMYLMSQ LPESVRPGLG APEDEDYEEQ SGRSKSKGHE KALPKPTPED
410 420 430 440 450
EHTYRLWMML VKRRLYVHNR DALGQLELKE RREELAKVFA GVEFDYARLL
460 470 480 490 500
IKAEEQGKLA QADGETAGDQ VPATPSAANG KRKLDEVEQA EGTAAASSKK

AKVESGHA
Length:508
Mass (Da):57,696
Last modified:December 15, 2003 - v1
Checksum:iD2DCF7829D6855D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM002238 Genomic DNA. Translation: EAA28127.1.
RefSeqiXP_957363.1. XM_952270.3.

Genome annotation databases

EnsemblFungiiEFNCRT00000006218; EFNCRP00000006210; EFNCRG00000006207.
GeneIDi3873462.
KEGGincr:NCU06472.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM002238 Genomic DNA. Translation: EAA28127.1.
RefSeqiXP_957363.1. XM_952270.3.

3D structure databases

ProteinModelPortaliQ7RYU8.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFNCRT00000006218; EFNCRP00000006210; EFNCRG00000006207.
GeneIDi3873462.
KEGGincr:NCU06472.

Organism-specific databases

EuPathDBiFungiDB:NCU06472.

Phylogenomic databases

eggNOGiNOG326277.
HOGENOMiHOG000164382.
InParanoidiQ7RYU8.
KOiK11303.
OMAiHISYDEK.
OrthoDBiEOG7HTHSD.

Family and domain databases

Gene3Di1.10.10.390. 1 hit.
3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
IPR013523. Hist_AcTrfase_HAT1_C.
[Graphical view]
PANTHERiPTHR12046. PTHR12046. 1 hit.
PfamiPF10394. Hat1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF038084. HAT-B_cat. 1 hit.
SUPFAMiSSF55729. SSF55729. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of the filamentous fungus Neurospora crassa."
    Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
    , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
    Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Entry informationi

Entry nameiHAT1_NEUCR
AccessioniPrimary (citable) accession number: Q7RYU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: December 15, 2003
Last modified: July 22, 2015
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.