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Protein

Hit family protein 1

Gene

HNT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2. Essential for growth on galactose media at elevated temperatures.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei116 – 1161Tele-AMP-histidine intermediate1 Publication

GO - Molecular functioni

  • hydrolase activity Source: SGD
  • identical protein binding Source: IntAct
  • nucleotide binding Source: SGD

GO - Biological processi

  • nucleotide metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29524-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Hit family protein 1 (EC:3.-.-.-)
Alternative name(s):
Adenosine 5'-monophosphoramidase
Gene namesi
Name:HNT1
Synonyms:HIT1
Ordered Locus Names:YDL125C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL125C.
SGDiS000002283. HNT1.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi116 – 1161H → A: Loss of enzymatic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 158158Hit family protein 1PRO_0000109800Add
BLAST

Proteomic databases

MaxQBiQ04344.
PeptideAtlasiQ04344.

Interactioni

Subunit structurei

Interacts with KIN28.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-8416,EBI-8416

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi31938. 20 interactions.
DIPiDIP-2760N.
IntActiQ04344. 4 interactions.
MINTiMINT-484107.

Structurei

3D structure databases

ProteinModelPortaliQ04344.
SMRiQ04344. Positions 21-154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 129104HITPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi114 – 1185Histidine triad motif

Sequence similaritiesi

Contains 1 HIT domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000061063.
InParanoidiQ04344.
OMAiEGHILIL.
OrthoDBiEOG7JQC1B.

Family and domain databases

Gene3Di3.30.428.10. 1 hit.
InterProiIPR019808. Histidine_triad_CS.
IPR001310. Histidine_triad_HIT.
IPR011146. HIT-like.
[Graphical view]
PANTHERiPTHR23089. PTHR23089. 1 hit.
PfamiPF01230. HIT. 1 hit.
[Graphical view]
PRINTSiPR00332. HISTRIAD.
SUPFAMiSSF54197. SSF54197. 1 hit.
PROSITEiPS00892. HIT_1. 1 hit.
PS51084. HIT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04344-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPLISAPYL TTTKMSAPAT LDAACIFCKI IKSEIPSFKL IETKYSYAFL
60 70 80 90 100
DIQPTAEGHA LIIPKYHGAK LHDIPDEFLT DAMPIAKRLA KAMKLDTYNV
110 120 130 140 150
LQNNGKIAHQ EVDHVHFHLI PKRDEKSGLI VGWPAQETDF DKLGKLHKEL

LAKLEGSD
Length:158
Mass (Da):17,680
Last modified:November 1, 1997 - v2
Checksum:i55BCD6CFCF666954
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56956 Genomic DNA. Translation: CAA40275.1.
Z74173 Genomic DNA. Translation: CAA98693.1.
BK006938 Genomic DNA. Translation: DAA11735.1.
PIRiB39977.
RefSeqiNP_010158.1. NM_001180184.1.

Genome annotation databases

EnsemblFungiiYDL125C; YDL125C; YDL125C.
GeneIDi851432.
KEGGisce:YDL125C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56956 Genomic DNA. Translation: CAA40275.1.
Z74173 Genomic DNA. Translation: CAA98693.1.
BK006938 Genomic DNA. Translation: DAA11735.1.
PIRiB39977.
RefSeqiNP_010158.1. NM_001180184.1.

3D structure databases

ProteinModelPortaliQ04344.
SMRiQ04344. Positions 21-154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31938. 20 interactions.
DIPiDIP-2760N.
IntActiQ04344. 4 interactions.
MINTiMINT-484107.

Proteomic databases

MaxQBiQ04344.
PeptideAtlasiQ04344.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL125C; YDL125C; YDL125C.
GeneIDi851432.
KEGGisce:YDL125C.

Organism-specific databases

EuPathDBiFungiDB:YDL125C.
SGDiS000002283. HNT1.

Phylogenomic databases

HOGENOMiHOG000061063.
InParanoidiQ04344.
OMAiEGHILIL.
OrthoDBiEOG7JQC1B.

Enzyme and pathway databases

BioCyciYEAST:G3O-29524-MONOMER.

Miscellaneous databases

NextBioi968657.
PROiQ04344.

Family and domain databases

Gene3Di3.30.428.10. 1 hit.
InterProiIPR019808. Histidine_triad_CS.
IPR001310. Histidine_triad_HIT.
IPR011146. HIT-like.
[Graphical view]
PANTHERiPTHR23089. PTHR23089. 1 hit.
PfamiPF01230. HIT. 1 hit.
[Graphical view]
PRINTSiPR00332. HISTRIAD.
SUPFAMiSSF54197. SSF54197. 1 hit.
PROSITEiPS00892. HIT_1. 1 hit.
PS51084. HIT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast cell cycle protein CDC48p shows full-length homology to the mammalian protein VCP and is a member of a protein family involved in secretion, peroxisome formation, and gene expression."
    Froehlich K.-U., Fries H.W., Ruediger M., Erdmann R., Botstein D., Mecke D.
    J. Cell Biol. 114:443-453(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "The HIT protein family: a new family of proteins present in prokaryotes, yeast and mammals."
    Seraphin B.
    DNA Seq. 3:177-179(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIMILARITY TO OTHER MEMBERS OF THE HIT FAMILY.
  5. "Adenosine monophosphoramidase activity of Hint and Hnt1 supports function of Kin28, Ccl1, and Tfb3."
    Bieganowski P., Garrison P.N., Hodawadekar S.C., Faye G., Barnes L.D., Brenner C.
    J. Biol. Chem. 277:10852-10860(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ACTIVE SITE, MUTAGENESIS OF HIS-116.
  6. "Interactions of Cdk7 and Kin28 with Hint/PKCI-1 and Hnt1 histidine triad proteins."
    Korsisaari N., Makela T.P.
    J. Biol. Chem. 275:34837-34840(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIN28.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHNT1_YEAST
AccessioniPrimary (citable) accession number: Q04344
Secondary accession number(s): D6VRM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: November 1, 1997
Last modified: May 11, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5410 molecules/cell in log phase SD medium.1 Publication

Caution

It is uncertain whether Met-1 or Met-15 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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 one 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.