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A2FNR0

- A2FNR0_TRIVA

UniProt

A2FNR0 - A2FNR0_TRIVA

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Protein

Alpha-amylase

Gene

TVAG_347480

Organism
Trichomonas vaginalis
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.UniRule annotation

GO - Molecular functioni

  1. alpha-amylase activity Source: UniProtKB-EC
  2. cation binding Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Keywords - Biological processi

Carbohydrate metabolismUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylaseUniRule annotation (EC:3.2.1.1UniRule annotation)
Gene namesi
ORF Names:TVAG_347480Imported
OrganismiTrichomonas vaginalisImported
Taxonomic identifieri5722 [NCBI]
Taxonomic lineageiEukaryotaParabasaliaTrichomonadidaTrichomonadidaeTrichomonas
ProteomesiUP000001542: Unassembled WGS genome

Organism-specific databases

EuPathDBiTrichDB:TVAG_347480.

Interactioni

Protein-protein interaction databases

STRINGi5722.A2FNR0.

Structurei

3D structure databases

ProteinModelPortaliA2FNR0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0366.
InParanoidiA2FNR0.
KOiK01176.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SUPFAMiSSF51445. SSF51445. 2 hits.

Sequencei

Sequence statusi: Complete.

A2FNR0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKELADNPLL DSQDELESVE RESEVPFYKK NYFIYGTMIC NSILIGAIIS
60 70 80 90 100
MIITFSVNSK VSSISNQYDT LPNCESYSSF TCNGSSSSMD YKYYNNTWNT
110 120 130 140 150
PKRGQDLWKP GFQDMSTLVG YAQLKYASGM KSCTVNILTK TSTSLNLTYY
160 170 180 190 200
FDDVAQTSNS KTFDSSYTKT LSVKVVAESG ETLILDGVDF IWNVASIKSR
210 220 230 240 250
DYDYRKGQKG AIVELFGWPD DDVAQECKFI ADAGYMGVKI FPHQEQIMSY
260 270 280 290 300
QPMENMMNPW YFMYQPVSYR LQGRMGTRDQ LRTMINTCRA LGVRVYADAV
310 320 330 340 350
VNHMSGNGND LSNHRNSGSG CTTWGNKTSS AYENGSPYYT PAYTYETNPN
360 370 380 390 400
TGRGTNVLEY PGVPYGPEDF HCDKALNSWN DANILDSGWL SGLADLDTSK
410 420 430 440 450
EYVRQRIADF MIDLISIGFS GYRVDAAKHI RPTDLAAIFG KVKEGLGGSL
460 470 480 490 500
PDDFISWLEV LTGGESQLLV QGDGDYSFTG GLTKYLKANN FTDDDVLKIK
510 520 530 540 550
IWWSGYPSEP NNDNGSLDIR RKAIQNDDHD QQSDGSSSRD MHDQGCVLIK
560 570 580
GCDASTHRSF EVKLFESPNG LSNQNGPFII L
Length:581
Mass (Da):64,940
Last modified:February 20, 2007 - v1
Checksum:i27E0D5896D09CE28
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS113911 Genomic DNA. Translation: EAX93461.1.
RefSeqiXP_001306391.1. XM_001306390.1.

Genome annotation databases

GeneIDi4751179.
KEGGitva:TVAG_347480.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS113911 Genomic DNA. Translation: EAX93461.1 .
RefSeqi XP_001306391.1. XM_001306390.1.

3D structure databases

ProteinModelPortali A2FNR0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5722.A2FNR0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 4751179.
KEGGi tva:TVAG_347480.

Organism-specific databases

EuPathDBi TrichDB:TVAG_347480.

Phylogenomic databases

eggNOGi COG0366.
InParanoidi A2FNR0.
KOi K01176.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
[Graphical view ]
PRINTSi PR00110. ALPHAAMYLASE.
SUPFAMi SSF51445. SSF51445. 2 hits.
ProtoNeti Search...

Publicationsi

  1. "Draft genome sequence of the sexually transmitted pathogen Trichomonas vaginalis."
    Carlton J.M., Hirt R.P., Silva J.C., Delcher A.L., Schatz M., Zhao Q., Wortman J.R., Bidwell S.L., Alsmark U.C.M., Besteiro S., Sicheritz-Ponten T., Noel C.J., Dacks J.B., Foster P.G., Simillion C., Van de Peer Y., Miranda-Saavedra D., Barton G.J.
    , Westrop G.D., Mueller S., Dessi D., Fiori P.L., Ren Q., Paulsen I., Zhang H., Bastida-Corcuera F.D., Simoes-Barbosa A., Brown M.T., Hayes R.D., Mukherjee M., Okumura C.Y., Schneider R., Smith A.J., Vanacova S., Villalvazo M., Haas B.J., Pertea M., Feldblyum T.V., Utterback T.R., Shu C.L., Osoegawa K., de Jong P.J., Hrdy I., Horvathova L., Zubacova Z., Dolezal P., Malik S.B., Logsdon J.M. Jr., Henze K., Gupta A., Wang C.C., Dunne R.L., Upcroft J.A., Upcroft P., White O., Salzberg S.L., Tang P., Chiu C.-H., Lee Y.-S., Embley T.M., Coombs G.H., Mottram J.C., Tachezy J., Fraser-Liggett C.M., Johnson P.J.
    Science 315:207-212(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC PRA-98 / G3Imported.

Entry informationi

Entry nameiA2FNR0_TRIVA
AccessioniPrimary (citable) accession number: A2FNR0
Entry historyi
Integrated into UniProtKB/TrEMBL: February 20, 2007
Last sequence update: February 20, 2007
Last modified: October 29, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3