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Q2U2I3

- MANF_ASPOR

UniProt

Q2U2I3 - MANF_ASPOR

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Protein

Probable mannan endo-1,4-beta-mannosidase F

Gene
manF, AO090038000444
Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans By similarity.

Catalytic activityi

Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei196 – 1961Proton donor By similarity
Active sitei305 – 3051Nucleophile By similarity

GO - Molecular functioni

  1. cellulose binding Source: InterPro
  2. mannan endo-1,4-beta-mannosidase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Probable mannan endo-1,4-beta-mannosidase F (EC:3.2.1.78)
Alternative name(s):
Endo-beta-1,4-mannanase F
Gene namesi
Name:manF
ORF Names:AO090038000444
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564: Chromosome 6

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed predictionAdd
BLAST
Chaini19 – 463445Probable mannan endo-1,4-beta-mannosidase FPRO_0000393716Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi87 – 871N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ2U2I3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 5436CBM1Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni75 – 11844Ser-rich linkerAdd
BLAST
Regioni119 – 463345CatalyticrAdd
BLAST

Domaini

Has a modular structure: a carbohydrate-binding module (CBM) at the N-terminus, a linker rich in serines, and a C-terminal endo-1,4-mannanase catalytic module. The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3934.
HOGENOMiHOG000169951.
OMAiEKNLAIP.
OrthoDBiEOG7M3J90.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q2U2I3-1 [UniParc]FASTAAdd to Basket

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MRSLSSIALL SVVGAASAQA GPWAQCGGKS FSGSSECASG WKCQELNEWF    50
SQCVPGAEST TPTVSSTPTP TDAPSVSITA SVTTGINKSI SVSSASKSTP 100
LPSSSSASPS PRPTGSGSFA KADGLQFSID GETKYFAGTN AYWLPFQMND 150
ADIDSVFDHL EQAGLKILRV WGFNDVNTAP SPGTVYFQLH DKEKGTSTIN 200
TGKDGLQRLD YVVAAAEKHG VKLIIPFVNS WDDYGGYNAY VKAYGGSKTE 250
WFTNEKIQSV YQAYIKAVVS RYRDSPAIFA WELGNEPRCS GCSTDVIHGW 300
ATKISAYIKS LDPNHMVALG DEGMGLTIGS DQSYPYGTSE GNDFEKNLAI 350
PDIDFGTLHL YTTDWGIKDN AWGNGWVENH AKACKAAGKP CLFEEYGMKG 400
NHCTDELKWQ KTSLSSGTAA DLIWQYGQQL STGESPKDAY SIFYGTDEWK 450
CAVMDHMENV NKN 463
Length:463
Mass (Da):49,992
Last modified:April 20, 2010 - v2
Checksum:i8926BA2E033A383B
GO

Sequence cautioni

The sequence BAE64232.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP007169 Genomic DNA. Translation: BAE64232.1. Sequence problems.
RefSeqiXP_001825365.2. XM_001825313.2.

Genome annotation databases

GeneIDi5997460.
KEGGiaor:AOR_1_742074.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP007169 Genomic DNA. Translation: BAE64232.1 . Sequence problems.
RefSeqi XP_001825365.2. XM_001825313.2.

3D structure databases

ProteinModelPortali Q2U2I3.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5997460.
KEGGi aor:AOR_1_742074.

Phylogenomic databases

eggNOGi COG3934.
HOGENOMi HOG000169951.
OMAi EKNLAIP.
OrthoDBi EOG7M3J90.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR000254. Cellulose-bd_dom_fun.
IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00734. CBM_1. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view ]
SMARTi SM00236. fCBD. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEi PS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiMANF_ASPOR
AccessioniPrimary (citable) accession number: Q2U2I3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 20, 2010
Last modified: May 14, 2014
This is version 52 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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