| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G443903_T01 |
| Family | GH89 |
| Protein Properties | Length: 1203 Molecular Weight: 135570 Isoelectric Point: 9.6362 |
| Chromosome | Chromosome/Scaffold: 2 Start: 5005786 End: 5031005 |
| Description | alpha-N-acetylglucosaminidase family / NAGLU family |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH89 | 102 | 349 | 0 |
| PEILILGASGVEISAGFHWYLKHYCAAHISWDKTGGAQLSTIPRPGSLPRVPDGGVLIQRPIDWSYYQNAVTSSYSFAWWDWDRWEKEIDWMALQGINLP LAFTGQESIWQRIFERYNISKSDLDDFFGGPAFLAWSRMANMHGWGGPLPQTWLDDQLVLQKKILSRMYSFGMFPVLPAFSGNIPAALKSKFPSAKVTHL GNWFTVDSNPRWCCTYLLDASDPLFVEIGKMFIEEQIREYGRTSHIYN | |||
| GH89 | 348 | 716 | 0 |
| YNWCMLHNFAADFEMYGVLDALASGPIDARLSDNSTMVGVGMSMEGIEQNPIVYDLMSEMAFHHRQVDLQVWVKTYPTRRYGKPVKGLQDAWWILYRTLY NCTDGKNDKNRDVIVAFPDVEPFVIATPGLHVNTRQMYSTVPSKNYIRKDVSSDAYEHPHLWYDTNAVIHALELFLQHGDEVSDSNTFRYDLVDLTRQVL AKYANDVFLKIIESYKSNNMNQVTILCQHFLSLVNDLDTLLSSHEGFLLGPWLESAKGLARNSEQEIQYEWNARTQITMWFDNTETKASLLRDYANKYWS GLLQDYYGPRAAIYFKHLLLSMENNAPFALKEWRREWISLTNNWQSDRKVFSTTATGDPLNISQSLYTK | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1203 Download |
| MRPRPSRFLQ LLLVVVIACA VPGVRCSDRR FPHLDRVREL QRREGSSSAE QEAAARGLLA 60 RLLPSHSTSF EFRVISTSTE LCGGKTCFVI NNHPLFDGEG TPEILILGAS GVEISAGFHW 120 YLKHYCAAHI SWDKTGGAQL STIPRPGSLP RVPDGGVLIQ RPIDWSYYQN AVTSSYSFAW 180 WDWDRWEKEI DWMALQGINL PLAFTGQESI WQRIFERYNI SKSDLDDFFG GPAFLAWSRM 240 ANMHGWGGPL PQTWLDDQLV LQKKILSRMY SFGMFPVLPA FSGNIPAALK SKFPSAKVTH 300 LGNWFTVDSN PRWCCTYLLD ASDPLFVEIG KMFIEEQIRE YGRTSHIYNW CMLHNFAADF 360 EMYGVLDALA SGPIDARLSD NSTMVGVGMS MEGIEQNPIV YDLMSEMAFH HRQVDLQVWV 420 KTYPTRRYGK PVKGLQDAWW ILYRTLYNCT DGKNDKNRDV IVAFPDVEPF VIATPGLHVN 480 TRQMYSTVPS KNYIRKDVSS DAYEHPHLWY DTNAVIHALE LFLQHGDEVS DSNTFRYDLV 540 DLTRQVLAKY ANDVFLKIIE SYKSNNMNQV TILCQHFLSL VNDLDTLLSS HEGFLLGPWL 600 ESAKGLARNS EQEIQYEWNA RTQITMWFDN TETKASLLRD YANKYWSGLL QDYYGPRAAI 660 YFKHLLLSME NNAPFALKEW RREWISLTNN WQSDRKVFST TATGDPLNIS QSLYTKYLSN 720 ADLLGLVEVG WGSFQLGYSG NADLEPGRCR RTDGKKWRCS RDAVADQKYC ERHMNRGRHR 780 SRKHVEGQPG HAAKAMSAVA VAAAVAALAG AEATAAAGLA VNQHRQPGKS YATVIGKSGA 840 NVRRVEQQTG ARIKVQEIDK DASGERLIIV SSNEIPTEPI SPTIEALILL HDKVAGPPAI 900 ARGALTEIAS RLRTRTLRDT STSGLWNGGN TKNCIYDVSS RGRALARSTE DLARATGSVA 960 ASPSGSTSST SSSPESRATS PFPALDSDPC RTFLHCYLQK GKECRAGSNV VGIYLRFLQL 1020 EYNCYKIGKT KVFLRAGQMA ELAARRAEIL ANAARLIQRR IKTHLMRKEF IKLRKASVQS 1080 QKFWRARLAK KIFEYMRRDV ASIRIQKHVR AHSARKAYLQ VYESATAIQT GLRAMAARNE 1140 HRFRRETRAS IIIQLSRFAL LCLSLFANGF SRKNIMNSSL NHRLGGANTE LMLLTNSNRK 1200 LL* 1260 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd02396 | PCBP_like_KH | 8.0e-9 | 827 | 891 | 65 | + K homology RNA-binding domain, PCBP_like. Members of this group possess KH domains in a tandem arrangement. Most members, similar to the poly(C) binding proteins (PCBPs) and Nova, containing three KH domains, with the first and second domains, which are represented here, in tandem arrangement, followed by a large spacer region, with the third domain near the C-terminal end of the protein. The poly(C) binding proteins (PCBPs) can be divided into two groups, hnRNPs K/J and the alphaCPs, which share a triple KH domain configuration and poly(C) binding specificity. They play roles in mRNA stabilization, translational activation, and translational silencing. Nova-1 and Nova-2 are nuclear RNA-binding proteins that regulate splicing. This group also contains plant proteins that seem to have two tandem repeat arrrangements, like Hen4, a protein that plays a role in AGAMOUS (AG) pre-mRNA processing and important step in plant development. In general, KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. | ||
| pfam12971 | NAGLU_N | 7.0e-17 | 64 | 152 | 89 | + Alpha-N-acetylglucosaminidase (NAGLU) N-terminal domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This N-terminal domain has an alpha-beta fold. | ||
| pfam08879 | WRC | 6.0e-21 | 743 | 787 | 45 | + WRC. The WRC domain, named after the conserved Trp-Arg-Cys motif, contains two distinctive features: a putative nuclear localisation signal and a zinc-finger motif (C3H). It is suggested that the WRC domain functions in DNA binding. | ||
| pfam05089 | NAGLU | 1.0e-95 | 167 | 349 | 183 | + Alpha-N-acetylglucosaminidase (NAGLU) tim-barrel domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This central domain has a tim barrel fold. | ||
| pfam12972 | NAGLU_C | 6.0e-98 | 419 | 717 | 299 | + Alpha-N-acetylglucosaminidase (NAGLU) C-terminal domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This C-terminal domain has an all alpha helical fold. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003723 | RNA binding |
| GO:0005515 | protein binding |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAJ86183.1 | 0 | 3 | 645 | 2 | 687 | H0212B02.15 [Oryza sativa (indica cultivar-group)] |
| GenBank | EEC78143.1 | 0 | 3 | 349 | 2 | 346 | hypothetical protein OsI_17702 [Oryza sativa Indica Group] |
| GenBank | EEC78143.1 | 0 | 325 | 724 | 418 | 813 | hypothetical protein OsI_17702 [Oryza sativa Indica Group] |
| RefSeq | NP_001054095.1 | 0 | 325 | 724 | 120 | 515 | Os04g0650900 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | XP_002465249.1 | 0 | 46 | 720 | 51 | 777 | hypothetical protein SORBIDRAFT_01g034960 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2vcc_A | 5.04467e-44 | 56 | 348 | 175 | 451 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
| PDB | 2vcc_A | 3e-40 | 350 | 707 | 535 | 866 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
| PDB | 2vcb_A | 5.04467e-44 | 56 | 348 | 175 | 451 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
| PDB | 2vcb_A | 3e-40 | 350 | 707 | 535 | 866 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
| PDB | 2vca_A | 5.04467e-44 | 56 | 348 | 175 | 451 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
