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Conserved domains on  [gi|2462631184|ref|XP_054183879|]
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putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 isoform X23 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tudor_TDRD13 cd20447
Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called ...
 3-82 5.54e-50

Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called asparagine-linked glycosylation 13 (ALG13), glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13, is a putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase (EC 2.4.1.141/EC 3.4.19.12). It is a potential member of the Alg7p/Alg13p/Alg14p complex catalyzing the first two initial reactions in the N-glycosylation process. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


:

Pssm-ID: 410518  Cd Length: 80  Bit Score: 168.49  E-value: 5.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631184   3 YAGRQYYLGDKCQVCLESEGRYYNAHIQEVGNENNSVTVFIEELAEKHVVPLANLKPVTQVMSVPAWNAMPSRKGRGYQK 82
Cdd:cd20447     1 FAGRQYYLGDKCQVRLEPGGKYYNAHIQEVGQDSNSVTVFIEELAEKHTVPLANLKPVTQVTPVPAWNMMPNRKGGNYQK 80
 
Name Accession Description Interval E-value
Tudor_TDRD13 cd20447
Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called ...
 3-82 5.54e-50

Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called asparagine-linked glycosylation 13 (ALG13), glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13, is a putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase (EC 2.4.1.141/EC 3.4.19.12). It is a potential member of the Alg7p/Alg13p/Alg14p complex catalyzing the first two initial reactions in the N-glycosylation process. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410518  Cd Length: 80  Bit Score: 168.49  E-value: 5.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631184   3 YAGRQYYLGDKCQVCLESEGRYYNAHIQEVGNENNSVTVFIEELAEKHVVPLANLKPVTQVMSVPAWNAMPSRKGRGYQK 82
Cdd:cd20447     1 FAGRQYYLGDKCQVRLEPGGKYYNAHIQEVGQDSNSVTVFIEELAEKHTVPLANLKPVTQVTPVPAWNMMPNRKGGNYQK 80
 
Name Accession Description Interval E-value
Tudor_TDRD13 cd20447
Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called ...
 3-82 5.54e-50

Tudor domain found in Tudor domain-containing protein 13 (TDRD13); TDRD13, also called asparagine-linked glycosylation 13 (ALG13), glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13, is a putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase (EC 2.4.1.141/EC 3.4.19.12). It is a potential member of the Alg7p/Alg13p/Alg14p complex catalyzing the first two initial reactions in the N-glycosylation process. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410518  Cd Length: 80  Bit Score: 168.49  E-value: 5.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631184   3 YAGRQYYLGDKCQVCLESEGRYYNAHIQEVGNENNSVTVFIEELAEKHVVPLANLKPVTQVMSVPAWNAMPSRKGRGYQK 82
Cdd:cd20447     1 FAGRQYYLGDKCQVRLEPGGKYYNAHIQEVGQDSNSVTVFIEELAEKHTVPLANLKPVTQVTPVPAWNMMPNRKGGNYQK 80
Tudor_TDRD13-like cd20380
Tudor domain found in Tudor domain-containing protein 13 (TDRD13) and similar proteins; The ...
 7-60 2.06e-22

Tudor domain found in Tudor domain-containing protein 13 (TDRD13) and similar proteins; The TDRD13 family includes TDRD13 and OTU domain-containing protein 4 (OTUD4). TDRD13, also called asparagine-linked glycosylation 13 (ALG13), glycosyltransferase 28 domain-containing protein 1 (GLT28D1), or UDP-N-acetylglucosamine transferase subunit ALG13, is a putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase (EC 2.4.1.141/EC 3.4.19.12). It is a potential member of the Alg7p/Alg13p/Alg14p complex catalyzing the first two initial reactions in the N-glycosylation process. OTUD4, also called HIV-1-induced protein HIN-1, is a phospho-activated K63 deubiquitinase that hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein. It may negatively regulate inflammatory and pathogen recognition signaling in innate immune response. Members of this family contain one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410451  Cd Length: 54  Bit Score: 90.72  E-value: 2.06e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462631184   7 QYYLGDKCQVCLESEGRYYNAHIQEVGNENNSVTVFIEELAEKHVVPLANLKPV 60
Cdd:cd20380     1 QFKPGDKCQVELDSPGKVYEAHIQEISPDKGPVTVFVEELGEKKTVPYENLKPL 54
Tudor_OTUD4 cd20448
Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called ...
 4-62 5.27e-22

Tudor domain found in OTU domain-containing protein 4 (OTUD4); OTUD4, also called HIV-1-induced protein HIN-1, is a phospho-activated K63 deubiquitinase that hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein. It may negatively regulate inflammatory and pathogen recognition signaling in innate immune response. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410519  Cd Length: 64  Bit Score: 89.94  E-value: 5.27e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462631184   4 AGRQYYLGDKCQVCLESEGRYYNAHIQEVGNENNSVTVFIEELAEKHVVPLANLKPVTQ 62
Cdd:cd20448     6 AGMQYSVGDKCKVRLDHNGKFYNAHIQEVSPENGPVVVFVEELGKKHTVPLKNLKPPPQ 64
Tudor_SMN_SPF30-like cd21182
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ...
 11-60 6.21e-07

Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing factor 30 (SPF30), and similar proteins; This group contains SMN, SPF30, Tudor domain-containing protein 3 (TDRD3), DNA excision repair protein ERCC-6-like 2 (ERCC6L2), and similar proteins. SMN, also called component of gems 1, or Gemin-1, is part of a multimeric SMN complex that includes spliceosomal Sm core proteins and plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. SPF30, also called 30 kDa splicing factor SMNrp, SMN-related protein, or survival motor neuron domain-containing protein 1 (SMNDC1), is an essential pre-mRNA splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. Members of this group contain a single Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410549  Cd Length: 50  Bit Score: 46.48  E-value: 6.21e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462631184  11 GDKCQVCLESEGRYYNAHIQEVGNENNSVTVFIEELAEKHVVPLANLKPV 60
Cdd:cd21182     1 GDKCLAPYSDDGKYYEATIEEITEESDTATVVFDGYGNSEEVPLSDLKPL 50
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 10-59 6.21e-06

Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar proteins; dTUD is required during oogenesis for the formation of primordial germ cells and for normal abdominal segmentation. It contains 11 Tudor domains. The family also includes mitochondrial A-kinase anchor protein 1 (AKAP1) and Tudor domain-containing proteins (TDRDs). AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), or dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), or protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. TDRDs have diverse biological functions and may contain one or more copies of the Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410450  Cd Length: 50  Bit Score: 43.66  E-value: 6.21e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462631184  10 LGDKCQVCLESEGRYYNAHIQEVgNENNSVTVFIEELAEKHVVPLANLKP 59
Cdd:cd20379     1 VGDLCAAKYEEDGKWYRARVLEV-LSNDKVEVFFVDYGNTETVPLSDLRP 49
Tudor_SPF30 cd20399
Tudor domain found in survival of motor neuron-related-splicing factor 30 (SPF30) and similar ...
 10-61 1.92e-05

Tudor domain found in survival of motor neuron-related-splicing factor 30 (SPF30) and similar proteins; SPF30, also called 30 kDa splicing factor SMNrp, SMN-related protein, or survival motor neuron domain-containing protein 1 (SMNDC1), is an essential pre-mRNA splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. Overexpression of SPF30 causes apoptosis. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410470 [Multi-domain]  Cd Length: 55  Bit Score: 42.29  E-value: 1.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462631184  10 LGDKCQVCLESEGRYYNAHIQEVGnENNSVTVFIEELAEKHVVPLANLKPVT 61
Cdd:cd20399     3 VGDKCMAVWSEDGQYYEATIEEIS-EDGTCTVTFDGYGNTEVTPLSQLKPRE 53
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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