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Conserved domains on  [gi|491647493|ref|WP_005505019|]
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N(4)-acetylcytidine aminohydrolase [Grimontia hollisae]

Protein Classification

ASCH domain-containing protein( domain architecture ID 10789948)

ASCH (ASC-1 homology) domain-containing protein, similar to Escherichia coli Yqfb protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YqfB COG3097
Uncharacterized conserved protein YqfB, UPF0267 family [Function unknown];
4-105 9.04e-54

Uncharacterized conserved protein YqfB, UPF0267 family [Function unknown];


:

Pssm-ID: 442331  Cd Length: 102  Bit Score: 162.74  E-value: 9.04e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647493   4 APTKITFFEWLTPLVASGKKTITIRDKSESYYVPGTRVDVHTLEKDEYVCQIDIVSVEKIGFDDINEEHAAQEFLPLEEL 83
Cdd:COG3097    1 MPNDITFFERFEPDILAGRKTITIRDESESHFKPGQILRVGTYEDDRYFCTIEVLSVTPVTLDELTEEHARQENMTLDEL 80

                         90       100
                 ....*....|....*....|..
gi 491647493  84 KPLIRNIYPNDDEFYVITYTLV 105
Cdd:COG3097   81 KQVIREIYPGEDQLYVIEFKLV 102
 
Name Accession Description Interval E-value
YqfB COG3097
Uncharacterized conserved protein YqfB, UPF0267 family [Function unknown];
4-105 9.04e-54

Uncharacterized conserved protein YqfB, UPF0267 family [Function unknown];


Pssm-ID: 442331  Cd Length: 102  Bit Score: 162.74  E-value: 9.04e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647493   4 APTKITFFEWLTPLVASGKKTITIRDKSESYYVPGTRVDVHTLEKDEYVCQIDIVSVEKIGFDDINEEHAAQEFLPLEEL 83
Cdd:COG3097    1 MPNDITFFERFEPDILAGRKTITIRDESESHFKPGQILRVGTYEDDRYFCTIEVLSVTPVTLDELTEEHARQENMTLDEL 80

                         90       100
                 ....*....|....*....|..
gi 491647493  84 KPLIRNIYPNDDEFYVITYTLV 105
Cdd:COG3097   81 KQVIREIYPGEDQLYVIEFKLV 102
PRK04980 PRK04980
hypothetical protein; Provisional
 4-105 1.57e-52

hypothetical protein; Provisional


Pssm-ID: 179908  Cd Length: 102  Bit Score: 159.65  E-value: 1.57e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647493   4 APTKITFFEWLTPLVASGKKTITIRDKSESYYVPGTRVDVHTLEKDEYVCQIDIVSVEKIGFDDINEEHAAQEFLPLEEL 83
Cdd:PRK04980   1 QPNKITFFERFEADILAGRKTITIRDESESHFKPGDVLRVGTFEDDRYFCTIEVLSVSPVTFDELNEKHAEQENMTLPEL 80

                         90       100
                 ....*....|....*....|..
gi 491647493  84 KPLIRNIYPNDDEFYVITYTLV 105
Cdd:PRK04980  81 KQVIAEIYPNLDQLYVIEFKLL 102
ASCH_yqfb_like cd06552
ASC-1 homology domain, subfamily similar to Escherichia coli Yqfb. The ASCH domain, a small ...
 7-104 1.23e-29

ASC-1 homology domain, subfamily similar to Escherichia coli Yqfb. The ASCH domain, a small beta-barrel domain found in all three kingdoms of life, resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation.


Pssm-ID: 119344  Cd Length: 100  Bit Score: 101.93  E-value: 1.23e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647493   7 KITFFEWLTPLVASGKKTITIRDKSESYYVPGTRVDVHTLEKdeYVCQIDIVSVEKIGFDDINEEHAAQE-FLPLEELKP 85
Cdd:cd06552    1 RILFFERYEEAILSGKKTATIRDGGESHLKPGDVVEVHTGER--IFGEAEITSVEEKTLGELTDEDARQEgFPSLEELKE 78

                         90       100
                 ....*....|....*....|..
gi 491647493  86 LIRNIYPN---DDEFYVITYTL 104
Cdd:cd06552   79 ALKEIYPGlkdDDEVYVIEFRL 100
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 8-105 1.78e-21

The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation.


Pssm-ID: 214979  Cd Length: 99  Bit Score: 81.23  E-value: 1.78e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647493     8 ITFFEWLTPLVASGKKTITIRDKSESYYVPGTRVDVHTLeKDEYVCQIDIVSVEKIGFDDINEEHAAQE-FLPLEELKPL 86
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRLENEPLPKVGDLLIVLDG-EGKPVCVIEVTSVEIIPFKDVTAEHAYLEgEGSLEEWRKV 79

                           90
                   ....*....|....*....
gi 491647493    87 IRNIYPNDDEFYVITYTLV 105
Cdd:smart01022  80 HKEFYPEDMEVVCEEFEVV 98
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 8-105 1.98e-20

ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation.


Pssm-ID: 398105  Cd Length: 102  Bit Score: 78.57  E-value: 1.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647493    8 ITFFEWLTPLVASGKKTITIRDKSESYYVPGtRVDVHTLEKDEYVCQIDIVSVEKIGFDDINEEHAAQEFLPLEELKPLI 87
Cdd:pfam04266   1 LSFGQEYADLILSGKKTAEIRVWDEPLPVVG-DLLILLDSTGRPVGVIEVTDVEIIPFEEVTEEHAYLEGESLEEWRKVH 79

                          90       100
                  ....*....|....*....|..
gi 491647493   88 RNIYPN----DDEFYVITYTLV 105
Cdd:pfam04266  80 KEFYPEekeeDEGVVVEEFELV 101
 
Name Accession Description Interval E-value
YqfB COG3097
Uncharacterized conserved protein YqfB, UPF0267 family [Function unknown];
4-105 9.04e-54

Uncharacterized conserved protein YqfB, UPF0267 family [Function unknown];


Pssm-ID: 442331  Cd Length: 102  Bit Score: 162.74  E-value: 9.04e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647493   4 APTKITFFEWLTPLVASGKKTITIRDKSESYYVPGTRVDVHTLEKDEYVCQIDIVSVEKIGFDDINEEHAAQEFLPLEEL 83
Cdd:COG3097    1 MPNDITFFERFEPDILAGRKTITIRDESESHFKPGQILRVGTYEDDRYFCTIEVLSVTPVTLDELTEEHARQENMTLDEL 80

                         90       100
                 ....*....|....*....|..
gi 491647493  84 KPLIRNIYPNDDEFYVITYTLV 105
Cdd:COG3097   81 KQVIREIYPGEDQLYVIEFKLV 102
PRK04980 PRK04980
hypothetical protein; Provisional
 4-105 1.57e-52

hypothetical protein; Provisional


Pssm-ID: 179908  Cd Length: 102  Bit Score: 159.65  E-value: 1.57e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647493   4 APTKITFFEWLTPLVASGKKTITIRDKSESYYVPGTRVDVHTLEKDEYVCQIDIVSVEKIGFDDINEEHAAQEFLPLEEL 83
Cdd:PRK04980   1 QPNKITFFERFEADILAGRKTITIRDESESHFKPGDVLRVGTFEDDRYFCTIEVLSVSPVTFDELNEKHAEQENMTLPEL 80

                         90       100
                 ....*....|....*....|..
gi 491647493  84 KPLIRNIYPNDDEFYVITYTLV 105
Cdd:PRK04980  81 KQVIAEIYPNLDQLYVIEFKLL 102
ASCH_yqfb_like cd06552
ASC-1 homology domain, subfamily similar to Escherichia coli Yqfb. The ASCH domain, a small ...
 7-104 1.23e-29

ASC-1 homology domain, subfamily similar to Escherichia coli Yqfb. The ASCH domain, a small beta-barrel domain found in all three kingdoms of life, resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation.


Pssm-ID: 119344  Cd Length: 100  Bit Score: 101.93  E-value: 1.23e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647493   7 KITFFEWLTPLVASGKKTITIRDKSESYYVPGTRVDVHTLEKdeYVCQIDIVSVEKIGFDDINEEHAAQE-FLPLEELKP 85
Cdd:cd06552    1 RILFFERYEEAILSGKKTATIRDGGESHLKPGDVVEVHTGER--IFGEAEITSVEEKTLGELTDEDARQEgFPSLEELKE 78

                         90       100
                 ....*....|....*....|..
gi 491647493  86 LIRNIYPN---DDEFYVITYTL 104
Cdd:cd06552   79 ALKEIYPGlkdDDEVYVIEFRL 100
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 8-105 1.78e-21

The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation.


Pssm-ID: 214979  Cd Length: 99  Bit Score: 81.23  E-value: 1.78e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647493     8 ITFFEWLTPLVASGKKTITIRDKSESYYVPGTRVDVHTLeKDEYVCQIDIVSVEKIGFDDINEEHAAQE-FLPLEELKPL 86
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRLENEPLPKVGDLLIVLDG-EGKPVCVIEVTSVEIIPFKDVTAEHAYLEgEGSLEEWRKV 79

                           90
                   ....*....|....*....
gi 491647493    87 IRNIYPNDDEFYVITYTLV 105
Cdd:smart01022  80 HKEFYPEDMEVVCEEFEVV 98
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 8-105 1.98e-20

ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is thought to function as an RNA-binding domain during coactivation, RNA-processing and possibly during prokaryotic translation regulation.


Pssm-ID: 398105  Cd Length: 102  Bit Score: 78.57  E-value: 1.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647493    8 ITFFEWLTPLVASGKKTITIRDKSESYYVPGtRVDVHTLEKDEYVCQIDIVSVEKIGFDDINEEHAAQEFLPLEELKPLI 87
Cdd:pfam04266   1 LSFGQEYADLILSGKKTAEIRVWDEPLPVVG-DLLILLDSTGRPVGVIEVTDVEIIPFEEVTEEHAYLEGESLEEWRKVH 79

                          90       100
                  ....*....|....*....|..
gi 491647493   88 RNIYPN----DDEFYVITYTLV 105
Cdd:pfam04266  80 KEFYPEekeeDEGVVVEEFELV 101
ASCH cd06541
ASC-1 homology or ASCH domain, a small beta-barrel domain found in all three kingdoms of life. ...
 8-102 6.56e-09

ASC-1 homology or ASCH domain, a small beta-barrel domain found in all three kingdoms of life. ASCH resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation. The domain has been named after the ASC-1 protein, the activating signal cointegrator 1 or thyroid hormone receptor interactor protein 4 (TRIP4). ASC-1 is conserved in many eukaryotes and has been suggested to participate in a protein complex that interacts with RNA. It has been shown that ASC-1 mediates the interaction between various transciption factors and the basal transcriptional machinery.


Pssm-ID: 119343  Cd Length: 105  Bit Score: 49.20  E-value: 6.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647493   8 ITFFEWLTPLVASGKKTITIRDKSESYYVPGTRVDVHTLEKDEYVCQIDIVSVEKIGFDDINEEHAAQEFLP-----LEE 82
Cdd:cd06541    2 LMFGDRYGQLVVSGRKTIEIRSLDIYEQLPKAGDYLIILDGQQPLAIAEVVKVEIMPMVNELSEEQEQAEGEgdltlLYE 81

                         90       100
                 ....*....|....*....|...
gi 491647493  83 LKPLIRNIYP---NDDEFYVITY 102
Cdd:cd06541   82 LKEHAAFFKEelaPDMLLYAISF 104
ASCH COG2411
Predicted RNA-binding protein, contains PUA-like ASCH domain [General function prediction only] ...
 20-105 5.66e-08

Predicted RNA-binding protein, contains PUA-like ASCH domain [General function prediction only];


Pssm-ID: 441966  Cd Length: 103  Bit Score: 46.79  E-value: 5.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491647493  20 SGKKTITIRdKSESYYVPGTRVDVHTLEKDEYVCQIDIVSVEKIGfdDINEEHAAQE-FLPLEELKPLIRNIYPN---DD 95
Cdd:COG2411   16 SGRKTATIR-LGDKRYKPGDEVYVTSGGRKIAKARITSVRVKKLS--ELTDEDARLDgFSSVEELIEALRKIYGDispDD 92

                         90
                 ....*....|
gi 491647493  96 EFYVITYTLV 105
Cdd:COG2411   93 EVTVIEFEVV 102
 
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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