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Conserved domains on  [gi|507083604|ref|WP_016154352|]
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MULTISPECIES: N(4)-acetylcytidine aminohydrolase [Citrobacter]

Protein Classification

ASCH domain-containing protein( domain architecture ID 10012240)

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
PRK04980 PRK04980
hypothetical protein; Provisional
 2-103 1.03e-64

hypothetical protein; Provisional


:

Pssm-ID: 179908  Cd Length: 102  Bit Score: 190.47  E-value: 1.03e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083604   2 QPNDITFFQRFQDDILAGRKTITIRDESESHFKAGDILRVGRFEDEGYFCTIEVVGTSTVTLDTLTEKHARQENMTLEEL 81
Cdd:PRK04980   1 QPNKITFFERFEADILAGRKTITIRDESESHFKPGDVLRVGTFEDDRYFCTIEVLSVSPVTFDELNEKHAEQENMTLPEL 80

                         90       100
                 ....*....|....*....|..
gi 507083604  82 KHVIAEIYPDQTQFYVIDFKCL 103
Cdd:PRK04980  81 KQVIAEIYPNLDQLYVIEFKLL 102
 
Name Accession Description Interval E-value
PRK04980 PRK04980
hypothetical protein; Provisional
 2-103 1.03e-64

hypothetical protein; Provisional


Pssm-ID: 179908  Cd Length: 102  Bit Score: 190.47  E-value: 1.03e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083604   2 QPNDITFFQRFQDDILAGRKTITIRDESESHFKAGDILRVGRFEDEGYFCTIEVVGTSTVTLDTLTEKHARQENMTLEEL 81
Cdd:PRK04980   1 QPNKITFFERFEADILAGRKTITIRDESESHFKPGDVLRVGTFEDDRYFCTIEVLSVSPVTFDELNEKHAEQENMTLPEL 80

                         90       100
                 ....*....|....*....|..
gi 507083604  82 KHVIAEIYPDQTQFYVIDFKCL 103
Cdd:PRK04980  81 KQVIAEIYPNLDQLYVIEFKLL 102
YqfB COG3097
Uncharacterized conserved protein YqfB, UPF0267 family [Function unknown];
2-103 2.43e-63

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


Pssm-ID: 442331  Cd Length: 102  Bit Score: 187.01  E-value: 2.43e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083604   2 QPNDITFFQRFQDDILAGRKTITIRDESESHFKAGDILRVGRFEDEGYFCTIEVVGTSTVTLDTLTEKHARQENMTLEEL 81
Cdd:COG3097    1 MPNDITFFERFEPDILAGRKTITIRDESESHFKPGQILRVGTYEDDRYFCTIEVLSVTPVTLDELTEEHARQENMTLDEL 80

                         90       100
                 ....*....|....*....|..
gi 507083604  82 KHVIAEIYPDQTQFYVIDFKCL 103
Cdd:COG3097   81 KQVIREIYPGEDQLYVIEFKLV 102
ASCH_yqfb_like cd06552
ASC-1 homology domain, subfamily similar to Escherichia coli Yqfb. The ASCH domain, a small ...
 5-101 1.04e-30

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: 104.24  E-value: 1.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083604   5 DITFFQRFQDDILAGRKTITIRDESESHFKAGDILRVgrFEDEGYFCTIEVVGTSTVTLDTLTEKHARQENM-TLEELKH 83
Cdd:cd06552    1 RILFFERYEEAILSGKKTATIRDGGESHLKPGDVVEV--HTGERIFGEAEITSVEEKTLGELTDEDARQEGFpSLEELKE 78

                         90       100
                 ....*....|....*....|.
gi 507083604  84 VIAEIYP---DQTQFYVIDFK 101
Cdd:cd06552   79 ALKEIYPglkDDDEVYVIEFR 99
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 6-101 1.01e-26

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: 94.33  E-value: 1.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083604     6 ITFFQRFQDDILAGRKTITIRDESESHFKAGDILRVGRFEDEgYFCTIEVVGTSTVTLDTLTEKHARQENMT-LEELKHV 84
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRLENEPLPKVGDLLIVLDGEGK-PVCVIEVTSVEIIPFKDVTAEHAYLEGEGsLEEWRKV 79

                           90
                   ....*....|....*..
gi 507083604    85 IAEIYPDQTQFYVIDFK 101
Cdd:smart01022  80 HKEFYPEDMEVVCEEFE 96
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 6-92 1.41e-19

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: 76.26  E-value: 1.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083604    6 ITFFQRFQDDILAGRKTITIRDESESHFKAGDILrVGRFEDEGYFCTIEVVGTSTVTLDTLTEKHARQENMTLEELKHVI 85
Cdd:pfam04266   1 LSFGQEYADLILSGKKTAEIRVWDEPLPVVGDLL-ILLDSTGRPVGVIEVTDVEIIPFEEVTEEHAYLEGESLEEWRKVH 79


                  ....*..
gi 507083604   86 AEIYPDQ 92
Cdd:pfam04266  80 KEFYPEE 86
 
Name Accession Description Interval E-value
PRK04980 PRK04980
hypothetical protein; Provisional
 2-103 1.03e-64

hypothetical protein; Provisional


Pssm-ID: 179908  Cd Length: 102  Bit Score: 190.47  E-value: 1.03e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083604   2 QPNDITFFQRFQDDILAGRKTITIRDESESHFKAGDILRVGRFEDEGYFCTIEVVGTSTVTLDTLTEKHARQENMTLEEL 81
Cdd:PRK04980   1 QPNKITFFERFEADILAGRKTITIRDESESHFKPGDVLRVGTFEDDRYFCTIEVLSVSPVTFDELNEKHAEQENMTLPEL 80

                         90       100
                 ....*....|....*....|..
gi 507083604  82 KHVIAEIYPDQTQFYVIDFKCL 103
Cdd:PRK04980  81 KQVIAEIYPNLDQLYVIEFKLL 102
YqfB COG3097
Uncharacterized conserved protein YqfB, UPF0267 family [Function unknown];
2-103 2.43e-63

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


Pssm-ID: 442331  Cd Length: 102  Bit Score: 187.01  E-value: 2.43e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083604   2 QPNDITFFQRFQDDILAGRKTITIRDESESHFKAGDILRVGRFEDEGYFCTIEVVGTSTVTLDTLTEKHARQENMTLEEL 81
Cdd:COG3097    1 MPNDITFFERFEPDILAGRKTITIRDESESHFKPGQILRVGTYEDDRYFCTIEVLSVTPVTLDELTEEHARQENMTLDEL 80

                         90       100
                 ....*....|....*....|..
gi 507083604  82 KHVIAEIYPDQTQFYVIDFKCL 103
Cdd:COG3097   81 KQVIREIYPGEDQLYVIEFKLV 102
ASCH_yqfb_like cd06552
ASC-1 homology domain, subfamily similar to Escherichia coli Yqfb. The ASCH domain, a small ...
 5-101 1.04e-30

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: 104.24  E-value: 1.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083604   5 DITFFQRFQDDILAGRKTITIRDESESHFKAGDILRVgrFEDEGYFCTIEVVGTSTVTLDTLTEKHARQENM-TLEELKH 83
Cdd:cd06552    1 RILFFERYEEAILSGKKTATIRDGGESHLKPGDVVEV--HTGERIFGEAEITSVEEKTLGELTDEDARQEGFpSLEELKE 78

                         90       100
                 ....*....|....*....|.
gi 507083604  84 VIAEIYP---DQTQFYVIDFK 101
Cdd:cd06552   79 ALKEIYPglkDDDEVYVIEFR 99
ASCH smart01022
The ASCH domain adopts a beta-barrel fold similar to that of the PUA domain; It is thought to ...
 6-101 1.01e-26

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: 94.33  E-value: 1.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083604     6 ITFFQRFQDDILAGRKTITIRDESESHFKAGDILRVGRFEDEgYFCTIEVVGTSTVTLDTLTEKHARQENMT-LEELKHV 84
Cdd:smart01022   1 LSFKDELADLILSGKKTATIRLENEPLPKVGDLLIVLDGEGK-PVCVIEVTSVEIIPFKDVTAEHAYLEGEGsLEEWRKV 79

                           90
                   ....*....|....*..
gi 507083604    85 IAEIYPDQTQFYVIDFK 101
Cdd:smart01022  80 HKEFYPEDMEVVCEEFE 96
ASCH cd06541
ASC-1 homology or ASCH domain, a small beta-barrel domain found in all three kingdoms of life. ...
 5-101 1.74e-25

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: 91.57  E-value: 1.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083604   5 DITFFQRFQDDILAGRKTITIRDES--ESHFKAGDILRVGRFedEGYFCTIEVVGTSTVTLDtlTEKHARQEN------- 75
Cdd:cd06541    1 VLMFGDRYGQLVVSGRKTIEIRSLDiyEQLPKAGDYLIILDG--QQPLAIAEVVKVEIMPMV--NELSEEQEQaegegdl 76

                         90       100
                 ....*....|....*....|....*....
gi 507083604  76 MTLEELKHVIAEIYPD---QTQFYVIDFK 101
Cdd:cd06541   77 TLLYELKEHAAFFKEElapDMLLYAISFE 105
ASCH pfam04266
ASCH domain; The ASCH domain adopts a beta-barrel fold similar to the pfam01472 domain. It is ...
 6-92 1.41e-19

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: 76.26  E-value: 1.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083604    6 ITFFQRFQDDILAGRKTITIRDESESHFKAGDILrVGRFEDEGYFCTIEVVGTSTVTLDTLTEKHARQENMTLEELKHVI 85
Cdd:pfam04266   1 LSFGQEYADLILSGKKTAEIRVWDEPLPVVGDLL-ILLDSTGRPVGVIEVTDVEIIPFEEVTEEHAYLEGESLEEWRKVH 79


                  ....*..
gi 507083604   86 AEIYPDQ 92
Cdd:pfam04266  80 KEFYPEE 86
ASCH COG2411
Predicted RNA-binding protein, contains PUA-like ASCH domain [General function prediction only] ...
 6-101 3.75e-09

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


Pssm-ID: 441966  Cd Length: 103  Bit Score: 49.49  E-value: 3.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083604   6 ITFFQRFQDDILAGRKTITIRDeSESHFKAGDILRVgrFEDEGYFCTIEVVGTSTVTLDTLTEKHARQENM-TLEELKHV 84
Cdd:COG2411    4 LNFKPKYLDAILSGRKTATIRL-GDKRYKPGDEVYV--TSGGRKIAKARITSVRVKKLSELTDEDARLDGFsSVEELIEA 80

                         90       100
                 ....*....|....*....|
gi 507083604  85 IAEIYPDQTQ---FYVIDFK 101
Cdd:COG2411   81 LRKIYGDISPddeVTVIEFE 100
cupin_TM1112-like cd02227
Thermotoga maritima TM1112 and related proteins, cupin domain; This family includes bacterial ...
 16-58 3.16e-03

Thermotoga maritima TM1112 and related proteins, cupin domain; This family includes bacterial and plant proteins homologous to TM1112, a Thermotoga maritima protein of unknown function with a cupin beta barrel domain. TM1112 (also known as DUF861) is a subfamily of RmlC-like cupins with a conserved "jelly roll-like" beta-barrel fold; structures indicate that a monomer is the biologically-relevant form.


Pssm-ID: 380356 [Multi-domain]  Cd Length: 69  Bit Score: 33.32  E-value: 3.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 507083604  16 ILAGRKTITIRDESESHFKAGDILRVgrfeDEGYFCTIEVVGT 58
Cdd:cd02227   24 ILEGEVRVTPEDGEPVTFKAGDLVVF----PAGFSGTWEVLEP 62
 
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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