NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|74761196|sp|Q9BQ15|]
View 

RecName: Full=SOSS complex subunit B1; AltName: Full=Nucleic acid-binding protein 2; AltName: Full=Oligonucleotide/oligosaccharide-binding fold-containing protein 2B; AltName: Full=Sensor of single-strand DNA complex subunit B1; AltName: Full=Sensor of ssDNA subunit B1; Short=SOSS-B1; AltName: Full=Single-stranded DNA-binding protein 1; Short=hSSB1

Protein Classification

SOSS complex subunit B family protein( domain architecture ID 10139587)

SOSS complex subunit B family protein that contains an OB-fold nucleic acid binding domain; such as human SOSS complex subunit B2 (SSB2/NABP1), a component of the SOSS multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
SoSSB_OBF cd04491
SoSSB_OBF: A subfamily of OB folds similar to the OB fold of the crenarchaeote Sulfolobus ...
18-95 1.59e-20

SoSSB_OBF: A subfamily of OB folds similar to the OB fold of the crenarchaeote Sulfolobus solfataricus single-stranded (ss) DNA-binding protein (SSoSSB). SSoSSB has a single OB fold, and it physically and functionally interacts with RNA polymerase. In vitro, SSoSSB can substitute for the basal transcription factor TBP, stimulating transcription from promoters under conditions in which TBP is limiting, and supporting transcription when TBP is absent. SSoSSB selectively melts the duplex DNA of promoter sequences. It also relieves transcriptional repression by the chromatin Alba. In addition, SSoSSB activates reverse gyrase activity, which involves DNA binding, DNA cleavage, strand passage and ligation. SSoSSB stimulates all these steps in the presence of the chromatin protein, Sul7d. SSoSSB antagonizes the inhibitory effect of Sul7d on reverse gyrase supercoiling activity. It also physically and functionally interacts with Mini-chromosome Maintenance (MCM), stimulating the DNA helicase activity of MCM.


:

Pssm-ID: 239937 [Multi-domain]  Cd Length: 82  Bit Score: 81.52  E-value: 1.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74761196  18 NLIFIVLETGRV-TKTKDGHE--VRTCKVADKTGSINISVWDD-VGNLIQPGDIIRLTKGYASVFKGCLTLYTGRGGDLQ 93
Cdd:cd04491   1 SVEGKVLSISEPrEFTRDGSEgkVQSGLVGDETGTIRFTLWDEkAADDLEPGDVVRIENAYVREFNGRLELSVGKNSEIE 80

                ..
gi 74761196  94 KI 95
Cdd:cd04491  81 KL 82
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
106-153 2.93e-03

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK14971:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 614  Bit Score: 38.22  E-value: 2.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 74761196  106 PNFSEPNPEYSTQQAPNKAVQNDSNPSASQPTTGPSAASPASENQNGN 153
Cdd:PRK14971 381 PVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVS 428
 
Name Accession Description Interval E-value
SoSSB_OBF cd04491
SoSSB_OBF: A subfamily of OB folds similar to the OB fold of the crenarchaeote Sulfolobus ...
18-95 1.59e-20

SoSSB_OBF: A subfamily of OB folds similar to the OB fold of the crenarchaeote Sulfolobus solfataricus single-stranded (ss) DNA-binding protein (SSoSSB). SSoSSB has a single OB fold, and it physically and functionally interacts with RNA polymerase. In vitro, SSoSSB can substitute for the basal transcription factor TBP, stimulating transcription from promoters under conditions in which TBP is limiting, and supporting transcription when TBP is absent. SSoSSB selectively melts the duplex DNA of promoter sequences. It also relieves transcriptional repression by the chromatin Alba. In addition, SSoSSB activates reverse gyrase activity, which involves DNA binding, DNA cleavage, strand passage and ligation. SSoSSB stimulates all these steps in the presence of the chromatin protein, Sul7d. SSoSSB antagonizes the inhibitory effect of Sul7d on reverse gyrase supercoiling activity. It also physically and functionally interacts with Mini-chromosome Maintenance (MCM), stimulating the DNA helicase activity of MCM.


Pssm-ID: 239937 [Multi-domain]  Cd Length: 82  Bit Score: 81.52  E-value: 1.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74761196  18 NLIFIVLETGRV-TKTKDGHE--VRTCKVADKTGSINISVWDD-VGNLIQPGDIIRLTKGYASVFKGCLTLYTGRGGDLQ 93
Cdd:cd04491   1 SVEGKVLSISEPrEFTRDGSEgkVQSGLVGDETGTIRFTLWDEkAADDLEPGDVVRIENAYVREFNGRLELSVGKNSEIE 80

                ..
gi 74761196  94 KI 95
Cdd:cd04491  81 KL 82
PRK06461 PRK06461
single-stranded DNA-binding protein; Reviewed
1-114 8.06e-18

single-stranded DNA-binding protein; Reviewed


Pssm-ID: 180574 [Multi-domain]  Cd Length: 129  Bit Score: 75.84  E-value: 8.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74761196    1 MTTETFVKDIKPGLKNLNLIFIVLETG--RVTKTKDG-HEVRTCKVADKTGSINISVWDDVGNLIQPGDIIRLTKGYASV 77
Cdd:PRK06461   1 MEMITKIKDLKPGMERVNVTVRVLEVGepKVIQTKGGpRTISEAVVGDETGRVKLTLWGEQAGSLKEGEVVEIENAWTTL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 74761196   78 FKGCLTLYTGRGGDLQKIGEfcmvySEVP---NFSEPNPE 114
Cdd:PRK06461  81 YRGKVQLNVGKYGSISESDD-----EEVPeaeEIPEETPE 115
RFA1 COG1599
ssDNA-binding replication factor A, large subunit [Replication, recombination and repair];
7-97 1.53e-12

ssDNA-binding replication factor A, large subunit [Replication, recombination and repair];


Pssm-ID: 441207 [Multi-domain]  Cd Length: 282  Bit Score: 64.70  E-value: 1.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74761196   7 VKDIKPGLKNLNLIFIVLETG--RVTKTKDGHE--VRTCKVADKTGSINISVWDDVGNL-IQPGDIIRLTKGYASVFKGC 81
Cdd:COG1599  24 ISDLSPGDRDVNVEGRVLEIGeeRTFDRKDGSEgrVQSGVIGDETGRIRFTLWDDKADLeLEEGDVVRIENAYVREFNGG 103
                        90
                ....*....|....*.
gi 74761196  82 LTLYTGRGGDLQKIGE 97
Cdd:COG1599 104 PELNLGERTTIEKLDE 119
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
106-153 2.93e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 38.22  E-value: 2.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 74761196  106 PNFSEPNPEYSTQQAPNKAVQNDSNPSASQPTTGPSAASPASENQNGN 153
Cdd:PRK14971 381 PVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVS 428
tRNA_anti-codon pfam01336
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ...
27-80 7.47e-03

OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.


Pssm-ID: 460164 [Multi-domain]  Cd Length: 75  Bit Score: 34.13  E-value: 7.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 74761196    27 GRVT-KTKDGHEVRTCKVADKTGSINISVWDD----VGNLIQPGDIIRLTkGYASVFKG 80
Cdd:pfam01336   5 GRVTsIRRSGGKLLFLTLRDGTGSIQVVVFKEeaekLAKKLKEGDVVRVT-GKVKKRKG 62
 
Name Accession Description Interval E-value
SoSSB_OBF cd04491
SoSSB_OBF: A subfamily of OB folds similar to the OB fold of the crenarchaeote Sulfolobus ...
18-95 1.59e-20

SoSSB_OBF: A subfamily of OB folds similar to the OB fold of the crenarchaeote Sulfolobus solfataricus single-stranded (ss) DNA-binding protein (SSoSSB). SSoSSB has a single OB fold, and it physically and functionally interacts with RNA polymerase. In vitro, SSoSSB can substitute for the basal transcription factor TBP, stimulating transcription from promoters under conditions in which TBP is limiting, and supporting transcription when TBP is absent. SSoSSB selectively melts the duplex DNA of promoter sequences. It also relieves transcriptional repression by the chromatin Alba. In addition, SSoSSB activates reverse gyrase activity, which involves DNA binding, DNA cleavage, strand passage and ligation. SSoSSB stimulates all these steps in the presence of the chromatin protein, Sul7d. SSoSSB antagonizes the inhibitory effect of Sul7d on reverse gyrase supercoiling activity. It also physically and functionally interacts with Mini-chromosome Maintenance (MCM), stimulating the DNA helicase activity of MCM.


Pssm-ID: 239937 [Multi-domain]  Cd Length: 82  Bit Score: 81.52  E-value: 1.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74761196  18 NLIFIVLETGRV-TKTKDGHE--VRTCKVADKTGSINISVWDD-VGNLIQPGDIIRLTKGYASVFKGCLTLYTGRGGDLQ 93
Cdd:cd04491   1 SVEGKVLSISEPrEFTRDGSEgkVQSGLVGDETGTIRFTLWDEkAADDLEPGDVVRIENAYVREFNGRLELSVGKNSEIE 80

                ..
gi 74761196  94 KI 95
Cdd:cd04491  81 KL 82
PRK06461 PRK06461
single-stranded DNA-binding protein; Reviewed
1-114 8.06e-18

single-stranded DNA-binding protein; Reviewed


Pssm-ID: 180574 [Multi-domain]  Cd Length: 129  Bit Score: 75.84  E-value: 8.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74761196    1 MTTETFVKDIKPGLKNLNLIFIVLETG--RVTKTKDG-HEVRTCKVADKTGSINISVWDDVGNLIQPGDIIRLTKGYASV 77
Cdd:PRK06461   1 MEMITKIKDLKPGMERVNVTVRVLEVGepKVIQTKGGpRTISEAVVGDETGRVKLTLWGEQAGSLKEGEVVEIENAWTTL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 74761196   78 FKGCLTLYTGRGGDLQKIGEfcmvySEVP---NFSEPNPE 114
Cdd:PRK06461  81 YRGKVQLNVGKYGSISESDD-----EEVPeaeEIPEETPE 115
RFA1 COG1599
ssDNA-binding replication factor A, large subunit [Replication, recombination and repair];
7-97 1.53e-12

ssDNA-binding replication factor A, large subunit [Replication, recombination and repair];


Pssm-ID: 441207 [Multi-domain]  Cd Length: 282  Bit Score: 64.70  E-value: 1.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74761196   7 VKDIKPGLKNLNLIFIVLETG--RVTKTKDGHE--VRTCKVADKTGSINISVWDDVGNL-IQPGDIIRLTKGYASVFKGC 81
Cdd:COG1599  24 ISDLSPGDRDVNVEGRVLEIGeeRTFDRKDGSEgrVQSGVIGDETGRIRFTLWDDKADLeLEEGDVVRIENAYVREFNGG 103
                        90
                ....*....|....*.
gi 74761196  82 LTLYTGRGGDLQKIGE 97
Cdd:COG1599 104 PELNLGERTTIEKLDE 119
YhaM COG3481
3'-5' exoribonuclease YhaM, can participate in 23S rRNA maturation, HD superfamily ...
1-84 7.03e-08

3'-5' exoribonuclease YhaM, can participate in 23S rRNA maturation, HD superfamily [Translation, ribosomal structure and biogenesis]; 3'-5' exoribonuclease YhaM, can participate in 23S rRNA maturation, HD superfamily is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 442704 [Multi-domain]  Cd Length: 316  Bit Score: 51.35  E-value: 7.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74761196   1 MTTETFVKDIKPGlKNLNLIFIVLETgRVTKTKDGHEVRTCKVADKTGSINISVWDD---VGNLIQPGDIIRLtKGYASV 77
Cdd:COG3481   1 MMKRKFIKDLKPG-EEVDGFFLIKSK-ELRTTKNGKPYLSLTLQDKTGTIEAKIWDAseeDIEEFQPGDVVKV-RGKVQE 77

                ....*..
gi 74761196  78 FKGCLTL 84
Cdd:COG3481  78 YQGRLQL 84
PRK14699 PRK14699
replication factor A; Provisional
7-130 9.38e-08

replication factor A; Provisional


Pssm-ID: 173162 [Multi-domain]  Cd Length: 484  Bit Score: 51.54  E-value: 9.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74761196    7 VKDIKPGLKNLNLIFIVLETG--RVTKTKDGH--EVRTCKVADKTGSINISVWDDVG---NLIQPGDIIRLTKGYA--SV 77
Cdd:PRK14699 169 IKDIKDGMGDLNLTGKVLEISeiRTFQRKDGTsgKVGNLLLGDETGTLRVTLWDDKTdflNQIEYGDTVELINAYAreNA 248
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 74761196   78 FKGCLTLYTGRGGDLQKigefcmvysevpnfSEPNPEYSTQQAPNKAVQNDSN 130
Cdd:PRK14699 249 FTQKVELQVGNRSIIRK--------------SEKKVEYEEEFTPIEDIKADMN 287
PRK07211 PRK07211
single-stranded DNA binding protein;
7-97 3.10e-07

single-stranded DNA binding protein;


Pssm-ID: 180887 [Multi-domain]  Cd Length: 485  Bit Score: 49.76  E-value: 3.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74761196    7 VKDIKPGLKNLNLIFIVLETG--RVTKTKDGHE--VRTCKVADKTGSINISVWDDVGNL---IQPGDIIRLTKGYASVFK 79
Cdd:PRK07211 164 VEDLSLGLSDVTLVGVVLDTDsvRTFDRDDGSEgrVSNLTVGDETGRVRVTLWDDRADLaeeLDAGESVEIVDGYVRERD 243
                         90
                 ....*....|....*...
gi 74761196   80 GCLTLYTGRGGDLQKIGE 97
Cdd:PRK07211 244 GSLELHVGDRGAVEEVDE 261
PRK12366 PRK12366
replication factor A; Reviewed
38-90 1.21e-06

replication factor A; Reviewed


Pssm-ID: 237078 [Multi-domain]  Cd Length: 637  Bit Score: 48.12  E-value: 1.21e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 74761196   38 VRTCKVADKTGSINISVWDDVGNL-IQPGDIIRLTKGYASVFKGCLTLYTGRGG 90
Cdd:PRK12366 436 VRNIELADGTGSIRLTLWDDDAEIeIKEGDAIKILHPYVKENGDYLDLSIGRYG 489
PRK15491 PRK15491
replication factor A; Provisional
7-97 3.37e-06

replication factor A; Provisional


Pssm-ID: 185388 [Multi-domain]  Cd Length: 374  Bit Score: 46.80  E-value: 3.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74761196    7 VKDIKPGLKNLNLI---FIVLETGRVTKTkDGHE--VRTCKVADKTGSINISVWDDVGNLIQPGDI-----IRLTkGYAS 76
Cdd:PRK15491  60 IADINESSSNVNFTakvVSIFEPKEFNRN-DGTTgrVGNIIVADETGSIRLTLWDDLADLIKTGDIevgksLNIS-GYAK 137
                         90       100
                 ....*....|....*....|.
gi 74761196   77 VFKGCLTLYTGRGGDLQKIGE 97
Cdd:PRK15491 138 EGYSGIEVNIGRYGGISESDE 158
PRK12366 PRK12366
replication factor A; Reviewed
7-72 6.66e-06

replication factor A; Reviewed


Pssm-ID: 237078 [Multi-domain]  Cd Length: 637  Bit Score: 46.19  E-value: 6.66e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74761196    7 VKDIKPGLKNLNLifivleTGRVT--------KTKDGHE--VRTCKVADKTGSINISVWDDVGNLIQP---GDIIRLTK 72
Cdd:PRK12366  66 ISDIEEGQINVEI------TGRIIeisniktfTRKDGSTgkLANITIADNTGTIRLTLWNDNAKLLKGlkeGDVIKIEN 138
PRK07218 PRK07218
Single-stranded DNA binding protein;
7-74 1.17e-05

Single-stranded DNA binding protein;


Pssm-ID: 180890 [Multi-domain]  Cd Length: 423  Bit Score: 45.00  E-value: 1.17e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74761196    7 VKDIKPGLKNLNLIFIVLETGRVTKTKDG--HEVRTCKVADKTGSINISVWDDVGnlIQPGDIIRLTKGY 74
Cdd:PRK07218  61 IKELSTDDKNVTVTGRVLTIGERSIRYQGddHVIYEGILADETGTISYTAWKDFG--LSPGDTVTIGNAG 128
PRK15491 PRK15491
replication factor A; Provisional
7-75 2.75e-04

replication factor A; Provisional


Pssm-ID: 185388 [Multi-domain]  Cd Length: 374  Bit Score: 41.02  E-value: 2.75e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74761196    7 VKDIKPGLKNLNLIFIVLETG--RVTKTKDGHE--VRTCKVADKTGSINISVWDDVGNL---IQPGDIIRLTKGYA 75
Cdd:PRK15491 169 ISDIKDGDSDINIVGKVLDISdvRTFQKKDGSQgrVRNITIGDETGKIRVTLWDGKTDLadkLENGDSVEIINGYA 244
PRK07211 PRK07211
single-stranded DNA binding protein;
7-77 3.95e-04

single-stranded DNA binding protein;


Pssm-ID: 180887 [Multi-domain]  Cd Length: 485  Bit Score: 40.51  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74761196    7 VKDIKPGLKNLNLIFIVLETGRV-TKTKDGHE----VRTCKVADKTGSINISVWDD-----VGNLiQPGDIIRL----TK 72
Cdd:PRK07211  56 IADIEPGMDEVKFLAKVLSIGDLrTFERDGEDedgrVINVEVADETGSVRVAFWDEqavaaEEEL-EVGQVLRIkgrpKD 134

                 ....*
gi 74761196   73 GYASV 77
Cdd:PRK07211 135 GYNGL 139
PRK14699 PRK14699
replication factor A; Provisional
4-118 4.60e-04

replication factor A; Provisional


Pssm-ID: 173162 [Multi-domain]  Cd Length: 484  Bit Score: 40.37  E-value: 4.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74761196    4 ETF--VKDIKPGLKNLNLIFIVLETG--RVTKTKDGHEVRTCKV--ADKTGSINISVWDDVGNLIQPGDI---IRLTKGY 74
Cdd:PRK14699 274 EEFtpIEDIKADMNNINISGRVLDISevRTFEKKDGSPGRVGNLllGDSTGKIRLTLWDEKTNFLDEIDFdetVEVLNAY 353
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 74761196   75 A--SVFKGCLTLYTGRGGDLQKiGEFCMVYSEvpNFSE-----PNPEYSTQ 118
Cdd:PRK14699 354 SreNTFSQQVELNLGARGIIQK-SEKKVEYRE--KFTDiadiiPGESYSVQ 401
YhaM_OBF_like cd04492
YhaM_OBF_like: A subfamily of OB folds similar to that found in Bacillus subtilis YhaM and ...
31-80 2.71e-03

YhaM_OBF_like: A subfamily of OB folds similar to that found in Bacillus subtilis YhaM and Staphylococcus aureus cmp-binding factor-1 (SaCBF1). Both these proteins are 3'-to-5'exoribonucleases. YhaM requires Mn2+ or Co2+ for activity and is inactive in the presence of Mg2+. YhaM also has a Mn2+ dependent 3'-to-5'single-stranded DNA exonuclease activity. SaCBF is also a double-stranded DNA binding protein, binding specifically to cmp, the replication enhancer found in S. aureus plasmid pT181. Proteins in this group combine an N-terminal OB fold with a C-terminal HD domain. The HD domain is found in metal-dependent phosphohydrolases.


Pssm-ID: 239938 [Multi-domain]  Cd Length: 83  Bit Score: 35.64  E-value: 2.71e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 74761196  31 KTKDGHEVRTCKVADKTGSINISVWDDVGNL---IQPGDIIRLtKGYASVFKG 80
Cdd:cd04492  13 TAKNGKPYLALTLQDKTGEIEAKLWDASEEDeekFKPGDIVHV-KGRVEEYRG 64
PRK12366 PRK12366
replication factor A; Reviewed
19-76 2.91e-03

replication factor A; Reviewed


Pssm-ID: 237078 [Multi-domain]  Cd Length: 637  Bit Score: 38.10  E-value: 2.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74761196   19 LIFIVLETGRVTKtKDGHE--VRTCKVADKTGSINISVWDDVGNL-IQPGDIIRLtKGYAS 76
Cdd:PRK12366 192 EVTKAYPIKEFTR-KDGSEgkLKSFILKDDTGSIRVTLWNDLTDIeVNKGDIVRV-KGYVK 250
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
106-153 2.93e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 38.22  E-value: 2.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 74761196  106 PNFSEPNPEYSTQQAPNKAVQNDSNPSASQPTTGPSAASPASENQNGN 153
Cdd:PRK14971 381 PVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVS 428
tRNA_anti-codon pfam01336
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ...
27-80 7.47e-03

OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.


Pssm-ID: 460164 [Multi-domain]  Cd Length: 75  Bit Score: 34.13  E-value: 7.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 74761196    27 GRVT-KTKDGHEVRTCKVADKTGSINISVWDD----VGNLIQPGDIIRLTkGYASVFKG 80
Cdd:pfam01336   5 GRVTsIRRSGGKLLFLTLRDGTGSIQVVVFKEeaekLAKKLKEGDVVRVT-GKVKKRKG 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH