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Conserved domains on  [gi|376319229|ref|NP_001243663|]
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single-stranded DNA-binding protein 2 isoform 4 [Homo sapiens]

Protein Classification

single-stranded DNA-binding protein( domain architecture ID 12218102)

single-stranded DNA-binding protein interacts with Lim domain binding proteins (LBDs) and stabilize LDBs by preventing their proteasomal degradation, thus promoting their functions in gene regulation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SSDP pfam04503
Single-stranded DNA binding protein, SSDP; This is a family of eukaryotic single-stranded DNA ...
 92-316 2.51e-45

Single-stranded DNA binding protein, SSDP; This is a family of eukaryotic single-stranded DNA binding proteins with specificity to a pyrimidine-rich element found in the promoter region of the alpha2(I) collagen gene.


:

Pssm-ID: 461334 [Multi-domain]  Cd Length: 293  Bit Score: 156.27  E-value: 2.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319229   92 HDYPFMSPRYPGGPRPPLRIPNQA--LGGVPGSQPLLPSGMDPTRQQGHPNMGGPMQRMTPPRG--MVPLGPQsdpwlsl 167
Cdd:pfam04503  73 HSQPFMGPRYPGGPRPSVRMPQQGndFNGPPGQQPMMPNSMDPTRPGGHPNMGGPMQRMNPPRGpgMGPMGPQ------- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319229  168 qNYGGAMR--PPLNALGGPGMPGMNMGPGGGRPWPNPTNANSIPYSSASPGNYVGPPGGGGPPGTPI-MPSPADSTNSGD 244
Cdd:pfam04503 146 -SYGPGMRgpPPNSTDGPGGMPPMNMGPGGRRPWPQPNASNPLPYSSSSPGSYGGPPGGGGPPGPTPiMPSPQDSTNSGE 224

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 376319229  245 NMYTLMNAVPPGPNRPNFPMGPGSDGPMGGlGGMESHHMNGSLGSGDMDSIsKNSPNNMsLSNQPGTPRDDG 316
Cdd:pfam04503 225 NMYTLMNPVGPGGNRANFPMGPGLEGPMGP-NGMEPHHSNGSLGSGDMDGM-KNSPANV-LSNGPGTPREDG 293
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 19-45 6.53e-03

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


:

Pssm-ID: 128913  Cd Length: 34  Bit Score: 33.95  E-value: 6.53e-03
                           10        20
                   ....*....|....*....|....*..
gi 376319229    19 REKLALYVYEYLLHVGAQKSAQTFLSE 45
Cdd:smart00667   3 RSELNRLILEYLLRNGYEETAETLQKE 29
 
Name Accession Description Interval E-value
SSDP pfam04503
Single-stranded DNA binding protein, SSDP; This is a family of eukaryotic single-stranded DNA ...
 92-316 2.51e-45

Single-stranded DNA binding protein, SSDP; This is a family of eukaryotic single-stranded DNA binding proteins with specificity to a pyrimidine-rich element found in the promoter region of the alpha2(I) collagen gene.


Pssm-ID: 461334 [Multi-domain]  Cd Length: 293  Bit Score: 156.27  E-value: 2.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319229   92 HDYPFMSPRYPGGPRPPLRIPNQA--LGGVPGSQPLLPSGMDPTRQQGHPNMGGPMQRMTPPRG--MVPLGPQsdpwlsl 167
Cdd:pfam04503  73 HSQPFMGPRYPGGPRPSVRMPQQGndFNGPPGQQPMMPNSMDPTRPGGHPNMGGPMQRMNPPRGpgMGPMGPQ------- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319229  168 qNYGGAMR--PPLNALGGPGMPGMNMGPGGGRPWPNPTNANSIPYSSASPGNYVGPPGGGGPPGTPI-MPSPADSTNSGD 244
Cdd:pfam04503 146 -SYGPGMRgpPPNSTDGPGGMPPMNMGPGGRRPWPQPNASNPLPYSSSSPGSYGGPPGGGGPPGPTPiMPSPQDSTNSGE 224

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 376319229  245 NMYTLMNAVPPGPNRPNFPMGPGSDGPMGGlGGMESHHMNGSLGSGDMDSIsKNSPNNMsLSNQPGTPRDDG 316
Cdd:pfam04503 225 NMYTLMNPVGPGGNRANFPMGPGLEGPMGP-NGMEPHHSNGSLGSGDMDGM-KNSPANV-LSNGPGTPREDG 293
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 19-45 6.53e-03

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 33.95  E-value: 6.53e-03
                           10        20
                   ....*....|....*....|....*..
gi 376319229    19 REKLALYVYEYLLHVGAQKSAQTFLSE 45
Cdd:smart00667   3 RSELNRLILEYLLRNGYEETAETLQKE 29
 
Name Accession Description Interval E-value
SSDP pfam04503
Single-stranded DNA binding protein, SSDP; This is a family of eukaryotic single-stranded DNA ...
 92-316 2.51e-45

Single-stranded DNA binding protein, SSDP; This is a family of eukaryotic single-stranded DNA binding proteins with specificity to a pyrimidine-rich element found in the promoter region of the alpha2(I) collagen gene.


Pssm-ID: 461334 [Multi-domain]  Cd Length: 293  Bit Score: 156.27  E-value: 2.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319229   92 HDYPFMSPRYPGGPRPPLRIPNQA--LGGVPGSQPLLPSGMDPTRQQGHPNMGGPMQRMTPPRG--MVPLGPQsdpwlsl 167
Cdd:pfam04503  73 HSQPFMGPRYPGGPRPSVRMPQQGndFNGPPGQQPMMPNSMDPTRPGGHPNMGGPMQRMNPPRGpgMGPMGPQ------- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319229  168 qNYGGAMR--PPLNALGGPGMPGMNMGPGGGRPWPNPTNANSIPYSSASPGNYVGPPGGGGPPGTPI-MPSPADSTNSGD 244
Cdd:pfam04503 146 -SYGPGMRgpPPNSTDGPGGMPPMNMGPGGRRPWPQPNASNPLPYSSSSPGSYGGPPGGGGPPGPTPiMPSPQDSTNSGE 224

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 376319229  245 NMYTLMNAVPPGPNRPNFPMGPGSDGPMGGlGGMESHHMNGSLGSGDMDSIsKNSPNNMsLSNQPGTPRDDG 316
Cdd:pfam04503 225 NMYTLMNPVGPGGNRANFPMGPGLEGPMGP-NGMEPHHSNGSLGSGDMDGM-KNSPANV-LSNGPGTPREDG 293
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 19-45 6.53e-03

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 33.95  E-value: 6.53e-03
                           10        20
                   ....*....|....*....|....*..
gi 376319229    19 REKLALYVYEYLLHVGAQKSAQTFLSE 45
Cdd:smart00667   3 RSELNRLILEYLLRNGYEETAETLQKE 29
 
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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