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Conserved domains on  [gi|1972261161|ref|NP_001380071|]
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Luc7-like protein 3 [Caenorhabditis elegans]

Protein Classification

LUC7 domain-containing protein( domain architecture ID 1903381)

LUC7 domain-containing protein similar to Homo sapiens Luc7-like protein 3 that may play a role in RNA splicing

Gene Ontology:  GO:0003729|GO:0006376|GO:0005685

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LUC7 super family cl44500
LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs ...
3-186 3.05e-64

LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs and only contains eukaryotic proteins. LUC7 has been shown to be a U1 snRNA associated protein with a role in splice site recognition. The family also contains human and mouse LUC7 like (LUC7L) proteins and human cisplatin resistance-associated overexpressed protein (CROP).


The actual alignment was detected with superfamily member pfam03194:

Pssm-ID: 460842 [Multi-domain]  Cd Length: 246  Bit Score: 199.36  E-value: 3.05e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972261161   3 DYMAQMLNELMGSQRDANPGERRE-IRYDDPNVCTDFLVGFCTHDIFRNTKNDLGFCKyTTHDENLKNSYKNSDKKWR-M 80
Cdd:pfam03194   1 DAQRALLDELMGRNRNLAPSEKKKkKHFDDPEVCKSYLVGFCPHDLFTNTKADLGPCP-KIHDEALKADYEKASKRKKkY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972261161  81 GFEKRFLERIRRIHEDVRRKIQKHEDRLAVTQGESKSAEETFGQKIleieqrrEQLTKKMEDLMDEAALEGEKGNVDAAQ 160
Cdd:pfam03194  80 GYEREFLRFLQKLIDDVDRKIRKGKQRLELTQEEIEQTDELKQEQI-------SVLEEKIKKLLEEAEELGEEGNVDEAQ 152
                         170       180
                  ....*....|....*....|....*.
gi 1972261161 161 TAVDRADKAKVEVEELTQEAEKLKSE 186
Cdd:pfam03194 153 KLMKKVEELKEEKEELEQQYESLTKE 178
 
Name Accession Description Interval E-value
LUC7 pfam03194
LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs ...
3-186 3.05e-64

LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs and only contains eukaryotic proteins. LUC7 has been shown to be a U1 snRNA associated protein with a role in splice site recognition. The family also contains human and mouse LUC7 like (LUC7L) proteins and human cisplatin resistance-associated overexpressed protein (CROP).


Pssm-ID: 460842 [Multi-domain]  Cd Length: 246  Bit Score: 199.36  E-value: 3.05e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972261161   3 DYMAQMLNELMGSQRDANPGERRE-IRYDDPNVCTDFLVGFCTHDIFRNTKNDLGFCKyTTHDENLKNSYKNSDKKWR-M 80
Cdd:pfam03194   1 DAQRALLDELMGRNRNLAPSEKKKkKHFDDPEVCKSYLVGFCPHDLFTNTKADLGPCP-KIHDEALKADYEKASKRKKkY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972261161  81 GFEKRFLERIRRIHEDVRRKIQKHEDRLAVTQGESKSAEETFGQKIleieqrrEQLTKKMEDLMDEAALEGEKGNVDAAQ 160
Cdd:pfam03194  80 GYEREFLRFLQKLIDDVDRKIRKGKQRLELTQEEIEQTDELKQEQI-------SVLEEKIKKLLEEAEELGEEGNVDEAQ 152
                         170       180
                  ....*....|....*....|....*.
gi 1972261161 161 TAVDRADKAKVEVEELTQEAEKLKSE 186
Cdd:pfam03194 153 KLMKKVEELKEEKEELEQQYESLTKE 178
LUC7 COG5200
U1 snRNP component, mediates U1 snRNP association with cap-binding complex [RNA processing and ...
1-200 4.50e-22

U1 snRNP component, mediates U1 snRNP association with cap-binding complex [RNA processing and modification];


Pssm-ID: 227527 [Multi-domain]  Cd Length: 258  Bit Score: 90.80  E-value: 4.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972261161   1 MTDYMAQMLNELMGSQRDaNPGERREIRYDDPNVCTDFLVGFCTHDIFRNTKNDLGFCKyTTHDENLKNSYKNSDKKWRM 80
Cdd:COG5200     1 MAAEQRKVLEQLMGPERS-TFDPCRPTHFTDKKVCISMLVGFCPFDLFRNTKRSLGKCP-TSHEEKYKAEYERNGRERAE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972261161  81 GFEKRFLERIRRIHEDVRRKIQKHEDRLAVTQgesksaeetfgqkilEIEQRREQLTKKMEDLMDEAALEGEKGNVDAAQ 160
Cdd:COG5200    79 EYEWEYLRLLVRIVLSCNDGIRAAGLEDRTTP---------------EEFGKIKEKEELFNRVDESIGELGMEGDALAKR 143
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1972261161 161 TAVDRADKAKVEVEELTqeaEKLKSEKERAINMEENVTAA 200
Cdd:COG5200   144 KLVERACSAFNELERLR---EERKEIKEAVYSMVENNGQG 180
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
85-189 3.20e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.13  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972261161   85 RFLERIRRIHEDV---RRKIQKHEDRLAVTQGESKSAEETFGQKILEIEQ----------RREQLTKKMEDLMDE-AALE 150
Cdd:TIGR02169  291 RVKEKIGELEAEIaslERSIAEKERELEDAEERLAKLEAEIDKLLAEIEElereieeerkRRDKLTEEYAELKEElEDLR 370
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1972261161  151 GEKGNVDA-AQTAVDRADKAKVEVEELTQEAEKLKSEKER 189
Cdd:TIGR02169  371 AELEEVDKeFAETRDELKDYREKLEKLKREINELKRELDR 410
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
87-195 4.83e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 37.71  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972261161  87 LERIRRIHEDVRRKI------QKHEDRLAVTQGESKSAEETFGQKILEIEQRREQLTKKMEDlMDEAALEGEkGNVDAAQ 160
Cdd:PRK02224  484 LEDLEEEVEEVEERLeraedlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-AAELEAEAE-EKREAAA 561
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1972261161 161 TAVDRADKAKVEVEELTQEAEKLKSEKERAINMEE 195
Cdd:PRK02224  562 EAEEEAEEAREEVAELNSKLAELKERIESLERIRT 596
 
Name Accession Description Interval E-value
LUC7 pfam03194
LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs ...
3-186 3.05e-64

LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs and only contains eukaryotic proteins. LUC7 has been shown to be a U1 snRNA associated protein with a role in splice site recognition. The family also contains human and mouse LUC7 like (LUC7L) proteins and human cisplatin resistance-associated overexpressed protein (CROP).


Pssm-ID: 460842 [Multi-domain]  Cd Length: 246  Bit Score: 199.36  E-value: 3.05e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972261161   3 DYMAQMLNELMGSQRDANPGERRE-IRYDDPNVCTDFLVGFCTHDIFRNTKNDLGFCKyTTHDENLKNSYKNSDKKWR-M 80
Cdd:pfam03194   1 DAQRALLDELMGRNRNLAPSEKKKkKHFDDPEVCKSYLVGFCPHDLFTNTKADLGPCP-KIHDEALKADYEKASKRKKkY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972261161  81 GFEKRFLERIRRIHEDVRRKIQKHEDRLAVTQGESKSAEETFGQKIleieqrrEQLTKKMEDLMDEAALEGEKGNVDAAQ 160
Cdd:pfam03194  80 GYEREFLRFLQKLIDDVDRKIRKGKQRLELTQEEIEQTDELKQEQI-------SVLEEKIKKLLEEAEELGEEGNVDEAQ 152
                         170       180
                  ....*....|....*....|....*.
gi 1972261161 161 TAVDRADKAKVEVEELTQEAEKLKSE 186
Cdd:pfam03194 153 KLMKKVEELKEEKEELEQQYESLTKE 178
LUC7 COG5200
U1 snRNP component, mediates U1 snRNP association with cap-binding complex [RNA processing and ...
1-200 4.50e-22

U1 snRNP component, mediates U1 snRNP association with cap-binding complex [RNA processing and modification];


Pssm-ID: 227527 [Multi-domain]  Cd Length: 258  Bit Score: 90.80  E-value: 4.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972261161   1 MTDYMAQMLNELMGSQRDaNPGERREIRYDDPNVCTDFLVGFCTHDIFRNTKNDLGFCKyTTHDENLKNSYKNSDKKWRM 80
Cdd:COG5200     1 MAAEQRKVLEQLMGPERS-TFDPCRPTHFTDKKVCISMLVGFCPFDLFRNTKRSLGKCP-TSHEEKYKAEYERNGRERAE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972261161  81 GFEKRFLERIRRIHEDVRRKIQKHEDRLAVTQgesksaeetfgqkilEIEQRREQLTKKMEDLMDEAALEGEKGNVDAAQ 160
Cdd:COG5200    79 EYEWEYLRLLVRIVLSCNDGIRAAGLEDRTTP---------------EEFGKIKEKEELFNRVDESIGELGMEGDALAKR 143
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1972261161 161 TAVDRADKAKVEVEELTqeaEKLKSEKERAINMEENVTAA 200
Cdd:COG5200   144 KLVERACSAFNELERLR---EERKEIKEAVYSMVENNGQG 180
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
85-189 3.20e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.13  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972261161   85 RFLERIRRIHEDV---RRKIQKHEDRLAVTQGESKSAEETFGQKILEIEQ----------RREQLTKKMEDLMDE-AALE 150
Cdd:TIGR02169  291 RVKEKIGELEAEIaslERSIAEKERELEDAEERLAKLEAEIDKLLAEIEElereieeerkRRDKLTEEYAELKEElEDLR 370
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1972261161  151 GEKGNVDA-AQTAVDRADKAKVEVEELTQEAEKLKSEKER 189
Cdd:TIGR02169  371 AELEEVDKeFAETRDELKDYREKLEKLKREINELKRELDR 410
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
87-195 4.83e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 37.71  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972261161  87 LERIRRIHEDVRRKI------QKHEDRLAVTQGESKSAEETFGQKILEIEQRREQLTKKMEDlMDEAALEGEkGNVDAAQ 160
Cdd:PRK02224  484 LEDLEEEVEEVEERLeraedlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER-AAELEAEAE-EKREAAA 561
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1972261161 161 TAVDRADKAKVEVEELTQEAEKLKSEKERAINMEE 195
Cdd:PRK02224  562 EAEEEAEEAREEVAELNSKLAELKERIESLERIRT 596
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
84-191 6.31e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 36.83  E-value: 6.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972261161  84 KRFLERIRRIHEDVRRKIQKHEDRLavtqGESKSAEE--TFGQKILEIEQRREQLTKKMEDLMD-----EAALEGEKGNV 156
Cdd:COG1579    58 EKEIKRLELEIEEVEARIKKYEEQL----GNVRNNKEyeALQKEIESLKRRISDLEDEILELMErieelEEELAELEAEL 133
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1972261161 157 DAAQTAVDRA-DKAKVEVEELTQEAEKLKSEKERAI 191
Cdd:COG1579   134 AELEAELEEKkAELDEELAELEAELEELEAEREELA 169
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
87-200 8.95e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 36.84  E-value: 8.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972261161  87 LERIRRIHEDVRRKIQKHEDRLAVTQGESKSAEETFGQKILEIEQRREQLTKKMEDLmdEAALEGEKGNVDAAQTAVDRA 166
Cdd:COG1196   318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL--AEAEEELEELAEELLEALRAA 395
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1972261161 167 DKAKVEVEELTQEAEKLKSEKERAINMEENVTAA 200
Cdd:COG1196   396 AELAAQLEELEEAEEALLERLERLEEELEELEEA 429
 
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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