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Conserved domains on  [gi|17562300|ref|NP_505661|]
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Pre-mRNA-splicing factor SLU7 [Caenorhabditis elegans]

Protein Classification

Slu7 domain-containing protein( domain architecture ID 10443465)

Slu7 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Slu7 pfam11708
Pre-mRNA splicing Prp18-interacting factor; The spliceosome, an assembly of snRNAs (U1, U2, U4 ...
 156-410 3.03e-117

Pre-mRNA splicing Prp18-interacting factor; The spliceosome, an assembly of snRNAs (U1, U2, U4/U6, and U5) and proteins, catalyzes the excision of introns from pre-mRNAs in two successive trans-esterification reactions. Step 2 depends upon integral spliceosome constituents such as U5 snRNA and Prp8 and non-spliceosomal proteins Prp16, Slu7, Prp18, and Prp22. ATP hydrolysis by the DEAH-box enzyme Prp16 promotes a conformational change in the spliceosome that leads to protection of the 3'ss from targeted RNase H cleavage. This change, which probably reflects binding of the 3'ss PyAG in the catalytic centre of the spliceosome, requires the ordered recruitment of Slu7, Prp18, and Prp22 to the spliceosome. There is a close functional relationship between Prp8, Prp18, and Slu7, and Prp18 interacts with Slu7, so that together they recruit Prp22 to the spliceosome. Most members of the family carry a zinc-finger of the CCHC-type upstream of this domain.


:

Pssm-ID: 463326  Cd Length: 258  Bit Score: 350.41  E-value: 3.03e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562300   156 LGFDAKRDRWNGYDPSTHKQVIEDYEHLEEARKVVREHEMKEGEVEPATTED------GAPKDEDMYAEDADMAGVSVDm 229
Cdd:pfam11708   1 LGYDAKRDRWNGYDPSEYKKVVEEYEKLEEARKKLKEEELDKKEKDDEGDDDdseeedNDDEDEDKYADEADMGGQKVD- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562300   230 dSRTRITVRNLRIREDTAKYLYNLAENSPYYDPKSRSMRENPFAGVAGKELEAaRFSGDNFVRYSGEVTAANEAQVFAWQ 309
Cdd:pfam11708  80 -SKQRTTVRNLRIREDTAKYLLNLDLNSAYYDPKTRSMRDNPLPNVDPSEDKA-LFAGDNFVRASGDAAEFEKLQRFAWE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562300   310 ATRGGVYAHSIAEPTKLEALKKEYEKEKSTLKNETQKELLDKYGGGEHMERPADELLLAQTESYIEYNRKGKVIKGKEKV 389
Cdd:pfam11708 158 AQEKGDDVHLQANPTQAELLYKEFKEKKEKLKEKKKKSILEKYGGEEHLEAPPKELLLAQTERYVEYDRSGRVIKGQEKA 237

                         250       260
                  ....*....|....*....|.
gi 17562300   390 AISSRFKEDIYPQNHTSVFGS 410
Cdd:pfam11708 238 KAKSKYEEDVYINNHTSVWGS 258
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
 113-128 3.79e-03

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


:

Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 35.20  E-value: 3.79e-03
                          10
                  ....*....|....*.
gi 17562300   113 GACENCGAMGHQKRDC 128
Cdd:pfam00098   1 GKCYNCGEPGHIARDC 16
 
Name Accession Description Interval E-value
Slu7 pfam11708
Pre-mRNA splicing Prp18-interacting factor; The spliceosome, an assembly of snRNAs (U1, U2, U4 ...
 156-410 3.03e-117

Pre-mRNA splicing Prp18-interacting factor; The spliceosome, an assembly of snRNAs (U1, U2, U4/U6, and U5) and proteins, catalyzes the excision of introns from pre-mRNAs in two successive trans-esterification reactions. Step 2 depends upon integral spliceosome constituents such as U5 snRNA and Prp8 and non-spliceosomal proteins Prp16, Slu7, Prp18, and Prp22. ATP hydrolysis by the DEAH-box enzyme Prp16 promotes a conformational change in the spliceosome that leads to protection of the 3'ss from targeted RNase H cleavage. This change, which probably reflects binding of the 3'ss PyAG in the catalytic centre of the spliceosome, requires the ordered recruitment of Slu7, Prp18, and Prp22 to the spliceosome. There is a close functional relationship between Prp8, Prp18, and Slu7, and Prp18 interacts with Slu7, so that together they recruit Prp22 to the spliceosome. Most members of the family carry a zinc-finger of the CCHC-type upstream of this domain.


Pssm-ID: 463326  Cd Length: 258  Bit Score: 350.41  E-value: 3.03e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562300   156 LGFDAKRDRWNGYDPSTHKQVIEDYEHLEEARKVVREHEMKEGEVEPATTED------GAPKDEDMYAEDADMAGVSVDm 229
Cdd:pfam11708   1 LGYDAKRDRWNGYDPSEYKKVVEEYEKLEEARKKLKEEELDKKEKDDEGDDDdseeedNDDEDEDKYADEADMGGQKVD- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562300   230 dSRTRITVRNLRIREDTAKYLYNLAENSPYYDPKSRSMRENPFAGVAGKELEAaRFSGDNFVRYSGEVTAANEAQVFAWQ 309
Cdd:pfam11708  80 -SKQRTTVRNLRIREDTAKYLLNLDLNSAYYDPKTRSMRDNPLPNVDPSEDKA-LFAGDNFVRASGDAAEFEKLQRFAWE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562300   310 ATRGGVYAHSIAEPTKLEALKKEYEKEKSTLKNETQKELLDKYGGGEHMERPADELLLAQTESYIEYNRKGKVIKGKEKV 389
Cdd:pfam11708 158 AQEKGDDVHLQANPTQAELLYKEFKEKKEKLKEKKKKSILEKYGGEEHLEAPPKELLLAQTERYVEYDRSGRVIKGQEKA 237

                         250       260
                  ....*....|....*....|.
gi 17562300   390 AISSRFKEDIYPQNHTSVFGS 410
Cdd:pfam11708 238 KAKSKYEEDVYINNHTSVWGS 258
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
 113-128 3.79e-03

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 35.20  E-value: 3.79e-03
                          10
                  ....*....|....*.
gi 17562300   113 GACENCGAMGHQKRDC 128
Cdd:pfam00098   1 GKCYNCGEPGHIARDC 16
 
Name Accession Description Interval E-value
Slu7 pfam11708
Pre-mRNA splicing Prp18-interacting factor; The spliceosome, an assembly of snRNAs (U1, U2, U4 ...
 156-410 3.03e-117

Pre-mRNA splicing Prp18-interacting factor; The spliceosome, an assembly of snRNAs (U1, U2, U4/U6, and U5) and proteins, catalyzes the excision of introns from pre-mRNAs in two successive trans-esterification reactions. Step 2 depends upon integral spliceosome constituents such as U5 snRNA and Prp8 and non-spliceosomal proteins Prp16, Slu7, Prp18, and Prp22. ATP hydrolysis by the DEAH-box enzyme Prp16 promotes a conformational change in the spliceosome that leads to protection of the 3'ss from targeted RNase H cleavage. This change, which probably reflects binding of the 3'ss PyAG in the catalytic centre of the spliceosome, requires the ordered recruitment of Slu7, Prp18, and Prp22 to the spliceosome. There is a close functional relationship between Prp8, Prp18, and Slu7, and Prp18 interacts with Slu7, so that together they recruit Prp22 to the spliceosome. Most members of the family carry a zinc-finger of the CCHC-type upstream of this domain.


Pssm-ID: 463326  Cd Length: 258  Bit Score: 350.41  E-value: 3.03e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562300   156 LGFDAKRDRWNGYDPSTHKQVIEDYEHLEEARKVVREHEMKEGEVEPATTED------GAPKDEDMYAEDADMAGVSVDm 229
Cdd:pfam11708   1 LGYDAKRDRWNGYDPSEYKKVVEEYEKLEEARKKLKEEELDKKEKDDEGDDDdseeedNDDEDEDKYADEADMGGQKVD- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562300   230 dSRTRITVRNLRIREDTAKYLYNLAENSPYYDPKSRSMRENPFAGVAGKELEAaRFSGDNFVRYSGEVTAANEAQVFAWQ 309
Cdd:pfam11708  80 -SKQRTTVRNLRIREDTAKYLLNLDLNSAYYDPKTRSMRDNPLPNVDPSEDKA-LFAGDNFVRASGDAAEFEKLQRFAWE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17562300   310 ATRGGVYAHSIAEPTKLEALKKEYEKEKSTLKNETQKELLDKYGGGEHMERPADELLLAQTESYIEYNRKGKVIKGKEKV 389
Cdd:pfam11708 158 AQEKGDDVHLQANPTQAELLYKEFKEKKEKLKEKKKKSILEKYGGEEHLEAPPKELLLAQTERYVEYDRSGRVIKGQEKA 237

                         250       260
                  ....*....|....*....|.
gi 17562300   390 AISSRFKEDIYPQNHTSVFGS 410
Cdd:pfam11708 238 KAKSKYEEDVYINNHTSVWGS 258
zf-CCHC pfam00098
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ...
 113-128 3.79e-03

Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.


Pssm-ID: 395050 [Multi-domain]  Cd Length: 18  Bit Score: 35.20  E-value: 3.79e-03
                          10
                  ....*....|....*.
gi 17562300   113 GACENCGAMGHQKRDC 128
Cdd:pfam00098   1 GKCYNCGEPGHIARDC 16
 
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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