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Conserved domains on  [gi|56549113|ref|NP_057300|]
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lariat debranching enzyme [Homo sapiens]

Protein Classification

lariat debranching enzyme( domain architecture ID 10096188)

lariat debranching enzyme cleaves the 2'-5' phosphodiester linkage at the branch point of lariat intron pre-mRNAs after splicing and converts them into linear molecules that are subsequently degraded

CATH:  3.60.21.10
EC:  3.1.-.-
Gene Ontology:  GO:0046872|GO:0008419|GO:0003723
PubMed:  25837850|11586896|8003970
SCOP:  3001067

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_Dbr1_N cd00844
Dbr1 RNA lariat debranching enzyme, N-terminal metallophosphatase domain; Dbr1 is an RNA ...
 3-264 0e+00

Dbr1 RNA lariat debranching enzyme, N-terminal metallophosphatase domain; Dbr1 is an RNA lariat debranching enzyme that hydrolyzes 2'-5' phosphodiester bonds at the branch points of excised intron lariats. This alignment model represents the N-terminal metallophosphatase domain of Dbr1. This domain belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


:

Pssm-ID: 277322 [Multi-domain]  Cd Length: 271  Bit Score: 537.61  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113   3 VAVAGCCHGELDKIYETLALAERRGPGPVDLLLCCGDFQAVRNEADLRCMAVPPKYRHMQTFYRYYSGEKKAPVLTLFIG 82
Cdd:cd00844   1 IAVEGCCHGELDKIYETLEKYEKKNGTKVDLLICCGDFQAVRNEADLKCMAVPPKYKKMGDFHKYYSGEKKAPILTIFIG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113  83 GNHEASNHLQELPYGGWVAPNIYYLGLAGVVKYRGVRIGGISGIFKSHDYRKGHFECPPYNSSTIRSIYHVRNIEVYKLK 162
Cdd:cd00844  81 GNHEASNYLWELPYGGWVAPNIYYLGYAGVVNFGGLRIGGISGIYKSHDYKKGHFERPPYNPSTIRSAYHVRNIDVFKLK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113 163 QLKQPIDIFLSHDWPRSIYHYGNKKQLLKTKSFFRQEVENNTLGSPAASELLEHLKPTYWFSAHLHVKFAALMQHQAKD- 241
Cdd:cd00844 161 QLKHPIDIFLSHDWPRGIEKHGDKKQLLRRKPFFRQDIESGTLGSPAAEELLEHLKPRYWFSAHLHVKFAALVQHENQEs 240

                       250       260       270
                ....*....|....*....|....*....|.
gi 56549113 242 --------KGQTARATKFLALDKCLPHRDFL 264
Cdd:cd00844 241 ttpigttnKTKTNLETRFLALDKCLPGRDFL 271
DBR1 pfam05011
Lariat debranching enzyme, C-terminal domain; This presumed domain is found at the C-terminus ...
 246-379 5.90e-52

Lariat debranching enzyme, C-terminal domain; This presumed domain is found at the C-terminus of lariat debranching enzyme. This domain is always found in association with pfam00149.


:

Pssm-ID: 461518  Cd Length: 136  Bit Score: 173.55  E-value: 5.90e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113   246 ARATKFLALDKCLPHRDFLQILEIEHDP----SAPDYLEYDIEWLTILRATDDLINVTGRLWNMPENNGLhaRWDYSATE 321
Cdd:pfam05011   1 NKVTKFLALDKCLPRRDFLQVLEIPSPEpspeSGPPELEYDPEWLAITRAFNPLLSVDPSQAPLPGDKGE--REYRPLIE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 56549113   322 EGMKEVLEKL-NHDLKVPCNFSVTAAcYDPSKPQTQMQLIHRINPQTTEFCAQLGIIDI 379
Cdd:pfam05011  79 EELKWVEENIvKGDLKIPENFVRTAP-VDPEGITTSEQPPEYTNPQTEAFCELLGIENK 136
 
Name Accession Description Interval E-value
MPP_Dbr1_N cd00844
Dbr1 RNA lariat debranching enzyme, N-terminal metallophosphatase domain; Dbr1 is an RNA ...
 3-264 0e+00

Dbr1 RNA lariat debranching enzyme, N-terminal metallophosphatase domain; Dbr1 is an RNA lariat debranching enzyme that hydrolyzes 2'-5' phosphodiester bonds at the branch points of excised intron lariats. This alignment model represents the N-terminal metallophosphatase domain of Dbr1. This domain belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277322 [Multi-domain]  Cd Length: 271  Bit Score: 537.61  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113   3 VAVAGCCHGELDKIYETLALAERRGPGPVDLLLCCGDFQAVRNEADLRCMAVPPKYRHMQTFYRYYSGEKKAPVLTLFIG 82
Cdd:cd00844   1 IAVEGCCHGELDKIYETLEKYEKKNGTKVDLLICCGDFQAVRNEADLKCMAVPPKYKKMGDFHKYYSGEKKAPILTIFIG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113  83 GNHEASNHLQELPYGGWVAPNIYYLGLAGVVKYRGVRIGGISGIFKSHDYRKGHFECPPYNSSTIRSIYHVRNIEVYKLK 162
Cdd:cd00844  81 GNHEASNYLWELPYGGWVAPNIYYLGYAGVVNFGGLRIGGISGIYKSHDYKKGHFERPPYNPSTIRSAYHVRNIDVFKLK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113 163 QLKQPIDIFLSHDWPRSIYHYGNKKQLLKTKSFFRQEVENNTLGSPAASELLEHLKPTYWFSAHLHVKFAALMQHQAKD- 241
Cdd:cd00844 161 QLKHPIDIFLSHDWPRGIEKHGDKKQLLRRKPFFRQDIESGTLGSPAAEELLEHLKPRYWFSAHLHVKFAALVQHENQEs 240

                       250       260       270
                ....*....|....*....|....*....|.
gi 56549113 242 --------KGQTARATKFLALDKCLPHRDFL 264
Cdd:cd00844 241 ttpigttnKTKTNLETRFLALDKCLPGRDFL 271
DBR1 pfam05011
Lariat debranching enzyme, C-terminal domain; This presumed domain is found at the C-terminus ...
 246-379 5.90e-52

Lariat debranching enzyme, C-terminal domain; This presumed domain is found at the C-terminus of lariat debranching enzyme. This domain is always found in association with pfam00149.


Pssm-ID: 461518  Cd Length: 136  Bit Score: 173.55  E-value: 5.90e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113   246 ARATKFLALDKCLPHRDFLQILEIEHDP----SAPDYLEYDIEWLTILRATDDLINVTGRLWNMPENNGLhaRWDYSATE 321
Cdd:pfam05011   1 NKVTKFLALDKCLPRRDFLQVLEIPSPEpspeSGPPELEYDPEWLAITRAFNPLLSVDPSQAPLPGDKGE--REYRPLIE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 56549113   322 EGMKEVLEKL-NHDLKVPCNFSVTAAcYDPSKPQTQMQLIHRINPQTTEFCAQLGIIDI 379
Cdd:pfam05011  79 EELKWVEENIvKGDLKIPENFVRTAP-VDPEGITTSEQPPEYTNPQTEAFCELLGIENK 136
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
2-228 4.23e-13

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 68.50  E-value: 4.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113   2 RVAVAGCCHGELDKIYETLALAERRGPgpvDLLLCCGDFqavrneadlrcmavpPKYRHMQTFYRYYSGEKKAPVLTLFI 81
Cdd:COG2129   1 KILAVSDLHGNFDLLEKLLELARAEDA---DLVILAGDL---------------TDFGTAEEAREVLEELAALGVPVLAV 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113  82 GGNHEASNHLQELPyggwvAPNIYYLglAG-VVKYRGVRIGGISGIfkshdyRKGHFECPPYNS-STIRSiyhvrnievy 159
Cdd:COG2129  63 PGNHDDPEVLDALE-----ESGVHNL--HGrVVEIGGLRIAGLGGS------RPTPFGTPYEYTeEEIEE---------- 119

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56549113 160 KLKQL-KQPIDIFLSHDWPRSIyhygnkkqllktksfFRQEVENNT-LGSPAASELLEHLKPTYWFSAHLH 228
Cdd:COG2129 120 RLAKLrEKDVDILLTHAPPYGT---------------TLDRVEDGPhVGSKALRELIEEFQPKLVLHGHIH 175
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-115 2.10e-03

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 37.96  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113     1 MRVAVAGCCH--GELDKIYETLALAERrgPGPVDLLLCCGDFqavrneadlrcmavPPKYRHMQTFYRYYSgEKKAPVLT 78
Cdd:pfam00149   1 MRILVIGDLHlpGQLDDLLELLKKLLE--EGKPDLVLHAGDL--------------VDRGPPSEEVLELLE-RLIKYVPV 63

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 56549113    79 LFIGGNHEASNHLQELPYGGWVAPNIYYLGLAGVVKY 115
Cdd:pfam00149  64 YLVRGNHDFDYGECLRLYPYLGLLARPWKRFLEVFNF 100
 
Name Accession Description Interval E-value
MPP_Dbr1_N cd00844
Dbr1 RNA lariat debranching enzyme, N-terminal metallophosphatase domain; Dbr1 is an RNA ...
 3-264 0e+00

Dbr1 RNA lariat debranching enzyme, N-terminal metallophosphatase domain; Dbr1 is an RNA lariat debranching enzyme that hydrolyzes 2'-5' phosphodiester bonds at the branch points of excised intron lariats. This alignment model represents the N-terminal metallophosphatase domain of Dbr1. This domain belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277322 [Multi-domain]  Cd Length: 271  Bit Score: 537.61  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113   3 VAVAGCCHGELDKIYETLALAERRGPGPVDLLLCCGDFQAVRNEADLRCMAVPPKYRHMQTFYRYYSGEKKAPVLTLFIG 82
Cdd:cd00844   1 IAVEGCCHGELDKIYETLEKYEKKNGTKVDLLICCGDFQAVRNEADLKCMAVPPKYKKMGDFHKYYSGEKKAPILTIFIG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113  83 GNHEASNHLQELPYGGWVAPNIYYLGLAGVVKYRGVRIGGISGIFKSHDYRKGHFECPPYNSSTIRSIYHVRNIEVYKLK 162
Cdd:cd00844  81 GNHEASNYLWELPYGGWVAPNIYYLGYAGVVNFGGLRIGGISGIYKSHDYKKGHFERPPYNPSTIRSAYHVRNIDVFKLK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113 163 QLKQPIDIFLSHDWPRSIYHYGNKKQLLKTKSFFRQEVENNTLGSPAASELLEHLKPTYWFSAHLHVKFAALMQHQAKD- 241
Cdd:cd00844 161 QLKHPIDIFLSHDWPRGIEKHGDKKQLLRRKPFFRQDIESGTLGSPAAEELLEHLKPRYWFSAHLHVKFAALVQHENQEs 240

                       250       260       270
                ....*....|....*....|....*....|.
gi 56549113 242 --------KGQTARATKFLALDKCLPHRDFL 264
Cdd:cd00844 241 ttpigttnKTKTNLETRFLALDKCLPGRDFL 271
DBR1 pfam05011
Lariat debranching enzyme, C-terminal domain; This presumed domain is found at the C-terminus ...
 246-379 5.90e-52

Lariat debranching enzyme, C-terminal domain; This presumed domain is found at the C-terminus of lariat debranching enzyme. This domain is always found in association with pfam00149.


Pssm-ID: 461518  Cd Length: 136  Bit Score: 173.55  E-value: 5.90e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113   246 ARATKFLALDKCLPHRDFLQILEIEHDP----SAPDYLEYDIEWLTILRATDDLINVTGRLWNMPENNGLhaRWDYSATE 321
Cdd:pfam05011   1 NKVTKFLALDKCLPRRDFLQVLEIPSPEpspeSGPPELEYDPEWLAITRAFNPLLSVDPSQAPLPGDKGE--REYRPLIE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 56549113   322 EGMKEVLEKL-NHDLKVPCNFSVTAAcYDPSKPQTQMQLIHRINPQTTEFCAQLGIIDI 379
Cdd:pfam05011  79 EELKWVEENIvKGDLKIPENFVRTAP-VDPEGITTSEQPPEYTNPQTEAFCELLGIENK 136
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
2-228 4.23e-13

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 68.50  E-value: 4.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113   2 RVAVAGCCHGELDKIYETLALAERRGPgpvDLLLCCGDFqavrneadlrcmavpPKYRHMQTFYRYYSGEKKAPVLTLFI 81
Cdd:COG2129   1 KILAVSDLHGNFDLLEKLLELARAEDA---DLVILAGDL---------------TDFGTAEEAREVLEELAALGVPVLAV 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113  82 GGNHEASNHLQELPyggwvAPNIYYLglAG-VVKYRGVRIGGISGIfkshdyRKGHFECPPYNS-STIRSiyhvrnievy 159
Cdd:COG2129  63 PGNHDDPEVLDALE-----ESGVHNL--HGrVVEIGGLRIAGLGGS------RPTPFGTPYEYTeEEIEE---------- 119

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56549113 160 KLKQL-KQPIDIFLSHDWPRSIyhygnkkqllktksfFRQEVENNT-LGSPAASELLEHLKPTYWFSAHLH 228
Cdd:COG2129 120 RLAKLrEKDVDILLTHAPPYGT---------------TLDRVEDGPhVGSKALRELIEEFQPKLVLHGHIH 175
MPP_CWF19_N cd07380
Schizosaccharomyces pombe CWF19 and related proteins, N-terminal metallophosphatase domain; ...
 165-254 1.19e-06

Schizosaccharomyces pombe CWF19 and related proteins, N-terminal metallophosphatase domain; CWF19 cell cycle control protein (also known as CWF19-like 1 (CWF19L1) in Homo sapiens), N-terminal metallophosphatase domain. CWF19 contains C-terminal domains similar to that found in the CwfJ cell cycle control protein. The metallophosphatase domain belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277326  Cd Length: 149  Bit Score: 48.45  E-value: 1.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113 165 KQPIDIFLSHDWPRSIYHYGnkkqllktKSFFrqEVENNTLGSPAASELLEHLKPTYWFSAhLHVKFAALMQHQ-AKDKG 243
Cdd:cd07380  67 NGGVDILLTSEWPKGISKLS--------KSPF--EPDLLISGSDLIAELAKKLKPRYHFAG-LEGVFYEREPYRnDSVLE 135

                        90
                ....*....|.
gi 56549113 244 QTARATKFLAL 254
Cdd:cd07380 136 KAEHVTRFIGL 146
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-115 2.10e-03

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 37.96  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56549113     1 MRVAVAGCCH--GELDKIYETLALAERrgPGPVDLLLCCGDFqavrneadlrcmavPPKYRHMQTFYRYYSgEKKAPVLT 78
Cdd:pfam00149   1 MRILVIGDLHlpGQLDDLLELLKKLLE--EGKPDLVLHAGDL--------------VDRGPPSEEVLELLE-RLIKYVPV 63

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 56549113    79 LFIGGNHEASNHLQELPYGGWVAPNIYYLGLAGVVKY 115
Cdd:pfam00149  64 YLVRGNHDFDYGECLRLYPYLGLLARPWKRFLEVFNF 100
 
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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