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Conserved domains on  [gi|2462510435|ref|XP_054193184|]
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transcriptional protein SWT1 isoform X1 [Homo sapiens]

Protein Classification

PIN_Swt1-like domain-containing protein( domain architecture ID 13036856)

PIN_Swt1-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PIN_Swt1-like cd18727
VapC-like PIN domain of Saccharomyces cerevisiae Swt1p, human SWT1 and related proteins; ...
 398-539 1.89e-46

VapC-like PIN domain of Saccharomyces cerevisiae Swt1p, human SWT1 and related proteins; Saccharomyces cerevisiae mRNA-processing endoribonuclease Swt1p plays an important role in quality control of nuclear mRNPs in eukaryotes. Human transcriptional protein SWT1 (RNA endoribonuclease homolog, also known as HsSwt1, C1orf26, and chromosome 1 open reading frame 26) is an RNA endonuclease that participates in quality control of nuclear mRNPs and can associate with the nuclear pore complex (NPC). This subfamily belongs to the Smg5 and Smg6-like PIN domain family. Smg5 and Smg6 are essential factors in NMD, a post-transcriptional regulatory pathway that recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN domain elicits degradation of bound mRNAs, as well as, metal-ion dependent, degradation of single-stranded RNA, in vitro. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Point mutation studies of the conserved aspartate residues in the catalytic center of the Smg6 PIN domain revealed that Smg6 is the endonuclease involved in human NMD. However, Smg5 lacks several of these key catalytic residues and does not degrade single-stranded RNA, in vivo.


:

Pssm-ID: 350294  Cd Length: 141  Bit Score: 162.73  E-value: 1.89e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510435 398 VIDTNILMNHLKFVRILKTTEVPGFDKLVLIIPWVVMQELDRMKEGKLLKRAQHKAIPAVHFINDSLKNQDRKLWGQSIQ 477
Cdd:cd18727     1 VLDTNVLISHLDLLKQLVEDVEKLSLPVVIVIPWVVLQELDGLKKSKRKSSLGWLARRASTWLLEKLRSKHPRVRGQALS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462510435 478 LASQkHYGLSDENNDDRVLKCCLQHQELFPCsFVILCTDDRNLRNKGLISGVKSLSKEELSA 539
Cdd:cd18727    81 ETLR-ASGDPGESNDDAILDCCLYFQEKYGA-PVVLLSNDKNLCNKALINGIPTISPEEGMT 140
 
Name Accession Description Interval E-value
PIN_Swt1-like cd18727
VapC-like PIN domain of Saccharomyces cerevisiae Swt1p, human SWT1 and related proteins; ...
 398-539 1.89e-46

VapC-like PIN domain of Saccharomyces cerevisiae Swt1p, human SWT1 and related proteins; Saccharomyces cerevisiae mRNA-processing endoribonuclease Swt1p plays an important role in quality control of nuclear mRNPs in eukaryotes. Human transcriptional protein SWT1 (RNA endoribonuclease homolog, also known as HsSwt1, C1orf26, and chromosome 1 open reading frame 26) is an RNA endonuclease that participates in quality control of nuclear mRNPs and can associate with the nuclear pore complex (NPC). This subfamily belongs to the Smg5 and Smg6-like PIN domain family. Smg5 and Smg6 are essential factors in NMD, a post-transcriptional regulatory pathway that recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN domain elicits degradation of bound mRNAs, as well as, metal-ion dependent, degradation of single-stranded RNA, in vitro. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Point mutation studies of the conserved aspartate residues in the catalytic center of the Smg6 PIN domain revealed that Smg6 is the endonuclease involved in human NMD. However, Smg5 lacks several of these key catalytic residues and does not degrade single-stranded RNA, in vivo.


Pssm-ID: 350294  Cd Length: 141  Bit Score: 162.73  E-value: 1.89e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510435 398 VIDTNILMNHLKFVRILKTTEVPGFDKLVLIIPWVVMQELDRMKEGKLLKRAQHKAIPAVHFINDSLKNQDRKLWGQSIQ 477
Cdd:cd18727     1 VLDTNVLISHLDLLKQLVEDVEKLSLPVVIVIPWVVLQELDGLKKSKRKSSLGWLARRASTWLLEKLRSKHPRVRGQALS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462510435 478 LASQkHYGLSDENNDDRVLKCCLQHQELFPCsFVILCTDDRNLRNKGLISGVKSLSKEELSA 539
Cdd:cd18727    81 ETLR-ASGDPGESNDDAILDCCLYFQEKYGA-PVVLLSNDKNLCNKALINGIPTISPEEGMT 140
PIN_4 pfam13638
PIN domain; Members of this family of bacterial domains are predicted to be RNases (from ...
 397-533 2.04e-27

PIN domain; Members of this family of bacterial domains are predicted to be RNases (from similarities to 5'-exonucleases).


Pssm-ID: 433369  Cd Length: 131  Bit Score: 108.09  E-value: 2.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510435 397 IVIDTNILMNHLKFVRILKttevpgfDKLVLIIPWVVMQELDRMKEGKLLK--RAQHKAIPAVHFINDSLKNQDRKLWGQ 474
Cdd:pfam13638   1 YVLDTNVLLHDPDALFNFG-------EENDVVIPITVLEELDGLKKGSDESgrELARLARQANRWLDELLENNGGRLRGQ 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462510435 475 SIQLASQKHyglSDENNDDRVLKCCLQHQELFPCSFVILCTDDRNLRNKGLISGVKSLS 533
Cdd:pfam13638  74 TLDERLPPD---PFDKNDNRILAVALYLKEELPDRPVILVSKDINLRIKADALGIPAED 129
PINc smart00670
Large family of predicted nucleotide-binding domains; From similarities to 5'-exonucleases, ...
 397-522 2.92e-07

Large family of predicted nucleotide-binding domains; From similarities to 5'-exonucleases, these domains are predicted to be RNases. PINc domains in nematode SMG-5 and yeast NMD4p are predicted to be involved in RNAi.


Pssm-ID: 214771 [Multi-domain]  Cd Length: 111  Bit Score: 49.73  E-value: 2.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510435  397 IVIDTNILMNHLkfvrILKTTEVPGFDKLVLIIPWVVMQELD---RMKEGKLLKRAQHKAIPAVHFINdslknqdRKLWG 473
Cdd:smart00670   3 VVLDTNVLIDGL----IRDALEKLLEKKGEVYIPQTVLEELEylaLRSLKKLEELALEGKIILKVLKE-------ERIEE 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462510435  474 QSIQLASQKhygLSDENNDDRVLKCCLQHQElfpcsfVILCTDDRNLRN 522
Cdd:smart00670  72 EILERLSLK---LELLPNDALILATAKELGN------VVLVTNDRDLRR 111
Fcf1 COG1412
rRNA-processing protein FCF1 [Translation, ribosomal structure and biogenesis];
397-533 8.72e-05

rRNA-processing protein FCF1 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441022 [Multi-domain]  Cd Length: 123  Bit Score: 42.89  E-value: 8.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510435 397 IVIDTNILMNHLKF-VRILKTTEVPgFDKLVLIIPWVVMQELDRMKEGkllkraqhkaipavhfindsLKNQDRKLWGQS 475
Cdd:COG1412     3 VLLDTNALMMPAQFgVDVFEELDRL-LGKYEFIVPEAVLEELEKLSRG--------------------AKGKEKRAARVA 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462510435 476 IQLASQ-KHYGLSDENNDDRVLKCCLQHQelfpcsfVILCTDDRNLRNKGLISGVKSLS 533
Cdd:COG1412    62 LDLAERcEIVETEGGYADDAILELAKENG-------VIVATNDKELRRRLLEAGIPVIY 113
 
Name Accession Description Interval E-value
PIN_Swt1-like cd18727
VapC-like PIN domain of Saccharomyces cerevisiae Swt1p, human SWT1 and related proteins; ...
 398-539 1.89e-46

VapC-like PIN domain of Saccharomyces cerevisiae Swt1p, human SWT1 and related proteins; Saccharomyces cerevisiae mRNA-processing endoribonuclease Swt1p plays an important role in quality control of nuclear mRNPs in eukaryotes. Human transcriptional protein SWT1 (RNA endoribonuclease homolog, also known as HsSwt1, C1orf26, and chromosome 1 open reading frame 26) is an RNA endonuclease that participates in quality control of nuclear mRNPs and can associate with the nuclear pore complex (NPC). This subfamily belongs to the Smg5 and Smg6-like PIN domain family. Smg5 and Smg6 are essential factors in NMD, a post-transcriptional regulatory pathway that recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN domain elicits degradation of bound mRNAs, as well as, metal-ion dependent, degradation of single-stranded RNA, in vitro. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Point mutation studies of the conserved aspartate residues in the catalytic center of the Smg6 PIN domain revealed that Smg6 is the endonuclease involved in human NMD. However, Smg5 lacks several of these key catalytic residues and does not degrade single-stranded RNA, in vivo.


Pssm-ID: 350294  Cd Length: 141  Bit Score: 162.73  E-value: 1.89e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510435 398 VIDTNILMNHLKFVRILKTTEVPGFDKLVLIIPWVVMQELDRMKEGKLLKRAQHKAIPAVHFINDSLKNQDRKLWGQSIQ 477
Cdd:cd18727     1 VLDTNVLISHLDLLKQLVEDVEKLSLPVVIVIPWVVLQELDGLKKSKRKSSLGWLARRASTWLLEKLRSKHPRVRGQALS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462510435 478 LASQkHYGLSDENNDDRVLKCCLQHQELFPCsFVILCTDDRNLRNKGLISGVKSLSKEELSA 539
Cdd:cd18727    81 ETLR-ASGDPGESNDDAILDCCLYFQEKYGA-PVVLLSNDKNLCNKALINGIPTISPEEGMT 140
PIN_Smg5-6-like cd09880
VapC-like PIN domain of nonsense-mediated decay (NMD) factors, Smg5 and Smg6, and related ...
 398-540 1.86e-34

VapC-like PIN domain of nonsense-mediated decay (NMD) factors, Smg5 and Smg6, and related proteins; PIN (PilT N terminus) domain of nonsense-mediated decay (NMD) factors, Smg5 and Smg6, and homologs are included in this family. Smg5 and Smg6 are essential factors in NMD, a post-transcriptional regulatory pathway that recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN domain elicits degradation of bound mRNAs, as well as, metal-ion dependent, degradation of single-stranded RNA, in vitro. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Point mutation studies of the conserved aspartate residues in the catalytic center of the Smg6 PIN domain revealed that Smg6 is the endonuclease involved in human NMD. However, Smg5 lacks several of these key catalytic residues and does not degrade single-stranded RNA, in vivo. Many of the bacterial homologs in this group have an N-terminal PIN domain and a C-terminal PhoH-like ATPase domain.


Pssm-ID: 350228  Cd Length: 152  Bit Score: 128.95  E-value: 1.86e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510435 398 VIDTNILMNHLKFVRILKTTEvpgfdKLVLIIPWVVMQELDRMKEGKllKRAQHKAIPAVHFINDSLKNQDRKLWGQSIQ 477
Cdd:cd09880     1 VFDTNILLSHLDVLKLLVESG-----KWTVVIPLIVITELDGLKKNP--DPLGPKARSALRYIEACLKKHSRWLRVQTSK 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462510435 478 LAS-----------QKHYGLSDENNDDRVLKCCLQHQELF-----PCSFVILCTDDRNLRNKGLISGVKSLSKEELSAE 540
Cdd:cd09880    74 GNYladltirseqlSDASELRRRNNDDRILECALWQQKHFvdredGDGKVVLVTNDRNLRLKARARGVEAVTVKELLKS 152
PIN_4 pfam13638
PIN domain; Members of this family of bacterial domains are predicted to be RNases (from ...
 397-533 2.04e-27

PIN domain; Members of this family of bacterial domains are predicted to be RNases (from similarities to 5'-exonucleases).


Pssm-ID: 433369  Cd Length: 131  Bit Score: 108.09  E-value: 2.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510435 397 IVIDTNILMNHLKFVRILKttevpgfDKLVLIIPWVVMQELDRMKEGKLLK--RAQHKAIPAVHFINDSLKNQDRKLWGQ 474
Cdd:pfam13638   1 YVLDTNVLLHDPDALFNFG-------EENDVVIPITVLEELDGLKKGSDESgrELARLARQANRWLDELLENNGGRLRGQ 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462510435 475 SIQLASQKHyglSDENNDDRVLKCCLQHQELFPCSFVILCTDDRNLRNKGLISGVKSLS 533
Cdd:pfam13638  74 TLDERLPPD---PFDKNDNRILAVALYLKEELPDRPVILVSKDINLRIKADALGIPAED 129
PIN_Smg6-like cd09885
VapC-like PIN domain of human telomerase-binding protein EST1, Smg6, and other similar ...
 397-529 8.44e-15

VapC-like PIN domain of human telomerase-binding protein EST1, Smg6, and other similar eukaryotic homologs; Nonsense-mediated decay (NMD) factors, Smg5 and Smg6 are essential to the post-transcriptional regulatory pathway, NMD, which recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN (PilT N terminus) domain elicits degradation of bound mRNAs, as well as, metal ion dependent, degradation of single-stranded RNA, in vitro. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. PIN domains within this subgroup contain four highly conserved acidic residues (putative metal-binding, active site residues) which cluster at the C-terminal end of the beta-sheet and form a negatively charged pocket near the center of the molecule. Point mutation studies of the conserved aspartate residues in the catalytic center of the Smg6 PIN domain revealed that Smg6 is the endonuclease involved in human NMD. However, Smg5 lacks several of these key catalytic residues and does not degrade single-stranded RNA, in vivo. Eukaryotic Smg6 PIN domains are present at the C-terminal end of the telomerase activating proteins, EST1.


Pssm-ID: 350233  Cd Length: 178  Bit Score: 73.45  E-value: 8.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510435 397 IVIDTNILMNHLK-FVRILKTtevpgfDKLVLIIPWVVMQELDRMKEGKLLK---------RAQHKAIPAVHFINDSLKN 466
Cdd:cd09885     8 LVPDTNCFIDHLElIEKLVES------RKFTVLVPLIVVNELDGLAKGSESDsyadeahaeEVQAKARKAVKFLEEQFEA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510435 467 QDRKLWGQ--------SIQLASQKHYGLSDENNDDRVLKCCLQHQELFPCSF--------------VILCTDDRNLRNKG 524
Cdd:cd09885    82 RNPYVRALtskgtlldTIAFRSEDINDGDGGNNDDLILSCCLNLCKDKAVDFmpaskdqpirlyreVVLLTDDRNLRVKA 161


                  ....*
gi 2462510435 525 LISGV 529
Cdd:cd09885   162 LSRNI 166
PIN_VapC_PhoHL-ATPase cd09883
VapC-like PIN domain of bacterial Smg6-like proteins with C-terminal PhoH-like ATPase domains; ...
 398-531 1.12e-09

VapC-like PIN domain of bacterial Smg6-like proteins with C-terminal PhoH-like ATPase domains; PIN (PilT N terminus) domain of Smg6-like bacterial proteins with C-terminal PhoH-like ATPase domains and other similar homologs are included in this family. Eukaryotic Smg5 and Smg6 nucleases are essential factors in nonsense-mediated mRNA decay (NMD), a post-transcriptional regulatory pathway that recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN domain elicits degradation of bound mRNAs, as well as, metal ion dependent, degradation of single-stranded RNA, in vitro. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. PIN domains within this subgroup contain four highly conserved acidic residues (putative metal-binding, active site residues). Many of the bacterial homologs in this group have an N-terminal PIN domain and a C-terminal PhoH-like ATPase domain and are predicted to be ATPases which are induced by phosphate starvation.


Pssm-ID: 350231  Cd Length: 146  Bit Score: 57.55  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510435 398 VIDTNILMNHLKFVRILKTTEVpgfdklvlIIPWVVMQELDRMKEGK-LLKRAQHKAIpavHFInDSLKNQDRKLWGQ-- 474
Cdd:cd09883     5 VLDTNVLLHDPNAIFKFEDNDV--------VIPITVLEELDKLKKRNdELGRNAREAI---RNL-DELREKGSLAEGVpl 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462510435 475 ------SIQLASQKH---YGLSDENNDDRVLKCCLQHQELFPCSfVILCTDDRNLRNKGLISGVKS 531
Cdd:cd09883    73 enggtlRVELNHKDLlplPELDLDKNDNRILAVALKLKEEGDRP-VILVTKDINLRIKADALGIKA 137
PINc smart00670
Large family of predicted nucleotide-binding domains; From similarities to 5'-exonucleases, ...
 397-522 2.92e-07

Large family of predicted nucleotide-binding domains; From similarities to 5'-exonucleases, these domains are predicted to be RNases. PINc domains in nematode SMG-5 and yeast NMD4p are predicted to be involved in RNAi.


Pssm-ID: 214771 [Multi-domain]  Cd Length: 111  Bit Score: 49.73  E-value: 2.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510435  397 IVIDTNILMNHLkfvrILKTTEVPGFDKLVLIIPWVVMQELD---RMKEGKLLKRAQHKAIPAVHFINdslknqdRKLWG 473
Cdd:smart00670   3 VVLDTNVLIDGL----IRDALEKLLEKKGEVYIPQTVLEELEylaLRSLKKLEELALEGKIILKVLKE-------ERIEE 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2462510435  474 QSIQLASQKhygLSDENNDDRVLKCCLQHQElfpcsfVILCTDDRNLRN 522
Cdd:smart00670  72 EILERLSLK---LELLPNDALILATAKELGN------VVLVTNDRDLRR 111
Fcf1 COG1412
rRNA-processing protein FCF1 [Translation, ribosomal structure and biogenesis];
397-533 8.72e-05

rRNA-processing protein FCF1 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441022 [Multi-domain]  Cd Length: 123  Bit Score: 42.89  E-value: 8.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462510435 397 IVIDTNILMNHLKF-VRILKTTEVPgFDKLVLIIPWVVMQELDRMKEGkllkraqhkaipavhfindsLKNQDRKLWGQS 475
Cdd:COG1412     3 VLLDTNALMMPAQFgVDVFEELDRL-LGKYEFIVPEAVLEELEKLSRG--------------------AKGKEKRAARVA 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462510435 476 IQLASQ-KHYGLSDENNDDRVLKCCLQHQelfpcsfVILCTDDRNLRNKGLISGVKSLS 533
Cdd:COG1412    62 LDLAERcEIVETEGGYADDAILELAKENG-------VIVATNDKELRRRLLEAGIPVIY 113
 
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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