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Conserved domains on  [gi|17737995|ref|NP_524372|]
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Retinoblastoma-family protein 2 [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF3452 pfam11934
Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. ...
83-213 7.55e-41

Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is typically between 124 to 150 amino acids in length. This domain is found associated with pfam01858, pfam01857. This domain has a single completely conserved residue W that may be functionally important.


:

Pssm-ID: 463402  Cd Length: 134  Bit Score: 146.20  E-value: 7.55e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737995    83 DSVAKNCCwnVSLTRLLRSFKMNVSQFLRRMEHWNWLTQNENTFQLEVEELRCRLGITSTLLRHYKHIFRSLFVHPGKGA 162
Cdd:pfam11934   1 DGTVEGNC--VSLTRLLRACKLSIIDFFKKMKQWADMANLDWEFRLEIKELERNFSVTTVLFKKYKRIFNELFLSPPPKE 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17737995   163 DPGAAN------HYQALYEFGWLLFLVIRNELPGfAITNLINGCQVLVCTMDLLFVN 213
Cdd:pfam11934  79 PKRSKKsrpapcSYSDLFEFGWLLFLAAKNEFPS-ISKDLVTSYHLLLCCLDLVYVN 134
RB_B super family cl47702
Retinoblastoma-associated protein B domain; The crystal structure of the Rb pocket bound to a ...
593-679 1.11e-23

Retinoblastoma-associated protein B domain; The crystal structure of the Rb pocket bound to a nine-residue E7 peptide containing the LxCxE motif, shared by other Rb-binding viral and cellular proteins, shows that the LxCxE peptide binds a highly conserved groove on the B domain. The B domain has a cyclin fold.


The actual alignment was detected with superfamily member pfam01857:

Pssm-ID: 460363  Cd Length: 131  Bit Score: 97.25  E-value: 1.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737995   593 QIWHLAEHSFTLESSrLLRNRHLDQLLLCAIHLHVRLEKLHLTFSMIIQHYRRQPHFRRSAYREVSLGNGQ--------- 663
Cdd:pfam01857  33 KIWTCFEHSLVHQTD-LMKDRHLDQILLCAIYVICKVTKEELTFKEIMKCYRKQPQASSHVYRSVLIRRRErerngknne 111
                          90
                  ....*....|....*....
gi 17737995   664 ---TADIITFYNSVYVQSM 679
Cdd:pfam01857 112 eeeRGDIIKFYNKVFVPAM 130
RB_A super family cl03387
Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted.
384-536 6.92e-21

Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted.


The actual alignment was detected with superfamily member pfam01858:

Pssm-ID: 460364  Cd Length: 195  Bit Score: 91.10  E-value: 6.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737995   384 DKIVNYLDQTLEEMNRTFTMAVKD--FLDAELSGKRFRQARGLYYKYLQKILGPELVQKPQLKIGQLMKQRKLTAALLAC 461
Cdd:pfam01858  41 ETILKRVKELGEIFCQKYTEASGEhpSFCIEIAEQRFRLAEKLYYKVLESILKSEKKRLPGNDLSSLLSNDIFHRSLLAC 120
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17737995   462 CLELALHVHhkLVEGLRFPFVLHCFSLDAYDFQKILELVVRYDHGfLGRELIKHLDVVEEMCLDSLIFRKSSQLW 536
Cdd:pfam01858 121 CLEIVLFAY--NSERLSFPWILEVFGLPPFDFYKVIESFIRAEDG-LPRELVKHLNSIEEQILESLAWKSDSPLW 192
 
Name Accession Description Interval E-value
DUF3452 pfam11934
Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. ...
83-213 7.55e-41

Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is typically between 124 to 150 amino acids in length. This domain is found associated with pfam01858, pfam01857. This domain has a single completely conserved residue W that may be functionally important.


Pssm-ID: 463402  Cd Length: 134  Bit Score: 146.20  E-value: 7.55e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737995    83 DSVAKNCCwnVSLTRLLRSFKMNVSQFLRRMEHWNWLTQNENTFQLEVEELRCRLGITSTLLRHYKHIFRSLFVHPGKGA 162
Cdd:pfam11934   1 DGTVEGNC--VSLTRLLRACKLSIIDFFKKMKQWADMANLDWEFRLEIKELERNFSVTTVLFKKYKRIFNELFLSPPPKE 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17737995   163 DPGAAN------HYQALYEFGWLLFLVIRNELPGfAITNLINGCQVLVCTMDLLFVN 213
Cdd:pfam11934  79 PKRSKKsrpapcSYSDLFEFGWLLFLAAKNEFPS-ISKDLVTSYHLLLCCLDLVYVN 134
RB_B pfam01857
Retinoblastoma-associated protein B domain; The crystal structure of the Rb pocket bound to a ...
593-679 1.11e-23

Retinoblastoma-associated protein B domain; The crystal structure of the Rb pocket bound to a nine-residue E7 peptide containing the LxCxE motif, shared by other Rb-binding viral and cellular proteins, shows that the LxCxE peptide binds a highly conserved groove on the B domain. The B domain has a cyclin fold.


Pssm-ID: 460363  Cd Length: 131  Bit Score: 97.25  E-value: 1.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737995   593 QIWHLAEHSFTLESSrLLRNRHLDQLLLCAIHLHVRLEKLHLTFSMIIQHYRRQPHFRRSAYREVSLGNGQ--------- 663
Cdd:pfam01857  33 KIWTCFEHSLVHQTD-LMKDRHLDQILLCAIYVICKVTKEELTFKEIMKCYRKQPQASSHVYRSVLIRRRErerngknne 111
                          90
                  ....*....|....*....
gi 17737995   664 ---TADIITFYNSVYVQSM 679
Cdd:pfam01857 112 eeeRGDIIKFYNKVFVPAM 130
RB_A pfam01858
Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted.
384-536 6.92e-21

Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted.


Pssm-ID: 460364  Cd Length: 195  Bit Score: 91.10  E-value: 6.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737995   384 DKIVNYLDQTLEEMNRTFTMAVKD--FLDAELSGKRFRQARGLYYKYLQKILGPELVQKPQLKIGQLMKQRKLTAALLAC 461
Cdd:pfam01858  41 ETILKRVKELGEIFCQKYTEASGEhpSFCIEIAEQRFRLAEKLYYKVLESILKSEKKRLPGNDLSSLLSNDIFHRSLLAC 120
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17737995   462 CLELALHVHhkLVEGLRFPFVLHCFSLDAYDFQKILELVVRYDHGfLGRELIKHLDVVEEMCLDSLIFRKSSQLW 536
Cdd:pfam01858 121 CLEIVLFAY--NSERLSFPWILEVFGLPPFDFYKVIESFIRAEDG-LPRELVKHLNSIEEQILESLAWKSDSPLW 192
CYCLIN_RB cd20599
cyclin box found in retinoblastoma-associated protein (RB) and similar proteins; RB, also ...
589-682 3.14e-20

cyclin box found in retinoblastoma-associated protein (RB) and similar proteins; RB, also called p105-Rb, pRb, or pp110, is a key regulator of entry into cell division and also acts as a tumor suppressor. It promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. It also acts as a transcription repressor of E2F1 target genes. RB is directly involved in heterochromatin formation by maintaining overall chromatin structure, especially that of constitutive heterochromatin by stabilizing histone methylation. It recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. It controls histone H4 'Lys-20' trimethylation. RB contains one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410302  Cd Length: 126  Bit Score: 86.96  E-value: 3.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737995 589 DSFPQIWHLAEHSFTLESsRLLRNRHLDQLLLCAIHLHVRLEKLHLTFSMIIQHYRRQPHFRRSAYREVSLGNGQTADII 668
Cdd:cd20599  30 DLEHRIWTCFEHCLQNRY-ELLKDRHLDQIMMCSMYGICKVKNKDLRFKTIVTAYKDLPHASQEVYKRVLIRGEEYDSII 108
                        90
                ....*....|....
gi 17737995 669 TFYNSVYVQSMGNY 682
Cdd:cd20599 109 GFYNRVFMQALKTN 122
 
Name Accession Description Interval E-value
DUF3452 pfam11934
Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. ...
83-213 7.55e-41

Domain of unknown function (DUF3452); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is typically between 124 to 150 amino acids in length. This domain is found associated with pfam01858, pfam01857. This domain has a single completely conserved residue W that may be functionally important.


Pssm-ID: 463402  Cd Length: 134  Bit Score: 146.20  E-value: 7.55e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737995    83 DSVAKNCCwnVSLTRLLRSFKMNVSQFLRRMEHWNWLTQNENTFQLEVEELRCRLGITSTLLRHYKHIFRSLFVHPGKGA 162
Cdd:pfam11934   1 DGTVEGNC--VSLTRLLRACKLSIIDFFKKMKQWADMANLDWEFRLEIKELERNFSVTTVLFKKYKRIFNELFLSPPPKE 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17737995   163 DPGAAN------HYQALYEFGWLLFLVIRNELPGfAITNLINGCQVLVCTMDLLFVN 213
Cdd:pfam11934  79 PKRSKKsrpapcSYSDLFEFGWLLFLAAKNEFPS-ISKDLVTSYHLLLCCLDLVYVN 134
RB_B pfam01857
Retinoblastoma-associated protein B domain; The crystal structure of the Rb pocket bound to a ...
593-679 1.11e-23

Retinoblastoma-associated protein B domain; The crystal structure of the Rb pocket bound to a nine-residue E7 peptide containing the LxCxE motif, shared by other Rb-binding viral and cellular proteins, shows that the LxCxE peptide binds a highly conserved groove on the B domain. The B domain has a cyclin fold.


Pssm-ID: 460363  Cd Length: 131  Bit Score: 97.25  E-value: 1.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737995   593 QIWHLAEHSFTLESSrLLRNRHLDQLLLCAIHLHVRLEKLHLTFSMIIQHYRRQPHFRRSAYREVSLGNGQ--------- 663
Cdd:pfam01857  33 KIWTCFEHSLVHQTD-LMKDRHLDQILLCAIYVICKVTKEELTFKEIMKCYRKQPQASSHVYRSVLIRRRErerngknne 111
                          90
                  ....*....|....*....
gi 17737995   664 ---TADIITFYNSVYVQSM 679
Cdd:pfam01857 112 eeeRGDIIKFYNKVFVPAM 130
RB_A pfam01858
Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted.
384-536 6.92e-21

Retinoblastoma-associated protein A domain; This domain has the cyclin fold as predicted.


Pssm-ID: 460364  Cd Length: 195  Bit Score: 91.10  E-value: 6.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737995   384 DKIVNYLDQTLEEMNRTFTMAVKD--FLDAELSGKRFRQARGLYYKYLQKILGPELVQKPQLKIGQLMKQRKLTAALLAC 461
Cdd:pfam01858  41 ETILKRVKELGEIFCQKYTEASGEhpSFCIEIAEQRFRLAEKLYYKVLESILKSEKKRLPGNDLSSLLSNDIFHRSLLAC 120
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17737995   462 CLELALHVHhkLVEGLRFPFVLHCFSLDAYDFQKILELVVRYDHGfLGRELIKHLDVVEEMCLDSLIFRKSSQLW 536
Cdd:pfam01858 121 CLEIVLFAY--NSERLSFPWILEVFGLPPFDFYKVIESFIRAEDG-LPRELVKHLNSIEEQILESLAWKSDSPLW 192
CYCLIN_RB cd20599
cyclin box found in retinoblastoma-associated protein (RB) and similar proteins; RB, also ...
589-682 3.14e-20

cyclin box found in retinoblastoma-associated protein (RB) and similar proteins; RB, also called p105-Rb, pRb, or pp110, is a key regulator of entry into cell division and also acts as a tumor suppressor. It promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. It also acts as a transcription repressor of E2F1 target genes. RB is directly involved in heterochromatin formation by maintaining overall chromatin structure, especially that of constitutive heterochromatin by stabilizing histone methylation. It recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. It controls histone H4 'Lys-20' trimethylation. RB contains one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410302  Cd Length: 126  Bit Score: 86.96  E-value: 3.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737995 589 DSFPQIWHLAEHSFTLESsRLLRNRHLDQLLLCAIHLHVRLEKLHLTFSMIIQHYRRQPHFRRSAYREVSLGNGQTADII 668
Cdd:cd20599  30 DLEHRIWTCFEHCLQNRY-ELLKDRHLDQIMMCSMYGICKVKNKDLRFKTIVTAYKDLPHASQEVYKRVLIRGEEYDSII 108
                        90
                ....*....|....
gi 17737995 669 TFYNSVYVQSMGNY 682
Cdd:cd20599 109 GFYNRVFMQALKTN 122
CYCLIN_RB-like cd20548
cyclin box found in retinoblastoma-associated protein (RB) family; The RB family includes ...
567-675 4.05e-20

cyclin box found in retinoblastoma-associated protein (RB) family; The RB family includes retinoblastoma-associated protein (RB), and two retinoblastoma-like proteins, RBL1 and RBL2. RB, also called p105-Rb, pRb, or pp110, is a key regulator of entry into cell division, and also acts as a tumor suppressor. It promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. It also acts as a transcription repressor of E2F1 target genes. RB is directly involved in heterochromatin formation by maintaining overall chromatin structure. It recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. RBL1 and RBL2 are also key regulators of entry into cell division. RBL1 and RBL2 recruit and target histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. They control histone H4 'Lys-20' trimethylation and probably act as transcription repressors by recruiting chromatin-modifying enzymes to promoters. They may also act as tumor suppressors. Members of this family contain one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410251  Cd Length: 122  Bit Score: 86.59  E-value: 4.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737995 567 LRKFYGLANRRLLLLCKSLCLVD--SFPQIWHLAEHSFTLESSrLLRNRHLDQLLLCAIHLHVRLEKLHLTFSMIIQHYR 644
Cdd:cd20548   5 FRKLYRLAAARLQDLCKRLDLLSppLRERIWTVFKHILSEETE-LLFDRHLDQIILCSIYAVCKVNNENLTFKEILDAYR 83
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 17737995 645 RQPHFRRSAYREV--------SLGNGQTADIITFYNSVY 675
Cdd:cd20548  84 KQPQAESEVYRSVlplfrsvgSDDEGESGDIIKFYNQVF 122
CYCLIN_AtRBR_like cd20601
cyclin box found in Arabidopsis thaliana retinoblastoma-related protein 1 (AtRBR1) and similar ...
593-682 4.70e-16

cyclin box found in Arabidopsis thaliana retinoblastoma-related protein 1 (AtRBR1) and similar proteins; AtRBR1 is a key regulator of entry into cell division. It acts as a transcription repressor of E2F target genes, whose activity is required for progress from the G1 to the S phase of the cell cycle. AtRBR1 plays a central role in the mechanism controlling meristem cell differentiation, cell fate establishment and cell fate maintenance during organogenesis and gametogenesis. AtRBR1 contains one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410304  Cd Length: 129  Bit Score: 75.12  E-value: 4.70e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737995 593 QIWHLAEHSFTlESSRLLRNRHLDQLLLCAIHLHVRLEKLHLTFSMIIQHYRRQPHFRRSAYREVSL-------GNGQTA 665
Cdd:cd20601  32 QVYRLIEHVLY-EQTGLFFNRHIDQIILCCLYGVCKVHKLNVTFREIIYQYRKQPQCKPDVFRNVVIeqrrptlGGPDHG 110
                        90
                ....*....|....*..
gi 17737995 666 DIITFYNSVYVQSMGNY 682
Cdd:cd20601 111 DIIAFYNEVFVPATKPF 127
CYCLIN_RBL1 cd20605
cyclin box found in retinoblastoma-like protein 1 (RBL1) and similar proteins; RBL1, also ...
561-679 7.08e-16

cyclin box found in retinoblastoma-like protein 1 (RBL1) and similar proteins; RBL1, also called 107 kDa retinoblastoma-associated protein (p107), retinoblastoma-related protein 1 (RBR-1), or pRb1, is a key regulator of entry into cell division. It is directly involved in heterochromatin formation by maintaining overall chromatin structure, especially that of constitutive heterochromatin by stabilizing histone methylation. RBL1 recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. It controls histone H4 'Lys-20' trimethylation. RBL1 probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. It may also act as a tumor suppressor. RBL1 contains one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410308  Cd Length: 130  Bit Score: 74.92  E-value: 7.08e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737995 561 TGS-SICLRKFYGLANRRLLLL-CKSLCLVDSFPQIWHLAEHSFtLESSRLLRNRHLDQLLLCAIHLHVRLEKLHLTFSM 638
Cdd:cd20605   5 TGSlALFYRKVYHLASVRLRDLcLKLDVSNELRRKIWTCFEFSL-VHCTDLMKDRHLDQLLLCAFYIMAKVTKEERTFQD 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17737995 639 IIQHYRRQPHFRRSAYREVSLGNgQTADIITFYNSVYVQSM 679
Cdd:cd20605  84 IMKCYRNQPQANSHVYRSVLLKE-ERGDLIKFYNTIYVGRV 123
CYCLIN_RBL cd20600
cyclin box found in retinoblastoma-like protein (RBL) subfamily; The RBL subfamily includes ...
568-682 1.74e-15

cyclin box found in retinoblastoma-like protein (RBL) subfamily; The RBL subfamily includes two retinoblastoma-like proteins, RBL1 and RBL2. They are key regulators of entry into cell division and are directly involved in heterochromatin formation by maintaining overall chromatin structure. RBL1 and RBL2 recruit and target histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. They control histone H4 'Lys-20' trimethylation and probably act as transcription repressors by recruiting chromatin-modifying enzymes to promoters. They may also act as tumor suppressors. Members of this family contain one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410303  Cd Length: 112  Bit Score: 73.21  E-value: 1.74e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737995 568 RKFYGLANRRLLLLCKSLCLVDSF-PQIWHLAEHSFtLESSRLLRNRHLDQLLLCAIHLHVRLEKLHLTFSMIIQHYRRQ 646
Cdd:cd20600   7 RKVYHLASVRLRDLCEKLEISEELrRKIWTCFEHSL-VHHIELMRDRHLDQLLMCAVYVIAKVTKQDKSFQEIMKCYRLQ 85
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 17737995 647 PHfrrsayrevslgnGQTADIITFYNSVYVQSMGNY 682
Cdd:cd20600  86 PQ-------------AQSGDLIQFYNSVYVKKMKEF 108
CYCLIN_RBL2 cd20606
cyclin box found in retinoblastoma-like protein 2 (RBL2) and similar proteins; RBL2, also ...
564-657 9.17e-10

cyclin box found in retinoblastoma-like protein 2 (RBL2) and similar proteins; RBL2, also called 130 kDa retinoblastoma-associated protein (p130), retinoblastoma-related protein 2 (RBR-2), or pRb2, is a key regulator of entry into cell division. It is directly involved in heterochromatin formation by maintaining overall chromatin structure, especially that of constitutive heterochromatin by stabilizing histone methylation. RBL2 recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. It controls histone H4 'Lys-20' trimethylation. It probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. It may also act as a tumor suppressor. RBL2 contains one cyclin box. The cyclin box is a protein binding domain.


Pssm-ID: 410309  Cd Length: 189  Bit Score: 58.76  E-value: 9.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737995 564 SICLRKFYGLANRRLLLLCKSLCLVDSFPQ-IWHLAEHSFtLESSRLLRNRHLDQLLLCAIHLHVRLEKLHLTFSMIIQH 642
Cdd:cd20606   3 SLFFRKVYHLASVRLRDLCAKLDISDELRKkIWTCFEYSL-VHCPELMMDRHLDQLLMCAIYVMAKVTKEDKSFQNIMRC 81
                        90
                ....*....|....*
gi 17737995 643 YRRQPHFRRSAYREV 657
Cdd:cd20606  82 YRTQPQASSSVYRSV 96
 
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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