NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24639370|ref|NP_524768|]
View 

SET and MYND domain containing, class 3 [Drosophila melanogaster]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SET super family cl40432
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 34-284 8.90e-38

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain superfamily corresponds to SET domain-containing lysine methyltransferases, which catalyze site and state-specific methylation of lysine residues in histones that are fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains has been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as N-SET and C-SET. C-SET forms an unusual and conserved knot-like structure of probable functional importance. In addition to N-SET and C-SET, an insert region (I-SET) and flanking regions of high structural variability form part of the overall structure. Some family members contain a pre-SET domain, which is found in a number of histone methyltransferases (HMTase), and a post-SET domain, which harbors a zinc-binding site.


The actual alignment was detected with superfamily member cd19203:

Pssm-ID: 394802 [Multi-domain]  Cd Length: 210  Bit Score: 137.11  E-value: 8.90e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639370  34 QIKRGQRILTEKPFAFVLKsqyrlercdncleatkvlkcsncryvsychrscqmQAWGQHKHECPFLKKVHPRVVPDAar 113
Cdd:cd19203  20 PLKPGELVLKADPFAYTVC-----------------------------------NPPDSVRLEGRIIFKLLDKAPSES-- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639370 114 mlCRLIlrlehggdlirgyytehgsrKFRDLMSHYAEIKNDpmRLEHLDSLHAVLTDMMAE---SPSTVPNKTELMSIYG 190
Cdd:cd19203  63 --EKLY--------------------SFYDLQSNINKLSED--RKEGLRQLAMVLQHYLREeiqDASQLPPAFDIFELFA 118

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639370 191 RLITNGFNILDAEMNSIATAIYLGVSITDHSCQPNAVATFEGNELHVHAIEDMECLDwsKIFISYIDLLNTPEQRRLDLK 270
Cdd:cd19203 119 KVTCNSFTICDAEMQEVGVGLYPSASLLNHSCDPNCVIVFNGPHLLLRAIREIEVGE--ELTISYIDMLMPSEERRKQLR 196

                       250
                ....*....|....
gi 24639370 271 EHYYFLCVCSKCTD 284
Cdd:cd19203 197 DQYCFECDCFRCQD 210
zf-MYND pfam01753
MYND finger;
60-97 6.40e-11

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 57.04  E-value: 6.40e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 24639370    60 CDNCL-EATKVLKCSNCRYVSYCHRSCQMQAWGQHKHEC 97
Cdd:pfam01753   1 CAVCGkEALKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
TPR_12 pfam13424
Tetratricopeptide repeat;
383-441 9.48e-04

Tetratricopeptide repeat;


:

Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 37.75  E-value: 9.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 24639370   383 GKWSDALDYGQRLLPGFRKYHGPWNPLLGLLHMKLGKIQLYEGHSKEALHHLEEAQRIL 441
Cdd:pfam13424  17 GRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALA 75
 
Name Accession Description Interval E-value
SET_SMYD3 cd19203
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ...
 34-284 8.90e-38

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 (SMYD3) and similar proteins; SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. It is overexpressed in colorectal, breast, prostate, and hepatocellular tumors, and has been implicated as an oncogene in human malignancies. Methylation of MEKK2 by SMYD3 is important for regulation of the MEK/ERK pathway, suggesting the possibility of selectively targeting SMYD3 in RAS-driven cancers.


Pssm-ID: 380980 [Multi-domain]  Cd Length: 210  Bit Score: 137.11  E-value: 8.90e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639370  34 QIKRGQRILTEKPFAFVLKsqyrlercdncleatkvlkcsncryvsychrscqmQAWGQHKHECPFLKKVHPRVVPDAar 113
Cdd:cd19203  20 PLKPGELVLKADPFAYTVC-----------------------------------NPPDSVRLEGRIIFKLLDKAPSES-- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639370 114 mlCRLIlrlehggdlirgyytehgsrKFRDLMSHYAEIKNDpmRLEHLDSLHAVLTDMMAE---SPSTVPNKTELMSIYG 190
Cdd:cd19203  63 --EKLY--------------------SFYDLQSNINKLSED--RKEGLRQLAMVLQHYLREeiqDASQLPPAFDIFELFA 118

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639370 191 RLITNGFNILDAEMNSIATAIYLGVSITDHSCQPNAVATFEGNELHVHAIEDMECLDwsKIFISYIDLLNTPEQRRLDLK 270
Cdd:cd19203 119 KVTCNSFTICDAEMQEVGVGLYPSASLLNHSCDPNCVIVFNGPHLLLRAIREIEVGE--ELTISYIDMLMPSEERRKQLR 196

                       250
                ....*....|....
gi 24639370 271 EHYYFLCVCSKCTD 284
Cdd:cd19203 197 DQYCFECDCFRCQD 210
zf-MYND pfam01753
MYND finger;
60-97 6.40e-11

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 57.04  E-value: 6.40e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 24639370    60 CDNCL-EATKVLKCSNCRYVSYCHRSCQMQAWGQHKHEC 97
Cdd:pfam01753   1 CAVCGkEALKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
TPR_12 pfam13424
Tetratricopeptide repeat;
383-441 9.48e-04

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 37.75  E-value: 9.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 24639370   383 GKWSDALDYGQRLLPGFRKYHGPWNPLLGLLHMKLGKIQLYEGHSKEALHHLEEAQRIL 441
Cdd:pfam13424  17 GRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALA 75
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
 49-89 8.09e-03

protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and similar proteins; MgcRacGAP, also called Rac GTPase-activating protein 1 (RACGAP1) or protein CYK4, plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling; and ii) after phosphorylation by aurora B, MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain an N-terminal C1 domain, and a C-terminal RhoGAP domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410371  Cd Length: 55  Bit Score: 34.69  E-value: 8.09e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24639370  49 FVLKSQYRLERCDNC----LEATKVLKCSNCRYVsyCHRSCQMQA 89
Cdd:cd20821   5 FVSKTVIKPETCVVCgkriKFGKKALKCKDCRVV--CHPDCKDKL 47
 
Name Accession Description Interval E-value
SET_SMYD3 cd19203
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ...
 34-284 8.90e-38

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 (SMYD3) and similar proteins; SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. It is overexpressed in colorectal, breast, prostate, and hepatocellular tumors, and has been implicated as an oncogene in human malignancies. Methylation of MEKK2 by SMYD3 is important for regulation of the MEK/ERK pathway, suggesting the possibility of selectively targeting SMYD3 in RAS-driven cancers.


Pssm-ID: 380980 [Multi-domain]  Cd Length: 210  Bit Score: 137.11  E-value: 8.90e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639370  34 QIKRGQRILTEKPFAFVLKsqyrlercdncleatkvlkcsncryvsychrscqmQAWGQHKHECPFLKKVHPRVVPDAar 113
Cdd:cd19203  20 PLKPGELVLKADPFAYTVC-----------------------------------NPPDSVRLEGRIIFKLLDKAPSES-- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639370 114 mlCRLIlrlehggdlirgyytehgsrKFRDLMSHYAEIKNDpmRLEHLDSLHAVLTDMMAE---SPSTVPNKTELMSIYG 190
Cdd:cd19203  63 --EKLY--------------------SFYDLQSNINKLSED--RKEGLRQLAMVLQHYLREeiqDASQLPPAFDIFELFA 118

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639370 191 RLITNGFNILDAEMNSIATAIYLGVSITDHSCQPNAVATFEGNELHVHAIEDMECLDwsKIFISYIDLLNTPEQRRLDLK 270
Cdd:cd19203 119 KVTCNSFTICDAEMQEVGVGLYPSASLLNHSCDPNCVIVFNGPHLLLRAIREIEVGE--ELTISYIDMLMPSEERRKQLR 196

                       250
                ....*....|....
gi 24639370 271 EHYYFLCVCSKCTD 284
Cdd:cd19203 197 DQYCFECDCFRCQD 210
SET_SMYD1_2_3-like cd19167
SET domain (including post-SET domain) found in SET and MYND domain-containing proteins, SMYD1, ...
 109-283 1.02e-30

SET domain (including post-SET domain) found in SET and MYND domain-containing proteins, SMYD1, SMYD2, SMYD3 and similar proteins; The family includes SET and MYND domain-containing proteins, SMYD1, SMYD2 and SMYD3. SMYD1 (EC 2.1.1.43; also termed BOP) is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD2 (also termed HSKM-B, or lysine N-methyltransferase 3C (KMT3C)) functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex.


Pssm-ID: 380944 [Multi-domain]  Cd Length: 205  Bit Score: 117.91  E-value: 1.02e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639370 109 PDAARMLCRLILRLEhggdlIRGYYTEHGSRKFRDLMSHYAeiKNDPMRLEHLDSLHAVLTDMMAESpSTVPNKTELMSI 188
Cdd:cd19167  40 PEHVRLTGRILYKQH-----IRKTRTSGKLLSVYDLESHVE--KLDEEKKDGLRSDVATLHQFMSKD-LQLPDAAYLVEL 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639370 189 YGRLITNGFNILDAEMNSIATAIYLGVSITDHSCQPNAVATFEGNELHVHAIEDMECLDwsKIFISYIDLLNTPEQRRLD 268
Cdd:cd19167 112 FGKVNCNGFTISDEELQHVGVGIYPQAALLNHSCCPNCIVTFNGPNIEVRAVQEIEPGE--EVFHSYIDLLYPTEERRDQ 189

                       170
                ....*....|....*
gi 24639370 269 LKEHYYFLCVCSKCT 283
Cdd:cd19167 190 LRDQYFFLCQCADCQ 204
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 194-282 8.56e-18

SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing protein, and similar proteins; The family includes SET and MYND domain-containing proteins, SMYD1-SYMD5. SMYD1 (EC 2.1.1.43; also termed BOP) is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD2 (also termed HSKM-B, or lysine N-methyltransferase 3C (KMT3C)) functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. SMYD4 functions as a potential tumor suppressor that plays a critical role in breast carcinogenesis at least partly through inhibiting the expression of PDGFR-alpha. SMYD5 (also termed protein NN8-4AG, or retinoic acid-induced protein 15) functions as histone lysine methyltransferase that mediates H4K20me3 at heterochromatin regions.


Pssm-ID: 380997 [Multi-domain]  Cd Length: 122  Bit Score: 79.34  E-value: 8.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639370 194 TNGFNILDaEMNSIATAIYLGVSITDHSCQPNAVATFEGN-ELHVHAIEDMEcldwsK---IFISYIDLLNTPEQRRLDL 269
Cdd:cd20071  36 SNSFSLTD-GLNEIGVGLFPLASLLNHSCDPNAVVVFDGNgTLRVRALRDIK-----AgeeLTISYIDPLLPRTERRREL 109

                        90
                ....*....|...
gi 24639370 270 KEHYYFLCVCSKC 282
Cdd:cd20071 110 LEKYGFTCSCPRC 122
SET_SMYD2 cd19202
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 2 ...
 180-283 1.13e-17

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 2 (SMYD2) and similar proteins; SMYD2 (also termed HSKM-B, lysine N-methyltransferase 3C (KMT3C)) functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). It plays a role in myofilament organization in both skeletal and cardiac muscles via Hsp90 methylation. SMYD2 overexpression is associated with tumor cell proliferation and a worse outcome in human papillomavirus-unrelated nonmultiple head and neck carcinomas. It regulates leukemia cell growth such that diminished SMYD2 expression upregulates SET7/9, thereby possibly shifting leukemia cells from growth to quiescence state associated with resistance to DNA damage associated with Acute Myeloid Leukemia (AML).


Pssm-ID: 380979 [Multi-domain]  Cd Length: 206  Bit Score: 81.41  E-value: 1.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639370 180 PNKTELMSIYGRLITNGFNILDAEMNSIATAIYLGVSITDHSCQPNAVATFEGNELHVHAIEDMECLDwsKIFISYIDLL 259
Cdd:cd19202 104 PDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGE--EVFTSYIDLL 181

                        90       100
                ....*....|....*....|....
gi 24639370 260 NTPEQRRLDLKEHYYFLCVCSKCT 283
Cdd:cd19202 182 YPTEDRNDRLRDSYFFTCECQECT 205
SET_SMYD1 cd10526
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 ...
 96-283 3.45e-17

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 (SMYD1) and similar proteins; SMYD1 (EC 2.1.1.43), also termed BOP, is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD1 plays a critical role in cardiomyocyte differentiation, cardiac morphogenesis and myofibril organization, as well as in the regulation of endothelial cells (ECs). It is expressed in vascular endothelial cells, it has beenshown that knockdown of SMYD1 in endothelial cells impairs EC migration and tube formation.


Pssm-ID: 380924 [Multi-domain]  Cd Length: 210  Bit Score: 80.15  E-value: 3.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639370  96 ECPFLKKVHPRVVPDAARMLCRLILRLEHGGDLIrgyyTEHGSRKFRDLMSHYaeiknDPMRLEHLDSLHAVLTDMMAES 175
Cdd:cd10526  30 EPPYAAVVFGKAPNENIRLAARILWRIEREGGGL----KEGELVSIEDLQDHL-----EDFSEEEKKDLREDVHSFLDYW 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639370 176 PS-TVPNKTELMS-IYGRLITNGFNILDAE-MNSIATAIYLGVSITDHSCQPNAVATFEGNELHVHAIEDMECLDwsKIF 252
Cdd:cd10526 101 PYqSQQFSMEYIShIFGVINCNGFTLSDQRgLQAVGVGIFPNLCLVNHDCWPNCTVIFNNGRIELRALGKISEGD--ELT 178

                       170       180       190
                ....*....|....*....|....*....|.
gi 24639370 253 ISYIDLLNTPEQRRLDLKEHYYFLCVCSKCT 283
Cdd:cd10526 179 VSYIDFLNTSEDRKEQLKKQYYFDCTCEHCT 209
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 207-282 3.99e-11

SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing protein 4 (SMYD4) and similar proteins; SMYD4 functions as a potential tumor suppressor that plays a critical role in breast carcinogenesis at least partly through inhibiting the expression of PDGFR-alpha. In zebrafish, SMYD4 is ubiquitously expressed in early embryos and becomes enriched in the developing heart; mutants show a strong defect in cardiomyocyte proliferation, which lead to a severe cardiac malformation.


Pssm-ID: 380934 [Multi-domain]  Cd Length: 218  Bit Score: 62.70  E-value: 3.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639370 207 IATAIYLGVSITDHSCQPNAVATFEGNELHVHAIEDMEcldwsK---IFISY--IDLLNTPEQRRLDLKEHYYFLCVCSK 281
Cdd:cd10536 143 IATAIYPTLSLLNHSCDPNTIRSFYGNTIVVRATRPIK-----KgeeITICYgpHFSRMKRSERQRLLKEQYFFDCSCEA 217


                .
gi 24639370 282 C 282
Cdd:cd10536 218 C 218
zf-MYND pfam01753
MYND finger;
60-97 6.40e-11

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 57.04  E-value: 6.40e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 24639370    60 CDNCL-EATKVLKCSNCRYVSYCHRSCQMQAWGQHKHEC 97
Cdd:pfam01753   1 CAVCGkEALKLLRCSRCKSVYYCSKECQKADWPYHKKEC 39
SET_SMYD5 cd10521
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 210-282 6.48e-10

SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing protein 5 (SMYD5) and similar proteins; SMYD5 (also termed protein NN8-4AG, or retinoic acid-induced protein 15) functions as histone lysine methyltransferase that mediates H4K20me3 at heterochromatin regions. It plays an important role in chromosome integrity by regulating heterochromatin and repressing endogenous repetitive DNA elements during differentiation. In zebrafish embryogenesis, it plays pivotal roles in both primitive and definitive hematopoiesis.


Pssm-ID: 380919 [Multi-domain]  Cd Length: 282  Bit Score: 60.01  E-value: 6.48e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24639370 210 AIYLGVSITDHSCQPNAVATFEGNE--LHVHAIEDMECLDwsKIFISYID--LLNTPEQRRLD-LKEHYYFLCVCSKC 282
Cdd:cd10521 204 GLYLLQSCCNHSCVPNAEITFPENNftLSLKALRDIQEGE--EICISYLDecQRERSRHSRQKiLRENYLFICNCPKC 279
TPR_12 pfam13424
Tetratricopeptide repeat;
383-441 9.48e-04

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 37.75  E-value: 9.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 24639370   383 GKWSDALDYGQRLLPGFRKYHGPWNPLLGLLHMKLGKIQLYEGHSKEALHHLEEAQRIL 441
Cdd:pfam13424  17 GRYDEALELLEKALEIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALA 75
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
 49-89 8.09e-03

protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and similar proteins; MgcRacGAP, also called Rac GTPase-activating protein 1 (RACGAP1) or protein CYK4, plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling; and ii) after phosphorylation by aurora B, MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain an N-terminal C1 domain, and a C-terminal RhoGAP domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410371  Cd Length: 55  Bit Score: 34.69  E-value: 8.09e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24639370  49 FVLKSQYRLERCDNC----LEATKVLKCSNCRYVsyCHRSCQMQA 89
Cdd:cd20821   5 FVSKTVIKPETCVVCgkriKFGKKALKCKDCRVV--CHPDCKDKL 47
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH