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Conserved domains on  [gi|332660572|gb|AEE85972|]
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transcriptional regulator [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDS5 super family cl47186
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. ...
 29-230 5.73e-60

Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. Together with WapI and Scc3, it is involved in the release of the cohesin complex from chromosomes during S phase. The core of the cohesin complex consists of a coiled-coiled heterodimer of Smc1 and Smc30, together with Scc1 (also called kleisin). Pds5 interacts with Scc1 via a conserved patch on the surface of its heat repeats. Pds5 also promotes the acetylation of Smc3 that protects cohesin from releasing activity in G2 phase.


The actual alignment was detected with superfamily member cd19953:

Pssm-ID: 410996 [Multi-domain]  Cd Length: 630  Bit Score: 215.47  E-value: 5.73e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  29 LLSFLDKLFVSLAEVEQSPPDSmqNALTPLMKGLVGGKLFKHSDVDVKVAVAACISEITRITAPDAPYDDDQMKEVFKLI 108
Cdd:cd19953    1 LLKRLKALHEELSELDQDEVDL--ESLEPVAKELVSPKLLKHKDKGVRALVACCLADILRLYAPDAPYTDDQLKDIFKLF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572 109 VSSFEDLVDKSSRSYAKRISILETVAKVRSCVVMLDLEC-DALLIEMFQHFLKAIRDHHSGNVFSSMENIMTLVLEESED 187
Cdd:cd19953   79 ISQLKGLLDPDSPYFSQYFYLLESLAEVKSIVLLLDLPDaDELILELFKTFFDLVRDDHPKNVENLMLDILVELIDESES 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 332660572 188 IPSEMLSPILHS-VKKDDEISQVSRRLAEQVLSNCASKLKTYLT 230
Cdd:cd19953  159 VPQEVLDIILAQfLKKNKSENPPAYRLAVEVCERCSDKLQRYVT 202
Tudor_Agenet_AtEML-like cd20404
Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and ...
 609-657 3.59e-17

Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and similar proteins; This family includes Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4), histone-lysine N-methyltransferase trithorax-like proteins ATX1-2 (AtATX1-2), histone-lysine N-methyltransferase ASHH3, DNA mismatch repair protein MSH6, and similar proteins. EMSY-like proteins contain an EMSY N-terminal domain, a central Tudor-like Agenet domain, and a C-terminal coiled-coil motif. AtEML1, AtEML2, and likely AtEML4, contribute to RPP7-mediated immunity. Besides this, AtEML1 and AtEML2 participate in a second EDM2-dependent function and affect floral transition. ATX-like proteins are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1, also called protein SET domain group 27, or trithorax-homolog protein 1 (TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2, also called protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain proteins that consist of an N-terminal Tudor-like Agenet domain, a PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. ASHR3, also called protein SET DOMAIN GROUP 7, functions as a histone-lysine N-methyltransferase (EC 2.1.1.43). It contains a SET domain and a Tudor-like Agenet domain. AtMSH6, also called MutS protein homolog 6, is a component of the post-replicative DNA mismatch repair system (MMR). It forms a heterodimer with MutS alpha (MSH2-MSH6 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. AtMSH6 contains a Tudor-like Agenet domain and a MutS domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


:

Pssm-ID: 410475 [Multi-domain]  Cd Length: 51  Bit Score: 75.78  E-value: 3.59e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 332660572 609 VGSRIKVWWPMDQAYYKGVVESYDAAKKKHLVIYDDGDQEILYLKNQKW 657
Cdd:cd20404    1 VGRRVRVYWPEDGTWYEGVVVDYDPSTGKHRVEYDDGDEEEVDLWRELV 49
PRK13808 super family cl31642
adenylate kinase; Provisional
 690-822 3.44e-04

adenylate kinase; Provisional


The actual alignment was detected with superfamily member PRK13808:

Pssm-ID: 172341 [Multi-domain]  Cd Length: 333  Bit Score: 43.72  E-value: 3.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572 690 AKTGKQSKMDNSSAKKGSGAGSSKAKATPASKSSKTSQDDKTASKSKDSKEASREEEASSEEESEEEEPPKTVGKSGSSR 769
Cdd:PRK13808 199 AKKAAKTPAAKSGAKKASAKAKSAAKKVSKKKAAKTAVSAKKAAKTAAKAAKKAKKTAKKALKKAAKAVKKAAKKAAKAA 278

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 332660572 770 SKKDISSVSKSGKSKASSKKKEEPSKATTSSKSKSGPVKSVpAKSKTGKGKAK 822
Cdd:PRK13808 279 AKAAKGAAKATKGKAKAKKKAGKKAAAGSKAKATAKAPKRG-AKGKKAKKVTK 330
PTZ00121 super family cl31754
MAEBL; Provisional
 276-808 2.24e-03

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  276 KRETEVEKAAEISTPERTDAPKDESGKSGVSNGVAQQNDSSVDTDSMKKQDDTGAKDEPQQLDNPRNTD-LNNTTEEKPD 354
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADeAKKKAEEAKK 1316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  355 VEhQIEEKENESSSVKQADLSKDSDIKEETEPAELLDSKDVLTSPPVDSSVTAATSSENEKNKSVQILPSKTSGDETANV 434
Cdd:PTZ00121 1317 AD-EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  435 SSPSM------AEELPEQSVPKKTANQKKKESS----TEEVKPSASIA-----TEEVSEEPNTSEPQVTKKSGKKVASSS 499
Cdd:PTZ00121 1396 AKKKAeedkkkADELKKAAAAKKKADEAKKKAEekkkADEAKKKAEEAkkadeAKKKAEEAKKAEEAKKKAEEAKKADEA 1475

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  500 KTKptVPPSKKSTSETKVAKQSEKKVVGSDNAQESTKPKEEKKKPGRGKAIDEeslhTSSGDNEKPAVSSGKLASKSKKE 579
Cdd:PTZ00121 1476 KKK--AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE----AKKAEEAKKADEAKKAEEKKKAD 1549

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  580 AKQTVEESPNSNTKRKRSLGQGKASGESLVGSRIKVWWPMDQAYYKGVVESYDAAKKKHLVIYDDGDQEILYLKN----- 654
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkae 1629

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  655 --QKWSPLDESELSQDEEAADQTGQEEDASTVpltKKAKTGKQSKMDNSSAKKGSGAGSSKAKATPASKSSKTSQDDKTA 732
Cdd:PTZ00121 1630 eeKKKVEQLKKKEAEEKKKAEELKKAEEENKI---KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332660572  733 SKSKDSKEASREEEASSEEESEEEEPPKTVGKSGSSRSKKDISSVSKSGKSKASSKKKEEPSKATTSSKSKSGPVK 808
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
 
Name Accession Description Interval E-value
PDS5 cd19953
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. ...
 29-230 5.73e-60

Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. Together with WapI and Scc3, it is involved in the release of the cohesin complex from chromosomes during S phase. The core of the cohesin complex consists of a coiled-coiled heterodimer of Smc1 and Smc30, together with Scc1 (also called kleisin). Pds5 interacts with Scc1 via a conserved patch on the surface of its heat repeats. Pds5 also promotes the acetylation of Smc3 that protects cohesin from releasing activity in G2 phase.


Pssm-ID: 410996 [Multi-domain]  Cd Length: 630  Bit Score: 215.47  E-value: 5.73e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  29 LLSFLDKLFVSLAEVEQSPPDSmqNALTPLMKGLVGGKLFKHSDVDVKVAVAACISEITRITAPDAPYDDDQMKEVFKLI 108
Cdd:cd19953    1 LLKRLKALHEELSELDQDEVDL--ESLEPVAKELVSPKLLKHKDKGVRALVACCLADILRLYAPDAPYTDDQLKDIFKLF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572 109 VSSFEDLVDKSSRSYAKRISILETVAKVRSCVVMLDLEC-DALLIEMFQHFLKAIRDHHSGNVFSSMENIMTLVLEESED 187
Cdd:cd19953   79 ISQLKGLLDPDSPYFSQYFYLLESLAEVKSIVLLLDLPDaDELILELFKTFFDLVRDDHPKNVENLMLDILVELIDESES 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 332660572 188 IPSEMLSPILHS-VKKDDEISQVSRRLAEQVLSNCASKLKTYLT 230
Cdd:cd19953  159 VPQEVLDIILAQfLKKNKSENPPAYRLAVEVCERCSDKLQRYVT 202
PDS5 pfam20168
Sister chromatid cohesion protein PDS5 protein; This entry represents the Sister chromatid ...
 27-230 3.21e-51

Sister chromatid cohesion protein PDS5 protein; This entry represents the Sister chromatid cohesion protein PDS5. The large PDS5 molecule is exclusively alpha helical, composed of a large number of HEAT-like repeats and helical extensions/additions that deviate from the HEAT repeat pattern.


Pssm-ID: 466319 [Multi-domain]  Cd Length: 1051  Bit Score: 195.12  E-value: 3.21e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572    27 DELLSFLDKLFVSLAEVEQSppDSMQNALTPLMKGLVGGKLFKHSDVDVKVAVAACISEITRITAPDAPYDDDQMKEVFK 106
Cdd:pfam20168    1 DELLKRLKALHEELSDLDQE--DVDLKSLDPVAKDLVSPKLLKHKDKGVRALVACCLADILRLYAPDAPYTDDQLKDIFK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572   107 LIVSSFEDLVDKSSRSYAKRISILETVAKVRSCVVMLDL-ECDALLIEMFQHFLKAIRDHHSGNVFSSMENIMTLVLEES 185
Cdd:pfam20168   79 LFISQLRGLADPDSPYFSQYFYLLESLAEVKSIVLILDLpDADDLITELFRTFFDLVSRPHSKKVENFMLDILSELIDES 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 332660572   186 EDIPSEMLSPILHS-VKKDDEISQVSRRLAEQVLSNCASKLKTYLT 230
Cdd:pfam20168  159 DSLPQEVLDLILAQfLRKKKKENPPAFRLAVDVCNACADKLQRYVC 204
Tudor_Agenet_AtEML-like cd20404
Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and ...
 609-657 3.59e-17

Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and similar proteins; This family includes Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4), histone-lysine N-methyltransferase trithorax-like proteins ATX1-2 (AtATX1-2), histone-lysine N-methyltransferase ASHH3, DNA mismatch repair protein MSH6, and similar proteins. EMSY-like proteins contain an EMSY N-terminal domain, a central Tudor-like Agenet domain, and a C-terminal coiled-coil motif. AtEML1, AtEML2, and likely AtEML4, contribute to RPP7-mediated immunity. Besides this, AtEML1 and AtEML2 participate in a second EDM2-dependent function and affect floral transition. ATX-like proteins are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1, also called protein SET domain group 27, or trithorax-homolog protein 1 (TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2, also called protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain proteins that consist of an N-terminal Tudor-like Agenet domain, a PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. ASHR3, also called protein SET DOMAIN GROUP 7, functions as a histone-lysine N-methyltransferase (EC 2.1.1.43). It contains a SET domain and a Tudor-like Agenet domain. AtMSH6, also called MutS protein homolog 6, is a component of the post-replicative DNA mismatch repair system (MMR). It forms a heterodimer with MutS alpha (MSH2-MSH6 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. AtMSH6 contains a Tudor-like Agenet domain and a MutS domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410475 [Multi-domain]  Cd Length: 51  Bit Score: 75.78  E-value: 3.59e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 332660572 609 VGSRIKVWWPMDQAYYKGVVESYDAAKKKHLVIYDDGDQEILYLKNQKW 657
Cdd:cd20404    1 VGRRVRVYWPEDGTWYEGVVVDYDPSTGKHRVEYDDGDEEEVDLWRELV 49
PRK13808 PRK13808
adenylate kinase; Provisional
 690-822 3.44e-04

adenylate kinase; Provisional


Pssm-ID: 172341 [Multi-domain]  Cd Length: 333  Bit Score: 43.72  E-value: 3.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572 690 AKTGKQSKMDNSSAKKGSGAGSSKAKATPASKSSKTSQDDKTASKSKDSKEASREEEASSEEESEEEEPPKTVGKSGSSR 769
Cdd:PRK13808 199 AKKAAKTPAAKSGAKKASAKAKSAAKKVSKKKAAKTAVSAKKAAKTAAKAAKKAKKTAKKALKKAAKAVKKAAKKAAKAA 278

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 332660572 770 SKKDISSVSKSGKSKASSKKKEEPSKATTSSKSKSGPVKSVpAKSKTGKGKAK 822
Cdd:PRK13808 279 AKAAKGAAKATKGKAKAKKKAGKKAAAGSKAKATAKAPKRG-AKGKKAKKVTK 330
PTZ00121 PTZ00121
MAEBL; Provisional
 276-808 2.24e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  276 KRETEVEKAAEISTPERTDAPKDESGKSGVSNGVAQQNDSSVDTDSMKKQDDTGAKDEPQQLDNPRNTD-LNNTTEEKPD 354
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADeAKKKAEEAKK 1316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  355 VEhQIEEKENESSSVKQADLSKDSDIKEETEPAELLDSKDVLTSPPVDSSVTAATSSENEKNKSVQILPSKTSGDETANV 434
Cdd:PTZ00121 1317 AD-EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  435 SSPSM------AEELPEQSVPKKTANQKKKESS----TEEVKPSASIA-----TEEVSEEPNTSEPQVTKKSGKKVASSS 499
Cdd:PTZ00121 1396 AKKKAeedkkkADELKKAAAAKKKADEAKKKAEekkkADEAKKKAEEAkkadeAKKKAEEAKKAEEAKKKAEEAKKADEA 1475

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  500 KTKptVPPSKKSTSETKVAKQSEKKVVGSDNAQESTKPKEEKKKPGRGKAIDEeslhTSSGDNEKPAVSSGKLASKSKKE 579
Cdd:PTZ00121 1476 KKK--AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE----AKKAEEAKKADEAKKAEEKKKAD 1549

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  580 AKQTVEESPNSNTKRKRSLGQGKASGESLVGSRIKVWWPMDQAYYKGVVESYDAAKKKHLVIYDDGDQEILYLKN----- 654
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkae 1629

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  655 --QKWSPLDESELSQDEEAADQTGQEEDASTVpltKKAKTGKQSKMDNSSAKKGSGAGSSKAKATPASKSSKTSQDDKTA 732
Cdd:PTZ00121 1630 eeKKKVEQLKKKEAEEKKKAEELKKAEEENKI---KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332660572  733 SKSKDSKEASREEEASSEEESEEEEPPKTVGKSGSSRSKKDISSVSKSGKSKASSKKKEEPSKATTSSKSKSGPVK 808
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
 
Name Accession Description Interval E-value
PDS5 cd19953
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. ...
 29-230 5.73e-60

Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. Together with WapI and Scc3, it is involved in the release of the cohesin complex from chromosomes during S phase. The core of the cohesin complex consists of a coiled-coiled heterodimer of Smc1 and Smc30, together with Scc1 (also called kleisin). Pds5 interacts with Scc1 via a conserved patch on the surface of its heat repeats. Pds5 also promotes the acetylation of Smc3 that protects cohesin from releasing activity in G2 phase.


Pssm-ID: 410996 [Multi-domain]  Cd Length: 630  Bit Score: 215.47  E-value: 5.73e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  29 LLSFLDKLFVSLAEVEQSPPDSmqNALTPLMKGLVGGKLFKHSDVDVKVAVAACISEITRITAPDAPYDDDQMKEVFKLI 108
Cdd:cd19953    1 LLKRLKALHEELSELDQDEVDL--ESLEPVAKELVSPKLLKHKDKGVRALVACCLADILRLYAPDAPYTDDQLKDIFKLF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572 109 VSSFEDLVDKSSRSYAKRISILETVAKVRSCVVMLDLEC-DALLIEMFQHFLKAIRDHHSGNVFSSMENIMTLVLEESED 187
Cdd:cd19953   79 ISQLKGLLDPDSPYFSQYFYLLESLAEVKSIVLLLDLPDaDELILELFKTFFDLVRDDHPKNVENLMLDILVELIDESES 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 332660572 188 IPSEMLSPILHS-VKKDDEISQVSRRLAEQVLSNCASKLKTYLT 230
Cdd:cd19953  159 VPQEVLDIILAQfLKKNKSENPPAYRLAVEVCERCSDKLQRYVT 202
PDS5 pfam20168
Sister chromatid cohesion protein PDS5 protein; This entry represents the Sister chromatid ...
 27-230 3.21e-51

Sister chromatid cohesion protein PDS5 protein; This entry represents the Sister chromatid cohesion protein PDS5. The large PDS5 molecule is exclusively alpha helical, composed of a large number of HEAT-like repeats and helical extensions/additions that deviate from the HEAT repeat pattern.


Pssm-ID: 466319 [Multi-domain]  Cd Length: 1051  Bit Score: 195.12  E-value: 3.21e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572    27 DELLSFLDKLFVSLAEVEQSppDSMQNALTPLMKGLVGGKLFKHSDVDVKVAVAACISEITRITAPDAPYDDDQMKEVFK 106
Cdd:pfam20168    1 DELLKRLKALHEELSDLDQE--DVDLKSLDPVAKDLVSPKLLKHKDKGVRALVACCLADILRLYAPDAPYTDDQLKDIFK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572   107 LIVSSFEDLVDKSSRSYAKRISILETVAKVRSCVVMLDL-ECDALLIEMFQHFLKAIRDHHSGNVFSSMENIMTLVLEES 185
Cdd:pfam20168   79 LFISQLRGLADPDSPYFSQYFYLLESLAEVKSIVLILDLpDADDLITELFRTFFDLVSRPHSKKVENFMLDILSELIDES 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 332660572   186 EDIPSEMLSPILHS-VKKDDEISQVSRRLAEQVLSNCASKLKTYLT 230
Cdd:pfam20168  159 DSLPQEVLDLILAQfLRKKKKENPPAFRLAVDVCNACADKLQRYVC 204
Tudor_Agenet_AtEML-like cd20404
Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and ...
 609-657 3.59e-17

Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and similar proteins; This family includes Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4), histone-lysine N-methyltransferase trithorax-like proteins ATX1-2 (AtATX1-2), histone-lysine N-methyltransferase ASHH3, DNA mismatch repair protein MSH6, and similar proteins. EMSY-like proteins contain an EMSY N-terminal domain, a central Tudor-like Agenet domain, and a C-terminal coiled-coil motif. AtEML1, AtEML2, and likely AtEML4, contribute to RPP7-mediated immunity. Besides this, AtEML1 and AtEML2 participate in a second EDM2-dependent function and affect floral transition. ATX-like proteins are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1, also called protein SET domain group 27, or trithorax-homolog protein 1 (TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2, also called protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain proteins that consist of an N-terminal Tudor-like Agenet domain, a PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. ASHR3, also called protein SET DOMAIN GROUP 7, functions as a histone-lysine N-methyltransferase (EC 2.1.1.43). It contains a SET domain and a Tudor-like Agenet domain. AtMSH6, also called MutS protein homolog 6, is a component of the post-replicative DNA mismatch repair system (MMR). It forms a heterodimer with MutS alpha (MSH2-MSH6 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. AtMSH6 contains a Tudor-like Agenet domain and a MutS domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410475 [Multi-domain]  Cd Length: 51  Bit Score: 75.78  E-value: 3.59e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 332660572 609 VGSRIKVWWPMDQAYYKGVVESYDAAKKKHLVIYDDGDQEILYLKNQKW 657
Cdd:cd20404    1 VGRRVRVYWPEDGTWYEGVVVDYDPSTGKHRVEYDDGDEEEVDLWRELV 49
Tudor_AtPTM-like cd20401
Tudor domain found in Arabidopsis thaliana DDT domain-containing protein PTM (AtPTM), Dirigent ...
 609-648 4.17e-05

Tudor domain found in Arabidopsis thaliana DDT domain-containing protein PTM (AtPTM), Dirigent protein 17 (AtDIR17), and similar proteins; This family includes AtPTM and AtDIR17. AtPTM, also called DDT domain-containing protein 1, or PHD type transcription factor with transmembrane domains, is a membrane-bound transcription factor required for plastid-to-nucleus retrograde signaling. AtDIR17 imparts stereoselectivity on the phenoxy radical-coupling reaction, yielding optically active lignans from two molecules of coniferyl alcohol in the biosynthesis of lignans, flavonolignans, and alkaloids, and thus plays a central role in plant secondary metabolism. Members of this family contain one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410472  Cd Length: 50  Bit Score: 41.78  E-value: 4.17e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 332660572 609 VGSRIKVWWpmDQAYYKGVVESYDAAKKKHLVIYDDGDQE 648
Cdd:cd20401    1 VGRRVRKKF--DGEWFDGTVVSYDKKTGLYHVEYEDGDAE 38
PRK13808 PRK13808
adenylate kinase; Provisional
 690-822 3.44e-04

adenylate kinase; Provisional


Pssm-ID: 172341 [Multi-domain]  Cd Length: 333  Bit Score: 43.72  E-value: 3.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572 690 AKTGKQSKMDNSSAKKGSGAGSSKAKATPASKSSKTSQDDKTASKSKDSKEASREEEASSEEESEEEEPPKTVGKSGSSR 769
Cdd:PRK13808 199 AKKAAKTPAAKSGAKKASAKAKSAAKKVSKKKAAKTAVSAKKAAKTAAKAAKKAKKTAKKALKKAAKAVKKAAKKAAKAA 278

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 332660572 770 SKKDISSVSKSGKSKASSKKKEEPSKATTSSKSKSGPVKSVpAKSKTGKGKAK 822
Cdd:PRK13808 279 AKAAKGAAKATKGKAKAKKKAGKKAAAGSKAKATAKAPKRG-AKGKKAKKVTK 330
Tudor_53BP1 cd20383
Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; ...
 609-654 1.47e-03

Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; 53BP1, also called p53-binding protein 1 (p53BP1), is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics, and class-switch recombination (CSR) during antibody genesis. It plays a key role in the repair of DSBs in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1. It is recruited to DSB sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSB sites. 53BP1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410454  Cd Length: 52  Bit Score: 37.24  E-value: 1.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 332660572 609 VGSRIKVWWPMDQAYYKGVVESyDAAKKKHLVIYDDGDQEILYLKN 654
Cdd:cd20383    1 VGTRVFAKWSSDGYYYPGIITR-VLGDGKYKVLFDDGYERDVKGKD 45
PTZ00121 PTZ00121
MAEBL; Provisional
 276-808 2.24e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  276 KRETEVEKAAEISTPERTDAPKDESGKSGVSNGVAQQNDSSVDTDSMKKQDDTGAKDEPQQLDNPRNTD-LNNTTEEKPD 354
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADeAKKKAEEAKK 1316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  355 VEhQIEEKENESSSVKQADLSKDSDIKEETEPAELLDSKDVLTSPPVDSSVTAATSSENEKNKSVQILPSKTSGDETANV 434
Cdd:PTZ00121 1317 AD-EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  435 SSPSM------AEELPEQSVPKKTANQKKKESS----TEEVKPSASIA-----TEEVSEEPNTSEPQVTKKSGKKVASSS 499
Cdd:PTZ00121 1396 AKKKAeedkkkADELKKAAAAKKKADEAKKKAEekkkADEAKKKAEEAkkadeAKKKAEEAKKAEEAKKKAEEAKKADEA 1475

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  500 KTKptVPPSKKSTSETKVAKQSEKKVVGSDNAQESTKPKEEKKKPGRGKAIDEeslhTSSGDNEKPAVSSGKLASKSKKE 579
Cdd:PTZ00121 1476 KKK--AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE----AKKAEEAKKADEAKKAEEKKKAD 1549

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  580 AKQTVEESPNSNTKRKRSLGQGKASGESLVGSRIKVWWPMDQAYYKGVVESYDAAKKKHLVIYDDGDQEILYLKN----- 654
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkae 1629

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572  655 --QKWSPLDESELSQDEEAADQTGQEEDASTVpltKKAKTGKQSKMDNSSAKKGSGAGSSKAKATPASKSSKTSQDDKTA 732
Cdd:PTZ00121 1630 eeKKKVEQLKKKEAEEKKKAEELKKAEEENKI---KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332660572  733 SKSKDSKEASREEEASSEEESEEEEPPKTVGKSGSSRSKKDISSVSKSGKSKASSKKKEEPSKATTSSKSKSGPVK 808
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
PRK08581 PRK08581
amidase domain-containing protein;
293-602 2.30e-03

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 41.70  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572 293 TDAPKDESGKSGVSNGVAQQNDSSVDTDSMKKQDDTGAKDEpqqlDNPRNTDLNNTTEEKPDVEhqieEKENESSSVKQA 372
Cdd:PRK08581  28 DDPQKDSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNT----SNQDNNDKKFSTIDSSTSD----SNNIIDFIYKNL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572 373 dlsKDSDIKEETEPAELLDSKDVLTSPPVDSSVTAATSSENEKNKSvqilpSKTSGDETANVSSPSMAEELPEQSVPKKT 452
Cdd:PRK08581 100 ---PQTNINQLLTKNKYDDNYSLTTLIQNLFNLNSDISDYEQPRNS-----EKSTNDSNKNSDSSIKNDTDTQSSKQDKA 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572 453 ANQKkkESSTEEVKPSASiateevSEEPNTSEPQVTKKSGKKVASSSKTkptvpPSKKSTSETKVAKQSEKKVVGSDNAQ 532
Cdd:PRK08581 172 DNQK--APSSNNTKPSTS------NKQPNSPKPTQPNQSNSQPASDDTA-----NQKSSSKDNQSMSDSALDSILDQYSE 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332660572 533 ESTKPKEEKKKPGrgkaideESLHTSSGDNEKPAVSSGKLASKSKKEAKQTVEESPNSNTKRKRSLGQGK 602
Cdd:PRK08581 239 DAKKTQKDYASQS-------KKDKTETSNTKNPQLPTQDELKHKSKPAQSFENDVNQSNTRSTSLFETGP 301
 
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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