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Conserved domains on  [gi|1907079522|ref|XP_036012101|]
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CCR4-NOT transcription complex subunit 6 isoform X1 [Mus musculus]

Protein Classification

LRR and Deadenylase_CCR4a domain-containing protein( domain architecture ID 11469388)

LRR and Deadenylase_CCR4a domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Deadenylase_CCR4a cd10313
C-terminal deadenylase domain of CCR4a, also known as CCR4-NOT transcription complex subunit 6; ...
 191-540 0e+00

C-terminal deadenylase domain of CCR4a, also known as CCR4-NOT transcription complex subunit 6; This subfamily contains the C-terminal catalytic domain of the deadenylase, CCR4a, also known as CCR4-NOT transcription complex subunit 6 (CNOT6). CCR4 belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. CCR4 is the major deadenylase subunit of the CCR4-NOT transcription complex, which contains two deadenylase subunits and several noncatalytic subunits. The other deadenylase subunit, Caf1, is a DEDD-type protein and does not belong in this superfamily. There are two vertebrate CCR4 proteins, CCR4a and CCR4b (also called CNOT6-like or CNOT6L). CCR4a associates with other components, such as CNOT1-3 and Caf1, to form a CCR4-NOT multisubunit complex, which regulates transcription and mRNA degradation. The nuclease domain of CCR4a exhibits Mg2+-dependent deadenylase activity with specificity for poly (A) RNA as substrate. CCR4a is a component of P-bodies and is necessary for foci formation of various P-body components. It also plays a role in cellular responses to DNA damage, by regulating Chk2 activity.


:

Pssm-ID: 197340  Cd Length: 350  Bit Score: 738.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 191 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 270
Cdd:cd10313     1 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIMQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 271 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAVLLELRKELIEMSSGKPHLGT 350
Cdd:cd10313    81 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAVLLELRKELIEMSSGKPHLGM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 351 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASRSLKSSVLGECGTIPLVLCADLNSLPDSGVVEYLSTGGV 430
Cdd:cd10313   161 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASRSLKSSVLGETGTIPLVLCADLNSLPDSGVVEYLSTGGV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 431 ETNHKDFKELRYNESLTNFSCNGKNGMTNGRITHGFKLKSAYENGLMPYTNYTFDFKGIIDYIFYSKPQLNTLAILGPLD 510
Cdd:cd10313   241 ETNHKDFKELRYNESLTNFSCNGKNGTTNGRITHGFKLKSAYENGLMPYTNYTFDFKGIIDYIFYSKPQLNTLGILGPLD 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 1907079522 511 HHWLVENNISGCPHPLIPSDHFSLFAQLEL 540
Cdd:cd10313   321 HHWLVENNISGCPHPLIPSDHFSLFAQLEL 350
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-133 2.94e-22

Leucine-rich repeat (LRR) protein [Transcription];


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 99.24  E-value: 2.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  51 THLTALHLSDNSLSCIPSDIAKLHNLVYLDLSHNQIQSLPAELGNMVSLRELHLNYNQLRVLPFELGKLFQLQTLSLKGN 130
Cdd:COG4886   136 TNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGN 215


                  ...
gi 1907079522 131 PLT 133
Cdd:COG4886   216 QLT 218
 
Name Accession Description Interval E-value
Deadenylase_CCR4a cd10313
C-terminal deadenylase domain of CCR4a, also known as CCR4-NOT transcription complex subunit 6; ...
 191-540 0e+00

C-terminal deadenylase domain of CCR4a, also known as CCR4-NOT transcription complex subunit 6; This subfamily contains the C-terminal catalytic domain of the deadenylase, CCR4a, also known as CCR4-NOT transcription complex subunit 6 (CNOT6). CCR4 belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. CCR4 is the major deadenylase subunit of the CCR4-NOT transcription complex, which contains two deadenylase subunits and several noncatalytic subunits. The other deadenylase subunit, Caf1, is a DEDD-type protein and does not belong in this superfamily. There are two vertebrate CCR4 proteins, CCR4a and CCR4b (also called CNOT6-like or CNOT6L). CCR4a associates with other components, such as CNOT1-3 and Caf1, to form a CCR4-NOT multisubunit complex, which regulates transcription and mRNA degradation. The nuclease domain of CCR4a exhibits Mg2+-dependent deadenylase activity with specificity for poly (A) RNA as substrate. CCR4a is a component of P-bodies and is necessary for foci formation of various P-body components. It also plays a role in cellular responses to DNA damage, by regulating Chk2 activity.


Pssm-ID: 197340  Cd Length: 350  Bit Score: 738.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 191 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 270
Cdd:cd10313     1 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIMQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 271 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAVLLELRKELIEMSSGKPHLGT 350
Cdd:cd10313    81 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAVLLELRKELIEMSSGKPHLGM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 351 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASRSLKSSVLGECGTIPLVLCADLNSLPDSGVVEYLSTGGV 430
Cdd:cd10313   161 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASRSLKSSVLGETGTIPLVLCADLNSLPDSGVVEYLSTGGV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 431 ETNHKDFKELRYNESLTNFSCNGKNGMTNGRITHGFKLKSAYENGLMPYTNYTFDFKGIIDYIFYSKPQLNTLAILGPLD 510
Cdd:cd10313   241 ETNHKDFKELRYNESLTNFSCNGKNGTTNGRITHGFKLKSAYENGLMPYTNYTFDFKGIIDYIFYSKPQLNTLGILGPLD 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 1907079522 511 HHWLVENNISGCPHPLIPSDHFSLFAQLEL 540
Cdd:cd10313   321 HHWLVENNISGCPHPLIPSDHFSLFAQLEL 350
PLN03144 PLN03144
Carbon catabolite repressor protein 4 homolog; Provisional
 160-537 1.67e-73

Carbon catabolite repressor protein 4 homolog; Provisional


Pssm-ID: 178689 [Multi-domain]  Cd Length: 606  Bit Score: 245.41  E-value: 1.67e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 160 TAKRISTEQPPPRSWIMLQEPDRTRPTAL---------FSVMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIIQEILS 230
Cdd:PLN03144  217 TSRVIPAPSPTPRRLIQVNGLDGMGHLDLdgrtssagtFTVLSYNILSDLYATSDMYSYCPPWALSWTYRRQNLLREIVG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 231 CNADIISLQEVETEQYYSFFLVELKERGYNGFFspKSRARTMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANS 310
Cdd:PLN03144  297 YRADILCLQEVQSDHFEEFFAPELDKHGYQALY--KKKTTEVYTGNTYVIDGCATFFRRDRFSLVKKYEVEFNKAAQSLT 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 311 EG------SEAMLNRVMtKDNIGVAVLLELRkelieMSSGKPHLGTEKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVK 384
Cdd:PLN03144  375 EAlipsaqKKAALNRLL-KDNVALIVVLEAK-----FGNQGADNGGKRQLLCVANTHIHANQELKDVKLWQVHTLLKGLE 448

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 385 NIIDKASrslkssvlgecgtIPLVLCADLNSLPDSGVVEYLSTGGVETNHKD-----FKELRYNESLtnfscngkngmtn 459
Cdd:PLN03144  449 KIAASAD-------------IPMLVCGDFNSVPGSAPHCLLATGKVDPLHPDlavdpLGILRPASKL------------- 502

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 460 griTHGFKLKSAYEN-GLMP---------------------YTNYTFDFKGIIDYIFYSKPQLNTLAILGPLDHHWLVEN 517
Cdd:PLN03144  503 ---THQLPLVSAYSSfARMPgsgsgleqqrrrmdpatneplFTNCTRDFIGTLDYIFYTADSLTVESLLELLDEESLRKD 579

                         410       420
                  ....*....|....*....|
gi 1907079522 518 niSGCPHPLIPSDHFSLFAQ 537
Cdd:PLN03144  580 --TALPSPEWSSDHIALLAE 597
CCR4 COG5239
mRNA deadenylase, 3'-5' endonuclease subunit Ccr4 [RNA processing and modification];
176-539 1.54e-66

mRNA deadenylase, 3'-5' endonuclease subunit Ccr4 [RNA processing and modification];


Pssm-ID: 227564 [Multi-domain]  Cd Length: 378  Bit Score: 220.80  E-value: 1.54e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 176 MLQEPDRTRPTALFSVMCYNVLCDKYATRQLYGYCpSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELK 255
Cdd:COG5239    18 FLSIGHYAEKDTDFTIMTYNVLAQTYATRKMYPYS-GWALKWSYRSRLLLQELLYYNADILCLQEVDAEDFEDFWKDQLG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 256 ERGYNGFFSPKSR-ARTMSEQERKHVDGCAIFFKTE----KFTLVQKHTVEFNQLAMANSE--GSEAMLNRVMTKDNIGV 328
Cdd:COG5239    97 KLGYDGIFIPKERkVKWMIDYDTTKVDGCAIFLKRFidssKLGLILAVTHLFWHPYGYYERfrQTYILLNRIGEKDNIAW 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 329 AVLLELrkeLIEMSSGKPhlgtekqlILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDK--ASRSLKSSVLGEcGTIP 406
Cdd:COG5239   177 VCLFVG---LFNKEPGDT--------PYVANTHLPWDPKYRDVKLIQCSLLYRELKKVLKEelNDDKEEGDIKSY-PEVD 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 407 LVLCADLNSLPDSGVVEYLSTGGVEtNHKDFKELRYNEsltnfscngkngMTNGR-ITHGFKLKSAYENGLMPYTNYTFD 485
Cdd:COG5239   245 ILITGDFNSLRASLVYKFLVTSQIQ-LHESLNGRDFSL------------YSVGYkFVHPENLKSDNSKGELGFTNWTPG 311

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907079522 486 FKGIIDYIFYSKPQLNTLA-ILGPLDHHWLVenNISGCPHPLIPSDHFSLFAQLE 539
Cdd:COG5239   312 FKGVIDYIFYHGGLLTRQTgLLGVVEGEYAS--KVIGLPNMPFPSDHIPLLAEFA 364
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-133 2.94e-22

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 99.24  E-value: 2.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  51 THLTALHLSDNSLSCIPSDIAKLHNLVYLDLSHNQIQSLPAELGNMVSLRELHLNYNQLRVLPFELGKLFQLQTLSLKGN 130
Cdd:COG4886   136 TNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGN 215


                  ...
gi 1907079522 131 PLT 133
Cdd:COG4886   216 QLT 218
PLN03150 PLN03150
hypothetical protein; Provisional
 66-133 4.10e-10

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 62.53  E-value: 4.10e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  66 IPSDIAKLHNLVYLDLSHNQIQ-SLPAELGNMVSLRELHLNYNQLR-VLPFELGKLFQLQTLSLKGNPLT 133
Cdd:PLN03150  434 IPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLS 503
LRR_8 pfam13855
Leucine rich repeat;
51-109 3.25e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 52.91  E-value: 3.25e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907079522  51 THLTALHLSDNSLSCIPSDIAK-LHNLVYLDLSHNQIQSL-PAELGNMVSLRELHLNYNQL 109
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 51-135 4.75e-09

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 56.72  E-value: 4.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  51 THLTALHLSDNSLSCIPsDIAKLHNLVYLDLSHNQIQSLPaELGNMVSLRELHLNYNQLRVLpfE-LGKLFQLQTLSL-- 127
Cdd:cd21340    24 KNLKVLYLYDNKITKIE-NLEFLTNLTHLYLQNNQIEKIE-NLENLVNLKKLYLGGNRISVV--EgLENLTNLEELHIen 99

                          90
                  ....*....|..
gi 1907079522 128 ----KGNPLTQD 135
Cdd:cd21340   100 qrlpPGEKLTFD 111
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 192-308 1.56e-07

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 51.84  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 192 MCYNVLCDkyatrqlygycPSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKsrart 271
Cdd:pfam03372   1 LTWNVNGG-----------NADAAGDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFLSYGGPG----- 64

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907079522 272 mseqERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMA 308
Cdd:pfam03372  65 ----GGGGGGGVAILSRYPLSSVILVDLGEFGDPALR 97
 
Name Accession Description Interval E-value
Deadenylase_CCR4a cd10313
C-terminal deadenylase domain of CCR4a, also known as CCR4-NOT transcription complex subunit 6; ...
 191-540 0e+00

C-terminal deadenylase domain of CCR4a, also known as CCR4-NOT transcription complex subunit 6; This subfamily contains the C-terminal catalytic domain of the deadenylase, CCR4a, also known as CCR4-NOT transcription complex subunit 6 (CNOT6). CCR4 belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. CCR4 is the major deadenylase subunit of the CCR4-NOT transcription complex, which contains two deadenylase subunits and several noncatalytic subunits. The other deadenylase subunit, Caf1, is a DEDD-type protein and does not belong in this superfamily. There are two vertebrate CCR4 proteins, CCR4a and CCR4b (also called CNOT6-like or CNOT6L). CCR4a associates with other components, such as CNOT1-3 and Caf1, to form a CCR4-NOT multisubunit complex, which regulates transcription and mRNA degradation. The nuclease domain of CCR4a exhibits Mg2+-dependent deadenylase activity with specificity for poly (A) RNA as substrate. CCR4a is a component of P-bodies and is necessary for foci formation of various P-body components. It also plays a role in cellular responses to DNA damage, by regulating Chk2 activity.


Pssm-ID: 197340  Cd Length: 350  Bit Score: 738.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 191 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 270
Cdd:cd10313     1 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIMQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 271 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAVLLELRKELIEMSSGKPHLGT 350
Cdd:cd10313    81 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAVLLELRKELIEMSSGKPHLGM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 351 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASRSLKSSVLGECGTIPLVLCADLNSLPDSGVVEYLSTGGV 430
Cdd:cd10313   161 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASRSLKSSVLGETGTIPLVLCADLNSLPDSGVVEYLSTGGV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 431 ETNHKDFKELRYNESLTNFSCNGKNGMTNGRITHGFKLKSAYENGLMPYTNYTFDFKGIIDYIFYSKPQLNTLAILGPLD 510
Cdd:cd10313   241 ETNHKDFKELRYNESLTNFSCNGKNGTTNGRITHGFKLKSAYENGLMPYTNYTFDFKGIIDYIFYSKPQLNTLGILGPLD 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 1907079522 511 HHWLVENNISGCPHPLIPSDHFSLFAQLEL 540
Cdd:cd10313   321 HHWLVENNISGCPHPLIPSDHFSLFAQLEL 350
Deadenylase_CCR4b cd10312
C-terminal deadenylase domain of CCR4b, also known as CCR4-NOT transcription complex subunit ...
 191-540 0e+00

C-terminal deadenylase domain of CCR4b, also known as CCR4-NOT transcription complex subunit 6-like; This subfamily contains the C-terminal catalytic domain of the deadenylase, CCR4b, also known as CCR4-NOT transcription complex subunit 6-like (CNOT6L). CCR4 belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. CCR4 is the major deadenylase subunit of the CCR4-NOT transcription complex, which contains two deadenylase subunits and several noncatalytic subunits. The other deadenylase subunit, Caf1, is a DEDD-type protein and does not belong in this superfamily. There are two vertebrate CCR4 proteins, CCR4a (also called CCR4-NOT transcription complex subunit 6 or CNOT6) and CCR4b. CCR4b associates with other components, such as CNOT1-3 and Caf1, to form a CCR4-NOT multisubunit complex, which regulates transcription and mRNA degradation. The nuclease domain of CCR4b exhibits Mg2+-dependent deadenylase activity with strict specificity for poly (A) RNA as substrate. CCR4b is mainly localized in the cytoplasm. It regulates cell growth and influences cell cycle progression by regulating p27/Kip1 mRNA levels. It contributes to the prevention of cell death by regulating insulin-like growth factor-binding protein 5.


Pssm-ID: 197339  Cd Length: 348  Bit Score: 675.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 191 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 270
Cdd:cd10312     1 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 271 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAVLLELRKELIEmSSGKPHLGT 350
Cdd:cd10312    81 IMSEQERKHVDGCAIFFKTEKFSLVQKHTVEFNQVAMANSEGSEAMLNRVMTKDNIGVAVVLEVHKELFG-AGMKPIHAA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 351 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASRSLkSSVLGECGTIPLVLCADLNSLPDSGVVEYLSTGGV 430
Cdd:cd10312   160 DKQLLIVANAHMHWDPEYSDVKLIQTMMFVSELKNILEKASSRP-GSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 431 ETNHKDFKELRYNESLTNFSCNGKNGMTNGRITHGFKLKSAYENGLMPYTNYTFDFKGIIDYIFYSKPQLNTLAILGPLD 510
Cdd:cd10312   239 ADNHKDFKELRYNECLMNFSCNGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLD 318

                         330       340       350
                  ....*....|....*....|....*....|
gi 1907079522 511 HHWLVENNISGCPHPLIPSDHFSLFAQLEL 540
Cdd:cd10312   319 PQWLVENNITGCPHPHIPSDHFSLLTQLEL 348
Deadenylase_CCR4 cd09097
C-terminal deadenylase domain of CCR4 and related domains; This subfamily contains the ...
 191-540 0e+00

C-terminal deadenylase domain of CCR4 and related domains; This subfamily contains the C-terminal catalytic domain of the deadenylases, Saccharomyces cerevisiae Ccr4p and two vertebrate homologs (CCR4a and CCR4b), and related domains. CCR4 belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. CCR4 is the major deadenylase subunit of the CCR4-NOT transcription complex, which contains two deadenylase subunits and several noncatalytic subunits. The other deadenylase subunit, Caf1 (called Pop2 in yeast), is a DEDD-type protein and does not belong in this superfamily. Saccharomyces cerevisiae CCR4 (or Ccr4p) is a 3'-5' poly(A) RNA and ssDNA exonuclease. It is the catalytic subunit of the yeast mRNA deadenylase (Ccr4p/Pop2p/Not complex). This complex participates in various ways in mRNA metabolism, including transcription initiation and elongation, and mRNA degradation. Ccr4p degrades both poly(A) and single-stranded DNA. There are two vertebrate homologs of Ccr4p, CCR4a (also called CCR4-NOT transcription complex subunit 6 or CNOT6) and CCR4b (also called CNOT6-like or CNOT6L), which independently associate with other components to form distinct CCR4-NOT multisubunit complexes. The nuclease domain of CNOT6 and CNOT6L exhibits Mg2+-dependent deadenylase activity, with specificity for poly (A) RNA as substrate. CCR4a is a component of P-bodies and is necessary for foci formation. CCR4b regulates p27/Kip1 mRNA levels, thereby influencing cell cycle progression. They both contribute to the prevention of cell death by regulating insulin-like growth factor-binding protein 5.


Pssm-ID: 197331 [Multi-domain]  Cd Length: 329  Bit Score: 574.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 191 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 270
Cdd:cd09097     1 VMCYNVLCDKYATRQQYGYCPSWALNWDYRKQNILKEILSYNADILCLQEVETDQYEDFFLPELKQHGYDGVFKPKSRAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 271 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMAN--SEGSEAMLNRVMTKDNIGVAVLLELRKELIEmssgkphl 348
Cdd:cd09097    81 TMSEAERKHVDGCAIFFKTSKFKLVEKHLIEFNQLAMANadAEGSEDMLNRVMTKDNIALIVVLEARETSYE-------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 349 GTEKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASRslksSVLGECGTIPLVLCADLNSLPDSGVVEYLSTG 428
Cdd:cd09097   153 GNKGQLLIVANTHIHWDPEFSDVKLVQTMMLLEELEKIAEKFSR----YPYEDSADIPLVVCGDFNSLPDSGVYELLSNG 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 429 GVETNHKDFKELRYNESLtnfscngkngmTNGRITHGFKLKSAYEN-GLMPYTNYTFDFKGIIDYIFYSKPQLNTLAILG 507
Cdd:cd09097   229 SVSPNHPDFKEDPYGEYL-----------TASGLTHSFKLKSAYANlGELPFTNYTPDFKGVIDYIFYSADTLSVLGLLG 297

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1907079522 508 PLDHHWlVENNISGCPHPLIPSDHFSLFAQLEL 540
Cdd:cd09097   298 PPDEDW-YLNKVVGLPNPHFPSDHIALLAEFRI 329
PLN03144 PLN03144
Carbon catabolite repressor protein 4 homolog; Provisional
 160-537 1.67e-73

Carbon catabolite repressor protein 4 homolog; Provisional


Pssm-ID: 178689 [Multi-domain]  Cd Length: 606  Bit Score: 245.41  E-value: 1.67e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 160 TAKRISTEQPPPRSWIMLQEPDRTRPTAL---------FSVMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIIQEILS 230
Cdd:PLN03144  217 TSRVIPAPSPTPRRLIQVNGLDGMGHLDLdgrtssagtFTVLSYNILSDLYATSDMYSYCPPWALSWTYRRQNLLREIVG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 231 CNADIISLQEVETEQYYSFFLVELKERGYNGFFspKSRARTMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANS 310
Cdd:PLN03144  297 YRADILCLQEVQSDHFEEFFAPELDKHGYQALY--KKKTTEVYTGNTYVIDGCATFFRRDRFSLVKKYEVEFNKAAQSLT 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 311 EG------SEAMLNRVMtKDNIGVAVLLELRkelieMSSGKPHLGTEKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVK 384
Cdd:PLN03144  375 EAlipsaqKKAALNRLL-KDNVALIVVLEAK-----FGNQGADNGGKRQLLCVANTHIHANQELKDVKLWQVHTLLKGLE 448

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 385 NIIDKASrslkssvlgecgtIPLVLCADLNSLPDSGVVEYLSTGGVETNHKD-----FKELRYNESLtnfscngkngmtn 459
Cdd:PLN03144  449 KIAASAD-------------IPMLVCGDFNSVPGSAPHCLLATGKVDPLHPDlavdpLGILRPASKL------------- 502

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 460 griTHGFKLKSAYEN-GLMP---------------------YTNYTFDFKGIIDYIFYSKPQLNTLAILGPLDHHWLVEN 517
Cdd:PLN03144  503 ---THQLPLVSAYSSfARMPgsgsgleqqrrrmdpatneplFTNCTRDFIGTLDYIFYTADSLTVESLLELLDEESLRKD 579

                         410       420
                  ....*....|....*....|
gi 1907079522 518 niSGCPHPLIPSDHFSLFAQ 537
Cdd:PLN03144  580 --TALPSPEWSSDHIALLAE 597
CCR4 COG5239
mRNA deadenylase, 3'-5' endonuclease subunit Ccr4 [RNA processing and modification];
176-539 1.54e-66

mRNA deadenylase, 3'-5' endonuclease subunit Ccr4 [RNA processing and modification];


Pssm-ID: 227564 [Multi-domain]  Cd Length: 378  Bit Score: 220.80  E-value: 1.54e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 176 MLQEPDRTRPTALFSVMCYNVLCDKYATRQLYGYCpSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELK 255
Cdd:COG5239    18 FLSIGHYAEKDTDFTIMTYNVLAQTYATRKMYPYS-GWALKWSYRSRLLLQELLYYNADILCLQEVDAEDFEDFWKDQLG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 256 ERGYNGFFSPKSR-ARTMSEQERKHVDGCAIFFKTE----KFTLVQKHTVEFNQLAMANSE--GSEAMLNRVMTKDNIGV 328
Cdd:COG5239    97 KLGYDGIFIPKERkVKWMIDYDTTKVDGCAIFLKRFidssKLGLILAVTHLFWHPYGYYERfrQTYILLNRIGEKDNIAW 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 329 AVLLELrkeLIEMSSGKPhlgtekqlILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDK--ASRSLKSSVLGEcGTIP 406
Cdd:COG5239   177 VCLFVG---LFNKEPGDT--------PYVANTHLPWDPKYRDVKLIQCSLLYRELKKVLKEelNDDKEEGDIKSY-PEVD 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 407 LVLCADLNSLPDSGVVEYLSTGGVEtNHKDFKELRYNEsltnfscngkngMTNGR-ITHGFKLKSAYENGLMPYTNYTFD 485
Cdd:COG5239   245 ILITGDFNSLRASLVYKFLVTSQIQ-LHESLNGRDFSL------------YSVGYkFVHPENLKSDNSKGELGFTNWTPG 311

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907079522 486 FKGIIDYIFYSKPQLNTLA-ILGPLDHHWLVenNISGCPHPLIPSDHFSLFAQLE 539
Cdd:COG5239   312 FKGVIDYIFYHGGLLTRQTgLLGVVEGEYAS--KVIGLPNMPFPSDHIPLLAEFA 364
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 191-538 3.95e-42

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes the catalytic domain (exonuclease/endonuclease/phosphatase or EEP domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins.


Pssm-ID: 197306 [Multi-domain]  Cd Length: 241  Bit Score: 151.48  E-value: 3.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 191 VMCYNVLCDKYATRqlygycpswalnwdyrKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRar 270
Cdd:cd08372     1 VASYNVNGLNAATR----------------ASGIARWVRELDPDIVCLQEVKDSQYSAVALNQLLPEGYHQYQSGPSR-- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 271 tmseqeRKHVDGCAIFFKTEKFTLVQKHTVEFNQlamansegseamlnrVMTKDNIGVAVllelrkeliemssgkpHLGT 350
Cdd:cd08372    63 ------KEGYEGVAILSKTPKFKIVEKHQYKFGE---------------GDSGERRAVVV----------------KFDV 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 351 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASrslkssvlgecgtIPLVLCADLNSLPDSGVVEYLStggv 430
Cdd:cd08372   106 HDKELCVVNAHLQAGGTRADVRDAQLKEVLEFLKRLRQPNS-------------APVVICGDFNVRPSEVDSENPS---- 168

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 431 etnhkdfkelrynesltnfscngkngmTNGRITHGFKLKSAYENGLMPYTNYTF--DFKGIIDYIFYSKPqlntlaiLGP 508
Cdd:cd08372   169 ---------------------------SMLRLFVALNLVDSFETLPHAYTFDTYmhNVKSRLDYIFVSKS-------LLP 214

                         330       340       350
                  ....*....|....*....|....*....|
gi 1907079522 509 LDHHWLVennISGCPHPLIPSDHFSLFAQL 538
Cdd:cd08372   215 SVKSSKI---LSDAARARIPSDHYPIEVTL 241
Deadenylase_nocturnin cd09096
C-terminal deadenylase domain of nocturnin and related domains; This subfamily contains the ...
 210-540 2.43e-26

C-terminal deadenylase domain of nocturnin and related domains; This subfamily contains the C-terminal catalytic domain of the deadenylase, nocturnin, and related domains. Nocturnin is a poly(A)-specific 3' exonuclease that specifically degrades the 3' poly(A) tail of RNA in a process known as deadenylation. This nuclease activity is manganese dependent. Nocturnin is expressed in the cytoplasm of Xenopus laevis retinal photoreceptor cells in a rhythmic fashion, and it has been proposed that it participates in posttranscriptional regulation of the circadian clock or its outputs, and that the mRNA target(s) of this deadenylase are circadian clock-related. In mouse, the nocturnin gene, mNoc, is expressed in a circadian pattern in a range of tissues including retina, spleen, heart, kidney, and liver. It is highly expressed in bone-marrow stromal cells, adipocytes and hepatocytes. In mammals, nocturnin plays a role in regulating mesenchymal stem-cell lineage allocation, perhaps through regulating PPAR-gamma (peroxisome proliferator-activated receptor-gamma) nuclear translocation. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197330 [Multi-domain]  Cd Length: 280  Bit Score: 108.66  E-value: 2.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 210 CPSWALNWDYRKKAIIQEILSCNADIISLQEVetEQYYSFFLVELKERGYNGFFSPKSRARTMSEQERKHVDGCAIFFKT 289
Cdd:cd09096    22 CPCEALKWEERKYLILEEILTYDPDILCLQEV--DHYKDTLQPLLSRLGYQGTFFPKPDSPCLYIENNNGPDGCALFFRK 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 290 EKFTLVqkhtvefnqlamaNSEGseAMLNRVMTKDNiGVAVLLELRKELiemsSGKPhlgtekqlILVANAHMHWDPEYS 369
Cdd:cd09096   100 DRFELV-------------NTEK--IRLSAMTLKTN-QVAIACTLRCKE----TGRE--------ICLAVTHLKARTGWE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 370 DVKLVQTMMFLSEVKNIIdkasrslkssvlgECGTIPLVLCADLNSLPDSGVveylstggvetnhkdfkelrYNEsLTNF 449
Cdd:cd09096   152 RLRSEQGKDLLQNLQSFI-------------EGAKIPLIICGDFNAEPTEPV--------------------YKT-FSNS 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 450 SCNgkngmtngrITHGFKLKSAYENGLMPYTNYTFDFKG----IIDYIFYSKPQLNTLAILGpldhhWLVENNI--SGCP 523
Cdd:cd09096   198 SLN---------LNSAYKLLSADGQSEPPYTTWKIRTSGecrhTLDYIFYSKDALSVEQLLD-----LPTEEQIgpNRLP 263

                         330
                  ....*....|....*..
gi 1907079522 524 HPLIPSDHFSLFAQLEL 540
Cdd:cd09096   264 SFNYPSDHLSLVCDFSL 280
Deadenylase cd09082
C-terminal deadenylase domain of CCR4, nocturnin, and related domains; This family contains ...
 191-534 2.36e-23

C-terminal deadenylase domain of CCR4, nocturnin, and related domains; This family contains the C-terminal catalytic domains of the deadenylases, CCR4 and nocturnin, and related domains. Nocturnin is a poly(A)-specific 3' exonuclease that specifically degrades the 3' poly(A) tail of RNA in a process known as deadenylation. This nuclease activity is manganese dependent. Nocturnin is expressed in the cytoplasm of the Xenopus laevis retinal photoreceptor cells in a rhythmic fashion, and it has been proposed that it participates in posttranscriptional regulation of the circadian clock or its outputs, and that the mRNA target(s) of this deadenylase are circadian clock-related. Saccharomyces cerevisiae CCR4p is a 3'-5' poly(A) RNA and ssDNA exonuclease. It is the catalytic subunit of the yeast mRNA deadenylase (Ccr4p/Pop2p/Not complex). This complex participates in various ways in mRNA metabolism, including transcription initiation and elongation, and mRNA degradation. The deadenylase activities of Ccr4p and nocturnin differ: nocturnin degrades poly(A), Ccr4p degrades both poly(A) and single-stranded DNA, and in contrast to Ccr4p, nocturnin appears to function in a highly processive manner. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197316 [Multi-domain]  Cd Length: 348  Bit Score: 101.66  E-value: 2.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 191 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 270
Cdd:cd09082     1 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 271 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDN-IGVAVLLELrKELIEMSSGKPHLG 349
Cdd:cd09082    81 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNiGVAVVLEVH-KELFGAGMKPIHAA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 350 TEKQLILvANAHMHWDPEYSDVKLVQTMMFLSEVKNIIdKASRSLKSSVLGECGTIPLVLCADLNSLPDSGVVEYLSTgg 429
Cdd:cd09082   160 DKQLLIV-ANAHMHWDPEYSDVKLIQTMMFVSEVKNIL-EKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSN-- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 430 vetnhkdfKELRYNESLTNFSCNGKNGMTNGRITHGFKLKSAYENGLMPYTNYTFDFKGII----------DYIFYSKPQ 499
Cdd:cd09082   236 --------GGVADNHKDFKELRYNECLMNFSCNGKNGSSEGRITHGFQLKSAYENNLMPYTnytfdfkgviDYIFYSKTH 307

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1907079522 500 LNTLAILGPLDHHWLVENNISGCPHPLIPSDHFSL 534
Cdd:cd09082   308 MNVLGVLGPLDPQWLVENNITGCPHPHIPSDHFSL 342
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-133 2.94e-22

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 99.24  E-value: 2.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  51 THLTALHLSDNSLSCIPSDIAKLHNLVYLDLSHNQIQSLPAELGNMVSLRELHLNYNQLRVLPFELGKLFQLQTLSLKGN 130
Cdd:COG4886   136 TNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGN 215


                  ...
gi 1907079522 131 PLT 133
Cdd:COG4886   216 QLT 218
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-133 1.00e-21

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 97.70  E-value: 1.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  51 THLTALHLSDNSLSCIPSDIAKLHNLVYLDLSHNQIQSLPAELGNMVSLRELHLNYNQLRVLPFELGKLFQLQTLSLKGN 130
Cdd:COG4886   159 TNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNN 238


                  ...
gi 1907079522 131 PLT 133
Cdd:COG4886   239 QLT 241
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-133 5.33e-21

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 95.39  E-value: 5.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  51 THLTALHLSDNSLSCIPSDIAKLHNLVYLDLSHNQIQSLPAELGNMVSLRELHLNYNQLRVLPFELGKLFQLQTLSLKGN 130
Cdd:COG4886   113 TNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNN 192


                  ...
gi 1907079522 131 PLT 133
Cdd:COG4886   193 QIT 195
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
 190-538 7.43e-20

Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds. Their substrates range from nucleic acids to phospholipids and perhaps, proteins.


Pssm-ID: 197317 [Multi-domain]  Cd Length: 252  Bit Score: 89.20  E-value: 7.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 190 SVMCYNVLCDkyatrqlygyCPSWALN-WDYRKKAIIQEILSCNADIISLQEVETEQyysffLVELKER--GYNGFfspk 266
Cdd:cd09083     1 RVMTFNIRYD----------NPSDGENsWENRKDLVAELIKFYDPDIIGTQEALPHQ-----LADLEELlpEYDWI---- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 267 SRARTMSEQERKHvdgCAIFFKTEKFTLVQKHTveF---NQLAMANSEGSEAMLNRVMTkdnigvAVLLELRKeliemsS 343
Cdd:cd09083    62 GVGRDDGKEKGEF---SAIFYRKDRFELLDSGT--FwlsETPDVVGSKGWDAALPRICT------WARFKDKK------T 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 344 GKPhlgtekqlILVANAHMhwDPEYSDVKLVQTMMFLSEVKNIidkasrslkssvlgeCGTIPLVLCADLNSLPDSGVVE 423
Cdd:cd09083   125 GKE--------FYVFNTHL--DHVGEEAREESAKLILERIKEI---------------AGDLPVILTGDFNAEPDSEPYK 179

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 424 YLSTGGvetnhkdfkelrynesltnfscngkngmtngrithgfkLKSAYENGLMPYTN--YTF-DFKGI-----IDYIFY 495
Cdd:cd09083   180 TLTSGG--------------------------------------LKDARDTAATTDGGpeGTFhGFKGPpggsrIDYIFV 221

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1907079522 496 SKPqlntlaiLGPLDHHwLVENNISGCphplIPSDHFSLFAQL 538
Cdd:cd09083   222 SPG-------VKVLSYE-ILTDRYDGR----YPSDHFPVVADL 252
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-157 1.59e-11

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 66.50  E-value: 1.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  51 THLTALHLSDNSLSCIPSdIAKLHNLVYLDLSHNQIQSLPaELGNMVSLRELHLNYNQLRVLPFE-LGKLFQLQTLSLKG 129
Cdd:COG4886   228 TNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLTDLKLKeLELLLGLNSLLLLL 305

                          90       100
                  ....*....|....*....|....*...
gi 1907079522 130 NPLTQDILNLCLEPDGTRRLLNYLLDNL 157
Cdd:COG4886   306 LLLNLLELLILLLLLTTLLLLLLLLKGL 333
PLN03150 PLN03150
hypothetical protein; Provisional
 66-133 4.10e-10

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 62.53  E-value: 4.10e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  66 IPSDIAKLHNLVYLDLSHNQIQ-SLPAELGNMVSLRELHLNYNQLR-VLPFELGKLFQLQTLSLKGNPLT 133
Cdd:PLN03150  434 IPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLS 503
LRR_8 pfam13855
Leucine rich repeat;
51-109 3.25e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 52.91  E-value: 3.25e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907079522  51 THLTALHLSDNSLSCIPSDIAK-LHNLVYLDLSHNQIQSL-PAELGNMVSLRELHLNYNQL 109
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 51-135 4.75e-09

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 56.72  E-value: 4.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  51 THLTALHLSDNSLSCIPsDIAKLHNLVYLDLSHNQIQSLPaELGNMVSLRELHLNYNQLRVLpfE-LGKLFQLQTLSL-- 127
Cdd:cd21340    24 KNLKVLYLYDNKITKIE-NLEFLTNLTHLYLQNNQIEKIE-NLENLVNLKKLYLGGNRISVV--EgLENLTNLEELHIen 99

                          90
                  ....*....|..
gi 1907079522 128 ----KGNPLTQD 135
Cdd:cd21340   100 qrlpPGEKLTFD 111
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
16-134 1.46e-08

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 56.87  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  16 TIMSSEEAANGKKSHWAELEISGKVRSLSSSLWSLTHLTALHLSDNSLSCIPSDIAKLHNLVYLDLSHNQiqslpaELGN 95
Cdd:COG4886    38 LLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE------ELSN 111

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907079522  96 MVSLRELHLNYNQLRVLPFELGKLFQLQTLSLKGNPLTQ 134
Cdd:COG4886   112 LTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTD 150
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 192-308 1.56e-07

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 51.84  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 192 MCYNVLCDkyatrqlygycPSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKsrart 271
Cdd:pfam03372   1 LTWNVNGG-----------NADAAGDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFLSYGGPG----- 64

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907079522 272 mseqERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMA 308
Cdd:pfam03372  65 ----GGGGGGGVAILSRYPLSSVILVDLGEFGDPALR 97
PLN03150 PLN03150
hypothetical protein; Provisional
 52-117 1.72e-07

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 54.05  E-value: 1.72e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  52 HLTALHLSDNSL-SCIPSDIAKLHNLVYLDLSHNQIQ-SLPAELGNMVSLRELHLNYNQL--RVlPFELG 117
Cdd:PLN03150  443 HLQSINLSGNSIrGNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLsgRV-PAALG 511
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
 191-536 2.81e-07

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps, proteins.


Pssm-ID: 197318 [Multi-domain]  Cd Length: 246  Bit Score: 51.91  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 191 VMCYNVlcdkyatRQLYGYcpswalNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 270
Cdd:cd09084     1 VMSYNV-------RSFNRY------KWKDDPDKILDFIKKQDPDILCLQEYYGSEGDKDDDLRLLLKGYPYYYVVYKSDS 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 271 TMSEQerkhvdgcAIFfktEKFTLVQKHTVEFnqlamansegseamlnrvmtKDNIGVAVLLELRKeliemssgkphlgt 350
Cdd:cd09084    68 GGTGL--------AIF---SKYPILNSGSIDF--------------------PNTNNNAIFADIRV-------------- 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 351 EKQLILVANAHMhwdpeysdvklvQTMMFLSEVKNII--DKASRSLKSSVLGE--------------------CGTIPLV 408
Cdd:cd09084   103 GGDTIRVYNVHL------------ESFRITPSDKELYkeEKKAKELSRNLLRKlaeafkrraaqadllaadiaASPYPVI 170

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 409 LCADLNSLPDSGVveylstggvetnhkdfkelrYNesltnfscngkngmtngRITHGfkLKSAYE---NGLMpytnYTFD 485
Cdd:cd09084   171 VCGDFNDTPASYV--------------------YR-----------------TLKKG--LTDAFVeagSGFG----YTFN 207

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907079522 486 FKGI---IDYIFYSKPqlntlaiLGPLDHHwlvennisgcPHPLIPSDHFSLFA 536
Cdd:cd09084   208 GLFFplrIDYILTSKG-------FKVLRYR----------VDPGKYSDHYPIVA 244
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 53-135 1.08e-06

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 49.78  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  53 LTALHLSDNSLSCIpSDIAKLHNLVYLDLSHNQIQSLpAELGNMvslrelhlnynqlrvlpfeLGKLFQLQTLSLKGNPL 132
Cdd:cd21340   122 LRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISDL-EELLDL-------------------LSSWPSLRELDLTGNPV 180


                  ...
gi 1907079522 133 TQD 135
Cdd:cd21340   181 CKK 183
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 53-136 1.19e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 51.39  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  53 LTALHLSDNSLSC-IPSDIAKLHNLVYLDLSHNQ-IQSLPAELGNMVSLRELHLNYNQLR-VLPFELGKLFQLQTLSLKG 129
Cdd:PLN00113  166 LKVLDLGGNVLVGkIPNSLTNLTSLEFLTLASNQlVGQIPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVY 245


                  ....*..
gi 1907079522 130 NPLTQDI 136
Cdd:PLN00113  246 NNLTGPI 252
LRR_8 pfam13855
Leucine rich repeat;
75-132 1.24e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 45.59  E-value: 1.24e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  75 NLVYLDLSHNQIQSLPAE-LGNMVSLRELHLNYNQLRVL-PFELGKLFQLQTLSLKGNPL 132
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 53-130 6.42e-06

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 47.47  E-value: 6.42e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907079522  53 LTALHLSDNSLSCIPsDIAKLHNLVYLDLSHNQIQSLPAeLGNMVSLRELHLNYNQLRVLPFeLGKLFQLQTLSLKGN 130
Cdd:cd21340     4 ITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIEN-LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLGGN 78
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
53-171 1.29e-04

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 45.07  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  53 LTALHLSDNSLSCIPSDIAKlhNLVYLDLSHNQIQSLPAELGNmvSLRELHLNYNQLRVLPFELGKlfQLQTLSLKGNPL 132
Cdd:PRK15370  264 LQSLDLFHNKISCLPENLPE--ELRYLSVYDNSIRTLPAHLPS--GITHLNVQSNSLTALPETLPP--GLKTLEAGENAL 337

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907079522 133 TQdiLNLCLEPDgtrrllnylLDNLSGTAKRIST--EQPPP 171
Cdd:PRK15370  338 TS--LPASLPPE---------LQVLDVSKNQITVlpETLPP 367
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 53-130 2.84e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 43.68  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  53 LTALHLSDNSLSC-IPSDIAKLHNLVYLDLSHNQIQ-SLPAELGNMVSLRELHLNYNQLR-VLPFElGKLFQLQTLSLKG 129
Cdd:PLN00113  525 LVSLDLSHNQLSGqIPASFSEMPVLSQLDLSQNQLSgEIPKNLGNVESLVQVNISHNHLHgSLPST-GAFLAINASAVAG 603


                  .
gi 1907079522 130 N 130
Cdd:PLN00113  604 N 604
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 51-136 3.68e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 43.68  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  51 THLTALHLSDNSLSC-IPSDIAKLHNLVYLDL-SHNQIQSLPAELGNMVSLRELHLNYNQLR-VLPFELGKLFQLQTLSL 127
Cdd:PLN00113  284 QKLISLDLSDNSLSGeIPELVIQLQNLEILHLfSNNFTGKIPVALTSLPRLQVLQLWSNKFSgEIPKNLGKHNNLTVLDL 363


                  ....*....
gi 1907079522 128 KGNPLTQDI 136
Cdd:PLN00113  364 STNNLTGEI 372
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 75-109 3.80e-04

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 38.38  E-value: 3.80e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907079522  75 NLVYLDLSHNQIQSLPAeLGNMVSLRELHLNYNQL 109
Cdd:pfam12799   2 NLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNNK 35
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-189 5.14e-04

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 42.61  E-value: 5.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  51 THLTALHLSDNSLSCIPsDIAKLHNLVYLDLSHNQIQSL-------PAELGNMVSLRELHLNYNQLRVLPFELGKLFQLQ 123
Cdd:COG4886   250 TNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLTDLklkelelLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLL 328

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907079522 124 TLSLKGNPLTQDILNLCLEPDGTRRLLNYLLDNLSGTAKRISTEQPPPRSWIMLQEPDRTRPTALF 189
Cdd:COG4886   329 LLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLL 394
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 51-91 1.31e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 36.84  E-value: 1.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907079522  51 THLTALHLSDNSLSCIPSdIAKLHNLVYLDLSHN-QIQSLPA 91
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNnKITDLSD 41
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 51-136 1.34e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 41.76  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  51 THLTALHLSDNSLSCIPSDIAKLHNLVYLDLSHNQIQ-SLPAELGNMVSLRELHLNYNQLR-VLPFELGKLFQLQTLSLK 128
Cdd:PLN00113  452 PSLQMLSLARNKFFGGLPDSFGSKRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDLS 531


                  ....*...
gi 1907079522 129 GNPLTQDI 136
Cdd:PLN00113  532 HNQLSGQI 539
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
 189-271 1.43e-03

Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related domains; Human TDP2, also known as TTRAP (TRAF/TNFR-associated factors, and tumor necrosis factor receptor/TNFR-associated protein), is a 5'-tyrosyl DNA phosphodiesterase. It is required for the efficient repair of topoisomerase II-induced DNA double strand breaks. The topoisomerase is covalently linked by a phosphotyrosyl bond to the 5'-terminus of the break. TDP2 cleaves the DNA 5'-phosphodiester bond and restores 5'-phosphate termini, needed for subsequent DNA ligation, and hence repair of the break. TDP2 and 3'-tyrosyl DNA phosphodiesterase (TDP1) are complementary activities; together, they allow cells to remove trapped topoisomerase from both 3'- and 5'-DNA termini. TTRAP has been reported as being involved in apoptosis, embryonic development, and transcriptional regulation, and it may inhibit the activation of nuclear factor-kB. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197314 [Multi-domain]  Cd Length: 248  Bit Score: 40.40  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522 189 FSVMCYNVLCDKYATRQLygycpswalnwdyRKKAIIQEILSCNADIISLQEVeTEQYYSFFLvELKERGYNGFFSPKSR 268
Cdd:cd09080     1 LKVLTWNVDFLDDVNLAE-------------RMRAILKLLEELDPDVIFLQEV-TPPFLAYLL-SQPWVRKNYYFSEGPP 65


                  ...
gi 1907079522 269 ART 271
Cdd:cd09080    66 SPA 68
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 98-139 2.21e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 36.07  E-value: 2.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907079522  98 SLRELHLNYNQLRVLPFeLGKLFQLQTLSLKGNPLTQDILNL 139
Cdd:pfam12799   2 NLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNNKITDLSDL 42
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 53-169 4.11e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 40.22  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  53 LTALHLSDNSLSC-IPSDIAKLHNLVYLDLSHNQIQ-SLPAELGNMVSLRELHLNYNQLR-VLPFELGKLFQLQTLSLKG 129
Cdd:PLN00113  214 LKWIYLGYNNLSGeIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSD 293

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907079522 130 NPLTQDILNLCLEPDgTRRLLNYLLDNLSGTAKRISTEQP 169
Cdd:PLN00113  294 NSLSGEIPELVIQLQ-NLEILHLFSNNFTGKIPVALTSLP 332
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 52-136 6.87e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 39.45  E-value: 6.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  52 HLTALHLSDNSLSC-IPSDIAKL-HNLVYLDLSHNQIqSLPAELGNMVSLRELHLNYNQLR-VLPFELGKLFQLQTLSLK 128
Cdd:PLN00113   94 YIQTINLSNNQLSGpIPDDIFTTsSSLRYLNLSNNNF-TGSIPRGSIPNLETLDLSNNMLSgEIPNDIGSFSSLKVLDLG 172


                  ....*...
gi 1907079522 129 GNPLTQDI 136
Cdd:PLN00113  173 GNVLVGKI 180
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 51-133 7.47e-03

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 39.00  E-value: 7.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079522  51 THLTALHLSDNSLSC-----IPSDIAKLHNLVYLDLSHNQI-----QSLPAELGNMVSLRELHLNYNQL-----RVLPFE 115
Cdd:COG5238   236 KSLTTLDLSNNQIGDegviaLAEALKNNTTVETLYLSGNQIgaegaIALAKALQGNTTLTSLDLSVNRIgdegaIALAEG 315

                          90
                  ....*....|....*...
gi 1907079522 116 LGKLFQLQTLSLKGNPLT 133
Cdd:COG5238   316 LQGNKTLHTLNLAYNGIG 333
 
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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