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Conserved domains on  [gi|121674807|ref|NP_849185|]
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CCR4-NOT transcription complex subunit 6-like isoform 2 [Mus musculus]

Protein Classification

LRR and Deadenylase_CCR4b domain-containing protein( domain architecture ID 11469387)

LRR and Deadenylase_CCR4b domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Deadenylase_CCR4b cd10312
C-terminal deadenylase domain of CCR4b, also known as CCR4-NOT transcription complex subunit ...
 191-538 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: 800.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 191 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSRAK 270
Cdd:cd10312    1 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 271 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNIGVAVVLEVHKELFGTGMKPIHAAD 350
Cdd:cd10312   81 IMSEQERKHVDGCAIFFKTEKFSLVQKHTVEFNQVAMANSEGSEAMLNRVMTKDNIGVAVVLEVHKELFGAGMKPIHAAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 351 KQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVAD 430
Cdd:cd10312  161 KQLLIVANAHMHWDPEYSDVKLIQTMMFVSELKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVAD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 431 NHKDFKELRYNECLMNFSCSGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQ 510
Cdd:cd10312  241 NHKDFKELRYNECLMNFSCNGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQ 320

                        330       340
                 ....*....|....*....|....*...
gi 121674807 511 WLVENNITGCPHPHIPSDHFSLLTQLEL 538
Cdd:cd10312  321 WLVENNITGCPHPHIPSDHFSLLTQLEL 348
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
38-138 1.16e-24

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 106.56  E-value: 1.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  38 ELEISG-RVRSLSTSLWSLTHLTALHLNDNNLARIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNDNYLRV 116
Cdd:COG4886  117 SLDLSGnQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITD 196

                         90       100
                 ....*....|....*....|..
gi 121674807 117 LPYELGRLFQLQTLGLTGNPLS 138
Cdd:COG4886  197 LPEPLGNLTNLEELDLSGNQLT 218
 
Name Accession Description Interval E-value
Deadenylase_CCR4b cd10312
C-terminal deadenylase domain of CCR4b, also known as CCR4-NOT transcription complex subunit ...
 191-538 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: 800.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 191 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSRAK 270
Cdd:cd10312    1 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 271 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNIGVAVVLEVHKELFGTGMKPIHAAD 350
Cdd:cd10312   81 IMSEQERKHVDGCAIFFKTEKFSLVQKHTVEFNQVAMANSEGSEAMLNRVMTKDNIGVAVVLEVHKELFGAGMKPIHAAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 351 KQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVAD 430
Cdd:cd10312  161 KQLLIVANAHMHWDPEYSDVKLIQTMMFVSELKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVAD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 431 NHKDFKELRYNECLMNFSCSGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQ 510
Cdd:cd10312  241 NHKDFKELRYNECLMNFSCNGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQ 320

                        330       340
                 ....*....|....*....|....*...
gi 121674807 511 WLVENNITGCPHPHIPSDHFSLLTQLEL 538
Cdd:cd10312  321 WLVENNITGCPHPHIPSDHFSLLTQLEL 348
PLN03144 PLN03144
Carbon catabolite repressor protein 4 homolog; Provisional
 163-535 5.02e-74

Carbon catabolite repressor protein 4 homolog; Provisional


Pssm-ID: 178689 [Multi-domain]  Cd Length: 606  Bit Score: 246.95  E-value: 5.02e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 163 AVHPeqlPPRPWITLKERD---------QILPSASFTVMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNWDA 233
Cdd:PLN03144 223 APSP---TPRRLIQVNGLDgmghldldgRTSSAGTFTVLSYNILSDLYATSDMYSYCPPWALSWTYRRQNLLREIVGYRA 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 234 DIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSrAKIMSEQerKHV-DGCAIFFKTEKFTLVQKHTVEFNQVAMANSDG 312
Cdd:PLN03144 300 DILCLQEVQSDHFEEFFAPELDKHGYQALYKKKT-TEVYTGN--TYViDGCATFFRRDRFSLVKKYEVEFNKAAQSLTEA 376

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 313 ------SEAMLNRVMtKDNIGVAVVLEVhkeLFGTGmKPIHAADKQLLIVANAHMHWDPEYSDVKLIQtmmfVSEVKNIL 386
Cdd:PLN03144 377 lipsaqKKAALNRLL-KDNVALIVVLEA---KFGNQ-GADNGGKRQLLCVANTHIHANQELKDVKLWQ----VHTLLKGL 447

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 387 EK-ASSrpgsptADpnsIPLVLCADLNSLPDSGVVEYLSNGGVADNHKD-----FKELRyneclmnfscsgkngsSEGRI 460
Cdd:PLN03144 448 EKiAAS------AD---IPMLVCGDFNSVPGSAPHCLLATGKVDPLHPDlavdpLGILR----------------PASKL 502

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 461 THGFQLKSAYEN-NLMP---------------------YTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQWLVENniT 518
Cdd:PLN03144 503 THQLPLVSAYSSfARMPgsgsgleqqrrrmdpatneplFTNCTRDFIGTLDYIFYTADSLTVESLLELLDEESLRKD--T 580

                        410
                 ....*....|....*..
gi 121674807 519 GCPHPHIPSDHFSLLTQ 535
Cdd:PLN03144 581 ALPSPEWSSDHIALLAE 597
CCR4 COG5239
mRNA deadenylase, 3'-5' endonuclease subunit Ccr4 [RNA processing and modification];
185-535 2.86e-73

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


Pssm-ID: 227564 [Multi-domain]  Cd Length: 378  Bit Score: 238.13  E-value: 2.86e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 185 PSASFTVMCYNVLCDKYATRQLYGYCpSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFS 264
Cdd:COG5239   27 KDTDFTIMTYNVLAQTYATRKMYPYS-GWALKWSYRSRLLLQELLYYNADILCLQEVDAEDFEDFWKDQLGKLGYDGIFI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 265 PKSR-AKIMSEQERKHVDGCAIFFKTE----KFTLVQKHTVEFNQVAMANSD--GSEAMLNRVMTKDNI--GVAVVLEVH 335
Cdd:COG5239  106 PKERkVKWMIDYDTTKVDGCAIFLKRFidssKLGLILAVTHLFWHPYGYYERfrQTYILLNRIGEKDNIawVCLFVGLFN 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 336 KELFGTgmkpihaadkqlLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEK--ASSRPGSPTADPNSIPLVLCADLNS 413
Cdd:COG5239  186 KEPGDT------------PYVANTHLPWDPKYRDVKLIQCSLLYRELKKVLKEelNDDKEEGDIKSYPEVDILITGDFNS 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 414 LPDSGVVEYLsNGGVADNHKDFkelryNECLMNFSCSGKNGSsegritHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFY 493
Cdd:COG5239  254 LRASLVYKFL-VTSQIQLHESL-----NGRDFSLYSVGYKFV------HPENLKSDNSKGELGFTNWTPGFKGVIDYIFY 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 121674807 494 S-KTHMNVLGVLGPLDPQWLVenNITGCPHPHIPSDHFSLLTQ 535
Cdd:COG5239  322 HgGLLTRQTGLLGVVEGEYAS--KVIGLPNMPFPSDHIPLLAE 362
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
38-138 1.16e-24

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 106.56  E-value: 1.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  38 ELEISG-RVRSLSTSLWSLTHLTALHLNDNNLARIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNDNYLRV 116
Cdd:COG4886  117 SLDLSGnQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITD 196

                         90       100
                 ....*....|....*....|..
gi 121674807 117 LPYELGRLFQLQTLGLTGNPLS 138
Cdd:COG4886  197 LPEPLGNLTNLEELDLSGNQLT 218
LRR_8 pfam13855
Leucine rich repeat;
56-114 8.16e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 54.84  E-value: 8.16e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 121674807   56 THLTALHLNDNNLARIPPDIAK-LHNLVYLDLSSNKLRSL-PAELGNMVSLRELLLNDNYL 114
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PLN03150 PLN03150
hypothetical protein; Provisional
 53-136 8.96e-10

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 61.37  E-value: 8.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  53 WS-LTHLTALHLNDNNL-ARIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLRELLLNDNYL--RVlPYELG-RLFQ 126
Cdd:PLN03150 438 ISkLRHLQSINLSGNSIrGNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLsgRV-PAALGgRLLH 516

                         90
                 ....*....|
gi 121674807 127 LQTLGLTGNP 136
Cdd:PLN03150 517 RASFNFTDNA 526
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 54-140 3.93e-07

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: 50.94  E-value: 3.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  54 SLTHLTALHLNDNNLARI-------------------PPD----------IAKLHNLVYLDLSSNKLRSLpAELGNMVSL 104
Cdd:cd21340   66 NLVNLKKLYLGGNRISVVeglenltnleelhienqrlPPGekltfdprslAALSNSLRVLNISGNNIDSL-EPLAPLRNL 144

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 121674807 105 RELLLNDNYLR---VLPYELGRLFQLQTLGLTGNPLSQD 140
Cdd:cd21340  145 EQLDASNNQISdleELLDLLSSWPSLRELDLTGNPVCKK 183
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 192-308 5.07e-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: 50.30  E-value: 5.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  192 MCYNVLCDkyatrqlygycPSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKsraki 271
Cdd:pfam03372   1 LTWNVNGG-----------NADAAGDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFLSYGGPG----- 64

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 121674807  272 mseqERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMA 308
Cdd:pfam03372  65 ----GGGGGGGVAILSRYPLSSVILVDLGEFGDPALR 97
LRR smart00370
Leucine-rich repeats, outliers;
78-98 9.68e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 33.86  E-value: 9.68e-03
                           10        20
                   ....*....|....*....|.
gi 121674807    78 LHNLVYLDLSSNKLRSLPAEL 98
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGA 21
 
Name Accession Description Interval E-value
Deadenylase_CCR4b cd10312
C-terminal deadenylase domain of CCR4b, also known as CCR4-NOT transcription complex subunit ...
 191-538 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: 800.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 191 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSRAK 270
Cdd:cd10312    1 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 271 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNIGVAVVLEVHKELFGTGMKPIHAAD 350
Cdd:cd10312   81 IMSEQERKHVDGCAIFFKTEKFSLVQKHTVEFNQVAMANSEGSEAMLNRVMTKDNIGVAVVLEVHKELFGAGMKPIHAAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 351 KQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVAD 430
Cdd:cd10312  161 KQLLIVANAHMHWDPEYSDVKLIQTMMFVSELKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVAD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 431 NHKDFKELRYNECLMNFSCSGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQ 510
Cdd:cd10312  241 NHKDFKELRYNECLMNFSCNGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQ 320

                        330       340
                 ....*....|....*....|....*...
gi 121674807 511 WLVENNITGCPHPHIPSDHFSLLTQLEL 538
Cdd:cd10312  321 WLVENNITGCPHPHIPSDHFSLLTQLEL 348
Deadenylase_CCR4a cd10313
C-terminal deadenylase domain of CCR4a, also known as CCR4-NOT transcription complex subunit 6; ...
 191-535 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: 616.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 191 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSRAK 270
Cdd:cd10313    1 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIMQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 271 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNIGVAVVLEVHKELFG-TGMKPIHAA 349
Cdd:cd10313   81 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAVLLELRKELIEmSSGKPHLGM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 350 DKQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKAS-SRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGV 428
Cdd:cd10313  161 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASrSLKSSVLGETGTIPLVLCADLNSLPDSGVVEYLSTGGV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 429 ADNHKDFKELRYNECLMNFSCSGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLD 508
Cdd:cd10313  241 ETNHKDFKELRYNESLTNFSCNGKNGTTNGRITHGFKLKSAYENGLMPYTNYTFDFKGIIDYIFYSKPQLNTLGILGPLD 320

                        330       340
                 ....*....|....*....|....*..
gi 121674807 509 PQWLVENNITGCPHPHIPSDHFSLLTQ 535
Cdd:cd10313  321 HHWLVENNISGCPHPLIPSDHFSLFAQ 347
Deadenylase_CCR4 cd09097
C-terminal deadenylase domain of CCR4 and related domains; This subfamily contains the ...
 191-535 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 121674807 191 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSRAK 270
Cdd:cd09097    1 VMCYNVLCDKYATRQQYGYCPSWALNWDYRKQNILKEILSYNADILCLQEVETDQYEDFFLPELKQHGYDGVFKPKSRAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 271 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSD--GSEAMLNRVMTKDNIGVAVVLEVHKELFGTGmkpiha 348
Cdd:cd09097   81 TMSEAERKHVDGCAIFFKTSKFKLVEKHLIEFNQLAMANADaeGSEDMLNRVMTKDNIALIVVLEARETSYEGN------ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 349 aDKQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADpnsIPLVLCADLNSLPDSGVVEYLSNGGV 428
Cdd:cd09097  155 -KGQLLIVANTHIHWDPEFSDVKLVQTMMLLEELEKIAEKFSRYPYEDSAD---IPLVVCGDFNSLPDSGVYELLSNGSV 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 429 ADNHKDFKELRYNECLmnfscsgkngsSEGRITHGFQLKSAYENN-LMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPL 507
Cdd:cd09097  231 SPNHPDFKEDPYGEYL-----------TASGLTHSFKLKSAYANLgELPFTNYTPDFKGVIDYIFYSADTLSVLGLLGPP 299

                        330       340
                 ....*....|....*....|....*...
gi 121674807 508 DPQWlVENNITGCPHPHIPSDHFSLLTQ 535
Cdd:cd09097  300 DEDW-YLNKVVGLPNPHFPSDHIALLAE 326
PLN03144 PLN03144
Carbon catabolite repressor protein 4 homolog; Provisional
 163-535 5.02e-74

Carbon catabolite repressor protein 4 homolog; Provisional


Pssm-ID: 178689 [Multi-domain]  Cd Length: 606  Bit Score: 246.95  E-value: 5.02e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 163 AVHPeqlPPRPWITLKERD---------QILPSASFTVMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNWDA 233
Cdd:PLN03144 223 APSP---TPRRLIQVNGLDgmghldldgRTSSAGTFTVLSYNILSDLYATSDMYSYCPPWALSWTYRRQNLLREIVGYRA 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 234 DIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSrAKIMSEQerKHV-DGCAIFFKTEKFTLVQKHTVEFNQVAMANSDG 312
Cdd:PLN03144 300 DILCLQEVQSDHFEEFFAPELDKHGYQALYKKKT-TEVYTGN--TYViDGCATFFRRDRFSLVKKYEVEFNKAAQSLTEA 376

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 313 ------SEAMLNRVMtKDNIGVAVVLEVhkeLFGTGmKPIHAADKQLLIVANAHMHWDPEYSDVKLIQtmmfVSEVKNIL 386
Cdd:PLN03144 377 lipsaqKKAALNRLL-KDNVALIVVLEA---KFGNQ-GADNGGKRQLLCVANTHIHANQELKDVKLWQ----VHTLLKGL 447

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 387 EK-ASSrpgsptADpnsIPLVLCADLNSLPDSGVVEYLSNGGVADNHKD-----FKELRyneclmnfscsgkngsSEGRI 460
Cdd:PLN03144 448 EKiAAS------AD---IPMLVCGDFNSVPGSAPHCLLATGKVDPLHPDlavdpLGILR----------------PASKL 502

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 461 THGFQLKSAYEN-NLMP---------------------YTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQWLVENniT 518
Cdd:PLN03144 503 THQLPLVSAYSSfARMPgsgsgleqqrrrmdpatneplFTNCTRDFIGTLDYIFYTADSLTVESLLELLDEESLRKD--T 580

                        410
                 ....*....|....*..
gi 121674807 519 GCPHPHIPSDHFSLLTQ 535
Cdd:PLN03144 581 ALPSPEWSSDHIALLAE 597
CCR4 COG5239
mRNA deadenylase, 3'-5' endonuclease subunit Ccr4 [RNA processing and modification];
185-535 2.86e-73

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


Pssm-ID: 227564 [Multi-domain]  Cd Length: 378  Bit Score: 238.13  E-value: 2.86e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 185 PSASFTVMCYNVLCDKYATRQLYGYCpSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFS 264
Cdd:COG5239   27 KDTDFTIMTYNVLAQTYATRKMYPYS-GWALKWSYRSRLLLQELLYYNADILCLQEVDAEDFEDFWKDQLGKLGYDGIFI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 265 PKSR-AKIMSEQERKHVDGCAIFFKTE----KFTLVQKHTVEFNQVAMANSD--GSEAMLNRVMTKDNI--GVAVVLEVH 335
Cdd:COG5239  106 PKERkVKWMIDYDTTKVDGCAIFLKRFidssKLGLILAVTHLFWHPYGYYERfrQTYILLNRIGEKDNIawVCLFVGLFN 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 336 KELFGTgmkpihaadkqlLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEK--ASSRPGSPTADPNSIPLVLCADLNS 413
Cdd:COG5239  186 KEPGDT------------PYVANTHLPWDPKYRDVKLIQCSLLYRELKKVLKEelNDDKEEGDIKSYPEVDILITGDFNS 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 414 LPDSGVVEYLsNGGVADNHKDFkelryNECLMNFSCSGKNGSsegritHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFY 493
Cdd:COG5239  254 LRASLVYKFL-VTSQIQLHESL-----NGRDFSLYSVGYKFV------HPENLKSDNSKGELGFTNWTPGFKGVIDYIFY 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 121674807 494 S-KTHMNVLGVLGPLDPQWLVenNITGCPHPHIPSDHFSLLTQ 535
Cdd:COG5239  322 HgGLLTRQTGLLGVVEGEYAS--KVIGLPNMPFPSDHIPLLAE 362
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 191-535 7.11e-54

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: 182.68  E-value: 7.11e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 191 VMCYNVLCDKYATRqlygycpswalnweyrKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSRak 270
Cdd:cd08372    1 VASYNVNGLNAATR----------------ASGIARWVRELDPDIVCLQEVKDSQYSAVALNQLLPEGYHQYQSGPSR-- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 271 imseqeRKHVDGCAIFFKTEKFTLVQKHTVEFNQvamansdgseamlnrVMTKDNIGVAVVLEVHKELFgtgmkpihaad 350
Cdd:cd08372   63 ------KEGYEGVAILSKTPKFKIVEKHQYKFGE---------------GDSGERRAVVVKFDVHDKEL----------- 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 351 kqllIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILekassrpgsptaDPNSIPLVLCADLNSLPDSGVVEYLsnggvad 430
Cdd:cd08372  111 ----CVVNAHLQAGGTRADVRDAQLKEVLEFLKRLR------------QPNSAPVVICGDFNVRPSEVDSENP------- 167

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 431 nhkdfkelryneclmnfscsgkngSSEGRITHGFQLKSAYENNLMPYTNYTF--DFKGVIDYIFYSKTH-MNVLGVLGPL 507
Cdd:cd08372  168 ------------------------SSMLRLFVALNLVDSFETLPHAYTFDTYmhNVKSRLDYIFVSKSLlPSVKSSKILS 223

                        330       340
                 ....*....|....*....|....*...
gi 121674807 508 DPQWlvennitgcphPHIPSDHFSLLTQ 535
Cdd:cd08372  224 DAAR-----------ARIPSDHYPIEVT 240
Deadenylase_nocturnin cd09096
C-terminal deadenylase domain of nocturnin and related domains; This subfamily contains the ...
 210-533 3.33e-28

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: 114.06  E-value: 3.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 210 CPSWALNWEYRKKGIMEEIVNWDADIISLQEVetEQYFTLFLPALKDRGYDGFFSPKSRAKIMSEQERKHVDGCAIFFKT 289
Cdd:cd09096   22 CPCEALKWEERKYLILEEILTYDPDILCLQEV--DHYKDTLQPLLSRLGYQGTFFPKPDSPCLYIENNNGPDGCALFFRK 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 290 EKFTLV-------QKHTVEFNQVAMAnsdgseAMLNRvmtkdnigvavvlevhkelfgtgmkpihAADKQLLIVANAHMH 362
Cdd:cd09096  100 DRFELVntekirlSAMTLKTNQVAIA------CTLRC----------------------------KETGREICLAVTHLK 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 363 WDPEYSDVKLIQTMMFVSEVKNILEKAssrpgsptadpnSIPLVLCADLNSLPDSGVVEYLSNGGvadnhkdfkelryne 442
Cdd:cd09096  146 ARTGWERLRSEQGKDLLQNLQSFIEGA------------KIPLIICGDFNAEPTEPVYKTFSNSS--------------- 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 443 clMNFSCSGKNGSSEGrithgfqlksAYENnlmPYTNYTFDFKG----VIDYIFYSKTHMNVLGVLGpLDPQWLVENNit 518
Cdd:cd09096  199 --LNLNSAYKLLSADG----------QSEP---PYTTWKIRTSGecrhTLDYIFYSKDALSVEQLLD-LPTEEQIGPN-- 260

                        330
                 ....*....|....*
gi 121674807 519 GCPHPHIPSDHFSLL 533
Cdd:cd09096  261 RLPSFNYPSDHLSLV 275
Deadenylase cd09082
C-terminal deadenylase domain of CCR4, nocturnin, and related domains; This family contains ...
 191-533 3.07e-27

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: 112.83  E-value: 3.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 191 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSRAK 270
Cdd:cd09082    1 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 271 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDN-IGVAVVLEVHKELFGTGMKPIHAA 349
Cdd:cd09082   81 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNiGVAVVLEVHKELFGAGMKPIHAAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 350 DKQLLIvANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVA 429
Cdd:cd09082  161 KQLLIV-ANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 430 DN-------HKDFKELRYNECLMNFSCSGKNGSSEGRIThgfqlksAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLG 502
Cdd:cd09082  240 DNhkdfkelRYNECLMNFSCNGKNGSSEGRITHGFQLKS-------AYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLG 312

                        330       340       350
                 ....*....|....*....|....*....|.
gi 121674807 503 VLGPLDPQWLVENNITGCPHPHIPSDHFSLL 533
Cdd:cd09082  313 VLGPLDPQWLVENNITGCPHPHIPSDHFSLL 343
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
38-138 1.16e-24

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 106.56  E-value: 1.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  38 ELEISG-RVRSLSTSLWSLTHLTALHLNDNNLARIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNDNYLRV 116
Cdd:COG4886  117 SLDLSGnQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITD 196

                         90       100
                 ....*....|....*....|..
gi 121674807 117 LPYELGRLFQLQTLGLTGNPLS 138
Cdd:COG4886  197 LPEPLGNLTNLEELDLSGNQLT 218
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
38-138 1.49e-23

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 103.09  E-value: 1.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  38 ELEISG-RVRSLSTSLWSLTHLTALHLNDNNLARIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNDNYLRV 116
Cdd:COG4886  140 ELDLSNnQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTD 219

                         90       100
                 ....*....|....*....|..
gi 121674807 117 LPYELGRLFQLQTLGLTGNPLS 138
Cdd:COG4886  220 LPEPLANLTNLETLDLSNNQLT 241
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
47-138 1.74e-21

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 96.93  E-value: 1.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  47 SLSTSLWSLTHLTALHLNDNNLARIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNDNYLRVLPYELGRLFQ 126
Cdd:COG4886  104 SGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTN 183

                         90
                 ....*....|..
gi 121674807 127 LQTLGLTGNPLS 138
Cdd:COG4886  184 LKELDLSNNQIT 195
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
 190-530 6.45e-16

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: 77.64  E-value: 6.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 190 TVMCYNVLCDkyatrqlygyCPSWALN-WEYRKKGIMEEIVNWDADIISLQEVETEQyftlfLPALKDR--GYDgffspk 266
Cdd:cd09083    1 RVMTFNIRYD----------NPSDGENsWENRKDLVAELIKFYDPDIIGTQEALPHQ-----LADLEELlpEYD------ 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 267 sraKIMSEQERKHVDG--CAIFFKTEKFTLVQKHTveF---NQVAMANSDGSEAMLNRVMTkdnigvAVVLEvhkelfgt 341
Cdd:cd09083   60 ---WIGVGRDDGKEKGefSAIFYRKDRFELLDSGT--FwlsETPDVVGSKGWDAALPRICT------WARFK-------- 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 342 gmkpiHAADKQLLIVANAHMhwdpeysDvkliqtmmFVSEV------KNILEKASSRPGSptadpnsIPLVLCADLNSLP 415
Cdd:cd09083  121 -----DKKTGKEFYVFNTHL-------D--------HVGEEareesaKLILERIKEIAGD-------LPVILTGDFNAEP 173

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 416 DSGVVEYLSNGGVADNHKDFKElryneclmnfscsgkngssegrithgfqlksAYENNLMPYTNYTFDFKGV-IDYIFYS 494
Cdd:cd09083  174 DSEPYKTLTSGGLKDARDTAAT-------------------------------TDGGPEGTFHGFKGPPGGSrIDYIFVS 222

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 121674807 495 KtHMNVL--GVlgpldpqwlvennITGCPHPHIPSDHF 530
Cdd:cd09083  223 P-GVKVLsyEI-------------LTDRYDGRYPSDHF 246
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
38-179 9.61e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 69.96  E-value: 9.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  38 ELEISG-RVRSLSTSLWSLTHLTALHLNDNNLARIPpDIAKLHNLVYLDLSSNKLRSLPaELGNMVSLRELLLNDNYLRV 116
Cdd:COG4886  209 ELDLSGnQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLTD 286

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 121674807 117 LPYE-LGRLFQLQTLGLTGNPLSQDIMSLYQDPDGTRKLLNFMLDNLAVHPEQLPPRPWITLKE 179
Cdd:COG4886  287 LKLKeLELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALL 350
LRR_8 pfam13855
Leucine rich repeat;
56-114 8.16e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 54.84  E-value: 8.16e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 121674807   56 THLTALHLNDNNLARIPPDIAK-LHNLVYLDLSSNKLRSL-PAELGNMVSLRELLLNDNYL 114
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PLN03150 PLN03150
hypothetical protein; Provisional
 53-136 8.96e-10

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 61.37  E-value: 8.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  53 WS-LTHLTALHLNDNNL-ARIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLRELLLNDNYL--RVlPYELG-RLFQ 126
Cdd:PLN03150 438 ISkLRHLQSINLSGNSIrGNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLsgRV-PAALGgRLLH 516

                         90
                 ....*....|
gi 121674807 127 LQTLGLTGNP 136
Cdd:PLN03150 517 RASFNFTDNA 526
PLN03150 PLN03150
hypothetical protein; Provisional
 60-138 2.29e-08

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 56.75  E-value: 2.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  60 ALHLNDNNL-ARIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLRELLLNDNYLR-VLPYELGRLFQLQTLGLTGNP 136
Cdd:PLN03150 422 GLGLDNQGLrGFIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNS 501


                 ..
gi 121674807 137 LS 138
Cdd:PLN03150 502 LS 503
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
21-139 1.52e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 53.78  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  21 TIMSAEEVANGKKSHWAELEISGRVRSLSTSLWSLTHLTALHLNDNNLARIPPDIAKLHNLVYLDLSSNKlrslpaELGN 100
Cdd:COG4886   38 LLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE------ELSN 111

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 121674807 101 MVSLRELLLNDNYLRVLPYELGRLFQLQTLGLTGNPLSQ 139
Cdd:COG4886  112 LTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTD 150
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 54-143 3.12e-07

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 53.31  E-value: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  54 SLTHLTALHLNDNNL-ARIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLRELLLNDNYLR-VLPYELGRLFQLQTL 130
Cdd:PLN00113 162 SFSSLKVLDLGGNVLvGKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHL 241

                         90
                 ....*....|...
gi 121674807 131 GLTGNPLSQDIMS 143
Cdd:PLN00113 242 DLVYNNLTGPIPS 254
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 54-140 3.93e-07

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: 50.94  E-value: 3.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  54 SLTHLTALHLNDNNLARI-------------------PPD----------IAKLHNLVYLDLSSNKLRSLpAELGNMVSL 104
Cdd:cd21340   66 NLVNLKKLYLGGNRISVVeglenltnleelhienqrlPPGekltfdprslAALSNSLRVLNISGNNIDSL-EPLAPLRNL 144

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 121674807 105 RELLLNDNYLR---VLPYELGRLFQLQTLGLTGNPLSQD 140
Cdd:cd21340  145 EQLDASNNQISdleELLDLLSSWPSLRELDLTGNPVCKK 183
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 192-308 5.07e-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: 50.30  E-value: 5.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  192 MCYNVLCDkyatrqlygycPSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKsraki 271
Cdd:pfam03372   1 LTWNVNGG-----------NADAAGDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFLSYGGPG----- 64

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 121674807  272 mseqERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMA 308
Cdd:pfam03372  65 ----GGGGGGGVAILSRYPLSSVILVDLGEFGDPALR 97
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 52-135 2.51e-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: 48.63  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  52 LWSLTHLtalHLNDNNLARIpPDIAKLHNLVYLDLSSNKLRSLPAeLGNMVSLRELLLNDNYLRVLPYeLGRLFQLQTLG 131
Cdd:cd21340    1 LKRITHL---YLNDKNITKI-DNLSLCKNLKVLYLYDNKITKIEN-LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLY 74


                 ....
gi 121674807 132 LTGN 135
Cdd:cd21340   75 LGGN 78
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
38-184 2.97e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.93  E-value: 2.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  38 ELEISG-RVRSLStSLWSLTHLTALHLNDNNLARIPPdIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNDNYLRV 116
Cdd:COG4886  232 TLDLSNnQLTDLP-ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLN 309

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 121674807 117 LPYELGRLFQLQTLGLTGNPLSQDIMSLYQDPDGTRKLLNFMLDNLAVHPEQLPPRPWITLKERDQIL 184
Cdd:COG4886  310 LLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEA 377
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 54-144 7.20e-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: 47.09  E-value: 7.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  54 SLTHLTALHLNDNNLARIpPDIAKLHNLVYLDLSSNKLRSLPaELGNMVSLRELLLNDNYLRVLpyE-LGRLFQLQTLGL 132
Cdd:cd21340   22 LCKNLKVLYLYDNKITKI-ENLEFLTNLTHLYLQNNQIEKIE-NLENLVNLKKLYLGGNRISVV--EgLENLTNLEELHI 97

                         90
                 ....*....|....*...
gi 121674807 133 ------TGNPLSQDIMSL 144
Cdd:cd21340   98 enqrlpPGEKLTFDPRSL 115
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 54-141 1.15e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 48.31  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  54 SLTHLTALHLNDNNLA-RIPPDIAKLHNLVYLDLSSNKLRS-LPAELGNMVSLRELLLNDNYLR-VLPYELGRLFQLQTL 130
Cdd:PLN00113 138 SIPNLETLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVGkIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWI 217

                         90
                 ....*....|.
gi 121674807 131 GLTGNPLSQDI 141
Cdd:PLN00113 218 YLGYNNLSGEI 228
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 47-141 2.66e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 47.15  E-value: 2.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  47 SLSTSLWSLTHLTALHLNDNNLA-RIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLREL-LLNDNYLRVLPYELGR 123
Cdd:PLN00113 251 PIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILhLFSNNFTGKIPVALTS 330

                         90
                 ....*....|....*...
gi 121674807 124 LFQLQTLGLTGNPLSQDI 141
Cdd:PLN00113 331 LPRLQVLQLWSNKFSGEI 348
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
 191-495 6.41e-05

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: 44.59  E-value: 6.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 191 VMCYNVlcdkyatRQLYGYcpswalNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSRAK 270
Cdd:cd09084    1 VMSYNV-------RSFNRY------KWKDDPDKILDFIKKQDPDILCLQEYYGSEGDKDDDLRLLLKGYPYYYVVYKSDS 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 271 IMSEQerkhvdgcAIFfktEKFTLVQKHTVEFNqvamaNSDGSEAMLNRVMTKDNIgvaVVLEVHKELFGtgmkpIHAAD 350
Cdd:cd09084   68 GGTGL--------AIF---SKYPILNSGSIDFP-----NTNNNAIFADIRVGGDTI---RVYNVHLESFR-----ITPSD 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 351 KQLLivanAHMHWDPEYSDvKLIQTM--MFV---SEVKNILEKASSRPGsptadpnsiPLVLCADLNSLPDSGVVEYLSN 425
Cdd:cd09084  124 KELY----KEEKKAKELSR-NLLRKLaeAFKrraAQADLLAADIAASPY---------PVIVCGDFNDTPASYVYRTLKK 189

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 121674807 426 GgvadnhkdfkelryneclmnfscsgkngssegrithgfqLKSAYE--NNLMPYTnYTFDFKGV-IDYIFYSK 495
Cdd:cd09084  190 G---------------------------------------LTDAFVeaGSGFGYT-FNGLFFPLrIDYILTSK 222
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
57-170 8.59e-05

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 45.46  E-value: 8.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  57 HLTALHLNDNNLARIPPDiakLH-NLVYLDLSSNKLRSLPAELGNmvSLRELLLNDNYLRVLPYELGRlfQLQTLGLTGN 135
Cdd:PRK15370 200 QITTLILDNNELKSLPEN---LQgNIKTLYANSNQLTSIPATLPD--TIQEMELSINRITELPERLPS--ALQSLDLFHN 272

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 121674807 136 PLSQDIMSLyqdPDGTRkLLNFMLDNLAVHPEQLP 170
Cdd:PRK15370 273 KISCLPENL---PEELR-YLSVYDNSIRTLPAHLP 303
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 41-147 9.37e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 45.61  E-value: 9.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  41 ISGRvrsLSTSLWSLTHLTALHLNDNNLARIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLRELLLNDNYLR-VLP 118
Cdd:PLN00113 440 LQGR---INSRKWDMPSLQMLSLARNKFFGGLPDSFGSKRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSENKLSgEIP 516

                         90       100
                 ....*....|....*....|....*....
gi 121674807 119 YELGRLFQLQTLGLTGNPLSQDIMSLYQD 147
Cdd:PLN00113 517 DELSSCKKLVSLDLSHNQLSGQIPASFSE 545
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 46-112 2.03e-04

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: 42.85  E-value: 2.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  46 RSLSTSLWSLTHLTALHlndNNLARIPPdIAKLHNLVYLDLSSNKLRSLPA---ELGNMVSLRELLLNDN 112
Cdd:cd21340  113 RSLAALSNSLRVLNISG---NNIDSLEP-LAPLRNLEQLDASNNQISDLEElldLLSSWPSLRELDLTGN 178
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 56-91 3.71e-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: 3.71e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 121674807   56 THLTALHLNDNNLARIPPdIAKLHNLVYLDLSSNKL 91
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNNK 35
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 51-144 3.92e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 43.30  E-value: 3.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  51 SLWSLTHLTALHLNDNNLA-RIPPDIAKLHNLVYLDLSSNKLRS-LPAELGNMVSLRELLLNDNYLR-VLPYELG----- 122
Cdd:PLN00113 327 ALTSLPRLQVLQLWSNKFSgEIPKNLGKHNNLTVLDLSTNNLTGeIPEGLCSSGNLFKLILFSNSLEgEIPKSLGacrsl 406

                         90       100
                 ....*....|....*....|..
gi 121674807 123 RLFQLQTLGLTGNpLSQDIMSL 144
Cdd:PLN00113 407 RRVRLQDNSFSGE-LPSEFTKL 427
LRR_8 pfam13855
Leucine rich repeat;
54-91 4.15e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 38.66  E-value: 4.15e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 121674807   54 SLTHLTALHLNDNNLARIPPD-IAKLHNLVYLDLSSNKL 91
Cdd:pfam13855  23 GLSNLKVLDLSNNLLTTLSPGaFSGLPSLRYLDLSGNRL 61
nSMase cd09078
Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological ...
 191-530 2.13e-03

Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological membranes to ceramide and phosphorylcholine; Sphingomyelinases (SMase) are phosphodiesterases that catalyze the hydrolysis of sphingomyelin to ceramide and phosphorylcholine. Eukaryotic SMases have been classified according to their pH optima and are known as acid SMase, alkaline SMase, and neutral SMase (nSMase). Eukaryotic proteins in this family are nSMases, and are activated by a variety of stress-inducing agents such as cytokines or UV radiation. Ceramides and other metabolic derivatives, including sphingosine, are lipid "second messenger" molecules that participate in the regulation of stress-induced cellular responses, including cell death, adhesion, differentiation, and proliferation. Bacterial neutral SMases, which also belong to this domain family, are secreted proteins that act as membrane-damaging virulence factors. They promote colonization of the host tissue. 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: 197312 [Multi-domain]  Cd Length: 280  Bit Score: 40.40  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 191 VMCYNVLCDKYATRQLygycPSWALNWEYRKkgIMEEIVNWDadIISLQEVeteqyFT-----LFLPALKDRGydGFFSP 265
Cdd:cd09078    3 VLTYNVFLLPPLLYNN----GDDGQDERLDL--IPKALLQYD--VVVLQEV-----FDararkRLLNGLKKEY--PYQTD 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 266 K-SRAKIMSEqeRKHVD-GCAIFfktEKFTLVQKHTVEFNqvamaNSDGSEAMLNR--VMTKDNIGvavvlevhkelfgt 341
Cdd:cd09078   68 VvGRSPSGWS--SKLVDgGVVIL---SRYPIVEKDQYIFP-----NGCGADCLAAKgvLYAKINKG-------------- 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 342 GMKPIHaadkqlliVANAHMH-WDPEYSDVK-----LIQTMMFVSEvKNIlekassrpgsptadPNSIPLVLCADLNslp 415
Cdd:cd09078  124 GTKVYH--------VFGTHLQaSDGSCLDRAvrqkqLDELRAFIEE-KNI--------------PDNEPVIIAGDFN--- 177

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807 416 dsgvveylsnggvADNHKDFKElrYNECLMNFSCSgkNGSSegRITHGFQLKS-AYENNLMPYTNYTFDFKGVIDYIFYS 494
Cdd:cd09078  178 -------------VDKRSSRDE--YDDMLEQLHDY--NAPE--PITAGETPLTwDPGTNLLAKYNYPGGGGERLDYILYS 238

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 121674807 495 KTHMNVLG----VLGPLDPQWLVENNITgcpHPHIpSDHF 530
Cdd:cd09078  239 NDHLQPSSwsneVEVPKSPTWSVTNGYT---FADL-SDHY 274
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 55-130 3.45e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 40.22  E-value: 3.45e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 121674807  55 LTHLTALHLNDNNLA-RIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLRELLLNDNYLRVLPYELgrLFQLQTL 130
Cdd:PLN00113 235 LTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSGEIPEL--VIQLQNL 310
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 37-114 5.56e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 39.83  E-value: 5.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121674807  37 AELEISGRVRSlstSLWSLTHLTALHLNDNNLA-RIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLRELLLNDNYL 114
Cdd:PLN00113 507 SENKLSGEIPD---ELSSCKKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQLSgEIPKNLGNVESLVQVNISHNHL 583
LRR smart00370
Leucine-rich repeats, outliers;
78-98 9.68e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 33.86  E-value: 9.68e-03
                           10        20
                   ....*....|....*....|.
gi 121674807    78 LHNLVYLDLSSNKLRSLPAEL 98
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGA 21
LRR_TYP smart00369
Leucine-rich repeats, typical (most populated) subfamily;
78-98 9.68e-03

Leucine-rich repeats, typical (most populated) subfamily;


Pssm-ID: 197687 [Multi-domain]  Cd Length: 24  Bit Score: 33.86  E-value: 9.68e-03
                           10        20
                   ....*....|....*....|.
gi 121674807    78 LHNLVYLDLSSNKLRSLPAEL 98
Cdd:smart00369   1 LPNLRELDLSNNQLSSLPPGA 21
 
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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