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Conserved domains on  [gi|568935494|ref|XP_006534934|]
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CCR4-NOT transcription complex subunit 6-like isoform X1 [Mus musculus]

Protein Classification

leucine-rich repeat domain-containing protein; leucine-rich repeat and calponin homology domain-containing protein( domain architecture ID 11469387)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions| leucine-rich repeat and calponin homology (LRCH) domain-containing protein similar to human LRCH4 which is a Toll-like receptor (TLR) accessory protein that regulates signaling by multiple TLRs

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 ...
 186-533 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 568935494 186 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSRAK 265
Cdd:cd10312    1 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 266 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNIGVAVVLEVHKELFGTGMKPIHAAD 345
Cdd:cd10312   81 IMSEQERKHVDGCAIFFKTEKFSLVQKHTVEFNQVAMANSEGSEAMLNRVMTKDNIGVAVVLEVHKELFGAGMKPIHAAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 346 KQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVAD 425
Cdd:cd10312  161 KQLLIVANAHMHWDPEYSDVKLIQTMMFVSELKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVAD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 426 NHKDFKELRYNECLMNFSCSGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQ 505
Cdd:cd10312  241 NHKDFKELRYNECLMNFSCNGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQ 320

                        330       340
                 ....*....|....*....|....*...
gi 568935494 506 WLVENNITGCPHPHIPSDHFSLLTQLEL 533
Cdd:cd10312  321 WLVENNITGCPHPHIPSDHFSLLTQLEL 348
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-133 1.28e-24

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 106.17  E-value: 1.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  33 ELEISG-RVRSLSTSLWSLTHLTALHLNDNNLARIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNDNYLRV 111
Cdd:COG4886  117 SLDLSGnQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITD 196

                         90       100
                 ....*....|....*....|..
gi 568935494 112 LPYELGRLFQLQTLGLTGNPLS 133
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 ...
 186-533 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 568935494 186 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSRAK 265
Cdd:cd10312    1 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 266 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNIGVAVVLEVHKELFGTGMKPIHAAD 345
Cdd:cd10312   81 IMSEQERKHVDGCAIFFKTEKFSLVQKHTVEFNQVAMANSEGSEAMLNRVMTKDNIGVAVVLEVHKELFGAGMKPIHAAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 346 KQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVAD 425
Cdd:cd10312  161 KQLLIVANAHMHWDPEYSDVKLIQTMMFVSELKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVAD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 426 NHKDFKELRYNECLMNFSCSGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQ 505
Cdd:cd10312  241 NHKDFKELRYNECLMNFSCNGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQ 320

                        330       340
                 ....*....|....*....|....*...
gi 568935494 506 WLVENNITGCPHPHIPSDHFSLLTQLEL 533
Cdd:cd10312  321 WLVENNITGCPHPHIPSDHFSLLTQLEL 348
PLN03144 PLN03144
Carbon catabolite repressor protein 4 homolog; Provisional
 158-530 4.42e-74

Carbon catabolite repressor protein 4 homolog; Provisional


Pssm-ID: 178689 [Multi-domain]  Cd Length: 606  Bit Score: 246.95  E-value: 4.42e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 158 AVHPeqlPPRPWITLKERD---------QILPSASFTVMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNWDA 228
Cdd:PLN03144 223 APSP---TPRRLIQVNGLDgmghldldgRTSSAGTFTVLSYNILSDLYATSDMYSYCPPWALSWTYRRQNLLREIVGYRA 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 229 DIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSrAKIMSEQerKHV-DGCAIFFKTEKFTLVQKHTVEFNQVAMANSDG 307
Cdd:PLN03144 300 DILCLQEVQSDHFEEFFAPELDKHGYQALYKKKT-TEVYTGN--TYViDGCATFFRRDRFSLVKKYEVEFNKAAQSLTEA 376

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 308 ------SEAMLNRVMtKDNIGVAVVLEVhkeLFGTGmKPIHAADKQLLIVANAHMHWDPEYSDVKLIQtmmfVSEVKNIL 381
Cdd:PLN03144 377 lipsaqKKAALNRLL-KDNVALIVVLEA---KFGNQ-GADNGGKRQLLCVANTHIHANQELKDVKLWQ----VHTLLKGL 447

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 382 EK-ASSrpgsptADpnsIPLVLCADLNSLPDSGVVEYLSNGGVADNHKD-----FKELRyneclmnfscsgkngsSEGRI 455
Cdd:PLN03144 448 EKiAAS------AD---IPMLVCGDFNSVPGSAPHCLLATGKVDPLHPDlavdpLGILR----------------PASKL 502

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 456 THGFQLKSAYEN-NLMP---------------------YTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQWLVENniT 513
Cdd:PLN03144 503 THQLPLVSAYSSfARMPgsgsgleqqrrrmdpatneplFTNCTRDFIGTLDYIFYTADSLTVESLLELLDEESLRKD--T 580

                        410
                 ....*....|....*..
gi 568935494 514 GCPHPHIPSDHFSLLTQ 530
Cdd:PLN03144 581 ALPSPEWSSDHIALLAE 597
CCR4 COG5239
mRNA deadenylase, 3'-5' endonuclease subunit Ccr4 [RNA processing and modification];
180-530 3.33e-73

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


Pssm-ID: 227564 [Multi-domain]  Cd Length: 378  Bit Score: 237.75  E-value: 3.33e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 180 PSASFTVMCYNVLCDKYATRQLYGYCpSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFS 259
Cdd:COG5239   27 KDTDFTIMTYNVLAQTYATRKMYPYS-GWALKWSYRSRLLLQELLYYNADILCLQEVDAEDFEDFWKDQLGKLGYDGIFI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 260 PKSR-AKIMSEQERKHVDGCAIFFKTE----KFTLVQKHTVEFNQVAMANSD--GSEAMLNRVMTKDNI--GVAVVLEVH 330
Cdd:COG5239  106 PKERkVKWMIDYDTTKVDGCAIFLKRFidssKLGLILAVTHLFWHPYGYYERfrQTYILLNRIGEKDNIawVCLFVGLFN 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 331 KELFGTgmkpihaadkqlLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEK--ASSRPGSPTADPNSIPLVLCADLNS 408
Cdd:COG5239  186 KEPGDT------------PYVANTHLPWDPKYRDVKLIQCSLLYRELKKVLKEelNDDKEEGDIKSYPEVDILITGDFNS 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 409 LPDSGVVEYLsNGGVADNHKDFkelryNECLMNFSCSGKNGSsegritHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFY 488
Cdd:COG5239  254 LRASLVYKFL-VTSQIQLHESL-----NGRDFSLYSVGYKFV------HPENLKSDNSKGELGFTNWTPGFKGVIDYIFY 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 568935494 489 S-KTHMNVLGVLGPLDPQWLVenNITGCPHPHIPSDHFSLLTQ 530
Cdd:COG5239  322 HgGLLTRQTGLLGVVEGEYAS--KVIGLPNMPFPSDHIPLLAE 362
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-133 1.28e-24

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 106.17  E-value: 1.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  33 ELEISG-RVRSLSTSLWSLTHLTALHLNDNNLARIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNDNYLRV 111
Cdd:COG4886  117 SLDLSGnQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITD 196

                         90       100
                 ....*....|....*....|..
gi 568935494 112 LPYELGRLFQLQTLGLTGNPLS 133
Cdd:COG4886  197 LPEPLGNLTNLEELDLSGNQLT 218
LRR_8 pfam13855
Leucine rich repeat;
51-109 8.00e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 54.84  E-value: 8.00e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568935494   51 THLTALHLNDNNLARIPPDIAK-LHNLVYLDLSSNKLRSL-PAELGNMVSLRELLLNDNYL 109
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PLN03150 PLN03150
hypothetical protein; Provisional
 48-131 8.82e-10

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 61.37  E-value: 8.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  48 WS-LTHLTALHLNDNNL-ARIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLRELLLNDNYL--RVlPYELG-RLFQ 121
Cdd:PLN03150 438 ISkLRHLQSINLSGNSIrGNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLsgRV-PAALGgRLLH 516

                         90
                 ....*....|
gi 568935494 122 LQTLGLTGNP 131
Cdd:PLN03150 517 RASFNFTDNA 526
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 49-135 3.81e-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: 3.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  49 SLTHLTALHLNDNNLARI-------------------PPD----------IAKLHNLVYLDLSSNKLRSLpAELGNMVSL 99
Cdd:cd21340   66 NLVNLKKLYLGGNRISVVeglenltnleelhienqrlPPGekltfdprslAALSNSLRVLNISGNNIDSL-EPLAPLRNL 144

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568935494 100 RELLLNDNYLR---VLPYELGRLFQLQTLGLTGNPLSQD 135
Cdd:cd21340  145 EQLDASNNQISdleELLDLLSSWPSLRELDLTGNPVCKK 183
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 187-303 5.11e-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: 5.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  187 MCYNVLCDkyatrqlygycPSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKsraki 266
Cdd:pfam03372   1 LTWNVNGG-----------NADAAGDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFLSYGGPG----- 64

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568935494  267 mseqERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMA 303
Cdd:pfam03372  65 ----GGGGGGGVAILSRYPLSSVILVDLGEFGDPALR 97
LRR smart00370
Leucine-rich repeats, outliers;
73-93 9.60e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 33.86  E-value: 9.60e-03
                           10        20
                   ....*....|....*....|.
gi 568935494    73 LHNLVYLDLSSNKLRSLPAEL 93
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 ...
 186-533 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 568935494 186 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSRAK 265
Cdd:cd10312    1 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 266 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNIGVAVVLEVHKELFGTGMKPIHAAD 345
Cdd:cd10312   81 IMSEQERKHVDGCAIFFKTEKFSLVQKHTVEFNQVAMANSEGSEAMLNRVMTKDNIGVAVVLEVHKELFGAGMKPIHAAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 346 KQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVAD 425
Cdd:cd10312  161 KQLLIVANAHMHWDPEYSDVKLIQTMMFVSELKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVAD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 426 NHKDFKELRYNECLMNFSCSGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQ 505
Cdd:cd10312  241 NHKDFKELRYNECLMNFSCNGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQ 320

                        330       340
                 ....*....|....*....|....*...
gi 568935494 506 WLVENNITGCPHPHIPSDHFSLLTQLEL 533
Cdd:cd10312  321 WLVENNITGCPHPHIPSDHFSLLTQLEL 348
Deadenylase_CCR4a cd10313
C-terminal deadenylase domain of CCR4a, also known as CCR4-NOT transcription complex subunit 6; ...
 186-530 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: 615.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 186 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSRAK 265
Cdd:cd10313    1 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIMQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 266 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNIGVAVVLEVHKELFG-TGMKPIHAA 344
Cdd:cd10313   81 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAVLLELRKELIEmSSGKPHLGM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 345 DKQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKAS-SRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGV 423
Cdd:cd10313  161 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASrSLKSSVLGETGTIPLVLCADLNSLPDSGVVEYLSTGGV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 424 ADNHKDFKELRYNECLMNFSCSGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLD 503
Cdd:cd10313  241 ETNHKDFKELRYNESLTNFSCNGKNGTTNGRITHGFKLKSAYENGLMPYTNYTFDFKGIIDYIFYSKPQLNTLGILGPLD 320

                        330       340
                 ....*....|....*....|....*..
gi 568935494 504 PQWLVENNITGCPHPHIPSDHFSLLTQ 530
Cdd:cd10313  321 HHWLVENNISGCPHPLIPSDHFSLFAQ 347
Deadenylase_CCR4 cd09097
C-terminal deadenylase domain of CCR4 and related domains; This subfamily contains the ...
 186-530 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: 573.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 186 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSRAK 265
Cdd:cd09097    1 VMCYNVLCDKYATRQQYGYCPSWALNWDYRKQNILKEILSYNADILCLQEVETDQYEDFFLPELKQHGYDGVFKPKSRAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 266 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSD--GSEAMLNRVMTKDNIGVAVVLEVHKELFGTGmkpiha 343
Cdd:cd09097   81 TMSEAERKHVDGCAIFFKTSKFKLVEKHLIEFNQLAMANADaeGSEDMLNRVMTKDNIALIVVLEARETSYEGN------ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 344 aDKQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADpnsIPLVLCADLNSLPDSGVVEYLSNGGV 423
Cdd:cd09097  155 -KGQLLIVANTHIHWDPEFSDVKLVQTMMLLEELEKIAEKFSRYPYEDSAD---IPLVVCGDFNSLPDSGVYELLSNGSV 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 424 ADNHKDFKELRYNECLmnfscsgkngsSEGRITHGFQLKSAYENN-LMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPL 502
Cdd:cd09097  231 SPNHPDFKEDPYGEYL-----------TASGLTHSFKLKSAYANLgELPFTNYTPDFKGVIDYIFYSADTLSVLGLLGPP 299

                        330       340
                 ....*....|....*....|....*...
gi 568935494 503 DPQWlVENNITGCPHPHIPSDHFSLLTQ 530
Cdd:cd09097  300 DEDW-YLNKVVGLPNPHFPSDHIALLAE 326
PLN03144 PLN03144
Carbon catabolite repressor protein 4 homolog; Provisional
 158-530 4.42e-74

Carbon catabolite repressor protein 4 homolog; Provisional


Pssm-ID: 178689 [Multi-domain]  Cd Length: 606  Bit Score: 246.95  E-value: 4.42e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 158 AVHPeqlPPRPWITLKERD---------QILPSASFTVMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNWDA 228
Cdd:PLN03144 223 APSP---TPRRLIQVNGLDgmghldldgRTSSAGTFTVLSYNILSDLYATSDMYSYCPPWALSWTYRRQNLLREIVGYRA 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 229 DIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSrAKIMSEQerKHV-DGCAIFFKTEKFTLVQKHTVEFNQVAMANSDG 307
Cdd:PLN03144 300 DILCLQEVQSDHFEEFFAPELDKHGYQALYKKKT-TEVYTGN--TYViDGCATFFRRDRFSLVKKYEVEFNKAAQSLTEA 376

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 308 ------SEAMLNRVMtKDNIGVAVVLEVhkeLFGTGmKPIHAADKQLLIVANAHMHWDPEYSDVKLIQtmmfVSEVKNIL 381
Cdd:PLN03144 377 lipsaqKKAALNRLL-KDNVALIVVLEA---KFGNQ-GADNGGKRQLLCVANTHIHANQELKDVKLWQ----VHTLLKGL 447

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 382 EK-ASSrpgsptADpnsIPLVLCADLNSLPDSGVVEYLSNGGVADNHKD-----FKELRyneclmnfscsgkngsSEGRI 455
Cdd:PLN03144 448 EKiAAS------AD---IPMLVCGDFNSVPGSAPHCLLATGKVDPLHPDlavdpLGILR----------------PASKL 502

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 456 THGFQLKSAYEN-NLMP---------------------YTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLDPQWLVENniT 513
Cdd:PLN03144 503 THQLPLVSAYSSfARMPgsgsgleqqrrrmdpatneplFTNCTRDFIGTLDYIFYTADSLTVESLLELLDEESLRKD--T 580

                        410
                 ....*....|....*..
gi 568935494 514 GCPHPHIPSDHFSLLTQ 530
Cdd:PLN03144 581 ALPSPEWSSDHIALLAE 597
CCR4 COG5239
mRNA deadenylase, 3'-5' endonuclease subunit Ccr4 [RNA processing and modification];
180-530 3.33e-73

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


Pssm-ID: 227564 [Multi-domain]  Cd Length: 378  Bit Score: 237.75  E-value: 3.33e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 180 PSASFTVMCYNVLCDKYATRQLYGYCpSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFS 259
Cdd:COG5239   27 KDTDFTIMTYNVLAQTYATRKMYPYS-GWALKWSYRSRLLLQELLYYNADILCLQEVDAEDFEDFWKDQLGKLGYDGIFI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 260 PKSR-AKIMSEQERKHVDGCAIFFKTE----KFTLVQKHTVEFNQVAMANSD--GSEAMLNRVMTKDNI--GVAVVLEVH 330
Cdd:COG5239  106 PKERkVKWMIDYDTTKVDGCAIFLKRFidssKLGLILAVTHLFWHPYGYYERfrQTYILLNRIGEKDNIawVCLFVGLFN 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 331 KELFGTgmkpihaadkqlLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEK--ASSRPGSPTADPNSIPLVLCADLNS 408
Cdd:COG5239  186 KEPGDT------------PYVANTHLPWDPKYRDVKLIQCSLLYRELKKVLKEelNDDKEEGDIKSYPEVDILITGDFNS 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 409 LPDSGVVEYLsNGGVADNHKDFkelryNECLMNFSCSGKNGSsegritHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFY 488
Cdd:COG5239  254 LRASLVYKFL-VTSQIQLHESL-----NGRDFSLYSVGYKFV------HPENLKSDNSKGELGFTNWTPGFKGVIDYIFY 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 568935494 489 S-KTHMNVLGVLGPLDPQWLVenNITGCPHPHIPSDHFSLLTQ 530
Cdd:COG5239  322 HgGLLTRQTGLLGVVEGEYAS--KVIGLPNMPFPSDHIPLLAE 362
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 186-530 8.15e-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: 182.30  E-value: 8.15e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 186 VMCYNVLCDKYATRqlygycpswalnweyrKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSRak 265
Cdd:cd08372    1 VASYNVNGLNAATR----------------ASGIARWVRELDPDIVCLQEVKDSQYSAVALNQLLPEGYHQYQSGPSR-- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 266 imseqeRKHVDGCAIFFKTEKFTLVQKHTVEFNQvamansdgseamlnrVMTKDNIGVAVVLEVHKELFgtgmkpihaad 345
Cdd:cd08372   63 ------KEGYEGVAILSKTPKFKIVEKHQYKFGE---------------GDSGERRAVVVKFDVHDKEL----------- 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 346 kqllIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILekassrpgsptaDPNSIPLVLCADLNSLPDSGVVEYLsnggvad 425
Cdd:cd08372  111 ----CVVNAHLQAGGTRADVRDAQLKEVLEFLKRLR------------QPNSAPVVICGDFNVRPSEVDSENP------- 167

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 426 nhkdfkelryneclmnfscsgkngSSEGRITHGFQLKSAYENNLMPYTNYTF--DFKGVIDYIFYSKTH-MNVLGVLGPL 502
Cdd:cd08372  168 ------------------------SSMLRLFVALNLVDSFETLPHAYTFDTYmhNVKSRLDYIFVSKSLlPSVKSSKILS 223

                        330       340
                 ....*....|....*....|....*...
gi 568935494 503 DPQWlvennitgcphPHIPSDHFSLLTQ 530
Cdd:cd08372  224 DAAR-----------ARIPSDHYPIEVT 240
Deadenylase_nocturnin cd09096
C-terminal deadenylase domain of nocturnin and related domains; This subfamily contains the ...
 205-528 3.88e-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: 113.67  E-value: 3.88e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 205 CPSWALNWEYRKKGIMEEIVNWDADIISLQEVetEQYFTLFLPALKDRGYDGFFSPKSRAKIMSEQERKHVDGCAIFFKT 284
Cdd:cd09096   22 CPCEALKWEERKYLILEEILTYDPDILCLQEV--DHYKDTLQPLLSRLGYQGTFFPKPDSPCLYIENNNGPDGCALFFRK 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 285 EKFTLV-------QKHTVEFNQVAMAnsdgseAMLNRvmtkdnigvavvlevhkelfgtgmkpihAADKQLLIVANAHMH 357
Cdd:cd09096  100 DRFELVntekirlSAMTLKTNQVAIA------CTLRC----------------------------KETGREICLAVTHLK 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 358 WDPEYSDVKLIQTMMFVSEVKNILEKAssrpgsptadpnSIPLVLCADLNSLPDSGVVEYLSNGGvadnhkdfkelryne 437
Cdd:cd09096  146 ARTGWERLRSEQGKDLLQNLQSFIEGA------------KIPLIICGDFNAEPTEPVYKTFSNSS--------------- 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 438 clMNFSCSGKNGSSEGrithgfqlksAYENnlmPYTNYTFDFKG----VIDYIFYSKTHMNVLGVLGpLDPQWLVENNit 513
Cdd:cd09096  199 --LNLNSAYKLLSADG----------QSEP---PYTTWKIRTSGecrhTLDYIFYSKDALSVEQLLD-LPTEEQIGPN-- 260

                        330
                 ....*....|....*
gi 568935494 514 GCPHPHIPSDHFSLL 528
Cdd:cd09096  261 RLPSFNYPSDHLSLV 275
Deadenylase cd09082
C-terminal deadenylase domain of CCR4, nocturnin, and related domains; This family contains ...
 186-528 2.86e-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: 2.86e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 186 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSRAK 265
Cdd:cd09082    1 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 266 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDN-IGVAVVLEVHKELFGTGMKPIHAA 344
Cdd:cd09082   81 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNiGVAVVLEVHKELFGAGMKPIHAAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 345 DKQLLIvANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVA 424
Cdd:cd09082  161 KQLLIV-ANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 425 DN-------HKDFKELRYNECLMNFSCSGKNGSSEGRIThgfqlksAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLG 497
Cdd:cd09082  240 DNhkdfkelRYNECLMNFSCNGKNGSSEGRITHGFQLKS-------AYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLG 312

                        330       340       350
                 ....*....|....*....|....*....|.
gi 568935494 498 VLGPLDPQWLVENNITGCPHPHIPSDHFSLL 528
Cdd:cd09082  313 VLGPLDPQWLVENNITGCPHPHIPSDHFSLL 343
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-133 1.28e-24

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 106.17  E-value: 1.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  33 ELEISG-RVRSLSTSLWSLTHLTALHLNDNNLARIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNDNYLRV 111
Cdd:COG4886  117 SLDLSGnQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITD 196

                         90       100
                 ....*....|....*....|..
gi 568935494 112 LPYELGRLFQLQTLGLTGNPLS 133
Cdd:COG4886  197 LPEPLGNLTNLEELDLSGNQLT 218
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-133 1.61e-23

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 103.09  E-value: 1.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  33 ELEISG-RVRSLSTSLWSLTHLTALHLNDNNLARIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNDNYLRV 111
Cdd:COG4886  140 ELDLSNnQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTD 219

                         90       100
                 ....*....|....*....|..
gi 568935494 112 LPYELGRLFQLQTLGLTGNPLS 133
Cdd:COG4886  220 LPEPLANLTNLETLDLSNNQLT 241
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
42-133 1.92e-21

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 96.93  E-value: 1.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  42 SLSTSLWSLTHLTALHLNDNNLARIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNDNYLRVLPYELGRLFQ 121
Cdd:COG4886  104 SGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTN 183

                         90
                 ....*....|..
gi 568935494 122 LQTLGLTGNPLS 133
Cdd:COG4886  184 LKELDLSNNQIT 195
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
 185-525 6.36e-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: 6.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 185 TVMCYNVLCDkyatrqlygyCPSWALN-WEYRKKGIMEEIVNWDADIISLQEVETEQyftlfLPALKDR--GYDgffspk 261
Cdd:cd09083    1 RVMTFNIRYD----------NPSDGENsWENRKDLVAELIKFYDPDIIGTQEALPHQ-----LADLEELlpEYD------ 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 262 sraKIMSEQERKHVDG--CAIFFKTEKFTLVQKHTveF---NQVAMANSDGSEAMLNRVMTkdnigvAVVLEvhkelfgt 336
Cdd:cd09083   60 ---WIGVGRDDGKEKGefSAIFYRKDRFELLDSGT--FwlsETPDVVGSKGWDAALPRICT------WARFK-------- 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 337 gmkpiHAADKQLLIVANAHMhwdpeysDvkliqtmmFVSEV------KNILEKASSRPGSptadpnsIPLVLCADLNSLP 410
Cdd:cd09083  121 -----DKKTGKEFYVFNTHL-------D--------HVGEEareesaKLILERIKEIAGD-------LPVILTGDFNAEP 173

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 411 DSGVVEYLSNGGVADNHKDFKElryneclmnfscsgkngssegrithgfqlksAYENNLMPYTNYTFDFKGV-IDYIFYS 489
Cdd:cd09083  174 DSEPYKTLTSGGLKDARDTAAT-------------------------------TDGGPEGTFHGFKGPPGGSrIDYIFVS 222

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 568935494 490 KtHMNVL--GVlgpldpqwlvennITGCPHPHIPSDHF 525
Cdd:cd09083  223 P-GVKVLsyEI-------------LTDRYDGRYPSDHF 246
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-174 1.01e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 69.96  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  33 ELEISG-RVRSLSTSLWSLTHLTALHLNDNNLARIPpDIAKLHNLVYLDLSSNKLRSLPaELGNMVSLRELLLNDNYLRV 111
Cdd:COG4886  209 ELDLSGnQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLTD 286

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568935494 112 LPYE-LGRLFQLQTLGLTGNPLSQDIMSLYQDPDGTRKLLNFMLDNLAVHPEQLPPRPWITLKE 174
Cdd:COG4886  287 LKLKeLELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALL 350
LRR_8 pfam13855
Leucine rich repeat;
51-109 8.00e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 54.84  E-value: 8.00e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568935494   51 THLTALHLNDNNLARIPPDIAK-LHNLVYLDLSSNKLRSL-PAELGNMVSLRELLLNDNYL 109
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PLN03150 PLN03150
hypothetical protein; Provisional
 48-131 8.82e-10

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 61.37  E-value: 8.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  48 WS-LTHLTALHLNDNNL-ARIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLRELLLNDNYL--RVlPYELG-RLFQ 121
Cdd:PLN03150 438 ISkLRHLQSINLSGNSIrGNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLsgRV-PAALGgRLLH 516

                         90
                 ....*....|
gi 568935494 122 LQTLGLTGNP 131
Cdd:PLN03150 517 RASFNFTDNA 526
PLN03150 PLN03150
hypothetical protein; Provisional
 55-133 2.26e-08

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 56.75  E-value: 2.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  55 ALHLNDNNL-ARIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLRELLLNDNYLR-VLPYELGRLFQLQTLGLTGNP 131
Cdd:PLN03150 422 GLGLDNQGLrGFIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNS 501


                 ..
gi 568935494 132 LS 133
Cdd:PLN03150 502 LS 503
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
16-134 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 568935494  16 TIMSAEEVANGKKSHWAELEISGRVRSLSTSLWSLTHLTALHLNDNNLARIPPDIAKLHNLVYLDLSSNKlrslpaELGN 95
Cdd:COG4886   38 LLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE------ELSN 111

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568935494  96 MVSLRELLLNDNYLRVLPYELGRLFQLQTLGLTGNPLSQ 134
Cdd:COG4886  112 LTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTD 150
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 49-138 3.07e-07

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 53.31  E-value: 3.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  49 SLTHLTALHLNDNNL-ARIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLRELLLNDNYLR-VLPYELGRLFQLQTL 125
Cdd:PLN00113 162 SFSSLKVLDLGGNVLvGKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHL 241

                         90
                 ....*....|...
gi 568935494 126 GLTGNPLSQDIMS 138
Cdd:PLN00113 242 DLVYNNLTGPIPS 254
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 49-135 3.81e-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: 3.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  49 SLTHLTALHLNDNNLARI-------------------PPD----------IAKLHNLVYLDLSSNKLRSLpAELGNMVSL 99
Cdd:cd21340   66 NLVNLKKLYLGGNRISVVeglenltnleelhienqrlPPGekltfdprslAALSNSLRVLNISGNNIDSL-EPLAPLRNL 144

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568935494 100 RELLLNDNYLR---VLPYELGRLFQLQTLGLTGNPLSQD 135
Cdd:cd21340  145 EQLDASNNQISdleELLDLLSSWPSLRELDLTGNPVCKK 183
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 187-303 5.11e-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: 5.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  187 MCYNVLCDkyatrqlygycPSWALNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKsraki 266
Cdd:pfam03372   1 LTWNVNGG-----------NADAAGDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFLSYGGPG----- 64

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568935494  267 mseqERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMA 303
Cdd:pfam03372  65 ----GGGGGGGVAILSRYPLSSVILVDLGEFGDPALR 97
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 47-130 2.46e-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: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  47 LWSLTHLtalHLNDNNLARIpPDIAKLHNLVYLDLSSNKLRSLPAeLGNMVSLRELLLNDNYLRVLPYeLGRLFQLQTLG 126
Cdd:cd21340    1 LKRITHL---YLNDKNITKI-DNLSLCKNLKVLYLYDNKITKIEN-LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLY 74


                 ....
gi 568935494 127 LTGN 130
Cdd:cd21340   75 LGGN 78
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-179 3.04e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.55  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  33 ELEISG-RVRSLStSLWSLTHLTALHLNDNNLARIPPdIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNDNYLRV 111
Cdd:COG4886  232 TLDLSNnQLTDLP-ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLN 309

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568935494 112 LPYELGRLFQLQTLGLTGNPLSQDIMSLYQDPDGTRKLLNFMLDNLAVHPEQLPPRPWITLKERDQIL 179
Cdd:COG4886  310 LLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEA 377
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 49-139 7.05e-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: 7.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  49 SLTHLTALHLNDNNLARIpPDIAKLHNLVYLDLSSNKLRSLPaELGNMVSLRELLLNDNYLRVLpyE-LGRLFQLQTLGL 127
Cdd:cd21340   22 LCKNLKVLYLYDNKITKI-ENLEFLTNLTHLYLQNNQIEKIE-NLENLVNLKKLYLGGNRISVV--EgLENLTNLEELHI 97

                         90
                 ....*....|....*...
gi 568935494 128 ------TGNPLSQDIMSL 139
Cdd:cd21340   98 enqrlpPGEKLTFDPRSL 115
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 49-136 1.13e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 48.31  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  49 SLTHLTALHLNDNNLA-RIPPDIAKLHNLVYLDLSSNKLRS-LPAELGNMVSLRELLLNDNYLR-VLPYELGRLFQLQTL 125
Cdd:PLN00113 138 SIPNLETLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVGkIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWI 217

                         90
                 ....*....|.
gi 568935494 126 GLTGNPLSQDI 136
Cdd:PLN00113 218 YLGYNNLSGEI 228
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 42-136 2.62e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 47.15  E-value: 2.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  42 SLSTSLWSLTHLTALHLNDNNLA-RIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLREL-LLNDNYLRVLPYELGR 118
Cdd:PLN00113 251 PIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILhLFSNNFTGKIPVALTS 330

                         90
                 ....*....|....*...
gi 568935494 119 LFQLQTLGLTGNPLSQDI 136
Cdd:PLN00113 331 LPRLQVLQLWSNKFSGEI 348
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
 186-490 6.57e-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: 6.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 186 VMCYNVlcdkyatRQLYGYcpswalNWEYRKKGIMEEIVNWDADIISLQEVETEQYFTLFLPALKDRGYDGFFSPKSRAK 265
Cdd:cd09084    1 VMSYNV-------RSFNRY------KWKDDPDKILDFIKKQDPDILCLQEYYGSEGDKDDDLRLLLKGYPYYYVVYKSDS 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 266 IMSEQerkhvdgcAIFfktEKFTLVQKHTVEFNqvamaNSDGSEAMLNRVMTKDNIgvaVVLEVHKELFGtgmkpIHAAD 345
Cdd:cd09084   68 GGTGL--------AIF---SKYPILNSGSIDFP-----NTNNNAIFADIRVGGDTI---RVYNVHLESFR-----ITPSD 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 346 KQLLivanAHMHWDPEYSDvKLIQTM--MFV---SEVKNILEKASSRPGsptadpnsiPLVLCADLNSLPDSGVVEYLSN 420
Cdd:cd09084  124 KELY----KEEKKAKELSR-NLLRKLaeAFKrraAQADLLAADIAASPY---------PVIVCGDFNDTPASYVYRTLKK 189

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568935494 421 GgvadnhkdfkelryneclmnfscsgkngssegrithgfqLKSAYE--NNLMPYTnYTFDFKGV-IDYIFYSK 490
Cdd:cd09084  190 G---------------------------------------LTDAFVeaGSGFGYT-FNGLFFPLrIDYILTSK 222
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
52-165 8.48e-05

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 45.46  E-value: 8.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  52 HLTALHLNDNNLARIPPDiakLH-NLVYLDLSSNKLRSLPAELGNmvSLRELLLNDNYLRVLPYELGRlfQLQTLGLTGN 130
Cdd:PRK15370 200 QITTLILDNNELKSLPEN---LQgNIKTLYANSNQLTSIPATLPD--TIQEMELSINRITELPERLPS--ALQSLDLFHN 272

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568935494 131 PLSQDIMSLyqdPDGTRkLLNFMLDNLAVHPEQLP 165
Cdd:PRK15370 273 KISCLPENL---PEELR-YLSVYDNSIRTLPAHLP 303
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 36-142 9.24e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 45.61  E-value: 9.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  36 ISGRvrsLSTSLWSLTHLTALHLNDNNLARIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLRELLLNDNYLR-VLP 113
Cdd:PLN00113 440 LQGR---INSRKWDMPSLQMLSLARNKFFGGLPDSFGSKRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSENKLSgEIP 516

                         90       100
                 ....*....|....*....|....*....
gi 568935494 114 YELGRLFQLQTLGLTGNPLSQDIMSLYQD 142
Cdd:PLN00113 517 DELSSCKKLVSLDLSHNQLSGQIPASFSE 545
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 41-107 1.94e-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: 1.94e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  41 RSLSTSLWSLTHLTALHlndNNLARIPPdIAKLHNLVYLDLSSNKLRSLPA---ELGNMVSLRELLLNDN 107
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 ...
 51-86 3.68e-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: 3.68e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568935494   51 THLTALHLNDNNLARIPPdIAKLHNLVYLDLSSNKL 86
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNNK 35
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 46-139 3.87e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 43.30  E-value: 3.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  46 SLWSLTHLTALHLNDNNLA-RIPPDIAKLHNLVYLDLSSNKLRS-LPAELGNMVSLRELLLNDNYLR-VLPYELG----- 117
Cdd:PLN00113 327 ALTSLPRLQVLQLWSNKFSgEIPKNLGKHNNLTVLDLSTNNLTGeIPEGLCSSGNLFKLILFSNSLEgEIPKSLGacrsl 406

                         90       100
                 ....*....|....*....|..
gi 568935494 118 RLFQLQTLGLTGNpLSQDIMSL 139
Cdd:PLN00113 407 RRVRLQDNSFSGE-LPSEFTKL 427
LRR_8 pfam13855
Leucine rich repeat;
49-86 4.07e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 38.66  E-value: 4.07e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 568935494   49 SLTHLTALHLNDNNLARIPPD-IAKLHNLVYLDLSSNKL 86
Cdd:pfam13855  23 GLSNLKVLDLSNNLLTTLSPGaFSGLPSLRYLDLSGNRL 61
nSMase cd09078
Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological ...
 186-525 2.26e-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: 40.02  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 186 VMCYNVLCDKYATRQLygycPSWALNWEYRKkgIMEEIVNWDadIISLQEVeteqyFT-----LFLPALKDRGydGFFSP 260
Cdd:cd09078    3 VLTYNVFLLPPLLYNN----GDDGQDERLDL--IPKALLQYD--VVVLQEV-----FDararkRLLNGLKKEY--PYQTD 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 261 K-SRAKIMSEqeRKHVD-GCAIFfktEKFTLVQKHTVEFNqvamaNSDGSEAMLNR--VMTKDNIGvavvlevhkelfgt 336
Cdd:cd09078   68 VvGRSPSGWS--SKLVDgGVVIL---SRYPIVEKDQYIFP-----NGCGADCLAAKgvLYAKINKG-------------- 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 337 GMKPIHaadkqlliVANAHMH-WDPEYSDVK-----LIQTMMFVSEvKNIlekassrpgsptadPNSIPLVLCADLNslp 410
Cdd:cd09078  124 GTKVYH--------VFGTHLQaSDGSCLDRAvrqkqLDELRAFIEE-KNI--------------PDNEPVIIAGDFN--- 177

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494 411 dsgvveylsnggvADNHKDFKElrYNECLMNFSCSgkNGSSegRITHGFQLKS-AYENNLMPYTNYTFDFKGVIDYIFYS 489
Cdd:cd09078  178 -------------VDKRSSRDE--YDDMLEQLHDY--NAPE--PITAGETPLTwDPGTNLLAKYNYPGGGGERLDYILYS 238

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 568935494 490 KTHMNVLG----VLGPLDPQWLVENNITgcpHPHIpSDHF 525
Cdd:cd09078  239 NDHLQPSSwsneVEVPKSPTWSVTNGYT---FADL-SDHY 274
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 50-125 3.40e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 40.22  E-value: 3.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568935494  50 LTHLTALHLNDNNLA-RIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLRELLLNDNYLRVLPYELgrLFQLQTL 125
Cdd:PLN00113 235 LTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSGEIPEL--VIQLQNL 310
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 32-109 5.50e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 39.83  E-value: 5.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935494  32 AELEISGRVRSlstSLWSLTHLTALHLNDNNLA-RIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLRELLLNDNYL 109
Cdd:PLN00113 507 SENKLSGEIPD---ELSSCKKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQLSgEIPKNLGNVESLVQVNISHNHL 583
LRR smart00370
Leucine-rich repeats, outliers;
73-93 9.60e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 33.86  E-value: 9.60e-03
                           10        20
                   ....*....|....*....|.
gi 568935494    73 LHNLVYLDLSSNKLRSLPAEL 93
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGA 21
LRR_TYP smart00369
Leucine-rich repeats, typical (most populated) subfamily;
73-93 9.60e-03

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


Pssm-ID: 197687 [Multi-domain]  Cd Length: 24  Bit Score: 33.86  E-value: 9.60e-03
                           10        20
                   ....*....|....*....|.
gi 568935494    73 LHNLVYLDLSSNKLRSLPAEL 93
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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