NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24649583|ref|NP_732966|]
View 

twin, isoform E [Drosophila melanogaster]

Protein Classification

CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4( domain architecture ID 11469374)

CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4 acts as the catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Deadenylase_CCR4 cd09097
C-terminal deadenylase domain of CCR4 and related domains; This subfamily contains the ...
 194-535 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: 528.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 194 VMCYNVLCDKYATRQMYGYCPSWALCWEYRKKSIIDEIRHYAADIISLQEIETEQFYHFFLPELKNDGYEGIFSPKSRAK 273
Cdd:cd09097   1 VMCYNVLCDKYATRQQYGYCPSWALNWDYRKQNILKEILSYNADILCLQEVETDQYEDFFLPELKQHGYDGVFKPKSRAK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 274 TMSELERKYVDGCAIFFRASKFTLIKESLIEFNQLAMAN--AEGSDNMLNRVMPKDNIGLAALLKVKENAWEPMSevtqi 351
Cdd:cd09097  81 TMSEAERKHVDGCAIFFKTSKFKLVEKHLIEFNQLAMANadAEGSEDMLNRVMTKDNIALIVVLEARETSYEGNK----- 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 352 SQPLLVCTAHIHWDPEFCDVKLIQTMMLSNELKTIIDEASHSFRPghknDSNAVQLLLCGDFNSLPDSGVVEFLGKGRVS 431
Cdd:cd09097 156 GQLLIVANTHIHWDPEFSDVKLVQTMMLLEELEKIAEKFSRYPYE----DSADIPLVVCGDFNSLPDSGVYELLSNGSVS 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 432 MDHLDFKDMGYKSCLqrllsnDTNEFTHSFKLASAY-NEDIMPHTNYTFDFKGIIDYIFYTKTGMVPLGLLGPVSNDWLr 510
Cdd:cd09097 232 PNHPDFKEDPYGEYL------TASGLTHSFKLKSAYaNLGELPFTNYTPDFKGVIDYIFYSADTLSVLGLLGPPDEDWY- 304

                       330       340
                ....*....|....*....|....*
gi 24649583 511 ENKVVGCPHPHIPSDHFPLLVELEL 535
Cdd:cd09097 305 LNKVVGLPNPHFPSDHIALLAEFRI 329
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
48-140 1.17e-19

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 91.53  E-value: 1.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  48 VRNISPSLWEFEHLTALYLNDNQLLRLPADVGMLTSLRTLDLSSNKLRSLPAELGELIQLRELLLNNNFLRVLPYEIGKL 127
Cdd:COG4886 125 LTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNL 204

                        90
                ....*....|...
gi 24649583 128 FHLVILGLMGNPL 140
Cdd:COG4886 205 TNLEELDLSGNQL 217
 
Name Accession Description Interval E-value
Deadenylase_CCR4 cd09097
C-terminal deadenylase domain of CCR4 and related domains; This subfamily contains the ...
 194-535 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: 528.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 194 VMCYNVLCDKYATRQMYGYCPSWALCWEYRKKSIIDEIRHYAADIISLQEIETEQFYHFFLPELKNDGYEGIFSPKSRAK 273
Cdd:cd09097   1 VMCYNVLCDKYATRQQYGYCPSWALNWDYRKQNILKEILSYNADILCLQEVETDQYEDFFLPELKQHGYDGVFKPKSRAK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 274 TMSELERKYVDGCAIFFRASKFTLIKESLIEFNQLAMAN--AEGSDNMLNRVMPKDNIGLAALLKVKENAWEPMSevtqi 351
Cdd:cd09097  81 TMSEAERKHVDGCAIFFKTSKFKLVEKHLIEFNQLAMANadAEGSEDMLNRVMTKDNIALIVVLEARETSYEGNK----- 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 352 SQPLLVCTAHIHWDPEFCDVKLIQTMMLSNELKTIIDEASHSFRPghknDSNAVQLLLCGDFNSLPDSGVVEFLGKGRVS 431
Cdd:cd09097 156 GQLLIVANTHIHWDPEFSDVKLVQTMMLLEELEKIAEKFSRYPYE----DSADIPLVVCGDFNSLPDSGVYELLSNGSVS 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 432 MDHLDFKDMGYKSCLqrllsnDTNEFTHSFKLASAY-NEDIMPHTNYTFDFKGIIDYIFYTKTGMVPLGLLGPVSNDWLr 510
Cdd:cd09097 232 PNHPDFKEDPYGEYL------TASGLTHSFKLKSAYaNLGELPFTNYTPDFKGVIDYIFYSADTLSVLGLLGPPDEDWY- 304

                       330       340
                ....*....|....*....|....*
gi 24649583 511 ENKVVGCPHPHIPSDHFPLLVELEL 535
Cdd:cd09097 305 LNKVVGLPNPHFPSDHIALLAEFRI 329
CCR4 COG5239
mRNA deadenylase, 3'-5' endonuclease subunit Ccr4 [RNA processing and modification];
174-539 2.24e-81

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


Pssm-ID: 227564 [Multi-domain]  Cd Length: 378  Bit Score: 259.32  E-value: 2.24e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 174 QRPWLPLAKPNktRPACIFTVMCYNVLCDKYATRQMYGYCpSWALCWEYRKKSIIDEIRHYAADIISLQEIETEQFYHFF 253
Cdd:COG5239  15 QRPFLSIGHYA--EKDTDFTIMTYNVLAQTYATRKMYPYS-GWALKWSYRSRLLLQELLYYNADILCLQEVDAEDFEDFW 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 254 LPELKNDGYEGIFSPKSR-AKTMSELERKYVDGCAIFFR----ASKFTLIKESLIEFNQLAMANAE--GSDNMLNRVMPK 326
Cdd:COG5239  92 KDQLGKLGYDGIFIPKERkVKWMIDYDTTKVDGCAIFLKrfidSSKLGLILAVTHLFWHPYGYYERfrQTYILLNRIGEK 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 327 DNIGLAALLKVKENawepmsevTQISQPLLVCTAHIHWDPEFCDVKLIQTMMLSNELKTIIDE--ASHSFRPGHKNDSnA 404
Cdd:COG5239 172 DNIAWVCLFVGLFN--------KEPGDTPYVANTHLPWDPKYRDVKLIQCSLLYRELKKVLKEelNDDKEEGDIKSYP-E 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 405 VQLLLCGDFNSLPDSGVVEFLGKGRV-SMDHLDFKDMGYKSclqrllsnDTNEFTHSFKLASAYNEDIMPHTNYTFDFKG 483
Cdd:COG5239 243 VDILITGDFNSLRASLVYKFLVTSQIqLHESLNGRDFSLYS--------VGYKFVHPENLKSDNSKGELGFTNWTPGFKG 314

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24649583 484 IIDYIFYTKTGMVPL-GLLGPVsnDWLRENKVVGCPHPHIPSDHFPLLVELELMHTA 539
Cdd:COG5239 315 VIDYIFYHGGLLTRQtGLLGVV--EGEYASKVIGLPNMPFPSDHIPLLAEFASDHKN 369
PLN03144 PLN03144
Carbon catabolite repressor protein 4 homolog; Provisional
 170-532 4.58e-73

Carbon catabolite repressor protein 4 homolog; Provisional


Pssm-ID: 178689 [Multi-domain]  Cd Length: 606  Bit Score: 244.25  E-value: 4.58e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  170 NPPPQR--------PWLPLAKPNKTRPACIFTVMCYNVLCDKYATRQMYGYCPSWALCWEYRKKSIIDEIRHYAADIISL 241
Cdd:PLN03144 225 SPTPRRliqvngldGMGHLDLDGRTSSAGTFTVLSYNILSDLYATSDMYSYCPPWALSWTYRRQNLLREIVGYRADILCL 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  242 QEIETEQFYHFFLPELKNDGYEGIFSPKSrAKTMSelERKYV-DGCAIFFRASKFTLIKESLIEFNQLAMANAEG----- 315
Cdd:PLN03144 305 QEVQSDHFEEFFAPELDKHGYQALYKKKT-TEVYT--GNTYViDGCATFFRRDRFSLVKKYEVEFNKAAQSLTEAlipsa 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  316 -SDNMLNRVMpKDNIGLAALLKVKEnawEPMSEVTQISQPLLvCTA--HIHWDPEFCDVKLIQTMMLSNELKTIIDEASh 392
Cdd:PLN03144 382 qKKAALNRLL-KDNVALIVVLEAKF---GNQGADNGGKRQLL-CVAntHIHANQELKDVKLWQVHTLLKGLEKIAASAD- 455

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  393 sfrpghkndsnaVQLLLCGDFNSLPDSGVVEFLGKGRVSMDHLDfkdmgyksclqrlLSND-------TNEFTHSFKLAS 465
Cdd:PLN03144 456 ------------IPMLVCGDFNSVPGSAPHCLLATGKVDPLHPD-------------LAVDplgilrpASKLTHQLPLVS 510

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  466 AY------------------------NEDIMphTNYTFDFKGIIDYIFYTKTGMVPLGLLGPVSNDWLRenKVVGCPHPH 521
Cdd:PLN03144 511 AYssfarmpgsgsgleqqrrrmdpatNEPLF--TNCTRDFIGTLDYIFYTADSLTVESLLELLDEESLR--KDTALPSPE 586

                        410
                 ....*....|.
gi 24649583  522 IPSDHFPLLVE 532
Cdd:PLN03144 587 WSSDHIALLAE 597
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
48-140 1.17e-19

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 91.53  E-value: 1.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  48 VRNISPSLWEFEHLTALYLNDNQLLRLPADVGMLTSLRTLDLSSNKLRSLPAELGELIQLRELLLNNNFLRVLPYEIGKL 127
Cdd:COG4886 125 LTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNL 204

                        90
                ....*....|...
gi 24649583 128 FHLVILGLMGNPL 140
Cdd:COG4886 205 TNLEELDLSGNQL 217
PLN03150 PLN03150
hypothetical protein; Provisional
 35-139 2.69e-09

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 59.83  E-value: 2.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583   35 KKTNWS----GLEITGcVRNISPSLW-EFEHLTALYLNDNQLL-RLPADVGMLTSLRTLDLSSNKLR-SLPAELGELIQL 107
Cdd:PLN03150 414 TKGKWFidglGLDNQG-LRGFIPNDIsKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSL 492

                         90       100       110
                 ....*....|....*....|....*....|....
gi 24649583  108 RELLLNNNFL--RVLPYEIGKLFHLVILGLMGNP 139
Cdd:PLN03150 493 RILNLNGNSLsgRVPAALGGRLLHRASFNFTDNA 526
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 195-324 4.29e-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: 4.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583   195 MCYNVLCDkyatrqmygycPSWALCWEYRKKSIIDEIRHYAADIISLQEIETEQFYHFFLPELKNDGYEGIFSPKsrakt 274
Cdd:pfam03372   1 LTWNVNGG-----------NADAAGDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFLSYGGPG----- 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 24649583   275 mselERKYVDGCAIFFRASKFTLIKESLIEFNQLAMANAEGSDNMLNRVM 324
Cdd:pfam03372  65 ----GGGGGGGVAILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVP 110
LRR_8 pfam13855
Leucine rich repeat;
60-115 7.33e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 46.36  E-value: 7.33e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 24649583    60 HLTALYLNDNQLLRLPADVGM-LTSLRTLDLSSNKLRSL-PAELGELIQLRELLLNNN 115
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGN 59
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 60-142 6.12e-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: 41.31  E-value: 6.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  60 HLTALYLNDNQLL-----------------------------------------RLPADVGML----------TSLRTLD 88
Cdd:cd21340  47 NLTHLYLQNNQIEkienlenlvnlkklylggnrisvveglenltnleelhienqRLPPGEKLTfdprslaalsNSLRVLN 126

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24649583  89 LSSNKLRSLpAELGELIQLRELLLNNNFLR---VLPYEIGKLFHLVILGLMGNPLQK 142
Cdd:cd21340 127 ISGNNIDSL-EPLAPLRNLEQLDASNNQISdleELLDLLSSWPSLRELDLTGNPVCK 182
LRR_TYP smart00369
Leucine-rich repeats, typical (most populated) subfamily;
81-101 8.70e-04

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


Pssm-ID: 197687 [Multi-domain]  Cd Length: 24  Bit Score: 36.56  E-value: 8.70e-04
                           10        20
                   ....*....|....*....|.
gi 24649583     81 LTSLRTLDLSSNKLRSLPAEL 101
Cdd:smart00369   1 LPNLRELDLSNNQLSSLPPGA 21
 
Name Accession Description Interval E-value
Deadenylase_CCR4 cd09097
C-terminal deadenylase domain of CCR4 and related domains; This subfamily contains the ...
 194-535 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: 528.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 194 VMCYNVLCDKYATRQMYGYCPSWALCWEYRKKSIIDEIRHYAADIISLQEIETEQFYHFFLPELKNDGYEGIFSPKSRAK 273
Cdd:cd09097   1 VMCYNVLCDKYATRQQYGYCPSWALNWDYRKQNILKEILSYNADILCLQEVETDQYEDFFLPELKQHGYDGVFKPKSRAK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 274 TMSELERKYVDGCAIFFRASKFTLIKESLIEFNQLAMAN--AEGSDNMLNRVMPKDNIGLAALLKVKENAWEPMSevtqi 351
Cdd:cd09097  81 TMSEAERKHVDGCAIFFKTSKFKLVEKHLIEFNQLAMANadAEGSEDMLNRVMTKDNIALIVVLEARETSYEGNK----- 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 352 SQPLLVCTAHIHWDPEFCDVKLIQTMMLSNELKTIIDEASHSFRPghknDSNAVQLLLCGDFNSLPDSGVVEFLGKGRVS 431
Cdd:cd09097 156 GQLLIVANTHIHWDPEFSDVKLVQTMMLLEELEKIAEKFSRYPYE----DSADIPLVVCGDFNSLPDSGVYELLSNGSVS 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 432 MDHLDFKDMGYKSCLqrllsnDTNEFTHSFKLASAY-NEDIMPHTNYTFDFKGIIDYIFYTKTGMVPLGLLGPVSNDWLr 510
Cdd:cd09097 232 PNHPDFKEDPYGEYL------TASGLTHSFKLKSAYaNLGELPFTNYTPDFKGVIDYIFYSADTLSVLGLLGPPDEDWY- 304

                       330       340
                ....*....|....*....|....*
gi 24649583 511 ENKVVGCPHPHIPSDHFPLLVELEL 535
Cdd:cd09097 305 LNKVVGLPNPHFPSDHIALLAEFRI 329
Deadenylase_CCR4b cd10312
C-terminal deadenylase domain of CCR4b, also known as CCR4-NOT transcription complex subunit ...
 194-535 2.57e-178

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: 506.10  E-value: 2.57e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 194 VMCYNVLCDKYATRQMYGYCPSWALCWEYRKKSIIDEIRHYAADIISLQEIETEQFYHFFLPELKNDGYEGIFSPKSRAK 273
Cdd:cd10312   1 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 274 TMSELERKYVDGCAIFFRASKFTLIKESLIEFNQLAMANAEGSDNMLNRVMPKDNIGLAALLKVKENAW------EPMSE 347
Cdd:cd10312  81 IMSEQERKHVDGCAIFFKTEKFSLVQKHTVEFNQVAMANSEGSEAMLNRVMTKDNIGVAVVLEVHKELFgagmkpIHAAD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 348 vtqiSQPLLVCTAHIHWDPEFCDVKLIQTMMLSNELKTIIDEASHsfRPGHKN-DSNAVQLLLCGDFNSLPDSGVVEFLG 426
Cdd:cd10312 161 ----KQLLIVANAHMHWDPEYSDVKLIQTMMFVSELKNILEKASS--RPGSPTaDPNSIPLVLCADLNSLPDSGVVEYLS 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 427 KGRVSMDHLDFKDMGYKSCLQRLLSNDTN-----EFTHSFKLASAYNEDIMPHTNYTFDFKGIIDYIFYTKTGMVPLGLL 501
Cdd:cd10312 235 NGGVADNHKDFKELRYNECLMNFSCNGKNgssegRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVL 314

                       330       340       350
                ....*....|....*....|....*....|....
gi 24649583 502 GPVSNDWLRENKVVGCPHPHIPSDHFPLLVELEL 535
Cdd:cd10312 315 GPLDPQWLVENNITGCPHPHIPSDHFSLLTQLEL 348
Deadenylase_CCR4a cd10313
C-terminal deadenylase domain of CCR4a, also known as CCR4-NOT transcription complex subunit 6; ...
 194-535 3.33e-159

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: 457.58  E-value: 3.33e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 194 VMCYNVLCDKYATRQMYGYCPSWALCWEYRKKSIIDEIRHYAADIISLQEIETEQFYHFFLPELKNDGYEGIFSPKSRAK 273
Cdd:cd10313   1 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIMQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 274 TMSELERKYVDGCAIFFRASKFTLIKESLIEFNQLAMANAEGSDNMLNRVMPKDNIGLAALLKVKENAWEPMSEVTQI-- 351
Cdd:cd10313  81 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAVLLELRKELIEMSSGKPHLgm 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 352 -SQPLLVCTAHIHWDPEFCDVKLIQTMMLSNELKTIIDEASHSFRPGHKNDSNAVQLLLCGDFNSLPDSGVVEFLGKGRV 430
Cdd:cd10313 161 eKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASRSLKSSVLGETGTIPLVLCADLNSLPDSGVVEYLSTGGV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 431 SMDHLDFKDMGYKSCLQRLLSNDTN-----EFTHSFKLASAYNEDIMPHTNYTFDFKGIIDYIFYTKTGMVPLGLLGPVS 505
Cdd:cd10313 241 ETNHKDFKELRYNESLTNFSCNGKNgttngRITHGFKLKSAYENGLMPYTNYTFDFKGIIDYIFYSKPQLNTLGILGPLD 320

                       330       340       350
                ....*....|....*....|....*....|
gi 24649583 506 NDWLRENKVVGCPHPHIPSDHFPLLVELEL 535
Cdd:cd10313 321 HHWLVENNISGCPHPLIPSDHFSLFAQLEL 350
CCR4 COG5239
mRNA deadenylase, 3'-5' endonuclease subunit Ccr4 [RNA processing and modification];
174-539 2.24e-81

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


Pssm-ID: 227564 [Multi-domain]  Cd Length: 378  Bit Score: 259.32  E-value: 2.24e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 174 QRPWLPLAKPNktRPACIFTVMCYNVLCDKYATRQMYGYCpSWALCWEYRKKSIIDEIRHYAADIISLQEIETEQFYHFF 253
Cdd:COG5239  15 QRPFLSIGHYA--EKDTDFTIMTYNVLAQTYATRKMYPYS-GWALKWSYRSRLLLQELLYYNADILCLQEVDAEDFEDFW 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 254 LPELKNDGYEGIFSPKSR-AKTMSELERKYVDGCAIFFR----ASKFTLIKESLIEFNQLAMANAE--GSDNMLNRVMPK 326
Cdd:COG5239  92 KDQLGKLGYDGIFIPKERkVKWMIDYDTTKVDGCAIFLKrfidSSKLGLILAVTHLFWHPYGYYERfrQTYILLNRIGEK 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 327 DNIGLAALLKVKENawepmsevTQISQPLLVCTAHIHWDPEFCDVKLIQTMMLSNELKTIIDE--ASHSFRPGHKNDSnA 404
Cdd:COG5239 172 DNIAWVCLFVGLFN--------KEPGDTPYVANTHLPWDPKYRDVKLIQCSLLYRELKKVLKEelNDDKEEGDIKSYP-E 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 405 VQLLLCGDFNSLPDSGVVEFLGKGRV-SMDHLDFKDMGYKSclqrllsnDTNEFTHSFKLASAYNEDIMPHTNYTFDFKG 483
Cdd:COG5239 243 VDILITGDFNSLRASLVYKFLVTSQIqLHESLNGRDFSLYS--------VGYKFVHPENLKSDNSKGELGFTNWTPGFKG 314

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24649583 484 IIDYIFYTKTGMVPL-GLLGPVsnDWLRENKVVGCPHPHIPSDHFPLLVELELMHTA 539
Cdd:COG5239 315 VIDYIFYHGGLLTRQtGLLGVV--EGEYASKVIGLPNMPFPSDHIPLLAEFASDHKN 369
PLN03144 PLN03144
Carbon catabolite repressor protein 4 homolog; Provisional
 170-532 4.58e-73

Carbon catabolite repressor protein 4 homolog; Provisional


Pssm-ID: 178689 [Multi-domain]  Cd Length: 606  Bit Score: 244.25  E-value: 4.58e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  170 NPPPQR--------PWLPLAKPNKTRPACIFTVMCYNVLCDKYATRQMYGYCPSWALCWEYRKKSIIDEIRHYAADIISL 241
Cdd:PLN03144 225 SPTPRRliqvngldGMGHLDLDGRTSSAGTFTVLSYNILSDLYATSDMYSYCPPWALSWTYRRQNLLREIVGYRADILCL 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  242 QEIETEQFYHFFLPELKNDGYEGIFSPKSrAKTMSelERKYV-DGCAIFFRASKFTLIKESLIEFNQLAMANAEG----- 315
Cdd:PLN03144 305 QEVQSDHFEEFFAPELDKHGYQALYKKKT-TEVYT--GNTYViDGCATFFRRDRFSLVKKYEVEFNKAAQSLTEAlipsa 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  316 -SDNMLNRVMpKDNIGLAALLKVKEnawEPMSEVTQISQPLLvCTA--HIHWDPEFCDVKLIQTMMLSNELKTIIDEASh 392
Cdd:PLN03144 382 qKKAALNRLL-KDNVALIVVLEAKF---GNQGADNGGKRQLL-CVAntHIHANQELKDVKLWQVHTLLKGLEKIAASAD- 455

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  393 sfrpghkndsnaVQLLLCGDFNSLPDSGVVEFLGKGRVSMDHLDfkdmgyksclqrlLSND-------TNEFTHSFKLAS 465
Cdd:PLN03144 456 ------------IPMLVCGDFNSVPGSAPHCLLATGKVDPLHPD-------------LAVDplgilrpASKLTHQLPLVS 510

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  466 AY------------------------NEDIMphTNYTFDFKGIIDYIFYTKTGMVPLGLLGPVSNDWLRenKVVGCPHPH 521
Cdd:PLN03144 511 AYssfarmpgsgsgleqqrrrmdpatNEPLF--TNCTRDFIGTLDYIFYTADSLTVESLLELLDEESLR--KDTALPSPE 586

                        410
                 ....*....|.
gi 24649583  522 IPSDHFPLLVE 532
Cdd:PLN03144 587 WSSDHIALLAE 597
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 194-533 6.96e-30

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: 117.58  E-value: 6.96e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 194 VMCYNVLCDKYATRqmygycpswalcweyrKKSIIDEIRHYAADIISLQEIETEQFYHFFLPELKNDGYEGIFSPKSRak 273
Cdd:cd08372   1 VASYNVNGLNAATR----------------ASGIARWVRELDPDIVCLQEVKDSQYSAVALNQLLPEGYHQYQSGPSR-- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 274 tmseleRKYVDGCAIFFRASKFTlikesliefnqlamaNAEGSDNMLNRVMPKDNIGLAAllKVKENAWEpmsevtqisq 353
Cdd:cd08372  63 ------KEGYEGVAILSKTPKFK---------------IVEKHQYKFGEGDSGERRAVVV--KFDVHDKE---------- 109

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 354 pLLVCTAHIHWDPEFCDVKLIQTMMLSNELKtiideashsFRPGHKNDSnavqLLLCGDFNSLPDSGVVEFLGKgrvsmd 433
Cdd:cd08372 110 -LCVVNAHLQAGGTRADVRDAQLKEVLEFLK---------RLRQPNSAP----VVICGDFNVRPSEVDSENPSS------ 169

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 434 hldfkdmgyksclqrllsndTNEFTHSFKLASAYNEDIMPHTNYTF--DFKGIIDYIFYTKTgmvplgLLGPVSNDWLRE 511
Cdd:cd08372 170 --------------------MLRLFVALNLVDSFETLPHAYTFDTYmhNVKSRLDYIFVSKS------LLPSVKSSKILS 223

                       330       340
                ....*....|....*....|..
gi 24649583 512 NKvvgcPHPHIPSDHFPLLVEL 533
Cdd:cd08372 224 DA----ARARIPSDHYPIEVTL 241
Deadenylase_nocturnin cd09096
C-terminal deadenylase domain of nocturnin and related domains; This subfamily contains the ...
 213-535 6.47e-23

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: 98.65  E-value: 6.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 213 CPSWALCWEYRKKSIIDEIRHYAADIISLQEIetEQFYHFFLPELKNDGYEGIFSPKSRAKTMSELERKYVDGCAIFFRA 292
Cdd:cd09096  22 CPCEALKWEERKYLILEEILTYDPDILCLQEV--DHYKDTLQPLLSRLGYQGTFFPKPDSPCLYIENNNGPDGCALFFRK 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 293 SKFTLIKESLIefnqlamanaegsdnMLNRVMPKDN-IGLAALLKVKENAwepmsevtqisQPLLVCTAHIHWDPEFCDV 371
Cdd:cd09096 100 DRFELVNTEKI---------------RLSAMTLKTNqVAIACTLRCKETG-----------REICLAVTHLKARTGWERL 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 372 KLIQTMMLSNELKTIIDEAshsFRPghkndsnavqLLLCGDFNSLPDSGVveflgkgrvsmdhldfkdmgYKSCLQRLLS 451
Cdd:cd09096 154 RSEQGKDLLQNLQSFIEGA---KIP----------LIICGDFNAEPTEPV--------------------YKTFSNSSLN 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 452 NDTnefthSFKLASAYNEDIMPHTNYTFDFKG----IIDYIFYTKTGMVPLGLLGPVSNDWLRENKVvgcPHPHIPSDHF 527
Cdd:cd09096 201 LNS-----AYKLLSADGQSEPPYTTWKIRTSGecrhTLDYIFYSKDALSVEQLLDLPTEEQIGPNRL---PSFNYPSDHL 272


                ....*...
gi 24649583 528 PLLVELEL 535
Cdd:cd09096 273 SLVCDFSL 280
Deadenylase cd09082
C-terminal deadenylase domain of CCR4, nocturnin, and related domains; This family contains ...
 194-535 1.80e-22

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: 98.96  E-value: 1.80e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 194 VMCYNVLCDKYATRQMYGYCPSWALCWEYRKKSIIDEIRHYAADIISLQEIETEQFYHFFLPELKNDGYEGIFSPKSRAK 273
Cdd:cd09082   1 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 274 TMSELERKYVDGCAIFFRASKFTLIKESLIEFNQLAMANAEGSDNMLNRVMPKDN-IGLAALLKVKENAWEPMSEVTQIS 352
Cdd:cd09082  81 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNiGVAVVLEVHKELFGAGMKPIHAAD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 353 -QPLLVCTAHIHWDPEFCDVKLIQTMMLSNELKTIIdEASHSFRPGHKNDSNAVQLLLCGDFNSLPDSGVVEFLGKGRVS 431
Cdd:cd09082 161 kQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNIL-EKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVA 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 432 MDHldfkdmGYKSCLQRLLSNDTNEFTHSFKLASAYN-EDIMPHTNYTFDFKGII----------DYIFYTKTGMVPLGL 500
Cdd:cd09082 240 DNH------KDFKELRYNECLMNFSCNGKNGSSEGRItHGFQLKSAYENNLMPYTnytfdfkgviDYIFYSKTHMNVLGV 313

                       330       340       350
                ....*....|....*....|....*....|....*
gi 24649583 501 LGPVSNDWLRENKVVGCPHPHIPSDHFPLLVELEL 535
Cdd:cd09082 314 LGPLDPQWLVENNITGCPHPHIPSDHFSLLTQLEL 348
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
48-140 1.17e-19

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 91.53  E-value: 1.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  48 VRNISPSLWEFEHLTALYLNDNQLLRLPADVGMLTSLRTLDLSSNKLRSLPAELGELIQLRELLLNNNFLRVLPYEIGKL 127
Cdd:COG4886 125 LTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNL 204

                        90
                ....*....|...
gi 24649583 128 FHLVILGLMGNPL 140
Cdd:COG4886 205 TNLEELDLSGNQL 217
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
48-140 1.45e-19

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 91.15  E-value: 1.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  48 VRNISPSLWEFEHLTALYLNDNQLLRLPADVGMLTSLRTLDLSSNKLRSLPAELGELIQLRELLLNNNFLRVLPYEIGKL 127
Cdd:COG4886 148 LTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANL 227

                        90
                ....*....|...
gi 24649583 128 FHLVILGLMGNPL 140
Cdd:COG4886 228 TNLETLDLSNNQL 240
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
53-141 6.35e-18

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 86.14  E-value: 6.35e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  53 PSLWEFEHLTALYLNDNQLLRLPADVGMLTSLRTLDLSSNKLRSLPAELGELIQLRELLLNNNFLRVLPYEIGKLFHLVI 132
Cdd:COG4886 107 EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKE 186


                ....*....
gi 24649583 133 LGLMGNPLQ 141
Cdd:COG4886 187 LDLSNNQIT 195
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
48-140 3.04e-17

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 84.21  E-value: 3.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  48 VRNISPSLWEFEHLTALYLNDNQLLRLPADVGMLTSLRTLDLSSNKLRSLPAELGELIQLRELLLNNNFLRVLPyEIGKL 127
Cdd:COG4886 171 LTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNL 249

                        90
                ....*....|...
gi 24649583 128 FHLVILGLMGNPL 140
Cdd:COG4886 250 TNLEELDLSNNQL 262
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
 193-533 3.47e-13

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: 69.55  E-value: 3.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 193 TVMCYNVLCDkyatrqmygyCPSW-ALCWEYRKKSIIDEIRHYAADIISLQEIETEQfyhffLPELKN--DGYEGIFSPK 269
Cdd:cd09083   1 RVMTFNIRYD----------NPSDgENSWENRKDLVAELIKFYDPDIIGTQEALPHQ-----LADLEEllPEYDWIGVGR 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 270 SRAKTMSElerkyvdGCAIFFRASKFTLIKESliEF---NQLAMANAEGSDNMLNRvmpkdnIGLAALLKVKENAwepms 346
Cdd:cd09083  66 DDGKEKGE-------FSAIFYRKDRFELLDSG--TFwlsETPDVVGSKGWDAALPR------ICTWARFKDKKTG----- 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 347 evtqisQPLLVCTAHI-HWDPEfcdVKLIQTMMLSNELKTIIDEAShsfrpghkndsnavqLLLCGDFNSLPDSGVVEFL 425
Cdd:cd09083 126 ------KEFYVFNTHLdHVGEE---AREESAKLILERIKEIAGDLP---------------VILTGDFNAEPDSEPYKTL 181

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 426 gkgrvsmdhldfkdmgyksclqrllsndtneftHSFKLASAYNEDIMPHTN--YTF-DFKGI-----IDYIFYTKtGMVP 497
Cdd:cd09083 182 ---------------------------------TSGGLKDARDTAATTDGGpeGTFhGFKGPpggsrIDYIFVSP-GVKV 227

                       330       340       350
                ....*....|....*....|....*....|....*...
gi 24649583 498 L--GLLGPVSNDwlrenkvvgcphpHIPSDHFPLLVEL 533
Cdd:cd09083 228 LsyEILTDRYDG-------------RYPSDHFPVVADL 252
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
50-141 1.43e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 66.50  E-value: 1.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  50 NISPSLWEFEHLTALYLNDNQLLrlpadvGMLTSLRTLDLSSNKLRSLPAELGELIQLRELLLNNNFLRVLPYEIGKLFH 129
Cdd:COG4886  87 LGLTDLGDLTNLTELDLSGNEEL------SNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTN 160

                        90
                ....*....|..
gi 24649583 130 LVILGLMGNPLQ 141
Cdd:COG4886 161 LKSLDLSNNQLT 172
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
48-189 1.07e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 60.72  E-value: 1.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  48 VRNISPSLWEFEHLTALYLNDNQLLRLPaDVGMLTSLRTLDLSSNKLRSLPaELGELIQLRELLLNNNFLRVLPYE-IGK 126
Cdd:COG4886 217 LTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLTDLKLKeLEL 294

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24649583 127 LFHLVILGLMGNPLQKEFMNIYNEPNGTQKLLTYMLDNLSFTVNPPPQRPWLPLAKPNKTRPA 189
Cdd:COG4886 295 LLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLN 357
PLN03150 PLN03150
hypothetical protein; Provisional
 35-139 2.69e-09

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 59.83  E-value: 2.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583   35 KKTNWS----GLEITGcVRNISPSLW-EFEHLTALYLNDNQLL-RLPADVGMLTSLRTLDLSSNKLR-SLPAELGELIQL 107
Cdd:PLN03150 414 TKGKWFidglGLDNQG-LRGFIPNDIsKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSL 492

                         90       100       110
                 ....*....|....*....|....*....|....
gi 24649583  108 RELLLNNNFL--RVLPYEIGKLFHLVILGLMGNP 139
Cdd:PLN03150 493 RILNLNGNSLsgRVPAALGGRLLHRASFNFTDNA 526
MnuA_DNase1-like cd10283
Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a ...
 231-533 1.01e-08

Mycoplasma pulmonis MnuA nuclease-like; This subfamily includes Mycoplasma pulmonis MnuA, a membrane-associated nuclease related to Deoxyribonuclease 1 (DNase1 or DNase I, EC 3.1.21.1). The in vivo role of MnuA is as yet undetermined. 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: 197338 [Multi-domain]  Cd Length: 266  Bit Score: 56.64  E-value: 1.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 231 IRHYAADIISLQEIETEQFYH----FFLPEL--KNDGYEGIFSPKSRAKTMSElERkyvdgCAIFFRASKFTLIKESLIE 304
Cdd:cd10283  27 ISAFDLDLIALQEVMDNGGGLdalaKLVNELnkPGGTWKYIVSDKTGGSSGDK-ER-----YAFLYKSSKVRKVGKAVLE 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 305 fnqlamanaegsdnmlnrvmpKDNiglaallKVKENAWEPMS---EVTQISQPLLVCTAHIHWDPEfcdVKLIQTMMLSN 381
Cdd:cd10283 101 ---------------------KDS-------NTDGFARPPYAakfKSGGTGFDFTLVNVHLKSGGS---SKSGQGAKRVA 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 382 ELKTIIDEASHSfrpgHKNDSNAvQLLLCGDFNSLPDSGVVEFLGKgrvsmdhldfkdMGYKSclqrLLSNDTNEFTHSF 461
Cdd:cd10283 150 EAQALAEYLKEL----ADEDPDD-DVILLGDFNIPADEDAFKALTK------------AGFKS----LLPDSTNLSTSFK 208

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24649583 462 KLASAYnedimphtnytfdfkgiiDYIFYTKTGMVPLGLLG----PVSNDWLRENKVVGCPHPHIPSDHFPLLVEL 533
Cdd:cd10283 209 GYANSY------------------DNIFVSGNLKEKFSNSGvfdfNILVDEAGEEDLDYSKWRKQISDHDPVWVEF 266
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 195-324 4.29e-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: 4.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583   195 MCYNVLCDkyatrqmygycPSWALCWEYRKKSIIDEIRHYAADIISLQEIETEQFYHFFLPELKNDGYEGIFSPKsrakt 274
Cdd:pfam03372   1 LTWNVNGG-----------NADAAGDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFLSYGGPG----- 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 24649583   275 mselERKYVDGCAIFFRASKFTLIKESLIEFNQLAMANAEGSDNMLNRVM 324
Cdd:pfam03372  65 ----GGGGGGGVAILSRYPLSSVILVDLGEFGDPALRGAIAPFAGVLVVP 110
LRR_8 pfam13855
Leucine rich repeat;
60-115 7.33e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 46.36  E-value: 7.33e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 24649583    60 HLTALYLNDNQLLRLPADVGM-LTSLRTLDLSSNKLRSL-PAELGELIQLRELLLNNN 115
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGN 59
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
 194-533 3.04e-06

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: 48.83  E-value: 3.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 194 VMCYNVlcdkyatRQMYGYCpswalcWEYRKKSIIDEIRHYAADIISLQEIETEQFYHFFLPELKNDGYEGIFSPKSRAK 273
Cdd:cd09084   1 VMSYNV-------RSFNRYK------WKDDPDKILDFIKKQDPDILCLQEYYGSEGDKDDDLRLLLKGYPYYYVVYKSDS 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 274 TMSELerkyvdgcAIFfraSKFTLIKESLIEFnqlamanaEGSDNMLNR---VMPKDNIGL-------AALLKVKENAWE 343
Cdd:cd09084  68 GGTGL--------AIF---SKYPILNSGSIDF--------PNTNNNAIFadiRVGGDTIRVynvhlesFRITPSDKELYK 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 344 PMSEVTQISQPLLvctahihwdpefcdVKLIQTMML-SNELKTIIDEASHSFRPghkndsnavqLLLCGDFNSLPDSGVV 422
Cdd:cd09084 129 EEKKAKELSRNLL--------------RKLAEAFKRrAAQADLLAADIAASPYP----------VIVCGDFNDTPASYVY 184

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 423 EFLGKGrvsmdhldFKDmGYKSClqrllsndtnefthsfklASAYnedimphtNYTFDFKGI---IDYIFYTKtgmvplg 499
Cdd:cd09084 185 RTLKKG--------LTD-AFVEA------------------GSGF--------GYTFNGLFFplrIDYILTSK------- 222

                       330       340       350
                ....*....|....*....|....*....|....*
gi 24649583 500 llgpvsndwlrENKVVGC-PHPHIPSDHFPLLVEL 533
Cdd:cd09084 223 -----------GFKVLRYrVDPGKYSDHYPIVATL 246
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
7-140 5.30e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.78  E-value: 5.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583   7 KMSRNKDKYDSANRRQQIFLSQEDIAAGKKTNWSGLEITGCVRNISPSLWEFEHLTALYLNDNQLLRLPADVGMLTSLRT 86
Cdd:COG4886  21 LTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTE 100

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 24649583  87 LDLSSNKlrslpaELGELIQLRELLLNNNFLRVLPYEIGKLFHLVILGLMGNPL 140
Cdd:COG4886 101 LDLSGNE------ELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQL 148
PLN03150 PLN03150
hypothetical protein; Provisional
 39-140 5.79e-06

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 49.04  E-value: 5.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583   39 WSGLEitgCVRNISPSLWefeHLTALYLnDNQLLR--LPADVGMLTSLRTLDLSSNKLR-SLPAELGELIQLRELLLNNN 115
Cdd:PLN03150 404 WSGAD---CQFDSTKGKW---FIDGLGL-DNQGLRgfIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYN 476

                         90       100
                 ....*....|....*....|....*.
gi 24649583  116 FLR-VLPYEIGKLFHLVILGLMGNPL 140
Cdd:PLN03150 477 SFNgSIPESLGQLTSLRILNLNGNSL 502
LRR_8 pfam13855
Leucine rich repeat;
82-140 1.18e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.20  E-value: 1.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24649583    82 TSLRTLDLSSNKLRSLPAELGE-LIQLRELLLNNNFLRVL-PYEIGKLFHLVILGLMGNPL 140
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
59-114 1.65e-04

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 44.69  E-value: 1.65e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 24649583   59 EHLTALYLNDNQLLRLPADvgMLTSLRTLDLSSNKLRSLPAELGELIQLRELLLNN 114
Cdd:PRK15370 199 EQITTLILDNNELKSLPEN--LQGNIKTLYANSNQLTSIPATLPDTIQEMELSINR 252
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
178-535 1.79e-04

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 43.86  E-value: 1.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 178 LPLAKPNKTRPACI----FTVMCYNVL----CDKYATRQMYGYcPSWAlcwEYRKK--SIIDEIRHYAADIISLQEIET- 246
Cdd:COG2374  51 QPTETFVNPRPEAPvggdLRVATFNVEnlfdTDDDDDDFGRGA-DTPE---EYERKlaKIAAAIAALDADIVGLQEVENn 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 247 ----EQF----------YHFFLPELKNDGyegifspksraktmselerkyvDG--CAIFFRASKFTLIKESLIEfnqlAM 310
Cdd:COG2374 127 gsalQDLvaalnlaggtYAFVHPPDGPDG----------------------DGirVALLYRPDRVTLVGSATIA----DL 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 311 ANAEGSDNMLNRVmPkdnigLAALLKVKENawEPMSevtqisqpLLVCtahiHW---------DPEFCDvkLIQTMMLSN 381
Cdd:COG2374 181 PDSPGNPDRFSRP-P-----LAVTFELANG--EPFT--------VIVN----HFkskgsddpgDGQGAS--EAKRTAQAE 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 382 ELKTIIDEashsfRPGHKNDSNavqLLLCGDFNSLPDSgvveflgkgrVSMDHLdFKDMGYKSCLQRLLSNDTneFTHSF 461
Cdd:COG2374 239 ALRAFVDS-----LLAADPDAP---VIVLGDFNDYPFE----------DPLRAL-LGAGGLTNLAEKLPAAER--YSYVY 297

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583 462 KlasaynedimphtnytfDFKGIIDYIFYTK------TGMVPLGLLGPVSNDWLRENKVVGCPHPHIPSDHFPLLVELEL 535
Cdd:COG2374 298 D-----------------GNSGLLDHILVSPalaarvTGADIWHINADIYNDDFKPDFRTYADDPGRASDHDPVVVGLRL 360
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 51-143 5.67e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 42.91  E-value: 5.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583   51 ISPSLWEFEHLTALYLNDNQLL-RLPADVGMLTSLRTLDLSSNklrSLPAELGEL-IQLREL----LLNNNFLRVLPYEI 124
Cdd:PLN00113 252 IPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDN---SLSGEIPELvIQLQNLeilhLFSNNFTGKIPVAL 328

                         90
                 ....*....|....*....
gi 24649583  125 GKLFHLVILGLMGNPLQKE 143
Cdd:PLN00113 329 TSLPRLQVLQLWSNKFSGE 347
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 60-142 6.12e-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: 41.31  E-value: 6.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583  60 HLTALYLNDNQLL-----------------------------------------RLPADVGML----------TSLRTLD 88
Cdd:cd21340  47 NLTHLYLQNNQIEkienlenlvnlkklylggnrisvveglenltnleelhienqRLPPGEKLTfdprslaalsNSLRVLN 126

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24649583  89 LSSNKLRSLpAELGELIQLRELLLNNNFLR---VLPYEIGKLFHLVILGLMGNPLQK 142
Cdd:cd21340 127 ISGNNIDSL-EPLAPLRNLEQLDASNNQISdleELLDLLSSWPSLRELDLTGNPVCK 182
LRR_TYP smart00369
Leucine-rich repeats, typical (most populated) subfamily;
81-101 8.70e-04

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


Pssm-ID: 197687 [Multi-domain]  Cd Length: 24  Bit Score: 36.56  E-value: 8.70e-04
                           10        20
                   ....*....|....*....|.
gi 24649583     81 LTSLRTLDLSSNKLRSLPAEL 101
Cdd:smart00369   1 LPNLRELDLSNNQLSSLPPGA 21
LRR smart00370
Leucine-rich repeats, outliers;
81-101 8.70e-04

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 36.56  E-value: 8.70e-04
                           10        20
                   ....*....|....*....|.
gi 24649583     81 LTSLRTLDLSSNKLRSLPAEL 101
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGA 21
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 37-143 1.40e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 41.76  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583   37 TNWSGLEITGCVRN-----ISPSLWEFEHLTALYLNDNQLL-RLPADVGMLTSLRTLDLSSNKLR-SLPAELGELIQLRE 109
Cdd:PLN00113 185 TNLTSLEFLTLASNqlvgqIPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQY 264

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 24649583  110 LLLNNNFLR-VLPYEIGKLFHLVILGLMGNPLQKE 143
Cdd:PLN00113 265 LFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSGE 299
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 58-120 1.86e-03

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: 39.77  E-value: 1.86e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24649583  58 FEHLTALYLNDNQLLRLPaDVGMLTSLRTLDLSSNKLRSLPaELGELIQLRELLLNNNFLRVL 120
Cdd:cd21340  23 CKNLKVLYLYDNKITKIE-NLEFLTNLTHLYLQNNQIEKIE-NLENLVNLKKLYLGGNRISVV 83
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 82-118 2.31e-03

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


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 36.07  E-value: 2.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 24649583    82 TSLRTLDLSSNKLRSLPAeLGELIQLREL-LLNNNFLR 118
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPP-LAKLPNLETLdLSGNNKIT 37
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 61-143 2.60e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 40.60  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583   61 LTALYLNDNQLL-RLPADVGMLTSLRTLDLSSNKLRS-LPAELGELIQLRELLL-NNNFLRVLPYEIGKLFHLVILGLMG 137
Cdd:PLN00113 142 LETLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVGkIPNSLTNLTSLEFLTLaSNQLVGQIPRELGQMKSLKWIYLGY 221


                 ....*.
gi 24649583  138 NPLQKE 143
Cdd:PLN00113 222 NNLSGE 227
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 61-138 2.68e-03

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: 39.38  E-value: 2.68e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24649583  61 LTALYLNDNQLLRLPaDVGMLTSLRTLDLSSNKLRSLPAeLGELIQLRELLLNNNFLRVLPYeIGKLFHLVILGLMGN 138
Cdd:cd21340   4 ITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIEN-LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLGGN 78
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 40-140 3.11e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 40.60  E-value: 3.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583   40 SGLEITGcvrNISPSLWEFEHLTALYLNDNQLL-RLPADV-----------------------GMLTSLRTLDLSSNKLR 95
Cdd:PLN00113  77 SGKNISG---KISSAIFRLPYIQTINLSNNQLSgPIPDDIfttssslrylnlsnnnftgsiprGSIPNLETLDLSNNMLS 153

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 24649583   96 -SLPAELGELIQLRELLLNNNFLR-VLPYEIGKLFHLVILGLMGNPL 140
Cdd:PLN00113 154 gEIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQL 200
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 485-535 4.52e-03

Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function prediction only];


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 38.35  E-value: 4.52e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24649583 485 IDYIFytktgmvplgllgpVSNDW-LRENKVVGCPHPHIPSDHFPLLVELEL 535
Cdd:COG3568 129 IDYIL--------------VSPGLrVLSAEVLDSPLGRAASDHLPVVADLEL 166
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 51-143 5.34e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 39.83  E-value: 5.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649583   51 ISPSLWEFEHLTALYLNDNQLL-RLPADVGMLTSLRTLDLSSNKLR-SLPAELGELIQLREL-LLNNNFLRVLPYEIGKL 127
Cdd:PLN00113 276 IPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNNFTgKIPVALTSLPRLQVLqLWSNKFSGEIPKNLGKH 355

                         90
                 ....*....|....*.
gi 24649583  128 FHLVILGLMGNPLQKE 143
Cdd:PLN00113 356 NNLTVLDLSTNNLTGE 371
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH