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Conserved domains on  [gi|47059015|ref|NP_997649|]
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CCR4-NOT transcription complex subunit 6 isoform 2 [Mus musculus]

Protein Classification

LRR and EEP domain-containing protein( domain architecture ID 11469477)

LRR and EEP domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EEP super family cl00490
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 186-535 0e+00

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.


The actual alignment was detected with superfamily member cd10313:

Pssm-ID: 469791  Cd Length: 350  Bit Score: 737.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 186 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 265
Cdd:cd10313   1 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIMQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 266 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAVLLELRKELIEMSSGKPHLGT 345
Cdd:cd10313  81 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAVLLELRKELIEMSSGKPHLGM 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 346 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASRSLKSSVLGECGTIPLVLCADLNSLPDSGVVEYLSTGGV 425
Cdd:cd10313 161 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASRSLKSSVLGETGTIPLVLCADLNSLPDSGVVEYLSTGGV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 426 ETNHKDFKELRYNESLTNFSCNGKNGMTNGRITHGFKLKSAYENGLMPYTNYTFDFKGIIDYIFYSKPQLNTLAILGPLD 505
Cdd:cd10313 241 ETNHKDFKELRYNESLTNFSCNGKNGTTNGRITHGFKLKSAYENGLMPYTNYTFDFKGIIDYIFYSKPQLNTLGILGPLD 320

                       330       340       350
                ....*....|....*....|....*....|
gi 47059015 506 HHWLVENNISGCPHPLIPSDHFSLFAQLEL 535
Cdd:cd10313 321 HHWLVENNISGCPHPLIPSDHFSLFAQLEL 350
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-133 3.55e-22

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 98.85  E-value: 3.55e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  51 THLTALHLSDNSLSCIPSDIAKLHNLVYLDLSHNQIQSLPAELGNMVSLRELHLNYNQLRVLPFELGKLFQLQTLSLKGN 130
Cdd:COG4886 136 TNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGN 215


                ...
gi 47059015 131 PLT 133
Cdd:COG4886 216 QLT 218
 
Name Accession Description Interval E-value
Deadenylase_CCR4a cd10313
C-terminal deadenylase domain of CCR4a, also known as CCR4-NOT transcription complex subunit 6; ...
 186-535 0e+00

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


Pssm-ID: 197340  Cd Length: 350  Bit Score: 737.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 186 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 265
Cdd:cd10313   1 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIMQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 266 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAVLLELRKELIEMSSGKPHLGT 345
Cdd:cd10313  81 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAVLLELRKELIEMSSGKPHLGM 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 346 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASRSLKSSVLGECGTIPLVLCADLNSLPDSGVVEYLSTGGV 425
Cdd:cd10313 161 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASRSLKSSVLGETGTIPLVLCADLNSLPDSGVVEYLSTGGV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 426 ETNHKDFKELRYNESLTNFSCNGKNGMTNGRITHGFKLKSAYENGLMPYTNYTFDFKGIIDYIFYSKPQLNTLAILGPLD 505
Cdd:cd10313 241 ETNHKDFKELRYNESLTNFSCNGKNGTTNGRITHGFKLKSAYENGLMPYTNYTFDFKGIIDYIFYSKPQLNTLGILGPLD 320

                       330       340       350
                ....*....|....*....|....*....|
gi 47059015 506 HHWLVENNISGCPHPLIPSDHFSLFAQLEL 535
Cdd:cd10313 321 HHWLVENNISGCPHPLIPSDHFSLFAQLEL 350
PLN03144 PLN03144
Carbon catabolite repressor protein 4 homolog; Provisional
 164-532 6.33e-73

Carbon catabolite repressor protein 4 homolog; Provisional


Pssm-ID: 178689 [Multi-domain]  Cd Length: 606  Bit Score: 243.87  E-value: 6.33e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  164 PPPRSWIMLQEPDRTRPTAL---------FSVMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIIQEILSCNADIISLQ 234
Cdd:PLN03144 226 PTPRRLIQVNGLDGMGHLDLdgrtssagtFTVLSYNILSDLYATSDMYSYCPPWALSWTYRRQNLLREIVGYRADILCLQ 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  235 EVETEQYYSFFLVELKERGYNGFFspKSRARTMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEG------S 308
Cdd:PLN03144 306 EVQSDHFEEFFAPELDKHGYQALY--KKKTTEVYTGNTYVIDGCATFFRRDRFSLVKKYEVEFNKAAQSLTEAlipsaqK 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  309 EAMLNRVMtKDNIGVAVLLELRkelieMSSGKPHLGTEKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASrs 388
Cdd:PLN03144 384 KAALNRLL-KDNVALIVVLEAK-----FGNQGADNGGKRQLLCVANTHIHANQELKDVKLWQVHTLLKGLEKIAASAD-- 455

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  389 lkssvlgecgtIPLVLCADLNSLPDSGVVEYLSTGGVETNHKD-----FKELRYNESLtnfscngkngmtngriTHGFKL 463
Cdd:PLN03144 456 -----------IPMLVCGDFNSVPGSAPHCLLATGKVDPLHPDlavdpLGILRPASKL----------------THQLPL 508

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  464 KSAYEN-GLMP---------------------YTNYTFDFKGIIDYIFYSKPQLNTLAILGPLDHHWLVENniSGCPHPL 521
Cdd:PLN03144 509 VSAYSSfARMPgsgsgleqqrrrmdpatneplFTNCTRDFIGTLDYIFYTADSLTVESLLELLDEESLRKD--TALPSPE 586

                        410
                 ....*....|.
gi 47059015  522 IPSDHFSLFAQ 532
Cdd:PLN03144 587 WSSDHIALLAE 597
CCR4 COG5239
mRNA deadenylase, 3'-5' endonuclease subunit Ccr4 [RNA processing and modification];
171-534 1.92e-66

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


Pssm-ID: 227564 [Multi-domain]  Cd Length: 378  Bit Score: 220.41  E-value: 1.92e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 171 MLQEPDRTRPTALFSVMCYNVLCDKYATRQLYGYCpSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELK 250
Cdd:COG5239  18 FLSIGHYAEKDTDFTIMTYNVLAQTYATRKMYPYS-GWALKWSYRSRLLLQELLYYNADILCLQEVDAEDFEDFWKDQLG 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 251 ERGYNGFFSPKSR-ARTMSEQERKHVDGCAIFFKTE----KFTLVQKHTVEFNQLAMANSE--GSEAMLNRVMTKDNIGV 323
Cdd:COG5239  97 KLGYDGIFIPKERkVKWMIDYDTTKVDGCAIFLKRFidssKLGLILAVTHLFWHPYGYYERfrQTYILLNRIGEKDNIAW 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 324 AVLLELrkeLIEMSSGKPhlgtekqlILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDK--ASRSLKSSVLGEcGTIP 401
Cdd:COG5239 177 VCLFVG---LFNKEPGDT--------PYVANTHLPWDPKYRDVKLIQCSLLYRELKKVLKEelNDDKEEGDIKSY-PEVD 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 402 LVLCADLNSLPDSGVVEYLSTGGVEtNHKDFKELRYNEsltnfscngkngMTNGR-ITHGFKLKSAYENGLMPYTNYTFD 480
Cdd:COG5239 245 ILITGDFNSLRASLVYKFLVTSQIQ-LHESLNGRDFSL------------YSVGYkFVHPENLKSDNSKGELGFTNWTPG 311

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 47059015 481 FKGIIDYIFYSKPQLNTLA-ILGPLDHHWLVenNISGCPHPLIPSDHFSLFAQLE 534
Cdd:COG5239 312 FKGVIDYIFYHGGLLTRQTgLLGVVEGEYAS--KVIGLPNMPFPSDHIPLLAEFA 364
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-133 3.55e-22

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 98.85  E-value: 3.55e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  51 THLTALHLSDNSLSCIPSDIAKLHNLVYLDLSHNQIQSLPAELGNMVSLRELHLNYNQLRVLPFELGKLFQLQTLSLKGN 130
Cdd:COG4886 136 TNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGN 215


                ...
gi 47059015 131 PLT 133
Cdd:COG4886 216 QLT 218
PLN03150 PLN03150
hypothetical protein; Provisional
 66-133 4.03e-10

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 62.53  E-value: 4.03e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015   66 IPSDIAKLHNLVYLDLSHNQIQ-SLPAELGNMVSLRELHLNYNQLR-VLPFELGKLFQLQTLSLKGNPLT 133
Cdd:PLN03150 434 IPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLS 503
LRR_8 pfam13855
Leucine rich repeat;
51-109 3.52e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 52.91  E-value: 3.52e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47059015    51 THLTALHLSDNSLSCIPSDIAK-LHNLVYLDLSHNQIQSL-PAELGNMVSLRELHLNYNQL 109
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 51-135 5.30e-09

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 56.72  E-value: 5.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  51 THLTALHLSDNSLSCIPsDIAKLHNLVYLDLSHNQIQSLPaELGNMVSLRELHLNYNQLRVLpfE-LGKLFQLQTLSL-- 127
Cdd:cd21340  24 KNLKVLYLYDNKITKIE-NLEFLTNLTHLYLQNNQIEKIE-NLENLVNLKKLYLGGNRISVV--EgLENLTNLEELHIen 99

                        90
                ....*....|..
gi 47059015 128 ----KGNPLTQD 135
Cdd:cd21340 100 qrlpPGEKLTFD 111
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 187-303 1.55e-07

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


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 51.84  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015   187 MCYNVLCDkyatrqlygycPSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKsrart 266
Cdd:pfam03372   1 LTWNVNGG-----------NADAAGDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFLSYGGPG----- 64

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 47059015   267 mseqERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMA 303
Cdd:pfam03372  65 ----GGGGGGGVAILSRYPLSSVILVDLGEFGDPALR 97
 
Name Accession Description Interval E-value
Deadenylase_CCR4a cd10313
C-terminal deadenylase domain of CCR4a, also known as CCR4-NOT transcription complex subunit 6; ...
 186-535 0e+00

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


Pssm-ID: 197340  Cd Length: 350  Bit Score: 737.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 186 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 265
Cdd:cd10313   1 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIMQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 266 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAVLLELRKELIEMSSGKPHLGT 345
Cdd:cd10313  81 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAVLLELRKELIEMSSGKPHLGM 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 346 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASRSLKSSVLGECGTIPLVLCADLNSLPDSGVVEYLSTGGV 425
Cdd:cd10313 161 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASRSLKSSVLGETGTIPLVLCADLNSLPDSGVVEYLSTGGV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 426 ETNHKDFKELRYNESLTNFSCNGKNGMTNGRITHGFKLKSAYENGLMPYTNYTFDFKGIIDYIFYSKPQLNTLAILGPLD 505
Cdd:cd10313 241 ETNHKDFKELRYNESLTNFSCNGKNGTTNGRITHGFKLKSAYENGLMPYTNYTFDFKGIIDYIFYSKPQLNTLGILGPLD 320

                       330       340       350
                ....*....|....*....|....*....|
gi 47059015 506 HHWLVENNISGCPHPLIPSDHFSLFAQLEL 535
Cdd:cd10313 321 HHWLVENNISGCPHPLIPSDHFSLFAQLEL 350
Deadenylase_CCR4b cd10312
C-terminal deadenylase domain of CCR4b, also known as CCR4-NOT transcription complex subunit ...
 186-535 0e+00

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


Pssm-ID: 197339  Cd Length: 348  Bit Score: 675.58  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 186 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 265
Cdd:cd10312   1 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 266 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAVLLELRKELIEmSSGKPHLGT 345
Cdd:cd10312  81 IMSEQERKHVDGCAIFFKTEKFSLVQKHTVEFNQVAMANSEGSEAMLNRVMTKDNIGVAVVLEVHKELFG-AGMKPIHAA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 346 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASRSLkSSVLGECGTIPLVLCADLNSLPDSGVVEYLSTGGV 425
Cdd:cd10312 160 DKQLLIVANAHMHWDPEYSDVKLIQTMMFVSELKNILEKASSRP-GSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGV 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 426 ETNHKDFKELRYNESLTNFSCNGKNGMTNGRITHGFKLKSAYENGLMPYTNYTFDFKGIIDYIFYSKPQLNTLAILGPLD 505
Cdd:cd10312 239 ADNHKDFKELRYNECLMNFSCNGKNGSSEGRITHGFQLKSAYENNLMPYTNYTFDFKGVIDYIFYSKTHMNVLGVLGPLD 318

                       330       340       350
                ....*....|....*....|....*....|
gi 47059015 506 HHWLVENNISGCPHPLIPSDHFSLFAQLEL 535
Cdd:cd10312 319 PQWLVENNITGCPHPHIPSDHFSLLTQLEL 348
Deadenylase_CCR4 cd09097
C-terminal deadenylase domain of CCR4 and related domains; This subfamily contains the ...
 186-535 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: 573.48  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 186 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 265
Cdd:cd09097   1 VMCYNVLCDKYATRQQYGYCPSWALNWDYRKQNILKEILSYNADILCLQEVETDQYEDFFLPELKQHGYDGVFKPKSRAK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 266 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMAN--SEGSEAMLNRVMTKDNIGVAVLLELRKELIEmssgkphl 343
Cdd:cd09097  81 TMSEAERKHVDGCAIFFKTSKFKLVEKHLIEFNQLAMANadAEGSEDMLNRVMTKDNIALIVVLEARETSYE-------- 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 344 GTEKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASRslksSVLGECGTIPLVLCADLNSLPDSGVVEYLSTG 423
Cdd:cd09097 153 GNKGQLLIVANTHIHWDPEFSDVKLVQTMMLLEELEKIAEKFSR----YPYEDSADIPLVVCGDFNSLPDSGVYELLSNG 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 424 GVETNHKDFKELRYNESLtnfscngkngmTNGRITHGFKLKSAYEN-GLMPYTNYTFDFKGIIDYIFYSKPQLNTLAILG 502
Cdd:cd09097 229 SVSPNHPDFKEDPYGEYL-----------TASGLTHSFKLKSAYANlGELPFTNYTPDFKGVIDYIFYSADTLSVLGLLG 297

                       330       340       350
                ....*....|....*....|....*....|...
gi 47059015 503 PLDHHWlVENNISGCPHPLIPSDHFSLFAQLEL 535
Cdd:cd09097 298 PPDEDW-YLNKVVGLPNPHFPSDHIALLAEFRI 329
PLN03144 PLN03144
Carbon catabolite repressor protein 4 homolog; Provisional
 164-532 6.33e-73

Carbon catabolite repressor protein 4 homolog; Provisional


Pssm-ID: 178689 [Multi-domain]  Cd Length: 606  Bit Score: 243.87  E-value: 6.33e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  164 PPPRSWIMLQEPDRTRPTAL---------FSVMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIIQEILSCNADIISLQ 234
Cdd:PLN03144 226 PTPRRLIQVNGLDGMGHLDLdgrtssagtFTVLSYNILSDLYATSDMYSYCPPWALSWTYRRQNLLREIVGYRADILCLQ 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  235 EVETEQYYSFFLVELKERGYNGFFspKSRARTMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEG------S 308
Cdd:PLN03144 306 EVQSDHFEEFFAPELDKHGYQALY--KKKTTEVYTGNTYVIDGCATFFRRDRFSLVKKYEVEFNKAAQSLTEAlipsaqK 383

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  309 EAMLNRVMtKDNIGVAVLLELRkelieMSSGKPHLGTEKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASrs 388
Cdd:PLN03144 384 KAALNRLL-KDNVALIVVLEAK-----FGNQGADNGGKRQLLCVANTHIHANQELKDVKLWQVHTLLKGLEKIAASAD-- 455

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  389 lkssvlgecgtIPLVLCADLNSLPDSGVVEYLSTGGVETNHKD-----FKELRYNESLtnfscngkngmtngriTHGFKL 463
Cdd:PLN03144 456 -----------IPMLVCGDFNSVPGSAPHCLLATGKVDPLHPDlavdpLGILRPASKL----------------THQLPL 508

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  464 KSAYEN-GLMP---------------------YTNYTFDFKGIIDYIFYSKPQLNTLAILGPLDHHWLVENniSGCPHPL 521
Cdd:PLN03144 509 VSAYSSfARMPgsgsgleqqrrrmdpatneplFTNCTRDFIGTLDYIFYTADSLTVESLLELLDEESLRKD--TALPSPE 586

                        410
                 ....*....|.
gi 47059015  522 IPSDHFSLFAQ 532
Cdd:PLN03144 587 WSSDHIALLAE 597
CCR4 COG5239
mRNA deadenylase, 3'-5' endonuclease subunit Ccr4 [RNA processing and modification];
171-534 1.92e-66

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


Pssm-ID: 227564 [Multi-domain]  Cd Length: 378  Bit Score: 220.41  E-value: 1.92e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 171 MLQEPDRTRPTALFSVMCYNVLCDKYATRQLYGYCpSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELK 250
Cdd:COG5239  18 FLSIGHYAEKDTDFTIMTYNVLAQTYATRKMYPYS-GWALKWSYRSRLLLQELLYYNADILCLQEVDAEDFEDFWKDQLG 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 251 ERGYNGFFSPKSR-ARTMSEQERKHVDGCAIFFKTE----KFTLVQKHTVEFNQLAMANSE--GSEAMLNRVMTKDNIGV 323
Cdd:COG5239  97 KLGYDGIFIPKERkVKWMIDYDTTKVDGCAIFLKRFidssKLGLILAVTHLFWHPYGYYERfrQTYILLNRIGEKDNIAW 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 324 AVLLELrkeLIEMSSGKPhlgtekqlILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDK--ASRSLKSSVLGEcGTIP 401
Cdd:COG5239 177 VCLFVG---LFNKEPGDT--------PYVANTHLPWDPKYRDVKLIQCSLLYRELKKVLKEelNDDKEEGDIKSY-PEVD 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 402 LVLCADLNSLPDSGVVEYLSTGGVEtNHKDFKELRYNEsltnfscngkngMTNGR-ITHGFKLKSAYENGLMPYTNYTFD 480
Cdd:COG5239 245 ILITGDFNSLRASLVYKFLVTSQIQ-LHESLNGRDFSL------------YSVGYkFVHPENLKSDNSKGELGFTNWTPG 311

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 47059015 481 FKGIIDYIFYSKPQLNTLA-ILGPLDHHWLVenNISGCPHPLIPSDHFSLFAQLE 534
Cdd:COG5239 312 FKGVIDYIFYHGGLLTRQTgLLGVVEGEYAS--KVIGLPNMPFPSDHIPLLAEFA 364
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 186-533 4.62e-42

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


Pssm-ID: 197306 [Multi-domain]  Cd Length: 241  Bit Score: 151.09  E-value: 4.62e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 186 VMCYNVLCDKYATRqlygycpswalnwdyrKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRar 265
Cdd:cd08372   1 VASYNVNGLNAATR----------------ASGIARWVRELDPDIVCLQEVKDSQYSAVALNQLLPEGYHQYQSGPSR-- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 266 tmseqeRKHVDGCAIFFKTEKFTLVQKHTVEFNQlamansegseamlnrVMTKDNIGVAVllelrkeliemssgkpHLGT 345
Cdd:cd08372  63 ------KEGYEGVAILSKTPKFKIVEKHQYKFGE---------------GDSGERRAVVV----------------KFDV 105

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 346 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASrslkssvlgecgtIPLVLCADLNSLPDSGVVEYLStggv 425
Cdd:cd08372 106 HDKELCVVNAHLQAGGTRADVRDAQLKEVLEFLKRLRQPNS-------------APVVICGDFNVRPSEVDSENPS---- 168

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 426 etnhkdfkelrynesltnfscngkngmTNGRITHGFKLKSAYENGLMPYTNYTF--DFKGIIDYIFYSKPqlntlaiLGP 503
Cdd:cd08372 169 ---------------------------SMLRLFVALNLVDSFETLPHAYTFDTYmhNVKSRLDYIFVSKS-------LLP 214

                       330       340       350
                ....*....|....*....|....*....|
gi 47059015 504 LDHHWLVennISGCPHPLIPSDHFSLFAQL 533
Cdd:cd08372 215 SVKSSKI---LSDAARARIPSDHYPIEVTL 241
Deadenylase_nocturnin cd09096
C-terminal deadenylase domain of nocturnin and related domains; This subfamily contains the ...
 205-535 3.07e-26

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


Pssm-ID: 197330 [Multi-domain]  Cd Length: 280  Bit Score: 108.28  E-value: 3.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 205 CPSWALNWDYRKKAIIQEILSCNADIISLQEVetEQYYSFFLVELKERGYNGFFSPKSRARTMSEQERKHVDGCAIFFKT 284
Cdd:cd09096  22 CPCEALKWEERKYLILEEILTYDPDILCLQEV--DHYKDTLQPLLSRLGYQGTFFPKPDSPCLYIENNNGPDGCALFFRK 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 285 EKFTLVqkhtvefnqlamaNSEGseAMLNRVMTKDNiGVAVLLELRKELiemsSGKPhlgtekqlILVANAHMHWDPEYS 364
Cdd:cd09096 100 DRFELV-------------NTEK--IRLSAMTLKTN-QVAIACTLRCKE----TGRE--------ICLAVTHLKARTGWE 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 365 DVKLVQTMMFLSEVKNIIdkasrslkssvlgECGTIPLVLCADLNSLPDSGVveylstggvetnhkdfkelrYNEsLTNF 444
Cdd:cd09096 152 RLRSEQGKDLLQNLQSFI-------------EGAKIPLIICGDFNAEPTEPV--------------------YKT-FSNS 197

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 445 SCNgkngmtngrITHGFKLKSAYENGLMPYTNYTFDFKG----IIDYIFYSKPQLNTLAILGpldhhWLVENNI--SGCP 518
Cdd:cd09096 198 SLN---------LNSAYKLLSADGQSEPPYTTWKIRTSGecrhTLDYIFYSKDALSVEQLLD-----LPTEEQIgpNRLP 263

                       330
                ....*....|....*..
gi 47059015 519 HPLIPSDHFSLFAQLEL 535
Cdd:cd09096 264 SFNYPSDHLSLVCDFSL 280
Deadenylase cd09082
C-terminal deadenylase domain of CCR4, nocturnin, and related domains; This family contains ...
 186-529 2.87e-23

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


Pssm-ID: 197316 [Multi-domain]  Cd Length: 348  Bit Score: 101.27  E-value: 2.87e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 186 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 265
Cdd:cd09082   1 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 266 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDN-IGVAVLLELrKELIEMSSGKPHLG 344
Cdd:cd09082  81 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNiGVAVVLEVH-KELFGAGMKPIHAA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 345 TEKQLILvANAHMHWDPEYSDVKLVQTMMFLSEVKNIIdKASRSLKSSVLGECGTIPLVLCADLNSLPDSGVVEYLSTgg 424
Cdd:cd09082 160 DKQLLIV-ANAHMHWDPEYSDVKLIQTMMFVSEVKNIL-EKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSN-- 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 425 vetnhkdfKELRYNESLTNFSCNGKNGMTNGRITHGFKLKSAYENGLMPYTNYTFDFKGII----------DYIFYSKPQ 494
Cdd:cd09082 236 --------GGVADNHKDFKELRYNECLMNFSCNGKNGSSEGRITHGFQLKSAYENNLMPYTnytfdfkgviDYIFYSKTH 307

                       330       340       350
                ....*....|....*....|....*....|....*
gi 47059015 495 LNTLAILGPLDHHWLVENNISGCPHPLIPSDHFSL 529
Cdd:cd09082 308 MNVLGVLGPLDPQWLVENNITGCPHPHIPSDHFSL 342
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-133 3.55e-22

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 98.85  E-value: 3.55e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  51 THLTALHLSDNSLSCIPSDIAKLHNLVYLDLSHNQIQSLPAELGNMVSLRELHLNYNQLRVLPFELGKLFQLQTLSLKGN 130
Cdd:COG4886 136 TNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGN 215


                ...
gi 47059015 131 PLT 133
Cdd:COG4886 216 QLT 218
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-133 1.20e-21

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 97.31  E-value: 1.20e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  51 THLTALHLSDNSLSCIPSDIAKLHNLVYLDLSHNQIQSLPAELGNMVSLRELHLNYNQLRVLPFELGKLFQLQTLSLKGN 130
Cdd:COG4886 159 TNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNN 238


                ...
gi 47059015 131 PLT 133
Cdd:COG4886 239 QLT 241
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-133 6.38e-21

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 95.39  E-value: 6.38e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  51 THLTALHLSDNSLSCIPSDIAKLHNLVYLDLSHNQIQSLPAELGNMVSLRELHLNYNQLRVLPFELGKLFQLQTLSLKGN 130
Cdd:COG4886 113 TNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNN 192


                ...
gi 47059015 131 PLT 133
Cdd:COG4886 193 QIT 195
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
 185-533 7.31e-20

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


Pssm-ID: 197317 [Multi-domain]  Cd Length: 252  Bit Score: 89.20  E-value: 7.31e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 185 SVMCYNVLCDkyatrqlygyCPSWALN-WDYRKKAIIQEILSCNADIISLQEVETEQyysffLVELKER--GYNGFfspk 261
Cdd:cd09083   1 RVMTFNIRYD----------NPSDGENsWENRKDLVAELIKFYDPDIIGTQEALPHQ-----LADLEELlpEYDWI---- 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 262 SRARTMSEQERKHvdgCAIFFKTEKFTLVQKHTveF---NQLAMANSEGSEAMLNRVMTkdnigvAVLLELRKeliemsS 338
Cdd:cd09083  62 GVGRDDGKEKGEF---SAIFYRKDRFELLDSGT--FwlsETPDVVGSKGWDAALPRICT------WARFKDKK------T 124

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 339 GKPhlgtekqlILVANAHMhwDPEYSDVKLVQTMMFLSEVKNIidkasrslkssvlgeCGTIPLVLCADLNSLPDSGVVE 418
Cdd:cd09083 125 GKE--------FYVFNTHL--DHVGEEAREESAKLILERIKEI---------------AGDLPVILTGDFNAEPDSEPYK 179

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 419 YLSTGGvetnhkdfkelrynesltnfscngkngmtngrithgfkLKSAYENGLMPYTN--YTF-DFKGI-----IDYIFY 490
Cdd:cd09083 180 TLTSGG--------------------------------------LKDARDTAATTDGGpeGTFhGFKGPpggsrIDYIFV 221

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 47059015 491 SKPqlntlaiLGPLDHHwLVENNISGCphplIPSDHFSLFAQL 533
Cdd:cd09083 222 SPG-------VKVLSYE-ILTDRYDGR----YPSDHFPVVADL 252
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-163 1.77e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 66.11  E-value: 1.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  51 THLTALHLSDNSLSCIPSdIAKLHNLVYLDLSHNQIQSLPaELGNMVSLRELHLNYNQLRVLPFE-LGKLFQLQTLSLKG 129
Cdd:COG4886 228 TNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLTDLKLKeLELLLGLNSLLLLL 305

                        90       100       110
                ....*....|....*....|....*....|....
gi 47059015 130 NPLTQDILNLCLEPDGTRRLLNYLLDNLSVSTEQ 163
Cdd:COG4886 306 LLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTT 339
PLN03150 PLN03150
hypothetical protein; Provisional
 66-133 4.03e-10

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 62.53  E-value: 4.03e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015   66 IPSDIAKLHNLVYLDLSHNQIQ-SLPAELGNMVSLRELHLNYNQLR-VLPFELGKLFQLQTLSLKGNPLT 133
Cdd:PLN03150 434 IPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLS 503
LRR_8 pfam13855
Leucine rich repeat;
51-109 3.52e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 52.91  E-value: 3.52e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47059015    51 THLTALHLSDNSLSCIPSDIAK-LHNLVYLDLSHNQIQSL-PAELGNMVSLRELHLNYNQL 109
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 51-135 5.30e-09

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 56.72  E-value: 5.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  51 THLTALHLSDNSLSCIPsDIAKLHNLVYLDLSHNQIQSLPaELGNMVSLRELHLNYNQLRVLpfE-LGKLFQLQTLSL-- 127
Cdd:cd21340  24 KNLKVLYLYDNKITKIE-NLEFLTNLTHLYLQNNQIEKIE-NLENLVNLKKLYLGGNRISVV--EgLENLTNLEELHIen 99

                        90
                ....*....|..
gi 47059015 128 ----KGNPLTQD 135
Cdd:cd21340 100 qrlpPGEKLTFD 111
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
16-134 1.61e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 56.87  E-value: 1.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  16 TIMSSEEAANGKKSHWAELEISGKVRSLSSSLWSLTHLTALHLSDNSLSCIPSDIAKLHNLVYLDLSHNQiqslpaELGN 95
Cdd:COG4886  38 LLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE------ELSN 111

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 47059015  96 MVSLRELHLNYNQLRVLPFELGKLFQLQTLSLKGNPLTQ 134
Cdd:COG4886 112 LTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTD 150
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 187-303 1.55e-07

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


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 51.84  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015   187 MCYNVLCDkyatrqlygycPSWALNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKsrart 266
Cdd:pfam03372   1 LTWNVNGG-----------NADAAGDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFLSYGGPG----- 64

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 47059015   267 mseqERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMA 303
Cdd:pfam03372  65 ----GGGGGGGVAILSRYPLSSVILVDLGEFGDPALR 97
PLN03150 PLN03150
hypothetical protein; Provisional
 52-117 1.69e-07

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 54.05  E-value: 1.69e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015   52 HLTALHLSDNSL-SCIPSDIAKLHNLVYLDLSHNQIQ-SLPAELGNMVSLRELHLNYNQL--RVlPFELG 117
Cdd:PLN03150 443 HLQSINLSGNSIrGNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLsgRV-PAALG 511
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
 186-531 2.78e-07

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


Pssm-ID: 197318 [Multi-domain]  Cd Length: 246  Bit Score: 51.91  E-value: 2.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 186 VMCYNVlcdkyatRQLYGYcpswalNWDYRKKAIIQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 265
Cdd:cd09084   1 VMSYNV-------RSFNRY------KWKDDPDKILDFIKKQDPDILCLQEYYGSEGDKDDDLRLLLKGYPYYYVVYKSDS 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 266 TMSEQerkhvdgcAIFfktEKFTLVQKHTVEFnqlamansegseamlnrvmtKDNIGVAVLLELRKeliemssgkphlgt 345
Cdd:cd09084  68 GGTGL--------AIF---SKYPILNSGSIDF--------------------PNTNNNAIFADIRV-------------- 102

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 346 EKQLILVANAHMhwdpeysdvklvQTMMFLSEVKNII--DKASRSLKSSVLGE--------------------CGTIPLV 403
Cdd:cd09084 103 GGDTIRVYNVHL------------ESFRITPSDKELYkeEKKAKELSRNLLRKlaeafkrraaqadllaadiaASPYPVI 170

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 404 LCADLNSLPDSGVveylstggvetnhkdfkelrYNesltnfscngkngmtngRITHGfkLKSAYE---NGLMpytnYTFD 480
Cdd:cd09084 171 VCGDFNDTPASYV--------------------YR-----------------TLKKG--LTDAFVeagSGFG----YTFN 207

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 47059015 481 FKGI---IDYIFYSKPqlntlaiLGPLDHHwlvennisgcPHPLIPSDHFSLFA 531
Cdd:cd09084 208 GLFFplrIDYILTSKG-------FKVLRYR----------VDPGKYSDHYPIVA 244
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 53-135 1.12e-06

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 49.78  E-value: 1.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  53 LTALHLSDNSLSCIpSDIAKLHNLVYLDLSHNQIQSLpAELGNMVSlrelhlnynqlrvlpfelgKLFQLQTLSLKGNPL 132
Cdd:cd21340 122 LRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISDL-EELLDLLS-------------------SWPSLRELDLTGNPV 180


                ...
gi 47059015 133 TQD 135
Cdd:cd21340 181 CKK 183
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 53-136 1.25e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 51.39  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015   53 LTALHLSDNSLSC-IPSDIAKLHNLVYLDLSHNQ-IQSLPAELGNMVSLRELHLNYNQLR-VLPFELGKLFQLQTLSLKG 129
Cdd:PLN00113 166 LKVLDLGGNVLVGkIPNSLTNLTSLEFLTLASNQlVGQIPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVY 245


                 ....*..
gi 47059015  130 NPLTQDI 136
Cdd:PLN00113 246 NNLTGPI 252
LRR_8 pfam13855
Leucine rich repeat;
75-132 1.33e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 45.59  E-value: 1.33e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015    75 NLVYLDLSHNQIQSLPAE-LGNMVSLRELHLNYNQLRVL-PFELGKLFQLQTLSLKGNPL 132
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 53-130 6.64e-06

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 47.47  E-value: 6.64e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47059015  53 LTALHLSDNSLSCIPsDIAKLHNLVYLDLSHNQIQSLPAeLGNMVSLRELHLNYNQLRVLPFeLGKLFQLQTLSLKGN 130
Cdd:cd21340   4 ITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIEN-LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLGGN 78
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
53-163 1.28e-04

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 45.07  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015   53 LTALHLSDNSLSCIPSDIAKlhNLVYLDLSHNQIQSLPAELGNmvSLRELHLNYNQLRVLPFELGKlfQLQTLSLKGNPL 132
Cdd:PRK15370 264 LQSLDLFHNKISCLPENLPE--ELRYLSVYDNSIRTLPAHLPS--GITHLNVQSNSLTALPETLPP--GLKTLEAGENAL 337

                         90       100       110
                 ....*....|....*....|....*....|.
gi 47059015  133 TQdiLNLCLEPDgtrrllnylLDNLSVSTEQ 163
Cdd:PRK15370 338 TS--LPASLPPE---------LQVLDVSKNQ 357
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 51-165 1.31e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 44.84  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015   51 THLTALHLSDNSLSC-IPSDIAKLHNLVYLDL-SHNQIQSLPAELGNMVSLRELHLNYNQLR-VLPFELGKLFQLQTLSL 127
Cdd:PLN00113 284 QKLISLDLSDNSLSGeIPELVIQLQNLEILHLfSNNFTGKIPVALTSLPRLQVLQLWSNKFSgEIPKNLGKHNNLTVLDL 363

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 47059015  128 KGNPLTQDIlnlclePDG---TRRLLNYLLDNLSVSTEQPP 165
Cdd:PLN00113 364 STNNLTGEI------PEGlcsSGNLFKLILFSNSLEGEIPK 398
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 53-130 3.06e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 43.68  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015   53 LTALHLSDNSLSC-IPSDIAKLHNLVYLDLSHNQIQ-SLPAELGNMVSLRELHLNYNQLR-VLPFElGKLFQLQTLSLKG 129
Cdd:PLN00113 525 LVSLDLSHNQLSGqIPASFSEMPVLSQLDLSQNQLSgEIPKNLGNVESLVQVNISHNHLHgSLPST-GAFLAINASAVAG 603


                 .
gi 47059015  130 N 130
Cdd:PLN00113 604 N 604
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 75-109 3.99e-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: 38.00  E-value: 3.99e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 47059015    75 NLVYLDLSHNQIQSLPAeLGNMVSLRELHLNYNQL 109
Cdd:pfam12799   2 NLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNNK 35
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-164 8.41e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.84  E-value: 8.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  51 THLTALHLSDNSLSCIPsDIAKLHNLVYLDLSHNQIQSLPAELGNMVSLRELHLNYNQLRVLPFELGKLFQLQTLSLKGN 130
Cdd:COG4886 250 TNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLL 328

                        90       100       110
                ....*....|....*....|....*....|....
gi 47059015 131 PLTQDILNLCLEPDGTRRLLNYLLDNLSVSTEQP 164
Cdd:COG4886 329 LLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLL 362
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 51-136 1.43e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 41.76  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015   51 THLTALHLSDNSLSCIPSDIAKLHNLVYLDLSHNQIQ-SLPAELGNMVSLRELHLNYNQLR-VLPFELGKLFQLQTLSLK 128
Cdd:PLN00113 452 PSLQMLSLARNKFFGGLPDSFGSKRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDLS 531


                 ....*...
gi 47059015  129 GNPLTQDI 136
Cdd:PLN00113 532 HNQLSGQI 539
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 51-91 1.44e-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: 36.45  E-value: 1.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 47059015    51 THLTALHLSDNSLSCIPSdIAKLHNLVYLDLSHN-QIQSLPA 91
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNnKITDLSD 41
TDP2 cd09080
Phosphodiesterase domain of human TDP2, a 5'-tyrosyl DNA phosphodiesterase, and related ...
 184-266 1.45e-03

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


Pssm-ID: 197314 [Multi-domain]  Cd Length: 248  Bit Score: 40.40  E-value: 1.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015 184 FSVMCYNVLCDKYATRQLygycpswalnwdyRKKAIIQEILSCNADIISLQEVeTEQYYSFFLvELKERGYNGFFSPKSR 263
Cdd:cd09080   1 LKVLTWNVDFLDDVNLAE-------------RMRAILKLLEELDPDVIFLQEV-TPPFLAYLL-SQPWVRKNYYFSEGPP 65


                ...
gi 47059015 264 ART 266
Cdd:cd09080  66 SPA 68
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 98-139 2.42e-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: 2.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 47059015    98 SLRELHLNYNQLRVLPFeLGKLFQLQTLSLKGNPLTQDILNL 139
Cdd:pfam12799   2 NLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNNKITDLSDL 42
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 51-161 5.40e-03

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 39.39  E-value: 5.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015  51 THLTALHLSDNSLSC-----IPSDIAKLHNLVYLDLSHNQI-----QSLPAELGNMVSLRELHLNYNQL-----RVLPFE 115
Cdd:COG5238 236 KSLTTLDLSNNQIGDegviaLAEALKNNTTVETLYLSGNQIgaegaIALAKALQGNTTLTSLDLSVNRIgdegaIALAEG 315

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 47059015 116 LGKLFQLQTLSLKGNPLTqdilnlclePDGTRRLLNYLLDNLSVST 161
Cdd:COG5238 316 LQGNKTLHTLNLAYNGIG---------AQGAIALAKALQENTTLHS 352
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 52-136 7.14e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 39.45  E-value: 7.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015   52 HLTALHLSDNSLSC-IPSDIAKL-HNLVYLDLSHNQIqSLPAELGNMVSLRELHLNYNQLR-VLPFELGKLFQLQTLSLK 128
Cdd:PLN00113  94 YIQTINLSNNQLSGpIPDDIFTTsSSLRYLNLSNNNF-TGSIPRGSIPNLETLDLSNNMLSgEIPNDIGSFSSLKVLDLG 172


                 ....*...
gi 47059015  129 GNPLTQDI 136
Cdd:PLN00113 173 GNVLVGKI 180
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 53-142 7.78e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 39.06  E-value: 7.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47059015   53 LTALHLSDNSLSC-IPSDIAKLHNLVYLDLSHNQIQ-SLPAELGNMVSLRELHLNYNQLR-VLPFELGKLFQLQTLSLKG 129
Cdd:PLN00113 214 LKWIYLGYNNLSGeIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSD 293

                         90
                 ....*....|...
gi 47059015  130 NPLTQDILNLCLE 142
Cdd:PLN00113 294 NSLSGEIPELVIQ 306
 
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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