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Conserved domains on  [gi|1915707683|ref|NP_001374768|]
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CCR4-NOT transcription complex subunit 6-like isoform 4 [Homo sapiens]

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 ...
 186-434 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 cd10312:

Pssm-ID: 469791  Cd Length: 348  Bit Score: 572.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 186 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 265
Cdd:cd10312     1 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 266 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNIGVAVVLEVHKELFGAGMKPIHAAD 345
Cdd:cd10312    81 IMSEQERKHVDGCAIFFKTEKFSLVQKHTVEFNQVAMANSEGSEAMLNRVMTKDNIGVAVVLEVHKELFGAGMKPIHAAD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 346 KQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVAD 425
Cdd:cd10312   161 KQLLIVANAHMHWDPEYSDVKLIQTMMFVSELKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVAD 240


                  ....*....
gi 1915707683 426 NHKDFKELR 434
Cdd:cd10312   241 NHKDFKELR 249
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-133 1.16e-15

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 78.44  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683  33 ELEISG-RVRSLSTSLWSLTHLTALHLNDNYLSRIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNNNLLRV 111
Cdd:COG4886   117 SLDLSGnQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITD 196

                          90       100
                  ....*....|....*....|..
gi 1915707683 112 LPYELGRLFQLQTLGLKGNPLS 133
Cdd:COG4886   197 LPEPLGNLTNLEELDLSGNQLT 218
 
Name Accession Description Interval E-value
Deadenylase_CCR4b cd10312
C-terminal deadenylase domain of CCR4b, also known as CCR4-NOT transcription complex subunit ...
 186-434 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: 572.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 186 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 265
Cdd:cd10312     1 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 266 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNIGVAVVLEVHKELFGAGMKPIHAAD 345
Cdd:cd10312    81 IMSEQERKHVDGCAIFFKTEKFSLVQKHTVEFNQVAMANSEGSEAMLNRVMTKDNIGVAVVLEVHKELFGAGMKPIHAAD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 346 KQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVAD 425
Cdd:cd10312   161 KQLLIVANAHMHWDPEYSDVKLIQTMMFVSELKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVAD 240


                  ....*....
gi 1915707683 426 NHKDFKELR 434
Cdd:cd10312   241 NHKDFKELR 249
PLN03144 PLN03144
Carbon catabolite repressor protein 4 homolog; Provisional
 158-429 4.03e-64

Carbon catabolite repressor protein 4 homolog; Provisional


Pssm-ID: 178689 [Multi-domain]  Cd Length: 606  Bit Score: 216.90  E-value: 4.03e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 158 AVHPeqlPPRPWITLKERD---------QILPSASFTVMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDA 228
Cdd:PLN03144  223 APSP---TPRRLIQVNGLDgmghldldgRTSSAGTFTVLSYNILSDLYATSDMYSYCPPWALSWTYRRQNLLREIVGYRA 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 229 DIISLQEVETEQYFTLFLPALKERGYDGFFSPKSrAKIMSEQerKHV-DGCAIFFKTEKFTLVQKHTVEFNQVAMANSDG 307
Cdd:PLN03144  300 DILCLQEVQSDHFEEFFAPELDKHGYQALYKKKT-TEVYTGN--TYViDGCATFFRRDRFSLVKKYEVEFNKAAQSLTEA 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 308 ------SEAMLNRVMtKDNIGVAVVLEVhkeLFGAGmKPIHAADKQLLIVANAHMHWDPEYSDVKLIQtmmfVSEVKNIL 381
Cdd:PLN03144  377 lipsaqKKAALNRLL-KDNVALIVVLEA---KFGNQ-GADNGGKRQLLCVANTHIHANQELKDVKLWQ----VHTLLKGL 447

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1915707683 382 EK-ASSrpgsptADpnsIPLVLCADLNSLPDSGVVEYLSNGGVADNHKD 429
Cdd:PLN03144  448 EKiAAS------AD---IPMLVCGDFNSVPGSAPHCLLATGKVDPLHPD 487
CCR4 COG5239
mRNA deadenylase, 3'-5' endonuclease subunit Ccr4 [RNA processing and modification];
180-430 5.21e-56

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


Pssm-ID: 227564 [Multi-domain]  Cd Length: 378  Bit Score: 189.60  E-value: 5.21e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 180 PSASFTVMCYNVLCDKYATRQLYGYCpSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFS 259
Cdd:COG5239    27 KDTDFTIMTYNVLAQTYATRKMYPYS-GWALKWSYRSRLLLQELLYYNADILCLQEVDAEDFEDFWKDQLGKLGYDGIFI 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 260 PKSR-AKIMSEQERKHVDGCAIFFKTE----KFTLVQKHTVEFNQVAMANSD--GSEAMLNRVMTKDNIGVAVVLevhke 332
Cdd:COG5239   106 PKERkVKWMIDYDTTKVDGCAIFLKRFidssKLGLILAVTHLFWHPYGYYERfrQTYILLNRIGEKDNIAWVCLF----- 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 333 lfgagMKPIHAADKQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEK--ASSRPGSPTADPNSIPLVLCADLNSLP 410
Cdd:COG5239   181 -----VGLFNKEPGDTPYVANTHLPWDPKYRDVKLIQCSLLYRELKKVLKEelNDDKEEGDIKSYPEVDILITGDFNSLR 255

                         250       260
                  ....*....|....*....|
gi 1915707683 411 DSGVVEYLsNGGVADNHKDF 430
Cdd:COG5239   256 ASLVYKFL-VTSQIQLHESL 274
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-133 1.16e-15

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 78.44  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683  33 ELEISG-RVRSLSTSLWSLTHLTALHLNDNYLSRIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNNNLLRV 111
Cdd:COG4886   117 SLDLSGnQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITD 196

                          90       100
                  ....*....|....*....|..
gi 1915707683 112 LPYELGRLFQLQTLGLKGNPLS 133
Cdd:COG4886   197 LPEPLGNLTNLEELDLSGNQLT 218
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 187-303 1.68e-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: 51.07  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 187 MCYNVLCDkyatrqlygycPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKsraki 266
Cdd:pfam03372   1 LTWNVNGG-----------NADAAGDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFLSYGGPG----- 64

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1915707683 267 mseqERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMA 303
Cdd:pfam03372  65 ----GGGGGGGVAILSRYPLSSVILVDLGEFGDPALR 97
LRR_8 pfam13855
Leucine rich repeat;
51-132 1.45e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 45.21  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683  51 THLTALHLNDNYLSRIPPDIAK-LHNLVYLDLSSNKLRSLPaelgnmvslrelllnnnllrvlPYELGRLFQLQTLGLKG 129
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLS----------------------PGAFSGLPSLRYLDLSG 58


                  ...
gi 1915707683 130 NPL 132
Cdd:pfam13855  59 NRL 61
PLN03150 PLN03150
hypothetical protein; Provisional
 55-133 2.15e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 43.65  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683  55 ALHLNDNYL-SRIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLRELLLNNNLLR-VLPYELGRLFQLQTLGLKGNP 131
Cdd:PLN03150  422 GLGLDNQGLrGFIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNS 501


                  ..
gi 1915707683 132 LS 133
Cdd:PLN03150  502 LS 503
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 41-135 3.31e-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: 41.70  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683  41 RSLSTSLWSLTHLTALHLNDNYLSrippDIAKLHNLVYLDLSSNKLRSLpAELGNMVSlrelllnnnllrvlpyelgRLF 120
Cdd:cd21340   113 RSLAALSNSLRVLNISGNNIDSLE----PLAPLRNLEQLDASNNQISDL-EELLDLLS-------------------SWP 168

                          90
                  ....*....|....*
gi 1915707683 121 QLQTLGLKGNPLSQD 135
Cdd:cd21340   169 SLRELDLTGNPVCKK 183
LRR smart00370
Leucine-rich repeats, outliers;
73-93 4.67e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 34.25  E-value: 4.67e-03
                           10        20
                   ....*....|....*....|.
gi 1915707683   73 LHNLVYLDLSSNKLRSLPAEL 93
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGA 21
 
Name Accession Description Interval E-value
Deadenylase_CCR4b cd10312
C-terminal deadenylase domain of CCR4b, also known as CCR4-NOT transcription complex subunit ...
 186-434 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: 572.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 186 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 265
Cdd:cd10312     1 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 266 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNIGVAVVLEVHKELFGAGMKPIHAAD 345
Cdd:cd10312    81 IMSEQERKHVDGCAIFFKTEKFSLVQKHTVEFNQVAMANSEGSEAMLNRVMTKDNIGVAVVLEVHKELFGAGMKPIHAAD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 346 KQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVAD 425
Cdd:cd10312   161 KQLLIVANAHMHWDPEYSDVKLIQTMMFVSELKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVAD 240


                  ....*....
gi 1915707683 426 NHKDFKELR 434
Cdd:cd10312   241 NHKDFKELR 249
Deadenylase_CCR4a cd10313
C-terminal deadenylase domain of CCR4a, also known as CCR4-NOT transcription complex subunit 6; ...
 186-434 1.87e-156

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: 446.03  E-value: 1.87e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 186 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 265
Cdd:cd10313     1 VMCYNVLCDKYATRQLYGYCPSWALNWDYRKKAIMQEILSCNADIISLQEVETEQYYSFFLVELKERGYNGFFSPKSRAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 266 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNIGVAVVLEVHKELFG-AGMKPIHAA 344
Cdd:cd10313    81 TMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQLAMANSEGSEAMLNRVMTKDNIGVAVLLELRKELIEmSSGKPHLGM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 345 DKQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKAS-SRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGV 423
Cdd:cd10313   161 EKQLILVANAHMHWDPEYSDVKLVQTMMFLSEVKNIIDKASrSLKSSVLGETGTIPLVLCADLNSLPDSGVVEYLSTGGV 240

                         250
                  ....*....|.
gi 1915707683 424 ADNHKDFKELR 434
Cdd:cd10313   241 ETNHKDFKELR 251
Deadenylase_CCR4 cd09097
C-terminal deadenylase domain of CCR4 and related domains; This subfamily contains the ...
 186-434 8.68e-155

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: 440.97  E-value: 8.68e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 186 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 265
Cdd:cd09097     1 VMCYNVLCDKYATRQQYGYCPSWALNWDYRKQNILKEILSYNADILCLQEVETDQYEDFFLPELKQHGYDGVFKPKSRAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 266 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSD--GSEAMLNRVMTKDNIGVAVVLEVHKELFGAGmkpiha 343
Cdd:cd09097    81 TMSEAERKHVDGCAIFFKTSKFKLVEKHLIEFNQLAMANADaeGSEDMLNRVMTKDNIALIVVLEARETSYEGN------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 344 aDKQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADpnsIPLVLCADLNSLPDSGVVEYLSNGGV 423
Cdd:cd09097   155 -KGQLLIVANTHIHWDPEFSDVKLVQTMMLLEELEKIAEKFSRYPYEDSAD---IPLVVCGDFNSLPDSGVYELLSNGSV 230

                         250
                  ....*....|.
gi 1915707683 424 ADNHKDFKELR 434
Cdd:cd09097   231 SPNHPDFKEDP 241
PLN03144 PLN03144
Carbon catabolite repressor protein 4 homolog; Provisional
 158-429 4.03e-64

Carbon catabolite repressor protein 4 homolog; Provisional


Pssm-ID: 178689 [Multi-domain]  Cd Length: 606  Bit Score: 216.90  E-value: 4.03e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 158 AVHPeqlPPRPWITLKERD---------QILPSASFTVMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDA 228
Cdd:PLN03144  223 APSP---TPRRLIQVNGLDgmghldldgRTSSAGTFTVLSYNILSDLYATSDMYSYCPPWALSWTYRRQNLLREIVGYRA 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 229 DIISLQEVETEQYFTLFLPALKERGYDGFFSPKSrAKIMSEQerKHV-DGCAIFFKTEKFTLVQKHTVEFNQVAMANSDG 307
Cdd:PLN03144  300 DILCLQEVQSDHFEEFFAPELDKHGYQALYKKKT-TEVYTGN--TYViDGCATFFRRDRFSLVKKYEVEFNKAAQSLTEA 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 308 ------SEAMLNRVMtKDNIGVAVVLEVhkeLFGAGmKPIHAADKQLLIVANAHMHWDPEYSDVKLIQtmmfVSEVKNIL 381
Cdd:PLN03144  377 lipsaqKKAALNRLL-KDNVALIVVLEA---KFGNQ-GADNGGKRQLLCVANTHIHANQELKDVKLWQ----VHTLLKGL 447

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1915707683 382 EK-ASSrpgsptADpnsIPLVLCADLNSLPDSGVVEYLSNGGVADNHKD 429
Cdd:PLN03144  448 EKiAAS------AD---IPMLVCGDFNSVPGSAPHCLLATGKVDPLHPD 487
CCR4 COG5239
mRNA deadenylase, 3'-5' endonuclease subunit Ccr4 [RNA processing and modification];
180-430 5.21e-56

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


Pssm-ID: 227564 [Multi-domain]  Cd Length: 378  Bit Score: 189.60  E-value: 5.21e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 180 PSASFTVMCYNVLCDKYATRQLYGYCpSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFS 259
Cdd:COG5239    27 KDTDFTIMTYNVLAQTYATRKMYPYS-GWALKWSYRSRLLLQELLYYNADILCLQEVDAEDFEDFWKDQLGKLGYDGIFI 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 260 PKSR-AKIMSEQERKHVDGCAIFFKTE----KFTLVQKHTVEFNQVAMANSD--GSEAMLNRVMTKDNIGVAVVLevhke 332
Cdd:COG5239   106 PKERkVKWMIDYDTTKVDGCAIFLKRFidssKLGLILAVTHLFWHPYGYYERfrQTYILLNRIGEKDNIAWVCLF----- 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 333 lfgagMKPIHAADKQLLIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILEK--ASSRPGSPTADPNSIPLVLCADLNSLP 410
Cdd:COG5239   181 -----VGLFNKEPGDTPYVANTHLPWDPKYRDVKLIQCSLLYRELKKVLKEelNDDKEEGDIKSYPEVDILITGDFNSLR 255

                         250       260
                  ....*....|....*....|
gi 1915707683 411 DSGVVEYLsNGGVADNHKDF 430
Cdd:COG5239   256 ASLVYKFL-VTSQIQLHESL 274
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 186-419 1.42e-39

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: 142.24  E-value: 1.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 186 VMCYNVLCDKYATRqlygycpswalnweyrKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRak 265
Cdd:cd08372     1 VASYNVNGLNAATR----------------ASGIARWVRELDPDIVCLQEVKDSQYSAVALNQLLPEGYHQYQSGPSR-- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 266 imseqeRKHVDGCAIFFKTEKFTLVQKHTVEFNQvamansdgseamlnrVMTKDNIGVAVVLEVHKELFgagmkpihaad 345
Cdd:cd08372    63 ------KEGYEGVAILSKTPKFKIVEKHQYKFGE---------------GDSGERRAVVVKFDVHDKEL----------- 110

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915707683 346 kqllIVANAHMHWDPEYSDVKLIQTMMFVSEVKNILekassrpgsptaDPNSIPLVLCADLNSLPDSGVVEYLS 419
Cdd:cd08372   111 ----CVVNAHLQAGGTRADVRDAQLKEVLEFLKRLR------------QPNSAPVVICGDFNVRPSEVDSENPS 168
Deadenylase cd09082
C-terminal deadenylase domain of CCR4, nocturnin, and related domains; This family contains ...
 186-426 3.30e-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: 97.04  E-value: 3.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 186 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 265
Cdd:cd09082     1 VMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 266 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDN-IGVAVVLEVHKELFGAGMKPIHAA 344
Cdd:cd09082    81 IMSEQERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMANSDGSEAMLNRVMTKDNiGVAVVLEVHKELFGAGMKPIHAAD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 345 DKQLLIvANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVA 424
Cdd:cd09082   161 KQLLIV-ANAHMHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVVEYLSNGGVA 239


                  ..
gi 1915707683 425 DN 426
Cdd:cd09082   240 DN 241
Deadenylase_nocturnin cd09096
C-terminal deadenylase domain of nocturnin and related domains; This subfamily contains the ...
 205-420 4.84e-21

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: 92.49  E-value: 4.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 205 CPSWALNWEYRKKGIMEEIVNCDADIISLQEVetEQYFTLFLPALKERGYDGFFSPKSRAKIMSEQERKHVDGCAIFFKT 284
Cdd:cd09096    22 CPCEALKWEERKYLILEEILTYDPDILCLQEV--DHYKDTLQPLLSRLGYQGTFFPKPDSPCLYIENNNGPDGCALFFRK 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 285 EKFTLV-------QKHTVEFNQVAMAnsdgseAMLNRvmtkdnigvavvlevhkelfgagmkpihAADKQLLIVANAHMH 357
Cdd:cd09096   100 DRFELVntekirlSAMTLKTNQVAIA------CTLRC----------------------------KETGREICLAVTHLK 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915707683 358 WDPEYSDVKLIQTMMFVSEVKNILEKAssrpgsptadpnSIPLVLCADLNSLPDSGVVEYLSN 420
Cdd:cd09096   146 ARTGWERLRSEQGKDLLQNLQSFIEGA------------KIPLIICGDFNAEPTEPVYKTFSN 196
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-133 1.16e-15

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 78.44  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683  33 ELEISG-RVRSLSTSLWSLTHLTALHLNDNYLSRIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNNNLLRV 111
Cdd:COG4886   117 SLDLSGnQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITD 196

                          90       100
                  ....*....|....*....|..
gi 1915707683 112 LPYELGRLFQLQTLGLKGNPLS 133
Cdd:COG4886   197 LPEPLGNLTNLEELDLSGNQLT 218
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-133 3.69e-14

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 73.81  E-value: 3.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683  33 ELEISG-RVRSLSTSLWSLTHLTALHLNDNYLSRIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNNNLLRV 111
Cdd:COG4886   140 ELDLSNnQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTD 219

                          90       100
                  ....*....|....*....|..
gi 1915707683 112 LPYELGRLFQLQTLGLKGNPLS 133
Cdd:COG4886   220 LPEPLANLTNLETLDLSNNQLT 241
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-180 4.93e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 70.35  E-value: 4.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683  33 ELEISG-RVRSLSTSLWSLTHLTALHLNDNYLSRIPPDIAKLHNLVYLDLSSNKLRSLPaELGNMVSLRELLLNNNLLRV 111
Cdd:COG4886   186 ELDLSNnQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTD 264

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915707683 112 LPyELGRLFQLQTLGLKGNPLSQDILNLYQDPDGTRKLLNFMLDNLAVHPEQLPPRPWITLKERDQILP 180
Cdd:COG4886   265 LP-PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKG 332
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
 185-425 8.46e-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: 68.01  E-value: 8.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 185 TVMCYNVLCDkyatrqlygyCPSWALN-WEYRKKGIMEEIVNCDADIISLQEVETEQyftlfLPALKER--GYDgffspk 261
Cdd:cd09083     1 RVMTFNIRYD----------NPSDGENsWENRKDLVAELIKFYDPDIIGTQEALPHQ-----LADLEELlpEYD------ 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 262 sraKIMSEQERKHVDG--CAIFFKTEKFTLVQKHTveF---NQVAMANSDGSEAMLNRVMTkdnigvAVVLEvhkelfga 336
Cdd:cd09083    60 ---WIGVGRDDGKEKGefSAIFYRKDRFELLDSGT--FwlsETPDVVGSKGWDAALPRICT------WARFK-------- 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 337 gmkpiHAADKQLLIVANAHMhwDpeysdvkliqtmmFVSEV------KNILEKASSRPGsptadpnSIPLVLCADLNSLP 410
Cdd:cd09083   121 -----DKKTGKEFYVFNTHL--D-------------HVGEEareesaKLILERIKEIAG-------DLPVILTGDFNAEP 173

                         250
                  ....*....|....*
gi 1915707683 411 DSGVVEYLSNGGVAD 425
Cdd:cd09083   174 DSEPYKTLTSGGLKD 188
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
42-133 1.58e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 68.81  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683  42 SLSTSLWSLTHLTALHLNDNYLSRIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNNNLLRVLPYELGRLFQ 121
Cdd:COG4886   104 SGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTN 183

                          90
                  ....*....|..
gi 1915707683 122 LQTLGLKGNPLS 133
Cdd:COG4886   184 LKELDLSNNQIT 195
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 187-303 1.68e-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: 51.07  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 187 MCYNVLCDkyatrqlygycPSWALNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKsraki 266
Cdd:pfam03372   1 LTWNVNGG-----------NADAAGDDRKLDALAALIRAYDPDVVALQETDDDDASRLLLALLAYGGFLSYGGPG----- 64

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1915707683 267 mseqERKHVDGCAIFFKTEKFTLVQKHTVEFNQVAMA 303
Cdd:pfam03372  65 ----GGGGGGGVAILSRYPLSSVILVDLGEFGDPALR 97
LRR_8 pfam13855
Leucine rich repeat;
51-132 1.45e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 45.21  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683  51 THLTALHLNDNYLSRIPPDIAK-LHNLVYLDLSSNKLRSLPaelgnmvslrelllnnnllrvlPYELGRLFQLQTLGLKG 129
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLS----------------------PGAFSGLPSLRYLDLSG 58


                  ...
gi 1915707683 130 NPL 132
Cdd:pfam13855  59 NRL 61
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-179 2.79e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.16  E-value: 2.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683  33 ELEISG-RVRSLStSLWSLTHLTALHLNDNYLSRIPPdIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNNNLLRV 111
Cdd:COG4886   232 TLDLSNnQLTDLP-ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLN 309

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1915707683 112 LPYELGRLFQLQTLGLKGNPLSQDILNLYQDPDGTRKLLNFMLDNLAVHPEQLPPRPWITLKERDQIL 179
Cdd:COG4886   310 LLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEA 377
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
 186-423 1.57e-05

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


Pssm-ID: 197318 [Multi-domain]  Cd Length: 246  Bit Score: 46.14  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 186 VMCYNVlcdkyatRQLYGYcpswalNWEYRKKGIMEEIVNCDADIISLQEVETEQYFTLFLPALKERGYDGFFSPKSRAK 265
Cdd:cd09084     1 VMSYNV-------RSFNRY------KWKDDPDKILDFIKKQDPDILCLQEYYGSEGDKDDDLRLLLKGYPYYYVVYKSDS 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 266 IMSEQerkhvdgcAIFfktEKFTLVQKHTVEFNqvamaNSDGSEAMLNRVMTKDNIgvaVVLEVHKELFGagmkpIHAAD 345
Cdd:cd09084    68 GGTGL--------AIF---SKYPILNSGSIDFP-----NTNNNAIFADIRVGGDTI---RVYNVHLESFR-----ITPSD 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683 346 KQLLivanAHMHWDPEYSDvKLIQTM--MFV---SEVKNILEKASSRPGsptadpnsiPLVLCADLNSLPDSGVVEYLSN 420
Cdd:cd09084   124 KELY----KEEKKAKELSR-NLLRKLaeAFKrraAQADLLAADIAASPY---------PVIVCGDFNDTPASYVYRTLKK 189


                  ...
gi 1915707683 421 GGV 423
Cdd:cd09084   190 GLT 192
LRR_8 pfam13855
Leucine rich repeat;
49-86 2.74e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 41.74  E-value: 2.74e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1915707683  49 SLTHLTALHLNDNYLSRIPPD-IAKLHNLVYLDLSSNKL 86
Cdd:pfam13855  23 GLSNLKVLDLSNNLLTTLSPGaFSGLPSLRYLDLSGNRL 61
PLN03150 PLN03150
hypothetical protein; Provisional
 55-133 2.15e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 43.65  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683  55 ALHLNDNYL-SRIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLRELLLNNNLLR-VLPYELGRLFQLQTLGLKGNP 131
Cdd:PLN03150  422 GLGLDNQGLrGFIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNS 501


                  ..
gi 1915707683 132 LS 133
Cdd:PLN03150  502 LS 503
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 41-135 3.31e-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: 41.70  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683  41 RSLSTSLWSLTHLTALHLNDNYLSrippDIAKLHNLVYLDLSSNKLRSLpAELGNMVSlrelllnnnllrvlpyelgRLF 120
Cdd:cd21340   113 RSLAALSNSLRVLNISGNNIDSLE----PLAPLRNLEQLDASNNQISDL-EELLDLLS-------------------SWP 168

                          90
                  ....*....|....*
gi 1915707683 121 QLQTLGLKGNPLSQD 135
Cdd:cd21340   169 SLRELDLTGNPVCKK 183
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 51-86 4.57e-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: 37.61  E-value: 4.57e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1915707683  51 THLTALHLNDNYLSRIPPdIAKLHNLVYLDLSSNKL 86
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNNK 35
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 49-136 7.26e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 42.14  E-value: 7.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683  49 SLTHLTALHLNDNYLS-RIPPDIAKLHNLVYLDLSSNKLR-SLPAELGNMVSLR-ELLLNNNLLRVLPYELGRLFQLQTL 125
Cdd:PLN00113  162 SFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKwIYLGYNNLSGEIPYEIGGLTSLNHL 241

                          90
                  ....*....|.
gi 1915707683 126 GLKGNPLSQDI 136
Cdd:PLN00113  242 DLVYNNLTGPI 252
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 49-136 3.31e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 39.83  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915707683  49 SLTHLTALHLNDNYLS-RIPPDIAKLHNLVYLDLSSNKLRS-LPAELGNMVSLRELLLNNNLLR-VLPYELGRLFQLQTL 125
Cdd:PLN00113  138 SIPNLETLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVGkIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWI 217

                          90
                  ....*....|.
gi 1915707683 126 GLKGNPLSQDI 136
Cdd:PLN00113  218 YLGYNNLSGEI 228
LRR smart00370
Leucine-rich repeats, outliers;
73-93 4.67e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 34.25  E-value: 4.67e-03
                           10        20
                   ....*....|....*....|.
gi 1915707683   73 LHNLVYLDLSSNKLRSLPAEL 93
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGA 21
LRR_TYP smart00369
Leucine-rich repeats, typical (most populated) subfamily;
73-93 4.67e-03

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


Pssm-ID: 197687 [Multi-domain]  Cd Length: 24  Bit Score: 34.25  E-value: 4.67e-03
                           10        20
                   ....*....|....*....|.
gi 1915707683   73 LHNLVYLDLSSNKLRSLPAEL 93
Cdd:smart00369   1 LPNLRELDLSNNQLSSLPPGA 21
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 49-89 5.93e-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: 37.84  E-value: 5.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1915707683  49 SLTHLTALHLNDNYLSRIpPDIAKLHNLVYLDLSSNKLRSL 89
Cdd:cd21340    44 FLTNLTHLYLQNNQIEKI-ENLENLVNLKKLYLGGNRISVV 83
 
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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