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Conserved domains on  [gi|62901504|sp|Q9P209|]
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RecName: Full=Centrosomal protein of 72 kDa; Short=Cep72

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 1903219)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions

CATH:  3.80.10.10
Gene Ontology:  GO:0005515
PubMed:  11751054|7583641|14747988
SCOP:  4003523

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 48-145 2.21e-14

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.


The actual alignment was detected with superfamily member cd21340:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 220  Bit Score: 72.51  E-value: 2.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504  48 HSLMSLTG-LKSLDLSRNSLVSLEGIQYLTALESLNLYYNCISSLAEVFR-LHALTELVDVDFRLNPVVKvEPDYRLFVV 125
Cdd:cd21340 113 RSLAALSNsLRVLNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELLDlLSSWPSLRELDLTGNPVCK-KPKYRDKII 191

                        90       100
                ....*....|....*....|
gi 62901504 126 HLLPKLQQLDDRPVRASERK 145
Cdd:cd21340 192 LASKSLEVLDGKEITDTERQ 211
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 407-628 2.20e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504    407 SHSALPGKKTALQAALLETLLDLVDRSWGGCRSLHSNEAFLAQARHILSSVEEFTAAQDSSAMVGEDVGSLALESKSLQS 486
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504    487 RLAEQQQQHAREMSEVTAELHHTHKELDDLRQHLDKSLEENSRLKSLLLSMKKEVK-SADTAATLNLQIAGLQTSVKRL- 564
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEdLEEQIEELSEDIESLAAEIEELe 865

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504    565 --CGEI-VELKQHLEHYDKIQELTQMLQESHSSLVSTNEHLLQELSQVRAQH---RAEVEQMHWSYQELK 628
Cdd:TIGR02168  866 elIEELeSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELeelREKLAQLELRLEGLE 935
 
Name Accession Description Interval E-value
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 48-145 2.21e-14

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: 72.51  E-value: 2.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504  48 HSLMSLTG-LKSLDLSRNSLVSLEGIQYLTALESLNLYYNCISSLAEVFR-LHALTELVDVDFRLNPVVKvEPDYRLFVV 125
Cdd:cd21340 113 RSLAALSNsLRVLNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELLDlLSSWPSLRELDLTGNPVCK-KPKYRDKII 191

                        90       100
                ....*....|....*....|
gi 62901504 126 HLLPKLQQLDDRPVRASERK 145
Cdd:cd21340 192 LASKSLEVLDGKEITDTERQ 211
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
26-164 1.78e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 69.58  E-value: 1.78e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504  26 DLAELQSLSIPGTyqeKITHLGHSLMSLTGLKSLDLSRNSLVSLEGIQYLTALESLNLYYNCISSLAEVFRLHALTELvd 105
Cdd:COG4886 203 NLTNLEELDLSGN---QLTDLPEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTL-- 277

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62901504 106 vDFRLNPVVKVEPDYRLFVVHLLPKLQQLDDRPVRASERKASRLHFASEDSLDSKESVP 164
Cdd:COG4886 278 -DLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLV 335
LRR_9 pfam14580
Leucine-rich repeat;
53-153 1.81e-10

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 60.16  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504    53 LTGLKSLDLSRNSLVSL-EGI-QYLTALESLNLYYNCISSLAEVFRLHALTELVDVDFRLNPVVKvEPDYRLFVVHLLPK 130
Cdd:pfam14580  63 LRRLKTLLLNNNRICRIgEGLgEALPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTN-KPHYRLYVIYKVPQ 141

                          90       100
                  ....*....|....*....|...
gi 62901504   131 LQQLDDRPVRASERKASRLHFAS 153
Cdd:pfam14580 142 LRLLDFRKVKQKERQAAEKMFRS 164
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 407-628 2.20e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504    407 SHSALPGKKTALQAALLETLLDLVDRSWGGCRSLHSNEAFLAQARHILSSVEEFTAAQDSSAMVGEDVGSLALESKSLQS 486
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504    487 RLAEQQQQHAREMSEVTAELHHTHKELDDLRQHLDKSLEENSRLKSLLLSMKKEVK-SADTAATLNLQIAGLQTSVKRL- 564
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEdLEEQIEELSEDIESLAAEIEELe 865

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504    565 --CGEI-VELKQHLEHYDKIQELTQMLQESHSSLVSTNEHLLQELSQVRAQH---RAEVEQMHWSYQELK 628
Cdd:TIGR02168  866 elIEELeSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELeelREKLAQLELRLEGLE 935
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
478-632 2.22e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 2.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504 478 ALESKSLQSRLAEQQQQhAREMSEVTAELHHTHKELDDLRQHLDKSLEENSRLKSLLLSMKKEVKSADTA--------AT 549
Cdd:COG4372  27 AALSEQLRKALFELDKL-QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAElaqaqeelES 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504 550 LNLQIAGLQTSVKRLCGEIVELKQhlehydKIQELTQMLQESHSSLVSTNEhLLQELSQVRAQHRAEVEQMHWSYQELKK 629
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQ------QRKQLEAQIAELQSEIAEREE-ELKELEEQLESLQEELAALEQELQALSE 178


                ...
gi 62901504 630 TMA 632
Cdd:COG4372 179 AEA 181
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 480-609 5.83e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.18  E-value: 5.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504    480 ESKSLQSRLAEQQQQHAREMSEVTAELHHTHKEL---------------------DDLRQHLDKSLEENSRLKSLLLSMK 538
Cdd:pfam15921  360 EARTERDQFSQESGNLDDQLQKLLADLHKREKELslekeqnkrlwdrdtgnsitiDHLRRELDDRNMEVQRLEALLKAMK 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504    539 KEVK---------------SADTAATLNLQIAGLQTSVKRLCGEIVELKQHLEHYDK-IQELTQMLQESHSSLVSTNEHL 602
Cdd:pfam15921  440 SECQgqmerqmaaiqgkneSLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERtVSDLTASLQEKERAIEATNAEI 519


                   ....*..
gi 62901504    603 LQELSQV 609
Cdd:pfam15921  520 TKLRSRV 526
LRRcap smart00446
occurring C-terminal to leucine-rich repeats; A motif occurring C-terminal to leucine-rich ...
 118-135 3.63e-03

occurring C-terminal to leucine-rich repeats; A motif occurring C-terminal to leucine-rich repeats in "sds22-like" and "typical" LRR-containing proteins.


Pssm-ID: 197729  Cd Length: 19  Bit Score: 34.98  E-value: 3.63e-03
                           10
                   ....*....|....*...
gi 62901504    118 PDYRLFVVHLLPKLQQLD 135
Cdd:smart00446   2 AHYREKVIELLPQLRKLD 19
46 PHA02562
endonuclease subunit; Provisional
 488-632 7.37e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.23  E-value: 7.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504  488 LAEQQQQHAREMSEVTAELHHTHKELDDLRQHLDKSLEENSRLKSLLLSMKKEVK---SADTAATLNLQI---------- 554
Cdd:PHA02562 225 LVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyeKGGVCPTCTQQIsegpdritki 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504  555 ----AGLQTSVKRLCGEIVELKQHLEHYD----KIQELTQMLQESHSSLVSTN------EHLLQELSQVRAQHRAEVEQM 620
Cdd:PHA02562 305 kdklKELQHSLEKLDTAIDELEEIMDEFNeqskKLLELKNKISTNKQSLITLVdkakkvKAAIEELQAEFVDNAEELAKL 384

                        170
                 ....*....|..
gi 62901504  621 HWSYQELKKTMA 632
Cdd:PHA02562 385 QDELDKIVKTKS 396
 
Name Accession Description Interval E-value
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 48-145 2.21e-14

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: 72.51  E-value: 2.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504  48 HSLMSLTG-LKSLDLSRNSLVSLEGIQYLTALESLNLYYNCISSLAEVFR-LHALTELVDVDFRLNPVVKvEPDYRLFVV 125
Cdd:cd21340 113 RSLAALSNsLRVLNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELLDlLSSWPSLRELDLTGNPVCK-KPKYRDKII 191

                        90       100
                ....*....|....*....|
gi 62901504 126 HLLPKLQQLDDRPVRASERK 145
Cdd:cd21340 192 LASKSLEVLDGKEITDTERQ 211
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
26-164 1.78e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 69.58  E-value: 1.78e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504  26 DLAELQSLSIPGTyqeKITHLGHSLMSLTGLKSLDLSRNSLVSLEGIQYLTALESLNLYYNCISSLAEVFRLHALTELvd 105
Cdd:COG4886 203 NLTNLEELDLSGN---QLTDLPEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTL-- 277

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62901504 106 vDFRLNPVVKVEPDYRLFVVHLLPKLQQLDDRPVRASERKASRLHFASEDSLDSKESVP 164
Cdd:COG4886 278 -DLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLV 335
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
26-135 1.86e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 69.58  E-value: 1.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504  26 DLAELQSLSIPGTyqeKITHLGHSLMSLTGLKSLDLSRNSLVSL-EGIQYLTALESLNLYYNCISSLAEVFRLHALTELv 104
Cdd:COG4886 180 NLTNLKELDLSNN---QITDLPEPLGNLTNLEELDLSGNQLTDLpEPLANLTNLETLDLSNNQLTDLPELGNLTNLEEL- 255

                        90       100       110
                ....*....|....*....|....*....|.
gi 62901504 105 dvDFRLNPVVKVEPDYRlfvvhlLPKLQQLD 135
Cdd:COG4886 256 --DLSNNQLTDLPPLAN------LTNLKTLD 278
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
26-103 5.68e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 68.04  E-value: 5.68e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504  26 DLAELQSLSIPGTyqeKITHLGHSLMSLTGLKSLDLSRNSLVSL-EGIQYLTALESLNLYYNCISSLAEVF-RLHALTEL 103
Cdd:COG4886 134 NLTNLKELDLSNN---QLTDLPEPLGNLTNLKSLDLSNNQLTDLpEELGNLTNLKELDLSNNQITDLPEPLgNLTNLEEL 210
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
19-103 1.52e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 66.88  E-value: 1.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504  19 SGLGPHRDLAELQSLSIPGTyqeKITHLGHSLMSLTGLKSLDLSRNSLVSL-EGIQYLTALESLNLYYNCISSL-AEVFR 96
Cdd:COG4886 104 SGNEELSNLTNLESLDLSGN---QLTDLPEELANLTNLKELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLpEELGN 180


                ....*..
gi 62901504  97 LHALTEL 103
Cdd:COG4886 181 LTNLKEL 187
LRR_9 pfam14580
Leucine-rich repeat;
53-153 1.81e-10

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 60.16  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504    53 LTGLKSLDLSRNSLVSL-EGI-QYLTALESLNLYYNCISSLAEVFRLHALTELVDVDFRLNPVVKvEPDYRLFVVHLLPK 130
Cdd:pfam14580  63 LRRLKTLLLNNNRICRIgEGLgEALPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTN-KPHYRLYVIYKVPQ 141

                          90       100
                  ....*....|....*....|...
gi 62901504   131 LQQLDDRPVRASERKASRLHFAS 153
Cdd:pfam14580 142 LRLLDFRKVKQKERQAAEKMFRS 164
LRR_8 pfam13855
Leucine rich repeat;
54-103 5.96e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 44.05  E-value: 5.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 62901504    54 TGLKSLDLSRNSLVSLEG--IQYLTALESLNLYYNCISSL-AEVFR-LHALTEL 103
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLLTTLsPGAFSgLPSLRYL 54
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
24-135 4.91e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 46.08  E-value: 4.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504  24 HRDLAELQSLSIPGTYQEKITHLGHSLMSLTGLKSLDLSRNslvslEGIQYLTALESLNLYYNCISSL-AEVFRLHALTE 102
Cdd:COG4886  66 LLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN-----EELSNLTNLESLDLSGNQLTDLpEELANLTNLKE 140

                        90       100       110
                ....*....|....*....|....*....|...
gi 62901504 103 LvdvDFRLNPVVKVEPDyrlfvVHLLPKLQQLD 135
Cdd:COG4886 141 L---DLSNNQLTDLPEP-----LGNLTNLKSLD 165
LRR_8 pfam13855
Leucine rich repeat;
29-86 7.51e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.97  E-value: 7.51e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62901504    29 ELQSLSIPGTYqekITHLG-HSLMSLTGLKSLDLSRNSLVSLEG--IQYLTALESLNLYYN 86
Cdd:pfam13855   2 NLRSLDLSNNR---LTSLDdGAFKGLSNLKVLDLSNNLLTTLSPgaFSGLPSLRYLDLSGN 59
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 41-103 1.23e-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: 43.62  E-value: 1.23e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62901504  41 EKITHLGhslmSLTGLKSLDLSRNSLVSLEGIQYLTALESLNLYYNCISSLAEVFRLHALTEL 103
Cdd:cd21340  37 TKIENLE----FLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVEGLENLTNLEEL 95
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 54-93 1.24e-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: 39.92  E-value: 1.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 62901504    54 TGLKSLDLSRNSLVSLEGIQYLTALESLNLYYN-CISSLAE 93
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSD 41
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 407-628 2.20e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504    407 SHSALPGKKTALQAALLETLLDLVDRSWGGCRSLHSNEAFLAQARHILSSVEEFTAAQDSSAMVGEDVGSLALESKSLQS 486
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504    487 RLAEQQQQHAREMSEVTAELHHTHKELDDLRQHLDKSLEENSRLKSLLLSMKKEVK-SADTAATLNLQIAGLQTSVKRL- 564
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEdLEEQIEELSEDIESLAAEIEELe 865

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504    565 --CGEI-VELKQHLEHYDKIQELTQMLQESHSSLVSTNEHLLQELSQVRAQH---RAEVEQMHWSYQELK 628
Cdd:TIGR02168  866 elIEELeSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELeelREKLAQLELRLEGLE 935
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
478-632 2.22e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 2.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504 478 ALESKSLQSRLAEQQQQhAREMSEVTAELHHTHKELDDLRQHLDKSLEENSRLKSLLLSMKKEVKSADTA--------AT 549
Cdd:COG4372  27 AALSEQLRKALFELDKL-QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAElaqaqeelES 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504 550 LNLQIAGLQTSVKRLCGEIVELKQhlehydKIQELTQMLQESHSSLVSTNEhLLQELSQVRAQHRAEVEQMHWSYQELKK 629
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQ------QRKQLEAQIAELQSEIAEREE-ELKELEEQLESLQEELAALEQELQALSE 178


                ...
gi 62901504 630 TMA 632
Cdd:COG4372 179 AEA 181
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 480-609 5.83e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.18  E-value: 5.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504    480 ESKSLQSRLAEQQQQHAREMSEVTAELHHTHKEL---------------------DDLRQHLDKSLEENSRLKSLLLSMK 538
Cdd:pfam15921  360 EARTERDQFSQESGNLDDQLQKLLADLHKREKELslekeqnkrlwdrdtgnsitiDHLRRELDDRNMEVQRLEALLKAMK 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504    539 KEVK---------------SADTAATLNLQIAGLQTSVKRLCGEIVELKQHLEHYDK-IQELTQMLQESHSSLVSTNEHL 602
Cdd:pfam15921  440 SECQgqmerqmaaiqgkneSLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERtVSDLTASLQEKERAIEATNAEI 519


                   ....*..
gi 62901504    603 LQELSQV 609
Cdd:pfam15921  520 TKLRSRV 526
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 473-619 2.84e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504 473 DVGSLALESKSLQSRLAEQQQQHA---REMSEVTAELHHTHKELDDLRQ-HLDKSLEENSRLKSLLLSMKKEVKSADTAA 548
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEeleAELEELEAELAELEAELEELRLeLEELELELEEAQAEEYELLAELARLEQDIA 305

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62901504 549 TLNLQIAGLQTSVKRLCGEIVELKQHLE-HYDKIQELTQMLQESHSSLVSTNEHLLQELSQVRAQHRAEVEQ 619
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
LRRcap smart00446
occurring C-terminal to leucine-rich repeats; A motif occurring C-terminal to leucine-rich ...
 118-135 3.63e-03

occurring C-terminal to leucine-rich repeats; A motif occurring C-terminal to leucine-rich repeats in "sds22-like" and "typical" LRR-containing proteins.


Pssm-ID: 197729  Cd Length: 19  Bit Score: 34.98  E-value: 3.63e-03
                           10
                   ....*....|....*...
gi 62901504    118 PDYRLFVVHLLPKLQQLD 135
Cdd:smart00446   2 AHYREKVIELLPQLRKLD 19
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 452-633 6.26e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 6.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504    452 HILSSVEEFTAAQDSSAMVGEDVGSLALESKSLQSRLAEQQQQHAR---EMSEVTAELHHTHKELDDLRQHLDKsleens 528
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEElrlEVSELEEEIEELQKELYALANEISR------ 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504    529 rlksllLSMKKEVKSAdtaatlnlQIAGLQTSVKRLCGEIVELKQHLEHY----DKIQELTQMLQESHSSL---VSTNEH 601
Cdd:TIGR02168  300 ------LEQQKQILRE--------RLANLERQLEELEAQLEELESKLDELaeelAELEEKLEELKEELESLeaeLEELEA 365

                          170       180       190
                   ....*....|....*....|....*....|..
gi 62901504    602 LLQELSQVRAQHRAEVEQMHWSYQELKKTMAL 633
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIAS 397
46 PHA02562
endonuclease subunit; Provisional
 488-632 7.37e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.23  E-value: 7.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504  488 LAEQQQQHAREMSEVTAELHHTHKELDDLRQHLDKSLEENSRLKSLLLSMKKEVK---SADTAATLNLQI---------- 554
Cdd:PHA02562 225 LVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyeKGGVCPTCTQQIsegpdritki 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62901504  555 ----AGLQTSVKRLCGEIVELKQHLEHYD----KIQELTQMLQESHSSLVSTN------EHLLQELSQVRAQHRAEVEQM 620
Cdd:PHA02562 305 kdklKELQHSLEKLDTAIDELEEIMDEFNeqskKLLELKNKISTNKQSLITLVdkakkvKAAIEELQAEFVDNAEELAKL 384

                        170
                 ....*....|..
gi 62901504  621 HWSYQELKKTMA 632
Cdd:PHA02562 385 QDELDKIVKTKS 396
 
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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