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Conserved domains on  [gi|530378853|ref|XP_005248379|]
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centrosomal protein of 72 kDa isoform X2 [Homo sapiens]

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 ...
 6-95 7.66e-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: 70.97  E-value: 7.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   6 LKSLDLSRNSLVSLEGIQYLTALESLNLYYNCISSLAEVFR-LHALTELVDVDFRLNPVVKvEPDYRLFVVHLLPKLQQL 84
Cdd:cd21340  122 LRVLNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELLDlLSSWPSLRELDLTGNPVCK-KPKYRDKIILASKSLEVL 200

                         90
                 ....*....|.
gi 530378853  85 DDRPVRASERK 95
Cdd:cd21340  201 DGKEITDTERQ 211
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 357-578 2.09e-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: 2.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   357 SHSALPGKKTALQAALLETLLDLVDRSWGGCRSLHSNEAFLAQARHILSSVEEFTAAQDSSAMVGEDVGSLALESKSLQS 436
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   437 RLAEQQQQHAREMSEVTAELHHTHKELDDLRQHLDKSLEENSRLKSLLLSMKKEVK-SADTAATLNLQIAGLQTSVKRL- 514
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEdLEEQIEELSEDIESLAAEIEELe 865

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   515 --CGEI-VELKQHLEHYDKIQELTQMLQESHSSLVSTNEHLLQELSQVRAQH---RAEVEQMHWSYQELK 578
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 ...
 6-95 7.66e-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: 70.97  E-value: 7.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   6 LKSLDLSRNSLVSLEGIQYLTALESLNLYYNCISSLAEVFR-LHALTELVDVDFRLNPVVKvEPDYRLFVVHLLPKLQQL 84
Cdd:cd21340  122 LRVLNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELLDlLSSWPSLRELDLTGNPVCK-KPKYRDKIILASKSLEVL 200

                         90
                 ....*....|.
gi 530378853  85 DDRPVRASERK 95
Cdd:cd21340  201 DGKEITDTERQ 211
LRR_9 pfam14580
Leucine-rich repeat;
3-103 1.66e-10

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 60.16  E-value: 1.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853    3 LTGLKSLDLSRNSLVSL-EGI-QYLTALESLNLYYNCISSLAEVFRLHALTELVDVDFRLNPVVKvEPDYRLFVVHLLPK 80
Cdd:pfam14580  63 LRRLKTLLLNNNRICRIgEGLgEALPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTN-KPHYRLYVIYKVPQ 141

                          90       100
                  ....*....|....*....|...
gi 530378853   81 LQQLDDRPVRASERKASRLHFAS 103
Cdd:pfam14580 142 LRLLDFRKVKQKERQAAEKMFRS 164
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
3-85 7.92e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 58.02  E-value: 7.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   3 LTGLKSLDLSRNSLVSL-EGIQYLTALESLNLYYNCISSLAEVFRLHALTELvdvDFRLNPVVKVEPDYRlfvvhlLPKL 81
Cdd:COG4886  204 LTNLEELDLSGNQLTDLpEPLANLTNLETLDLSNNQLTDLPELGNLTNLEEL---DLSNNQLTDLPPLAN------LTNL 274


                 ....
gi 530378853  82 QQLD 85
Cdd:COG4886  275 KTLD 278
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 357-578 2.09e-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: 2.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   357 SHSALPGKKTALQAALLETLLDLVDRSWGGCRSLHSNEAFLAQARHILSSVEEFTAAQDSSAMVGEDVGSLALESKSLQS 436
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   437 RLAEQQQQHAREMSEVTAELHHTHKELDDLRQHLDKSLEENSRLKSLLLSMKKEVK-SADTAATLNLQIAGLQTSVKRL- 514
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEdLEEQIEELSEDIESLAAEIEELe 865

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   515 --CGEI-VELKQHLEHYDKIQELTQMLQESHSSLVSTNEHLLQELSQVRAQH---RAEVEQMHWSYQELK 578
Cdd:TIGR02168  866 elIEELeSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELeelREKLAQLELRLEGLE 935
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
428-582 2.36e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853 428 ALESKSLQSRLAEQQQQhAREMSEVTAELHHTHKELDDLRQHLDKSLEENSRLKSLLLSMKKEVKSADTA-ATLNLQIAG 506
Cdd:COG4372   27 AALSEQLRKALFELDKL-QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAElAQAQEELES 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530378853 507 LQTSVKRLCGEIVELKQHLEHYDKIQELTQMLQESHSSLVSTNEHLLQELSQVRAQHRAEVEQMHWSYQELKKTMA 582
Cdd:COG4372  106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 430-559 5.95e-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: 5.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   430 ESKSLQSRLAEQQQQHAREMSEVTAELHHTHKEL---------------------DDLRQHLDKSLEENSRLKSLLLSMK 488
Cdd:pfam15921  360 EARTERDQFSQESGNLDDQLQKLLADLHKREKELslekeqnkrlwdrdtgnsitiDHLRRELDDRNMEVQRLEALLKAMK 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   489 KEVK---------------SADTAATLNLQIAGLQTSVKRLCGEIVELKQHLEHYDK-IQELTQMLQESHSSLVSTNEHL 552
Cdd:pfam15921  440 SECQgqmerqmaaiqgkneSLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERtVSDLTASLQEKERAIEATNAEI 519


                   ....*..
gi 530378853   553 LQELSQV 559
Cdd:pfam15921  520 TKLRSRV 526
LRRcap smart00446
occurring C-terminal to leucine-rich repeats; A motif occurring C-terminal to leucine-rich ...
 68-85 3.20e-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: 3.20e-03
                           10
                   ....*....|....*...
gi 530378853    68 PDYRLFVVHLLPKLQQLD 85
Cdd:smart00446   2 AHYREKVIELLPQLRKLD 19
46 PHA02562
endonuclease subunit; Provisional
 438-582 6.64e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.23  E-value: 6.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853 438 LAEQQQQHAREMSEVTAELHHTHKELDDLRQHLDKSLEENSRLKSLLLSMKKEVK---SADTAATLNLQI---------- 504
Cdd:PHA02562 225 LVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyeKGGVCPTCTQQIsegpdritki 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853 505 ----AGLQTSVKRLCGEIVELKQHLEHYD----KIQELTQMLQESHSSLVSTN------EHLLQELSQVRAQHRAEVEQM 570
Cdd:PHA02562 305 kdklKELQHSLEKLDTAIDELEEIMDEFNeqskKLLELKNKISTNKQSLITLVdkakkvKAAIEELQAEFVDNAEELAKL 384

                        170
                 ....*....|..
gi 530378853 571 HWSYQELKKTMA 582
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 ...
 6-95 7.66e-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: 70.97  E-value: 7.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   6 LKSLDLSRNSLVSLEGIQYLTALESLNLYYNCISSLAEVFR-LHALTELVDVDFRLNPVVKvEPDYRLFVVHLLPKLQQL 84
Cdd:cd21340  122 LRVLNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELLDlLSSWPSLRELDLTGNPVCK-KPKYRDKIILASKSLEVL 200

                         90
                 ....*....|.
gi 530378853  85 DDRPVRASERK 95
Cdd:cd21340  201 DGKEITDTERQ 211
LRR_9 pfam14580
Leucine-rich repeat;
3-103 1.66e-10

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 60.16  E-value: 1.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853    3 LTGLKSLDLSRNSLVSL-EGI-QYLTALESLNLYYNCISSLAEVFRLHALTELVDVDFRLNPVVKvEPDYRLFVVHLLPK 80
Cdd:pfam14580  63 LRRLKTLLLNNNRICRIgEGLgEALPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTN-KPHYRLYVIYKVPQ 141

                          90       100
                  ....*....|....*....|...
gi 530378853   81 LQQLDDRPVRASERKASRLHFAS 103
Cdd:pfam14580 142 LRLLDFRKVKQKERQAAEKMFRS 164
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
3-85 7.92e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 58.02  E-value: 7.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   3 LTGLKSLDLSRNSLVSL-EGIQYLTALESLNLYYNCISSLAEVFRLHALTELvdvDFRLNPVVKVEPDYRlfvvhlLPKL 81
Cdd:COG4886  204 LTNLEELDLSGNQLTDLpEPLANLTNLETLDLSNNQLTDLPELGNLTNLEEL---DLSNNQLTDLPPLAN------LTNL 274


                 ....
gi 530378853  82 QQLD 85
Cdd:COG4886  275 KTLD 278
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
2-114 1.89e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 56.87  E-value: 1.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   2 SLTGLKSLDLSRNSLVSLEGIQYLTALESLNLYYNCISSLAEVFRLHALTELvdvDFRLNPVVKVEPDYRLFVVHLLPKL 81
Cdd:COG4886  226 NLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTL---DLSNNQLTDLKLKELELLLGLNSLL 302

                         90       100       110
                 ....*....|....*....|....*....|...
gi 530378853  82 QQLDDRPVRASERKASRLHFASEDSLDSKESVP 114
Cdd:COG4886  303 LLLLLLNLLELLILLLLLTTLLLLLLLLKGLLV 335
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
2-53 6.28e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 55.32  E-value: 6.28e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530378853   2 SLTGLKSLDLSRNSLVSL-EGIQYLTALESLNLYYNCISSLAEVF-RLHALTEL 53
Cdd:COG4886  157 NLTNLKSLDLSNNQLTDLpEELGNLTNLKELDLSNNQITDLPEPLgNLTNLEEL 210
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
2-53 2.57e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 53.40  E-value: 2.57e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530378853   2 SLTGLKSLDLSRNSLVSL-EGIQYLTALESLNLYYNCISSL-AEVFRLHALTEL 53
Cdd:COG4886  134 NLTNLKELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLpEELGNLTNLKEL 187
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
2-85 5.71e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 52.24  E-value: 5.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   2 SLTGLKSLDLSRNSLVSL-EGIQYLTALESLNLYYNCISSLAEVF-RLHALTELvdvDFRLNPVVKvepdyrLFVVHLLP 79
Cdd:COG4886  180 NLTNLKELDLSNNQITDLpEPLGNLTNLEELDLSGNQLTDLPEPLaNLTNLETL---DLSNNQLTD------LPELGNLT 250


                 ....*.
gi 530378853  80 KLQQLD 85
Cdd:COG4886  251 NLEELD 256
LRR_8 pfam13855
Leucine rich repeat;
4-53 4.97e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 44.05  E-value: 4.97e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530378853    4 TGLKSLDLSRNSLVSLEG--IQYLTALESLNLYYNCISSL-AEVFR-LHALTEL 53
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLLTTLsPGAFSgLPSLRYL 54
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 4-43 1.16e-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: 1.16e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 530378853    4 TGLKSLDLSRNSLVSLEGIQYLTALESLNLYYN-CISSLAE 43
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSD 41
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
2-85 1.50e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.54  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   2 SLTGLKSLDLSRNslvslEGIQYLTALESLNLYYNCISSL-AEVFRLHALTELvdvDFRLNPVVKVEPDyrlfvVHLLPK 80
Cdd:COG4886   94 DLTNLTELDLSGN-----EELSNLTNLESLDLSGNQLTDLpEELANLTNLKEL---DLSNNQLTDLPEP-----LGNLTN 160


                 ....*
gi 530378853  81 LQQLD 85
Cdd:COG4886  161 LKSLD 165
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 357-578 2.09e-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: 2.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   357 SHSALPGKKTALQAALLETLLDLVDRSWGGCRSLHSNEAFLAQARHILSSVEEFTAAQDSSAMVGEDVGSLALESKSLQS 436
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   437 RLAEQQQQHAREMSEVTAELHHTHKELDDLRQHLDKSLEENSRLKSLLLSMKKEVK-SADTAATLNLQIAGLQTSVKRL- 514
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEdLEEQIEELSEDIESLAAEIEELe 865

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   515 --CGEI-VELKQHLEHYDKIQELTQMLQESHSSLVSTNEHLLQELSQVRAQH---RAEVEQMHWSYQELK 578
Cdd:TIGR02168  866 elIEELeSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELeelREKLAQLELRLEGLE 935
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
428-582 2.36e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853 428 ALESKSLQSRLAEQQQQhAREMSEVTAELHHTHKELDDLRQHLDKSLEENSRLKSLLLSMKKEVKSADTA-ATLNLQIAG 506
Cdd:COG4372   27 AALSEQLRKALFELDKL-QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAElAQAQEELES 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530378853 507 LQTSVKRLCGEIVELKQHLEHYDKIQELTQMLQESHSSLVSTNEHLLQELSQVRAQHRAEVEQMHWSYQELKKTMA 582
Cdd:COG4372  106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 430-559 5.95e-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: 5.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   430 ESKSLQSRLAEQQQQHAREMSEVTAELHHTHKEL---------------------DDLRQHLDKSLEENSRLKSLLLSMK 488
Cdd:pfam15921  360 EARTERDQFSQESGNLDDQLQKLLADLHKREKELslekeqnkrlwdrdtgnsitiDHLRRELDDRNMEVQRLEALLKAMK 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   489 KEVK---------------SADTAATLNLQIAGLQTSVKRLCGEIVELKQHLEHYDK-IQELTQMLQESHSSLVSTNEHL 552
Cdd:pfam15921  440 SECQgqmerqmaaiqgkneSLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERtVSDLTASLQEKERAIEATNAEI 519


                   ....*..
gi 530378853   553 LQELSQV 559
Cdd:pfam15921  520 TKLRSRV 526
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 2-53 6.10e-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: 6.10e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530378853   2 SLTGLKSLDLSRNSLVSLEGIQYLTALESLNLYYNCISSLAEVFRLHALTEL 53
Cdd:cd21340   44 FLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVEGLENLTNLEEL 95
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 423-569 2.34e-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: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853 423 DVGSLALESKSLQSRLAEQQQQHA---REMSEVTAELHHTHKELDDLRQ-HLDKSLEENSRLKSLLLSMKKEVKSADTAA 498
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELEeleAELEELEAELAELEAELEELRLeLEELELELEEAQAEEYELLAELARLEQDIA 305

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530378853 499 TLNLQIAGLQTSVKRLCGEIVELKQHLE-HYDKIQELTQMLQESHSSLVSTNEHLLQELSQVRAQHRAEVEQ 569
Cdd:COG1196  306 RLEERRRELEERLEELEEELAELEEELEeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
LRR_8 pfam13855
Leucine rich repeat;
2-36 3.11e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 36.35  E-value: 3.11e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 530378853    2 SLTGLKSLDLSRNSLVSLEG--IQYLTALESLNLYYN 36
Cdd:pfam13855  23 GLSNLKVLDLSNNLLTTLSPgaFSGLPSLRYLDLSGN 59
LRRcap smart00446
occurring C-terminal to leucine-rich repeats; A motif occurring C-terminal to leucine-rich ...
 68-85 3.20e-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: 3.20e-03
                           10
                   ....*....|....*...
gi 530378853    68 PDYRLFVVHLLPKLQQLD 85
Cdd:smart00446   2 AHYREKVIELLPQLRKLD 19
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 402-583 6.03e-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: 6.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   402 HILSSVEEFTAAQDSSAMVGEDVGSLALESKSLQSRLAEQQQQHAR---EMSEVTAELHHTHKELDDLRQHLDKsleens 478
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEElrlEVSELEEEIEELQKELYALANEISR------ 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853   479 rlksllLSMKKEVKSAdtaatlnlQIAGLQTSVKRLCGEIVELKQHLEHY----DKIQELTQMLQESHSSL---VSTNEH 551
Cdd:TIGR02168  300 ------LEQQKQILRE--------RLANLERQLEELEAQLEELESKLDELaeelAELEEKLEELKEELESLeaeLEELEA 365

                          170       180       190
                   ....*....|....*....|....*....|..
gi 530378853   552 LLQELSQVRAQHRAEVEQMHWSYQELKKTMAL 583
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIAS 397
46 PHA02562
endonuclease subunit; Provisional
 438-582 6.64e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.23  E-value: 6.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853 438 LAEQQQQHAREMSEVTAELHHTHKELDDLRQHLDKSLEENSRLKSLLLSMKKEVK---SADTAATLNLQI---------- 504
Cdd:PHA02562 225 LVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyeKGGVCPTCTQQIsegpdritki 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853 505 ----AGLQTSVKRLCGEIVELKQHLEHYD----KIQELTQMLQESHSSLVSTN------EHLLQELSQVRAQHRAEVEQM 570
Cdd:PHA02562 305 kdklKELQHSLEKLDTAIDELEEIMDEFNeqskKLLELKNKISTNKQSLITLVdkakkvKAAIEELQAEFVDNAEELAKL 384

                        170
                 ....*....|..
gi 530378853 571 HWSYQELKKTMA 582
Cdd:PHA02562 385 QDELDKIVKTKS 396
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 395-582 9.95e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.59  E-value: 9.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853 395 AFLAQARHILSSVEEFTAAQDSSAMVGEDVGSLALESKSLQSRLAEQQQQhareMSEVTAELHHTHKELDDLRQHLDKSL 474
Cdd:COG4942   14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378853 475 EENSRLKSLLLSMKKEVK-------------------SADTAATLNLQIAGLQTSVKRLCGEIVELKQHLEHYDKIQELT 535
Cdd:COG4942   90 KEIAELRAELEAQKEELAellralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 530378853 536 QMLQESHSSLVSTNEHLLQELSQVRAQHRAEVEQMHWSYQELKKTMA 582
Cdd:COG4942  170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
 
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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