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Conserved domains on  [gi|341940537|sp|Q9D3R3|]
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RecName: Full=Centrosomal protein of 72 kDa; Short=Cep72

Protein Classification

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 ...
 42-144 1.17e-13

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: 70.59  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537  42 ITHLGNSLMHLtalkslDLSRNSLVSLEGIQYLVSLESLNLYYNCISSLAEVFR-LHTLLELQDVDFRLNPVVKNeSDYR 120
Cdd:cd21340  115 LAALSNSLRVL------NISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELLDlLSSWPSLRELDLTGNPVCKK-PKYR 187

                         90       100
                 ....*....|....*....|....
gi 341940537 121 LFVVHMLPKLRQLDDRPVRESERK 144
Cdd:cd21340  188 DKIILASKSLEVLDGKEITDTERQ 211
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
476-631 3.25e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537 476 LSLENKTLQSRLAEQQQQYTATVTKMTAELNNTKRELDTLRQHLDKSLEENSHLKSLLYNVKKEVKTADTS-TALTLQIT 554
Cdd:COG4372   18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlQAAQAELA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537 555 GLQASMKQLSGEVVELKQHVEH----YDKIQELTQMLQESHSSL---VSTNEHLLQELSRTRAQHRAEVEQMRWSFQEFK 627
Cdd:COG4372   98 QAQEELESLQEEAEELQEELEElqkeRQDLEQQRKQLEAQIAELqseIAEREEELKELEEQLESLQEELAALEQELQALS 177


                 ....
gi 341940537 628 KTTA 631
Cdd:COG4372  178 EAEA 181
 
Name Accession Description Interval E-value
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 42-144 1.17e-13

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: 70.59  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537  42 ITHLGNSLMHLtalkslDLSRNSLVSLEGIQYLVSLESLNLYYNCISSLAEVFR-LHTLLELQDVDFRLNPVVKNeSDYR 120
Cdd:cd21340  115 LAALSNSLRVL------NISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELLDlLSSWPSLRELDLTGNPVCKK-PKYR 187

                         90       100
                 ....*....|....*....|....
gi 341940537 121 LFVVHMLPKLRQLDDRPVRESERK 144
Cdd:cd21340  188 DKIILASKSLEVLDGKEITDTERQ 211
LRR_9 pfam14580
Leucine-rich repeat;
51-150 2.68e-11

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 62.47  E-value: 2.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537   51 HLTALKSLDLSRNSLVSL-EGI-QYLVSLESLNLYYNCISSLAEVFRLHTLLELQDVDFRLNPVVkNESDYRLFVVHMLP 128
Cdd:pfam14580  62 LLRRLKTLLLNNNRICRIgEGLgEALPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVT-NKPHYRLYVIYKVP 140

                          90       100
                  ....*....|....*....|..
gi 341940537  129 KLRQLDDRPVRESERKASQLHF 150
Cdd:pfam14580 141 QLRLLDFRKVKQKERQAAEKMF 162
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
25-112 4.57e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 62.26  E-value: 4.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537  25 DLAELRSLSIPGTyqeKITHLGNSLMHLTALKSLDLSRNSLVSLEGIQYLVSLESLNLYYNCISSLAEVFRLHtllELQD 104
Cdd:COG4886  203 NLTNLEELDLSGN---QLTDLPEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLT---NLKT 276


                 ....*...
gi 341940537 105 VDFRLNPV 112
Cdd:COG4886  277 LDLSNNQL 284
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
476-631 3.25e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537 476 LSLENKTLQSRLAEQQQQYTATVTKMTAELNNTKRELDTLRQHLDKSLEENSHLKSLLYNVKKEVKTADTS-TALTLQIT 554
Cdd:COG4372   18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlQAAQAELA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537 555 GLQASMKQLSGEVVELKQHVEH----YDKIQELTQMLQESHSSL---VSTNEHLLQELSRTRAQHRAEVEQMRWSFQEFK 627
Cdd:COG4372   98 QAQEELESLQEEAEELQEELEElqkeRQDLEQQRKQLEAQIAELqseIAEREEELKELEEQLESLQEELAALEQELQALS 177


                 ....
gi 341940537 628 KTTA 631
Cdd:COG4372  178 EAEA 181
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 479-589 1.35e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.93  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537  479 ENKTLQSR---LAEQQQQYTATVTKMTAELNNTKRELDTLRQHLDKSLEENSHLKSLLYNVKKEVKTADTstaltlQITG 555
Cdd:TIGR04523 212 KNKSLESQiseLKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK------KIKE 285

                          90       100       110
                  ....*....|....*....|....*....|....
gi 341940537  556 LQASMKQLSGEVVELKQhvehyDKIQELTQMLQE 589
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNN-----QKEQDWNKELKS 314
LRRcap smart00446
occurring C-terminal to leucine-rich repeats; A motif occurring C-terminal to leucine-rich ...
 117-134 1.36e-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: 36.13  E-value: 1.36e-03
                           10
                   ....*....|....*...
gi 341940537   117 SDYRLFVVHMLPKLRQLD 134
Cdd:smart00446   2 AHYREKVIELLPQLRKLD 19
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 443-560 4.12e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 39.66  E-value: 4.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537 443 EAFLAQAKHVLSSLQEF-TATRD------------SSALEKEGIGYLSLENKTLQSRLAEQQQQYTAtvtKMTAELNNTK 509
Cdd:cd22656  131 KKYQDKAAKVVDKLTDFeNQTEKdqtaletlekalKDLLTDEGGAIARKEIKDLQKELEKLNEEYAA---KLKAKIDELK 207

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 341940537 510 RELDTLRQHLdksleenshlksllynvKKEVKTADTSTALTLQITGLQASM 560
Cdd:cd22656  208 ALIADDEAKL-----------------AAALRLIADLTAADTDLDNLLALI 241
 
Name Accession Description Interval E-value
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 42-144 1.17e-13

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: 70.59  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537  42 ITHLGNSLMHLtalkslDLSRNSLVSLEGIQYLVSLESLNLYYNCISSLAEVFR-LHTLLELQDVDFRLNPVVKNeSDYR 120
Cdd:cd21340  115 LAALSNSLRVL------NISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELLDlLSSWPSLRELDLTGNPVCKK-PKYR 187

                         90       100
                 ....*....|....*....|....
gi 341940537 121 LFVVHMLPKLRQLDDRPVRESERK 144
Cdd:cd21340  188 DKIILASKSLEVLDGKEITDTERQ 211
LRR_9 pfam14580
Leucine-rich repeat;
51-150 2.68e-11

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 62.47  E-value: 2.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537   51 HLTALKSLDLSRNSLVSL-EGI-QYLVSLESLNLYYNCISSLAEVFRLHTLLELQDVDFRLNPVVkNESDYRLFVVHMLP 128
Cdd:pfam14580  62 LLRRLKTLLLNNNRICRIgEGLgEALPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVT-NKPHYRLYVIYKVP 140

                          90       100
                  ....*....|....*....|..
gi 341940537  129 KLRQLDDRPVRESERKASQLHF 150
Cdd:pfam14580 141 QLRLLDFRKVKQKERQAAEKMF 162
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
25-112 4.57e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 62.26  E-value: 4.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537  25 DLAELRSLSIPGTyqeKITHLGNSLMHLTALKSLDLSRNSLVSLEGIQYLVSLESLNLYYNCISSLAEVFRLHtllELQD 104
Cdd:COG4886  203 NLTNLEELDLSGN---QLTDLPEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLT---NLKT 276


                 ....*...
gi 341940537 105 VDFRLNPV 112
Cdd:COG4886  277 LDLSNNQL 284
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
25-102 1.65e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 60.33  E-value: 1.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537  25 DLAELRSLSIPGTyqeKITHLGNSLMHLTALKSLDLSRNSLVSL-EGIQYLVSLESLNLYYNCISSLAEVF-RLHTLLEL 102
Cdd:COG4886  134 NLTNLKELDLSNN---QLTDLPEPLGNLTNLKSLDLSNNQLTDLpEELGNLTNLKELDLSNNQITDLPEPLgNLTNLEEL 210
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
25-102 1.11e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 57.64  E-value: 1.11e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341940537  25 DLAELRSLSIPGTyqeKITHLGNSLMHLTALKSLDLSRNSLVSL-EGIQYLVSLESLNLYYNCISSLAEVFRLHTLLEL 102
Cdd:COG4886  180 NLTNLKELDLSNN---QITDLPEPLGNLTNLEELDLSGNQLTDLpEPLANLTNLETLDLSNNQLTDLPELGNLTNLEEL 255
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
18-102 1.69e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 57.25  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537  18 SGLGPHRDLAELRSLSIPGTyqeKITHLGNSLMHLTALKSLDLSRNSLVSL-EGIQYLVSLESLNLYYNCISSL-AEVFR 95
Cdd:COG4886  104 SGNEELSNLTNLESLDLSGN---QLTDLPEELANLTNLKELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLpEELGN 180


                 ....*..
gi 341940537  96 LHTLLEL 102
Cdd:COG4886  181 LTNLKEL 187
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
25-90 8.05e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 45.31  E-value: 8.05e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341940537  25 DLAELRSLSIPGTyqeKITHLGnSLMHLTALKSLDLSRNSLVSLEGIQYLVSLESLNLYYNCISSL 90
Cdd:COG4886  226 NLTNLETLDLSNN---QLTDLP-ELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQLTDL 287
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
476-631 3.25e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537 476 LSLENKTLQSRLAEQQQQYTATVTKMTAELNNTKRELDTLRQHLDKSLEENSHLKSLLYNVKKEVKTADTS-TALTLQIT 554
Cdd:COG4372   18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlQAAQAELA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537 555 GLQASMKQLSGEVVELKQHVEH----YDKIQELTQMLQESHSSL---VSTNEHLLQELSRTRAQHRAEVEQMRWSFQEFK 627
Cdd:COG4372   98 QAQEELESLQEEAEELQEELEElqkeRQDLEQQRKQLEAQIAELqseIAEREEELKELEEQLESLQEELAALEQELQALS 177


                 ....
gi 341940537 628 KTTA 631
Cdd:COG4372  178 EAEA 181
LRR_8 pfam13855
Leucine rich repeat;
28-85 3.69e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 39.04  E-value: 3.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940537   28 ELRSLSIPGTYqekITHLGN-SLMHLTALKSLDLSRNSLVSLEG--IQYLVSLESLNLYYN 85
Cdd:pfam13855   2 NLRSLDLSNNR---LTSLDDgAFKGLSNLKVLDLSNNLLTTLSPgaFSGLPSLRYLDLSGN 59
LRR_8 pfam13855
Leucine rich repeat;
55-90 9.86e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.89  E-value: 9.86e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 341940537   55 LKSLDLSRNSLVSLEG--IQYLVSLESLNLYYNCISSL 90
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLLTTL 40
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 40-103 1.07e-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: 40.92  E-value: 1.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341940537  40 EKITHLGNslmhLTALKSLDLSRNSLVSLEGIQYLVSLESLNLYYNCISSLAEVFRLHTLLELQ 103
Cdd:cd21340   37 TKIENLEF----LTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVEGLENLTNLEELH 96
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 53-92 1.26e-03

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


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 36.84  E-value: 1.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 341940537   53 TALKSLDLSRNSLVSLEGIQYLVSLESLNLYYN-CISSLAE 92
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSD 41
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 479-589 1.35e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.93  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537  479 ENKTLQSR---LAEQQQQYTATVTKMTAELNNTKRELDTLRQHLDKSLEENSHLKSLLYNVKKEVKTADTstaltlQITG 555
Cdd:TIGR04523 212 KNKSLESQiseLKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK------KIKE 285

                          90       100       110
                  ....*....|....*....|....*....|....
gi 341940537  556 LQASMKQLSGEVVELKQhvehyDKIQELTQMLQE 589
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNN-----QKEQDWNKELKS 314
LRRcap smart00446
occurring C-terminal to leucine-rich repeats; A motif occurring C-terminal to leucine-rich ...
 117-134 1.36e-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: 36.13  E-value: 1.36e-03
                           10
                   ....*....|....*...
gi 341940537   117 SDYRLFVVHMLPKLRQLD 134
Cdd:smart00446   2 AHYREKVIELLPQLRKLD 19
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 443-560 4.12e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 39.66  E-value: 4.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537 443 EAFLAQAKHVLSSLQEF-TATRD------------SSALEKEGIGYLSLENKTLQSRLAEQQQQYTAtvtKMTAELNNTK 509
Cdd:cd22656  131 KKYQDKAAKVVDKLTDFeNQTEKdqtaletlekalKDLLTDEGGAIARKEIKDLQKELEKLNEEYAA---KLKAKIDELK 207

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 341940537 510 RELDTLRQHLdksleenshlksllynvKKEVKTADTSTALTLQITGLQASM 560
Cdd:cd22656  208 ALIADDEAKL-----------------AAALRLIADLTAADTDLDNLLALI 241
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
469-619 7.02e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 7.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537 469 EKEGIGYLSLENKTLQSRLAEQQQQYTATvtkmTAELNNTKRELDTLRQHLDKSLEENShlksllynvkkEVKTADTSTA 548
Cdd:COG3206  203 QKNGLVDLSEEAKLLLQQLSELESQLAEA----RAELAEAEARLAALRAQLGSGPDALP-----------ELLQSPVIQQ 267

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341940537 549 LTLQITGLQASMKQLSG-------EVVELKQHVEHYDK-IQELTQMLQESHSSLVSTNEHLLQELSRTRAQHRAEVEQM 619
Cdd:COG3206  268 LRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAqLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL 346
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 475-620 7.56e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 7.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940537 475 YLSLENKTLQSRLAEQQQQYTATVTKM---TAELNNTKRELDTLRQHLDKSLEENSHLKSLLYNVKKEVKTADTS-TALT 550
Cdd:COG1196  229 LLLLKLRELEAELEELEAELEELEAELeelEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDiARLE 308

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341940537 551 LQITGLQASMKQLSGEVVELKQHVE-HYDKIQELTQMLQESHSSLVSTNEHLLQELSRTRAQHRAEVEQMR 620
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
 
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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