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Conserved domains on  [gi|2165635432|ref|WP_232002140|]
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Ig-like domain-containing protein [Listeria ivanovii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
92-229 1.14e-19

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 88.84  E-value: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432  92 KYLNCDGSNIKSL-EGVQFLTNLEELHACENQISDLS-PLKDLTNLSSLYLKNNKLKSLSGVPTA--QLVHLVVDNNELS 167
Cdd:COG4886   139 KELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLPeELGNLTNLKELDLSNNQITDLPEPLGNltNLEELDLSGNQLT 218

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2165635432 168 EV-NPLNHSQYLENLSMSKNKLKNINGLANLTNLRTLNLSKNELSDLSPLRKLKKLNSLNASG 229
Cdd:COG4886   219 DLpEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSN 281
LRR_adjacent super family cl08470
LRR adjacent; These are small, all beta strand domains, structurally described for the protein ...
 255-309 5.69e-14

LRR adjacent; These are small, all beta strand domains, structurally described for the protein Internalin (InlA) and related proteins InlB, InlE, InlH from the pathogenic bacterium Listeria monocytogenes. Their function appears to be mainly structural: They are fused to the C-terminal end of leucine-rich repeats (LRR), significantly stabilising the LRR, and forming a common rigid entity with the LRR. They are themselves not involved in protein-protein-interactions but help to present the adjacent LRR-domain for this purpose. These domains belong to the family of Ig-like domains in that they consist of two sandwiched beta sheets that follow the classical connectivity of Ig-domains. The beta strands in one of the sheets is, however, much smaller than in most standard Ig-like domains, making it somewhat of an outlier.


The actual alignment was detected with superfamily member pfam08191:

Pssm-ID: 369739 [Multi-domain]  Cd Length: 57  Bit Score: 65.47  E-value: 5.69e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2165635432 255 ALVFPRDISDNGEYANGHITWNLPFYKKEVVYTFKKNERVWEIETKFDGTVIQPL 309
Cdd:pfam08191   2 SLVAPSTISNNGTYADPNITWNLPSFTSEVSYTFNQPITIGKGTATFSGTVTQPL 56
Internalin_N super family cl13750
Bacterial adhesion/invasion protein N terminal; This domain family is found in bacteria, and ...
 50-70 2.13e-05

Bacterial adhesion/invasion protein N terminal; This domain family is found in bacteria, and is approximately 60 amino acids in length. The family is found in association with pfam00560, pfam08191, pfam09479. There are two completely conserved residues (I and F) that may be functionally important. Internalin mediates bacterial adhesion and invasion of epithelial cells in the human intestine through specific interaction with its host cell receptor E-cadherin. This family is the N terminal of internalin, the cap domain of the protein. The cap domain is conserved between different internalin types. The cap domain does not interact with E cadherin, therefore its function is presumably structural: capping the hydrophobic core.


The actual alignment was detected with superfamily member pfam12354:

Pssm-ID: 289150  Cd Length: 50  Bit Score: 41.17  E-value: 2.13e-05
                          10        20
                  ....*....|....*....|.
gi 2165635432  50 ISKPRPINDIFPDPSLANEVK 70
Cdd:pfam12354  30 ITPPAPINQIFPDPALAEEVK 50
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
92-229 1.14e-19

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 88.84  E-value: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432  92 KYLNCDGSNIKSL-EGVQFLTNLEELHACENQISDLS-PLKDLTNLSSLYLKNNKLKSLSGVPTA--QLVHLVVDNNELS 167
Cdd:COG4886   139 KELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLPeELGNLTNLKELDLSNNQITDLPEPLGNltNLEELDLSGNQLT 218

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2165635432 168 EV-NPLNHSQYLENLSMSKNKLKNINGLANLTNLRTLNLSKNELSDLSPLRKLKKLNSLNASG 229
Cdd:COG4886   219 DLpEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSN 281
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 100-229 9.86e-18

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: 80.60  E-value: 9.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432 100 NIKSLEGVQFLTNLEELHACENQISDLSPLKDLTNLSSLYLKNNKLKSLSGVPTA-QLVHLVVDNNELSEVNPL------ 172
Cdd:cd21340    35 KITKIENLEFLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVEGLENLtNLEELHIENQRLPPGEKLtfdprs 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2165635432 173 --NHSQYLENLSMSKNKLKNINGLANLTNLRTLNLSKNELSDLS----PLRKLKKLNSLNASG 229
Cdd:cd21340   115 laALSNSLRVLNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEelldLLSSWPSLRELDLTG 177
LRR_adjacent pfam08191
LRR adjacent; These are small, all beta strand domains, structurally described for the protein ...
 255-309 5.69e-14

LRR adjacent; These are small, all beta strand domains, structurally described for the protein Internalin (InlA) and related proteins InlB, InlE, InlH from the pathogenic bacterium Listeria monocytogenes. Their function appears to be mainly structural: They are fused to the C-terminal end of leucine-rich repeats (LRR), significantly stabilising the LRR, and forming a common rigid entity with the LRR. They are themselves not involved in protein-protein-interactions but help to present the adjacent LRR-domain for this purpose. These domains belong to the family of Ig-like domains in that they consist of two sandwiched beta sheets that follow the classical connectivity of Ig-domains. The beta strands in one of the sheets is, however, much smaller than in most standard Ig-like domains, making it somewhat of an outlier.


Pssm-ID: 369739 [Multi-domain]  Cd Length: 57  Bit Score: 65.47  E-value: 5.69e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2165635432 255 ALVFPRDISDNGEYANGHITWNLPFYKKEVVYTFKKNERVWEIETKFDGTVIQPL 309
Cdd:pfam08191   2 SLVAPSTISNNGTYADPNITWNLPSFTSEVSYTFNQPITIGKGTATFSGTVTQPL 56
Internalin_N pfam12354
Bacterial adhesion/invasion protein N terminal; This domain family is found in bacteria, and ...
 50-70 2.13e-05

Bacterial adhesion/invasion protein N terminal; This domain family is found in bacteria, and is approximately 60 amino acids in length. The family is found in association with pfam00560, pfam08191, pfam09479. There are two completely conserved residues (I and F) that may be functionally important. Internalin mediates bacterial adhesion and invasion of epithelial cells in the human intestine through specific interaction with its host cell receptor E-cadherin. This family is the N terminal of internalin, the cap domain of the protein. The cap domain is conserved between different internalin types. The cap domain does not interact with E cadherin, therefore its function is presumably structural: capping the hydrophobic core.


Pssm-ID: 289150  Cd Length: 50  Bit Score: 41.17  E-value: 2.13e-05
                          10        20
                  ....*....|....*....|.
gi 2165635432  50 ISKPRPINDIFPDPSLANEVK 70
Cdd:pfam12354  30 ITPPAPINQIFPDPALAEEVK 50
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 178-218 1.02e-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: 39.15  E-value: 1.02e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2165635432 178 LENLSMSKNKLKNINGLANLTNLRTLNLSKN-ELSDLSPLRK 218
Cdd:pfam12799   3 LEVLDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSDLAN 44
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 65-231 6.42e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 41.37  E-value: 6.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432  65 LANEVKRVLGKK---SVSDIVTQKELNKIKKYLnCDGSNI-------KSLEG-----VQFLTNLEELHACENQIS-DLSp 128
Cdd:PLN00113  344 FSGEIPKNLGKHnnlTVLDLSTNNLTGEIPEGL-CSSGNLfklilfsNSLEGeipksLGACRSLRRVRLQDNSFSgELP- 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432 129 lKDLTNLSSLYLKNNKLKSLSG--------VPTAQLVHLVVdNNELSEVNPLNHSQYLENLSMSKNKLKNI--NGLANLT 198
Cdd:PLN00113  422 -SEFTKLPLVYFLDISNNNLQGrinsrkwdMPSLQMLSLAR-NKFFGGLPDSFGSKRLENLDLSRNQFSGAvpRKLGSLS 499

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2165635432 199 NLRTLNLSKNELSDLSP--LRKLKKLNSLNAS-----GQI 231
Cdd:PLN00113  500 ELMQLKLSENKLSGEIPdeLSSCKKLVSLDLShnqlsGQI 539
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
92-229 1.14e-19

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 88.84  E-value: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432  92 KYLNCDGSNIKSL-EGVQFLTNLEELHACENQISDLS-PLKDLTNLSSLYLKNNKLKSLSGVPTA--QLVHLVVDNNELS 167
Cdd:COG4886   139 KELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLPeELGNLTNLKELDLSNNQITDLPEPLGNltNLEELDLSGNQLT 218

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2165635432 168 EV-NPLNHSQYLENLSMSKNKLKNINGLANLTNLRTLNLSKNELSDLSPLRKLKKLNSLNASG 229
Cdd:COG4886   219 DLpEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSN 281
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 100-229 9.86e-18

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: 80.60  E-value: 9.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432 100 NIKSLEGVQFLTNLEELHACENQISDLSPLKDLTNLSSLYLKNNKLKSLSGVPTA-QLVHLVVDNNELSEVNPL------ 172
Cdd:cd21340    35 KITKIENLEFLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVEGLENLtNLEELHIENQRLPPGEKLtfdprs 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2165635432 173 --NHSQYLENLSMSKNKLKNINGLANLTNLRTLNLSKNELSDLS----PLRKLKKLNSLNASG 229
Cdd:cd21340   115 laALSNSLRVLNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEelldLLSSWPSLRELDLTG 177
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 116-229 2.03e-16

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: 76.75  E-value: 2.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432 116 LHACENQISDLSPLKDLTNLSSLYLKNNKLKSLSGVPTA-QLVHLVVDNNELSEVNPLNHSQYLENLSMSKNKLKNINGL 194
Cdd:cd21340     7 LYLNDKNITKIDNLSLCKNLKVLYLYDNKITKIENLEFLtNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVEGL 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2165635432 195 ANLTN------------------------------LRTLNLSKNELSDLSPLRKLKKLNSLNASG 229
Cdd:cd21340    87 ENLTNleelhienqrlppgekltfdprslaalsnsLRVLNISGNNIDSLEPLAPLRNLEQLDASN 151
LRR_adjacent pfam08191
LRR adjacent; These are small, all beta strand domains, structurally described for the protein ...
 255-309 5.69e-14

LRR adjacent; These are small, all beta strand domains, structurally described for the protein Internalin (InlA) and related proteins InlB, InlE, InlH from the pathogenic bacterium Listeria monocytogenes. Their function appears to be mainly structural: They are fused to the C-terminal end of leucine-rich repeats (LRR), significantly stabilising the LRR, and forming a common rigid entity with the LRR. They are themselves not involved in protein-protein-interactions but help to present the adjacent LRR-domain for this purpose. These domains belong to the family of Ig-like domains in that they consist of two sandwiched beta sheets that follow the classical connectivity of Ig-domains. The beta strands in one of the sheets is, however, much smaller than in most standard Ig-like domains, making it somewhat of an outlier.


Pssm-ID: 369739 [Multi-domain]  Cd Length: 57  Bit Score: 65.47  E-value: 5.69e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2165635432 255 ALVFPRDISDNGEYANGHITWNLPFYKKEVVYTFKKNERVWEIETKFDGTVIQPL 309
Cdd:pfam08191   2 SLVAPSTISNNGTYADPNITWNLPSFTSEVSYTFNQPITIGKGTATFSGTVTQPL 56
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
92-228 6.52e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 59.95  E-value: 6.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432  92 KYLNCDGSNIKSL-EGVQFLTNLEELHACENQISDLS-PLKDLTNLSSLYLKNNKLKSLSGVPT-AQLVHLVVDNNELSE 168
Cdd:COG4886   185 KELDLSNNQITDLpEPLGNLTNLEELDLSGNQLTDLPePLANLTNLETLDLSNNQLTDLPELGNlTNLEELDLSNNQLTD 264

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2165635432 169 VNPLNHSQYLENLSMSKNKLKNIN--GLANLTNLRTLNLSKNELSDLSPLRKLKKLNSLNAS 228
Cdd:COG4886   265 LPPLANLTNLKTLDLSNNQLTDLKlkELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLL 326
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
50-229 3.56e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 54.55  E-value: 3.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432  50 ISKPRPINDIFPDPSLANEVKRVLGKKSVSDIVTQKELNKIKKYLNCDGSNIKSLEGVQFLTNLEELHACEN-QISDLSP 128
Cdd:COG4886    29 LLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTElDLSGNEE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432 129 LKDLTNLSSLYLKNNKLKSLSgvptaqlvhlvvdnnelsevNPLNHSQYLENLSMSKNKLKNI-NGLANLTNLRTLNLSK 207
Cdd:COG4886   109 LSNLTNLESLDLSGNQLTDLP--------------------EELANLTNLKELDLSNNQLTDLpEPLGNLTNLKSLDLSN 168

                         170       180
                  ....*....|....*....|...
gi 2165635432 208 NELSDLS-PLRKLKKLNSLNASG 229
Cdd:COG4886   169 NQLTDLPeELGNLTNLKELDLSN 191
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 87-208 7.74e-08

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: 52.10  E-value: 7.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432  87 LNKIKK-YLncDGSNIKSLEGVQFLTNLEELHaCENQISDLSplkdltnlSSLYLKNNKLKSLSGvptaQLVHLVVDNNE 165
Cdd:cd21340    67 LVNLKKlYL--GGNRISVVEGLENLTNLEELH-IENQRLPPG--------EKLTFDPRSLAALSN----SLRVLNISGNN 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2165635432 166 LSEVNPLNHSQYLENLSMSKNKLKNINGLA----NLTNLRTLNLSKN 208
Cdd:cd21340   132 IDSLEPLAPLRNLEQLDASNNQISDLEELLdllsSWPSLRELDLTGN 178
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
81-229 1.50e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 52.63  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432  81 IVTQKELNKIKKYLNCDGSNIKSLEGVQFLTNLEELHACENQISDLSPLKDLTNLSSLYLKNNKLKSLSGVPTAQLVHLV 160
Cdd:COG4886    20 LLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLT 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2165635432 161 VDNneLSEVNPLNHSQYLENLSMSKNKLKNI-NGLANLTNLRTLNLSKNELSDL-SPLRKLKKLNSLNASG 229
Cdd:COG4886   100 ELD--LSGNEELSNLTNLESLDLSGNQLTDLpEELANLTNLKELDLSNNQLTDLpEPLGNLTNLKSLDLSN 168
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
92-226 2.01e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 52.24  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432  92 KYLNCDGSNIKSLEGVQFLTNLEELHACENQISDLSPLKDLTNLSSLYLKNNKLKSLSGVPTAQLVHLVVDNNELSEVNP 171
Cdd:COG4886   231 ETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNL 310

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2165635432 172 LNHSQYLENLSMSKNKLKNINGLANLTNLRTLNLSKNELSDLSPLRKLKKLNSLN 226
Cdd:COG4886   311 LELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTL 365
Internalin_N pfam12354
Bacterial adhesion/invasion protein N terminal; This domain family is found in bacteria, and ...
 50-70 2.13e-05

Bacterial adhesion/invasion protein N terminal; This domain family is found in bacteria, and is approximately 60 amino acids in length. The family is found in association with pfam00560, pfam08191, pfam09479. There are two completely conserved residues (I and F) that may be functionally important. Internalin mediates bacterial adhesion and invasion of epithelial cells in the human intestine through specific interaction with its host cell receptor E-cadherin. This family is the N terminal of internalin, the cap domain of the protein. The cap domain is conserved between different internalin types. The cap domain does not interact with E cadherin, therefore its function is presumably structural: capping the hydrophobic core.


Pssm-ID: 289150  Cd Length: 50  Bit Score: 41.17  E-value: 2.13e-05
                          10        20
                  ....*....|....*....|.
gi 2165635432  50 ISKPRPINDIFPDPSLANEVK 70
Cdd:pfam12354  30 ITPPAPINQIFPDPALAEEVK 50
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 178-218 1.02e-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: 39.15  E-value: 1.02e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2165635432 178 LENLSMSKNKLKNINGLANLTNLRTLNLSKN-ELSDLSPLRK 218
Cdd:pfam12799   3 LEVLDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSDLAN 44
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 111-152 1.06e-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: 39.15  E-value: 1.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2165635432 111 TNLEELHACENQISDLSPLKDLTNLSSLYLK-NNKLKSLSGVP 152
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPPLAKLPNLETLDLSgNNKITDLSDLA 43
LRR_8 pfam13855
Leucine rich repeat;
178-229 2.30e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 38.66  E-value: 2.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2165635432 178 LENLSMSKNKLKNING--LANLTNLRTLNLSKNELSDLSP--LRKLKKLNSLNASG 229
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLLTTLSPgaFSGLPSLRYLDLSG 58
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
87-229 4.25e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.84  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432  87 LNKIKKYLNCDGSNIKSLEGVQFLTNLEELHACENQISDLSPLKDLTNLSSLYLKNNKLKSLSGVPTAQLVHLVVDNNEL 166
Cdd:COG4886     1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2165635432 167 SEVNPLNHSQYLENLSMSKN-KLKNINGLANLTNLRTLNLSKNELSDLSP-LRKLKKLNSLNASG 229
Cdd:COG4886    81 LLSLLLLGLTDLGDLTNLTElDLSGNEELSNLTNLESLDLSGNQLTDLPEeLANLTNLKELDLSN 145
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 65-231 6.42e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 41.37  E-value: 6.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432  65 LANEVKRVLGKK---SVSDIVTQKELNKIKKYLnCDGSNI-------KSLEG-----VQFLTNLEELHACENQIS-DLSp 128
Cdd:PLN00113  344 FSGEIPKNLGKHnnlTVLDLSTNNLTGEIPEGL-CSSGNLfklilfsNSLEGeipksLGACRSLRRVRLQDNSFSgELP- 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432 129 lKDLTNLSSLYLKNNKLKSLSG--------VPTAQLVHLVVdNNELSEVNPLNHSQYLENLSMSKNKLKNI--NGLANLT 198
Cdd:PLN00113  422 -SEFTKLPLVYFLDISNNNLQGrinsrkwdMPSLQMLSLAR-NKFFGGLPDSFGSKRLENLDLSRNQFSGAvpRKLGSLS 499

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2165635432 199 NLRTLNLSKNELSDLSP--LRKLKKLNSLNAS-----GQI 231
Cdd:PLN00113  500 ELMQLKLSENKLSGEIPdeLSSCKKLVSLDLShnqlsGQI 539
LRR_8 pfam13855
Leucine rich repeat;
92-145 9.49e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.12  E-value: 9.49e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2165635432  92 KYLNCDGSNIKSLEGVQF--LTNLEELHACENQISDLSP--LKDLTNLSSLYLKNNKL 145
Cdd:pfam13855   4 RSLDLSNNRLTSLDDGAFkgLSNLKVLDLSNNLLTTLSPgaFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
111-166 1.07e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 36.73  E-value: 1.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2165635432 111 TNLEELHACENQISDLSP--LKDLTNLSSLYLKNNKLKSLSG---VPTAQLVHLVVDNNEL 166
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLLTTLSPgafSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 154-222 1.08e-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: 39.77  E-value: 1.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2165635432 154 AQLVHLVVDNNELSEVNPLNHSQYLENLSMSKNKLKNINGLANLTNLRTLNLSKNELS---DLSPLRKLKKL 222
Cdd:cd21340     2 KRITHLYLNDKNITKIDNLSLCKNLKVLYLYDNKITKIENLEFLTNLTHLYLQNNQIEkieNLENLVNLKKL 73
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 198-229 1.81e-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: 35.68  E-value: 1.81e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2165635432 198 TNLRTLNLSKNELSDLSPLRKLKKLNSLNASG 229
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPPLAKLPNLETLDLSG 32
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 111-223 2.10e-03

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 39.26  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432 111 TNLEELHACENQISDL------SPLKDLT-NLSSLYLKNNKLKSLSGVPTAQ-------LVHLVVDNNELSE------VN 170
Cdd:cd00116   108 SSLQELKLNNNGLGDRglrllaKGLKDLPpALEKLVLGRNRLEGASCEALAKalranrdLKELNLANNGIGDagiralAE 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2165635432 171 PLNHSQYLENLSMSKNKLKNING------LANLTNLRTLNLSKNELSD----------LSPLRKLKKLN 223
Cdd:cd00116   188 GLKANCNLEVLDLNNNGLTDEGAsalaetLASLKSLEVLNLGDNNLTDagaaalasalLSPNISLLTLS 256
LRR_8 pfam13855
Leucine rich repeat;
155-210 5.27e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 34.81  E-value: 5.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165635432 155 QLVHLVVDNNELSEVNP--LNHSQYLENLSMSKNKLKNING--LANLTNLRTLNLSKNEL 210
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLLTTLSPgaFSGLPSLRYLDLSGNRL 61
 
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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