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Conserved domains on  [gi|109039650|ref|XP_001107400|]
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amphoterin-induced protein 3 [Macaca mulatta]

Protein Classification

LRR and IG_like domain-containing protein( domain architecture ID 11471650)

LRR and IG_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
66-221 4.23e-20

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 92.30  E-value: 4.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650  66 LDLSHNALQRLrPGWLAPLFQLRALHLGHNELEALGLgVFANASGLRLLDLSSNALRALGRHdLDGLGALEKLLLFNNRL 145
Cdd:COG4886  118 LDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDLPEE-LGNLTNLKELDLSNNQI 194

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109039650 146 VHLDEhAFHGLSALSHLYLGCNELASFSFDhLHGLsaTHLLTLDLSSNRLGHIsvPELAALPAfLKNgLYLHNNPL 221
Cdd:COG4886  195 TDLPE-PLGNLTNLEELDLSGNQLTDLPEP-LANL--TNLETLDLSNNQLTDL--PELGNLTN-LEE-LDLSNNQL 262
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 286-371 3.60e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


:

Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 42.11  E-value: 3.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650   286 EHLYALVGRSLRLYCN-TSVPAMRIAWVSPQQELLRAPG----SRDGSIAvladgSLAIGNVQEQHAGLFVCLATGPrlH 360
Cdd:smart00410   2 PSVTVKEGESVTLSCEaSGSPPPEVTWYKQGGKLLAESGrfsvSRSGSTS-----TLTISNVTPEDSGTYTCAATNS--S 74

                           90
                   ....*....|.
gi 109039650   361 HNQTHEYNVSV 371
Cdd:smart00410  75 GSASSGTTLTV 85
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
66-221 4.23e-20

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 92.30  E-value: 4.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650  66 LDLSHNALQRLrPGWLAPLFQLRALHLGHNELEALGLgVFANASGLRLLDLSSNALRALGRHdLDGLGALEKLLLFNNRL 145
Cdd:COG4886  118 LDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDLPEE-LGNLTNLKELDLSNNQI 194

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109039650 146 VHLDEhAFHGLSALSHLYLGCNELASFSFDhLHGLsaTHLLTLDLSSNRLGHIsvPELAALPAfLKNgLYLHNNPL 221
Cdd:COG4886  195 TDLPE-PLGNLTNLEELDLSGNQLTDLPEP-LANL--TNLETLDLSNNQLTDL--PELGNLTN-LEE-LDLSNNQL 262
LRR_8 pfam13855
Leucine rich repeat;
86-145 1.03e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 57.15  E-value: 1.03e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650   86 QLRALHLGHNELEALGLGVFANASGLRLLDLSSNALRALGRHDLDGLGALEKLLLFNNRL 145
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 66-164 1.38e-05

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: 46.32  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650  66 LDLSHNALQRLRPgwLAPLFQLRALHLGHNELEAL-GLG---------------------------VFANASGLRLLDLS 117
Cdd:cd21340   51 LYLQNNQIEKIEN--LENLVNLKKLYLGGNRISVVeGLEnltnleelhienqrlppgekltfdprsLAALSNSLRVLNIS 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 109039650 118 SNALRALgrHDLDGLGALEKLLLFNNRLVHLDE--HAFHGLSALSHLYL 164
Cdd:cd21340  129 GNNIDSL--EPLAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDL 175
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
52-221 3.26e-05

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 46.61  E-value: 3.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650  52 LQDVPAELPAATADLDLSHNALQRLrPGWLAPLFQlrALHLGHNELEALGLGVfanASGLRLLDLSSNALRALGRHDLDG 131
Cdd:PRK15370 232 LTSIPATLPDTIQEMELSINRITEL-PERLPSALQ--SLDLFHNKISCLPENL---PEELRYLSVYDNSIRTLPAHLPSG 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650 132 lgaLEKLLLFNNRLVHLDEHAFHGLSALShlyLGCNELASfsfdhLHGLSATHLLTLDLSSNRLghISVPElaALPAFLK 211
Cdd:PRK15370 306 ---ITHLNVQSNSLTALPETLPPGLKTLE---AGENALTS-----LPASLPPELQVLDVSKNQI--TVLPE--TLPPTIT 370

                        170
                 ....*....|
gi 109039650 212 NgLYLHNNPL 221
Cdd:PRK15370 371 T-LDVSRNAL 379
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 286-371 3.60e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 42.11  E-value: 3.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650   286 EHLYALVGRSLRLYCN-TSVPAMRIAWVSPQQELLRAPG----SRDGSIAvladgSLAIGNVQEQHAGLFVCLATGPrlH 360
Cdd:smart00410   2 PSVTVKEGESVTLSCEaSGSPPPEVTWYKQGGKLLAESGrfsvSRSGSTS-----TLTISNVTPEDSGTYTCAATNS--S 74

                           90
                   ....*....|.
gi 109039650   361 HNQTHEYNVSV 371
Cdd:smart00410  75 GSASSGTTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 284-355 2.31e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 39.86  E-value: 2.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109039650  284 PEEHLYALVGRSLRLYCN-TSVPAMRIAWVSPQQELLraPGSRDGSIAVLADGSLAIGNVQEQHAGLFVCLAT 355
Cdd:pfam13927   7 SPSSVTVREGETVTLTCEaTGSPPPTITWYKNGEPIS--SGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 281-354 2.50e-03

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 37.22  E-value: 2.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109039650 281 LERPEEHLYALVGRSLRLYCNT-SVPAMRIAWVSpQQELLRApgsrDGSIAVLADGSLAIGNVQEQHAGLFVCLA 354
Cdd:cd20968    2 ITRPPTNVTIIEGLKAVLPCTTmGNPKPSVSWIK-GDDLIKE----NNRIAVLESGSLRIHNVQKEDAGQYRCVA 71
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
66-221 4.23e-20

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 92.30  E-value: 4.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650  66 LDLSHNALQRLrPGWLAPLFQLRALHLGHNELEALGLgVFANASGLRLLDLSSNALRALGRHdLDGLGALEKLLLFNNRL 145
Cdd:COG4886  118 LDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDLPEE-LGNLTNLKELDLSNNQI 194

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109039650 146 VHLDEhAFHGLSALSHLYLGCNELASFSFDhLHGLsaTHLLTLDLSSNRLGHIsvPELAALPAfLKNgLYLHNNPL 221
Cdd:COG4886  195 TDLPE-PLGNLTNLEELDLSGNQLTDLPEP-LANL--TNLETLDLSNNQLTDL--PELGNLTN-LEE-LDLSNNQL 262
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
45-232 2.11e-18

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 87.30  E-value: 2.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650  45 LSCTGLGLQDVPAELPAATA--DLDLSHNALQRLrPGWLAPLFQLRALHLGHNELEALGLgVFANASGLRLLDLSSNALR 122
Cdd:COG4886  141 LDLSNNQLTDLPEPLGNLTNlkSLDLSNNQLTDL-PEELGNLTNLKELDLSNNQITDLPE-PLGNLTNLEELDLSGNQLT 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650 123 ALGRhDLDGLGALEKLLLFNNRLVHLDEhaFHGLSALSHLYLGCNELASFSFdhlhGLSATHLLTLDLSSNRLGHISVPE 202
Cdd:COG4886  219 DLPE-PLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDLPP----LANLTNLKTLDLSNNQLTDLKLKE 291

                        170       180       190
                 ....*....|....*....|....*....|
gi 109039650 203 LAALPAFLKNGLYLHNNPLPCDCRLYHLLQ 232
Cdd:COG4886  292 LELLLGLNSLLLLLLLLNLLELLILLLLLT 321
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
81-221 6.38e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 64.18  E-value: 6.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650  81 LAPLFQLRALHLGHNELealglgvFANASGLRLLDLSSNALRALGrHDLDGLGALEKLLLFNNRLVHLDEhAFHGLSALS 160
Cdd:COG4886   92 LGDLTNLTELDLSGNEE-------LSNLTNLESLDLSGNQLTDLP-EELANLTNLKELDLSNNQLTDLPE-PLGNLTNLK 162

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109039650 161 HLYLGCNELASFSfDHLHGLsaTHLLTLDLSSNRLGHISvPELAALPAfLKNgLYLHNNPL 221
Cdd:COG4886  163 SLDLSNNQLTDLP-EELGNL--TNLKELDLSNNQITDLP-EPLGNLTN-LEE-LDLSGNQL 217
LRR_8 pfam13855
Leucine rich repeat;
86-145 1.03e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 57.15  E-value: 1.03e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650   86 QLRALHLGHNELEALGLGVFANASGLRLLDLSSNALRALGRHDLDGLGALEKLLLFNNRL 145
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
135-195 2.97e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 55.99  E-value: 2.97e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109039650  135 LEKLLLFNNRLVHLDEHAFHGLSALSHLYLGCNELASFSFDHLHGLsaTHLLTLDLSSNRL 195
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGL--PSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
109-169 1.23e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 51.37  E-value: 1.23e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109039650  109 SGLRLLDLSSNALRALGRHDLDGLGALEKLLLFNNRLVHLDEHAFHGLSALSHLYLGCNEL 169
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
66-121 6.11e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 49.45  E-value: 6.11e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 109039650   66 LDLSHNALQRLRPGWLAPLFQLRALHLGHNELEALGLGVFANASGLRLLDLSSNAL 121
Cdd:pfam13855   6 LDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 66-164 1.38e-05

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: 46.32  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650  66 LDLSHNALQRLRPgwLAPLFQLRALHLGHNELEAL-GLG---------------------------VFANASGLRLLDLS 117
Cdd:cd21340   51 LYLQNNQIEKIEN--LENLVNLKKLYLGGNRISVVeGLEnltnleelhienqrlppgekltfdprsLAALSNSLRVLNIS 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 109039650 118 SNALRALgrHDLDGLGALEKLLLFNNRLVHLDE--HAFHGLSALSHLYL 164
Cdd:cd21340  129 GNNIDSL--EPLAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDL 175
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 81-221 2.56e-05

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: 45.55  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650  81 LAPLFQLRALHLGHNELEAL-GLGvfaNASGLRLLDLSSNALRALGrhDLDGLGALEKLLLFNNRLVHLdEHaFHGLSAL 159
Cdd:cd21340   20 LSLCKNLKVLYLYDNKITKIeNLE---FLTNLTHLYLQNNQIEKIE--NLENLVNLKKLYLGGNRISVV-EG-LENLTNL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650 160 SHLYLGCNELA---SFSFD--HLHGLSAT---------------------HLLTLDLSSNRLGHIS--VPELAALPaFLK 211
Cdd:cd21340   93 EELHIENQRLPpgeKLTFDprSLAALSNSlrvlnisgnnidsleplaplrNLEQLDASNNQISDLEelLDLLSSWP-SLR 171

                        170
                 ....*....|
gi 109039650 212 NgLYLHNNPL 221
Cdd:cd21340  172 E-LDLTGNPV 180
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
52-221 3.26e-05

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 46.61  E-value: 3.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650  52 LQDVPAELPAATADLDLSHNALQRLrPGWLAPLFQlrALHLGHNELEALGLGVfanASGLRLLDLSSNALRALGRHDLDG 131
Cdd:PRK15370 232 LTSIPATLPDTIQEMELSINRITEL-PERLPSALQ--SLDLFHNKISCLPENL---PEELRYLSVYDNSIRTLPAHLPSG 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650 132 lgaLEKLLLFNNRLVHLDEHAFHGLSALShlyLGCNELASfsfdhLHGLSATHLLTLDLSSNRLghISVPElaALPAFLK 211
Cdd:PRK15370 306 ---ITHLNVQSNSLTALPETLPPGLKTLE---AGENALTS-----LPASLPPELQVLDVSKNQI--TVLPE--TLPPTIT 370

                        170
                 ....*....|
gi 109039650 212 NgLYLHNNPL 221
Cdd:PRK15370 371 T-LDVSRNAL 379
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
80-221 3.29e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 46.08  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650  80 WLAPLFQLRALHLGHNELEALGLGVFANASGLRLLDLSSNALRALGRHDLDGLGALEKLLLFNNRlvhldehAFHGLSAL 159
Cdd:COG4886   43 LSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE-------ELSNLTNL 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109039650 160 SHLYLGCNELASFsFDHLHGLsaTHLLTLDLSSNRLGHISvPELAALPAfLKNgLYLHNNPL 221
Cdd:COG4886  116 ESLDLSGNQLTDL-PEELANL--TNLKELDLSNNQLTDLP-EPLGNLTN-LKS-LDLSNNQL 171
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 286-371 3.60e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 42.11  E-value: 3.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650   286 EHLYALVGRSLRLYCN-TSVPAMRIAWVSPQQELLRAPG----SRDGSIAvladgSLAIGNVQEQHAGLFVCLATGPrlH 360
Cdd:smart00410   2 PSVTVKEGESVTLSCEaSGSPPPEVTWYKQGGKLLAESGrfsvSRSGSTS-----TLTISNVTPEDSGTYTCAATNS--S 74

                           90
                   ....*....|.
gi 109039650   361 HNQTHEYNVSV 371
Cdd:smart00410  75 GSASSGTTLTV 85
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 45-221 4.24e-05

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: 45.42  E-value: 4.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650  45 LSCTGLG---LQDVPAELPA--ATADLDLSHNALQRLRPGWLAPL------FQLRALHLGHNELEALGLGVFANA---SG 110
Cdd:cd00116   30 LEGNTLGeeaAKALASALRPqpSLKELCLSLNETGRIPRGLQSLLqgltkgCGLQELDLSDNALGPDGCGVLESLlrsSS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650 111 LRLLDLSSNAL-RALGRHDLDGLG----ALEKLLLFNNRLVHLD----EHAFHGLSALSHLYLGCNELASFSFDHL-HGL 180
Cdd:cd00116  110 LQELKLNNNGLgDRGLRLLAKGLKdlppALEKLVLGRNRLEGAScealAKALRANRDLKELNLANNGIGDAGIRALaEGL 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 109039650 181 SA-THLLTLDLSSNRLGHISVPELAALPAFLKNGLYLH--NNPL 221
Cdd:cd00116  190 KAnCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNlgDNNL 233
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 66-217 2.24e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 44.07  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650  66 LDLSHNALQRLRPGWLAPLFQLRALHLGHNELEALGLGVFANASGLRLLDLSSNAL-----RALGR-------------- 126
Cdd:PLN00113 145 LDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLvgqipRELGQmkslkwiylgynnl 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650 127 -----HDLDGLGALEKLLLFNNRLVHLDEHAFHGLSALSHLYLGCNELASFSFDHLHGLsaTHLLTLDLSSNRL-GHIsv 200
Cdd:PLN00113 225 sgeipYEIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSL--QKLISLDLSDNSLsGEI-- 300

                        170
                 ....*....|....*..
gi 109039650 201 PELAALpafLKNGLYLH 217
Cdd:PLN00113 301 PELVIQ---LQNLEILH 314
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 284-355 2.31e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 39.86  E-value: 2.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109039650  284 PEEHLYALVGRSLRLYCN-TSVPAMRIAWVSPQQELLraPGSRDGSIAVLADGSLAIGNVQEQHAGLFVCLAT 355
Cdd:pfam13927   7 SPSSVTVREGETVTLTCEaTGSPPPTITWYKNGEPIS--SGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 281-354 2.50e-03

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 37.22  E-value: 2.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109039650 281 LERPEEHLYALVGRSLRLYCNT-SVPAMRIAWVSpQQELLRApgsrDGSIAVLADGSLAIGNVQEQHAGLFVCLA 354
Cdd:cd20968    2 ITRPPTNVTIIEGLKAVLPCTTmGNPKPSVSWIK-GDDLIKE----NNRIAVLESGSLRIHNVQKEDAGQYRCVA 71
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 87-204 2.59e-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: 40.03  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650  87 LRALHLGHNELEALGL----GVFANASGLRLLDLSSNALRALG----RHDLDGLGALEKLLLFNNRLVHLD----EHAFH 154
Cdd:cd00116  139 LEKLVLGRNRLEGASCealaKALRANRDLKELNLANNGIGDAGiralAEGLKANCNLEVLDLNNNGLTDEGasalAETLA 218

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 109039650 155 GLSALSHLYLGCNELASFSFDHLH---GLSATHLLTLDLSSNRLGHISVPELA 204
Cdd:cd00116  219 SLKSLEVLNLGDNNLTDAGAAALAsalLSPNISLLTLSLSCNDITDDGAKDLA 271
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 91-195 8.62e-03

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 37.84  E-value: 8.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109039650  91 HLGHNELEALGLGVFANASGLRLLDLSSNALRALGrhDLDGLGALEKLLLFNNRLVHLDEhaFHGLSALSHLYLGCNELA 170
Cdd:cd21340    6 HLYLNDKNITKIDNLSLCKNLKVLYLYDNKITKIE--NLEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLGGNRIS 81

                         90       100
                 ....*....|....*....|....*.
gi 109039650 171 sfsfdHLHGL-SATHLLTLDLSSNRL 195
Cdd:cd21340   82 -----VVEGLeNLTNLEELHIENQRL 102
 
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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