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Conserved domains on  [gi|30017449|ref|NP_835215|]
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amphoterin-induced protein 2 precursor [Mus musculus]

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];
69-229 1.93e-25

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 108.48  E-value: 1.93e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449  69 IKRLDLSYNRIGLLDADwIPvSFVKLSTLILRHNNITSISTgSFSTTPNLKCLDLSSNRLKSVkSATFQELKALEVLLLY 148
Cdd:COG4886 115 LESLDLSGNQLTDLPEE-LA-NLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDL-PEELGNLTNLKELDLS 190

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449 149 NNHISYLdPAAFGGLSHLQKLYLSGNFLTQFPMDLytgrFKLADLTFLDVSYNRIPSIPmhhiNLVPGRQLRGIYLHGNP 228
Cdd:COG4886 191 NNQITDL-PEPLGNLTNLEELDLSGNQLTDLPEPL----ANLTNLETLDLSNNQLTDLP----ELGNLTNLEELDLSNNQ 261


                .
gi 30017449 229 F 229
Cdd:COG4886 262 L 262
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 297-367 5.99e-08

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


:

Pssm-ID: 395002  Cd Length: 86  Bit Score: 50.27  E-value: 5.99e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30017449   297 HEAQVGERAIVHCDSKTGNGNTDFIWVGPDNRLLEPDKDMGNFRVFYNGSLVIENPGFEDAGVYSCIAMNR 367
Cdd:pfam00047   6 VTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNP 76
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
69-229 1.93e-25

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 108.48  E-value: 1.93e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449  69 IKRLDLSYNRIGLLDADwIPvSFVKLSTLILRHNNITSISTgSFSTTPNLKCLDLSSNRLKSVkSATFQELKALEVLLLY 148
Cdd:COG4886 115 LESLDLSGNQLTDLPEE-LA-NLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDL-PEELGNLTNLKELDLS 190

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449 149 NNHISYLdPAAFGGLSHLQKLYLSGNFLTQFPMDLytgrFKLADLTFLDVSYNRIPSIPmhhiNLVPGRQLRGIYLHGNP 228
Cdd:COG4886 191 NNQITDL-PEPLGNLTNLEELDLSGNQLTDLPEPL----ANLTNLETLDLSNNQLTDLP----ELGNLTNLEELDLSNNQ 261


                .
gi 30017449 229 F 229
Cdd:COG4886 262 L 262
LRR_8 pfam13855
Leucine rich repeat;
116-174 6.06e-14

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 66.39  E-value: 6.06e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 30017449   116 PNLKCLDLSSNRLKSVKSATFQELKALEVLLLYNNHISYLDPAAFGGLSHLQKLYLSGN 174
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGN 59
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 93-229 8.94e-10

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: 58.64  E-value: 8.94e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449  93 KLSTLILRHNNITSIstGSFSTTPNLKCLDLSSNRLKSVKSatFQELKALEVLLLYNNHISYLDPaaFGGLSHLQKLYLS 172
Cdd:cd21340   3 RITHLYLNDKNITKI--DNLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449 173 GNF------LTQFPM--DLYTGRFKLAD-----------------LTFLDVSYNRIPSI----PMHHI------------ 211
Cdd:cd21340  77 GNRisvvegLENLTNleELHIENQRLPPgekltfdprslaalsnsLRVLNISGNNIDSLeplaPLRNLeqldasnnqisd 156

                       170       180
                ....*....|....*....|....
gi 30017449 212 -----NLVPG-RQLRGIYLHGNPF 229
Cdd:cd21340 157 leellDLLSSwPSLRELDLTGNPV 180
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 297-367 5.99e-08

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 50.27  E-value: 5.99e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30017449   297 HEAQVGERAIVHCDSKTGNGNTDFIWVGPDNRLLEPDKDMGNFRVFYNGSLVIENPGFEDAGVYSCIAMNR 367
Cdd:pfam00047   6 VTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNP 76
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 300-371 1.37e-07

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 49.47  E-value: 1.37e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30017449 300 QVGERAIVHCDSkTGNGNTDFIWV----GPDNRLLEPDKDMGNFRVFYNGSLVIENPGFEDAGVYSCIAMNRQRLL 371
Cdd:cd05765  13 KVGETASFHCDV-TGRPQPEITWEkqvpGKENLIMRPNHVRGNVVVTNIGQLVIYNAQPQDAGLYTCTARNSGGLL 87
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 57-204 2.82e-07

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 53.31  E-value: 2.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449   57 NLS-KVPGNLFRLI--KRLDLSYNRIglldADWIPVSFVKLSTL---ILRHNNIT-SISTGSFSTTpNLKCLDLSSNRLK 129
Cdd:PLN00113 223 NLSgEIPYEIGGLTslNHLDLVYNNL----TGPIPSSLGNLKNLqylFLYQNKLSgPIPPSIFSLQ-KLISLDLSDNSLS 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449  130 SVKSATFQELKALEVLLLYNNHISYLDPAAFGGLSHLQKLYL-SGNFLTQFPMDLYtgrfKLADLTFLDVSYN----RIP 204
Cdd:PLN00113 298 GEIPELVIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLwSNKFSGEIPKNLG----KHNNLTVLDLSTNnltgEIP 373
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 297-379 7.29e-07

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: 47.11  E-value: 7.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449    297 HEAQVGERAIVHCDSkTGNGNTDFIWVGPDNRLLEPDkdmGNFRVFYNG---SLVIENPGFEDAGVYSCIAMNRQRLLNE 373
Cdd:smart00410   4 VTVKEGESVTLSCEA-SGSPPPEVTWYKQGGKLLAES---GRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSASS 79


                   ....*.
gi 30017449    374 TVDIMI 379
Cdd:smart00410  80 GTTLTV 85
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
69-229 1.93e-25

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 108.48  E-value: 1.93e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449  69 IKRLDLSYNRIGLLDADwIPvSFVKLSTLILRHNNITSISTgSFSTTPNLKCLDLSSNRLKSVkSATFQELKALEVLLLY 148
Cdd:COG4886 115 LESLDLSGNQLTDLPEE-LA-NLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDL-PEELGNLTNLKELDLS 190

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449 149 NNHISYLdPAAFGGLSHLQKLYLSGNFLTQFPMDLytgrFKLADLTFLDVSYNRIPSIPmhhiNLVPGRQLRGIYLHGNP 228
Cdd:COG4886 191 NNQITDL-PEPLGNLTNLEELDLSGNQLTDLPEPL----ANLTNLETLDLSNNQLTDLP----ELGNLTNLEELDLSNNQ 261


                .
gi 30017449 229 F 229
Cdd:COG4886 262 L 262
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
50-206 2.98e-21

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 96.16  E-value: 2.98e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449  50 IVSCTNKNLSKVPGNLFRL--IKRLDLSYNRIGLLDADWIpvSFVKLSTLILRHNNITSISTgSFSTTPNLKCLDLSSNR 127
Cdd:COG4886 140 ELDLSNNQLTDLPEPLGNLtnLKSLDLSNNQLTDLPEELG--NLTNLKELDLSNNQITDLPE-PLGNLTNLEELDLSGNQ 216

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30017449 128 LKSVkSATFQELKALEVLLLYNNHISYLdpAAFGGLSHLQKLYLSGNFLTQFPMDLytgrfKLADLTFLDVSYNRIPSI 206
Cdd:COG4886 217 LTDL-PEPLANLTNLETLDLSNNQLTDL--PELGNLTNLEELDLSNNQLTDLPPLA-----NLTNLKTLDLSNNQLTDL 287
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-306 1.14e-16

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 82.29  E-value: 1.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449  51 VSCTNKNLSKVPGNLFRL--IKRLDLSYNRIGLLdadwiPVSFVKLS---TLILRHNNITSISTgSFSTTPNLKCLDLSS 125
Cdd:COG4886 164 LDLSNNQLTDLPEELGNLtnLKELDLSNNQITDL-----PEPLGNLTnleELDLSGNQLTDLPE-PLANLTNLETLDLSN 237

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449 126 NRLKSVKSatFQELKALEVLLLYNNHISYLDPAafGGLSHLQKLYLSGNFLTQFPMDLYTGRFKLADLTFLDVSYNRIPS 205
Cdd:COG4886 238 NQLTDLPE--LGNLTNLEELDLSNNQLTDLPPL--ANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLEL 313

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449 206 IPMHHINLVPGRQLRGIYLHGNPFVCDCSLYSLLIFWYRRHFSSVMDFKNDYTCRLWSDSRHSHQLQLLQESFLNCSYSV 285
Cdd:COG4886 314 LILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLL 393

                       250       260
                ....*....|....*....|.
gi 30017449 286 INGSFHALGFIHEAQVGERAI 306
Cdd:COG4886 394 LTTTAGVLLLTLALLDAVNTE 414
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
54-229 3.33e-15

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 77.67  E-value: 3.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449  54 TNKNLSKVPGNLFRLIKRLDLSYNRIGLLDADWIPVSFVKLSTLILRHNNITSISTGSFSTTPNLKCLDLSSNRlksvks 133
Cdd:COG4886  34 LLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE------ 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449 134 aTFQELKALEVLLLYNNHISYLdPAAFGGLSHLQKLYLSGNFLTQFPMDLytgrFKLADLTFLDVSYNRIPSIPMHHINL 213
Cdd:COG4886 108 -ELSNLTNLESLDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDLPEPL----GNLTNLKSLDLSNNQLTDLPEELGNL 181

                       170
                ....*....|....*.
gi 30017449 214 VpgrQLRGIYLHGNPF 229
Cdd:COG4886 182 T---NLKELDLSNNQI 194
LRR_8 pfam13855
Leucine rich repeat;
116-174 6.06e-14

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 66.39  E-value: 6.06e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 30017449   116 PNLKCLDLSSNRLKSVKSATFQELKALEVLLLYNNHISYLDPAAFGGLSHLQKLYLSGN 174
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGN 59
LRR_8 pfam13855
Leucine rich repeat;
93-152 4.32e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 61.00  E-value: 4.32e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449    93 KLSTLILRHNNITSISTGSFSTTPNLKCLDLSSNRLKSVKSATFQELKALEVLLLYNNHI 152
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 93-229 8.94e-10

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: 58.64  E-value: 8.94e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449  93 KLSTLILRHNNITSIstGSFSTTPNLKCLDLSSNRLKSVKSatFQELKALEVLLLYNNHISYLDPaaFGGLSHLQKLYLS 172
Cdd:cd21340   3 RITHLYLNDKNITKI--DNLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449 173 GNF------LTQFPM--DLYTGRFKLAD-----------------LTFLDVSYNRIPSI----PMHHI------------ 211
Cdd:cd21340  77 GNRisvvegLENLTNleELHIENQRLPPgekltfdprslaalsnsLRVLNISGNNIDSLeplaPLRNLeqldasnnqisd 156

                       170       180
                ....*....|....*....|....
gi 30017449 212 -----NLVPG-RQLRGIYLHGNPF 229
Cdd:cd21340 157 leellDLLSSwPSLRELDLTGNPV 180
LRR_8 pfam13855
Leucine rich repeat;
142-203 6.62e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 52.14  E-value: 6.62e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30017449   142 LEVLLLYNNHISYLDPAAFGGLSHLQKLYLSGNFLTQFPMDLYTGrfkLADLTFLDVSYNRI 203
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSG---LPSLRYLDLSGNRL 61
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 297-367 5.99e-08

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 50.27  E-value: 5.99e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30017449   297 HEAQVGERAIVHCDSKTGNGNTDFIWVGPDNRLLEPDKDMGNFRVFYNGSLVIENPGFEDAGVYSCIAMNR 367
Cdd:pfam00047   6 VTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNP 76
LRR_8 pfam13855
Leucine rich repeat;
67-128 8.61e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 49.06  E-value: 8.61e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30017449    67 RLIKRLDLSYNRIGLLDADWIpVSFVKLSTLILRHNNITSISTGSFSTTPNLKCLDLSSNRL 128
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAF-KGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 300-371 1.37e-07

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 49.47  E-value: 1.37e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30017449 300 QVGERAIVHCDSkTGNGNTDFIWV----GPDNRLLEPDKDMGNFRVFYNGSLVIENPGFEDAGVYSCIAMNRQRLL 371
Cdd:cd05765  13 KVGETASFHCDV-TGRPQPEITWEkqvpGKENLIMRPNHVRGNVVVTNIGQLVIYNAQPQDAGLYTCTARNSGGLL 87
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 57-204 2.82e-07

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 53.31  E-value: 2.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449   57 NLS-KVPGNLFRLI--KRLDLSYNRIglldADWIPVSFVKLSTL---ILRHNNIT-SISTGSFSTTpNLKCLDLSSNRLK 129
Cdd:PLN00113 223 NLSgEIPYEIGGLTslNHLDLVYNNL----TGPIPSSLGNLKNLqylFLYQNKLSgPIPPSIFSLQ-KLISLDLSDNSLS 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449  130 SVKSATFQELKALEVLLLYNNHISYLDPAAFGGLSHLQKLYL-SGNFLTQFPMDLYtgrfKLADLTFLDVSYN----RIP 204
Cdd:PLN00113 298 GEIPELVIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLwSNKFSGEIPKNLG----KHNNLTVLDLSTNnltgEIP 373
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 297-366 3.23e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 47.95  E-value: 3.23e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449   297 HEAQVGERAIVHCDSkTGNGNTDFIWVgPDNRLLEPDKDMGNFRVFYNGSLVIENPGFEDAGVYSCIAMN 366
Cdd:pfam13927  11 VTVREGETVTLTCEA-TGSPPPTITWY-KNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
50-229 3.33e-07

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 53.16  E-value: 3.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449   50 IVSCtNKnLSKVPGNLFRLIKRLDLSYNRIGLLDADwIPVSFVKLStliLRHNNITSISTgsfSTTPNLKCLDLSSNRLK 129
Cdd:PRK15370 268 DLFH-NK-ISCLPENLPEELRYLSVYDNSIRTLPAH-LPSGITHLN---VQSNSLTALPE---TLPPGLKTLEAGENALT 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449  130 SVKSATFQELKALEVlllYNNHISYLdPAAFGglSHLQKLYLSGNFLTQFPMDLytgrfkLADLTFLDVSYNRIPSIP-- 207
Cdd:PRK15370 339 SLPASLPPELQVLDV---SKNQITVL-PETLP--PTITTLDVSRNALTNLPENL------PAALQIMQASRNNLVRLPes 406

                        170       180
                 ....*....|....*....|..
gi 30017449  208 MHHInLVPGRQLRGIYLHGNPF 229
Cdd:PRK15370 407 LPHF-RGEGPQPTRIIVEYNPF 427
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 297-379 7.29e-07

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: 47.11  E-value: 7.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449    297 HEAQVGERAIVHCDSkTGNGNTDFIWVGPDNRLLEPDkdmGNFRVFYNG---SLVIENPGFEDAGVYSCIAMNRQRLLNE 373
Cdd:smart00410   4 VTVKEGESVTLSCEA-SGSPPPEVTWYKQGGKLLAES---GRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSASS 79


                   ....*.
gi 30017449    374 TVDIMI 379
Cdd:smart00410  80 GTTLTV 85
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 55-174 1.49e-06

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: 49.01  E-value: 1.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449  55 NKNLSKVPG--NLFRLIKrLDLSYNRI----GLLDADwipvsfvKLSTLILRHNN-------------ITSIStgsfstt 115
Cdd:cd21340  55 NNQIEKIENleNLVNLKK-LYLGGNRIsvveGLENLT-------NLEELHIENQRlppgekltfdprsLAALS------- 119

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30017449 116 PNLKCLDLSSNRLKSVKSatFQELKALEVLLLYNNHISYLDP--AAFGGLSHLQKLYLSGN 174
Cdd:cd21340 120 NSLRVLNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGN 178
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 69-176 1.79e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 51.00  E-value: 1.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449   69 IKRLDLSYNRIglldADWIPVSFVKLSTLI---LRHNNITSISTGSFSTTPNLKCLDLSSNRLKSVKSATFQELKALEVL 145
Cdd:PLN00113 477 LENLDLSRNQF----SGAVPRKLGSLSELMqlkLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQL 552

                         90       100       110
                 ....*....|....*....|....*....|.
gi 30017449  146 LLYNNHISYLDPAAFGGLSHLQKLYLSGNFL 176
Cdd:PLN00113 553 DLSQNQLSGEIPKNLGNVESLVQVNISHNHL 583
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 305-366 7.71e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (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. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 43.86  E-value: 7.71e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30017449 305 AIVHCDSkTGNGNTDFIWVGpDNRLLEPDKDMGNFRVFYNGSLVIENPGFEDAGVYSCIAMN 366
Cdd:cd00096   1 VTLTCSA-SGNPPPTITWYK-NGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASN 60
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 70-203 2.53e-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: 46.19  E-value: 2.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449  70 KRLDLSYNRIGllDADWIPVSFV-----KLSTLILRHNNITSISTGS----FSTTPNLKCLDLSSNRL--KSVK--SATF 136
Cdd:cd00116 140 EKLVLGRNRLE--GASCEALAKAlranrDLKELNLANNGIGDAGIRAlaegLKANCNLEVLDLNNNGLtdEGASalAETL 217

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30017449 137 QELKALEVLLLYNNHI-----SYLDPAAFGGLSHLQKLYLSGNFLTQFP-MDLYTGRFKLADLTFLDVSYNRI 203
Cdd:cd00116 218 ASLKSLEVLNLGDNNLtdagaAALASALLSPNISLLTLSLSCNDITDDGaKDLAEVLAEKESLLELDLRGNKF 290
PLN03150 PLN03150
hypothetical protein; Provisional
 118-177 3.26e-05

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 46.73  E-value: 3.26e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449  118 LKCLDLSSNRLKSVKSATFQELKALEVLLLYNNHISYLDPAAFGGLSHLQKLYLSGNFLT 177
Cdd:PLN03150 444 LQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLS 503
PLN03150 PLN03150
hypothetical protein; Provisional
 80-163 3.59e-05

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 46.35  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449   80 GLLDADWipVSFVKLSTLILRHNNITSISTGSFSTTPNLKCLDLSSNRLKSVKSATFQELKALEVLLLYNNHISYLDPAA 159
Cdd:PLN03150 432 GFIPNDI--SKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLSGRVPAA 509


                 ....
gi 30017449  160 FGGL 163
Cdd:PLN03150 510 LGGR 513
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 302-366 1.23e-04

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (IgSF) domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 40.92  E-value: 1.23e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30017449 302 GERAIVHCDSKtGNGNTDFIWVGPDNRLlepdkdMGN---FRVFYNGSLVIENPGFEDAGVYSCIAMN 366
Cdd:cd05764  15 GQRATLRCKAR-GDPEPAIHWISPEGKL------ISNssrTLVYDNGTLDILITTVKDTGAFTCIASN 75
I-set pfam07679
Immunoglobulin I-set domain;
298-367 1.29e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 40.70  E-value: 1.29e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30017449   298 EAQVGERAIVHCDSkTGNGNTDFIWVgPDNRLLEPDKDmgnFRVFYNG---SLVIENPGFEDAGVYSCIAMNR 367
Cdd:pfam07679  11 EVQEGESARFTCTV-TGTPDPEVSWF-KDGQPLRSSDR---FKVTYEGgtyTLTISNVQPDDSGKYTCVATNS 78
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 340-368 1.72e-04

Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 40.63  E-value: 1.72e-04
                        10        20        30
                ....*....|....*....|....*....|
gi 30017449 340 RVFYNGSLVIEN-PGFEDAGVYSCIAMNRQ 368
Cdd:cd20958  48 RVFPNGTLVIENvQRSSDEGEYTCTARNQQ 77
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 116-157 3.40e-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: 38.38  E-value: 3.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 30017449   116 PNLKCLDLSSNRLKSVKSatFQELKALEVL-LLYNNHISYLDP 157
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPP--LAKLPNLETLdLSGNNKITDLSD 41
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 57-179 4.50e-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: 4.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449  57 NLSKVPG-NLFRLIKRLDLSYNRI----GLldadwipVSFVKLSTLILRHNNITSIStgSFSTTPNLKCLDLSSNRLKSV 131
Cdd:cd21340  35 KITKIENlEFLTNLTHLYLQNNQIekieNL-------ENLVNLKKLYLGGNRISVVE--GLENLTNLEELHIENQRLPPG 105

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 30017449 132 KSATFQE------LKALEVLLLYNNHISYLDPaaFGGLSHLQKLYLSGNFLTQF 179
Cdd:cd21340 106 EKLTFDPrslaalSNSLRVLNISGNNIDSLEP--LAPLRNLEQLDASNNQISDL 157
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 93-128 6.98e-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: 37.22  E-value: 6.98e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 30017449    93 KLSTLILRHNNITSIStgSFSTTPNLKCLDLSSNRL 128
Cdd:pfam12799   2 NLEVLDLSNNQITDIP--PLAKLPNLETLDLSGNNK 35
IgI_1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the ...
 298-379 8.38e-04

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1). NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-nonNCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409451  Cd Length: 97  Bit Score: 38.87  E-value: 8.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449 298 EAQVGERAIVHCDSKTGNGNTDFIWVGPDNRLLEPDKDmgNFRVFYN----GSLVIENPGFEDAGVYSCIAMNRQRLLNE 373
Cdd:cd05865  11 EISVGESKFFLCQVAGEAKDKDISWFSPNGEKLTPNQQ--RISVVRNddysSTLTIYNANIDDAGIYKCVVSNEDEGESE 88


                ....*..
gi 30017449 374 -TVDIMI 379
Cdd:cd05865  89 aTVNVKI 95
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 140-174 8.67e-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: 37.22  E-value: 8.67e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 30017449   140 KALEVLLLYNNHISYLDPaaFGGLSHLQKLYLSGN 174
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPP--LAKLPNLETLDLSGN 33
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
72-229 1.50e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.07  E-value: 1.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449  72 LDLSYNRIGLLDADWIPVSFVKLSTLILRHNNITSISTGSFSTTPNLKCLDLSSNRLKSVKSATFQELKALEVLLLYNNH 151
Cdd:COG4886   4 LLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLS 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30017449 152 ISYLDPAAFGGLSHLQKLYLSGNfltqfpmdlyTGRFKLADLTFLDVSYNRIPSIPMHHINLvpgRQLRGIYLHGNPF 229
Cdd:COG4886  84 LLLLGLTDLGDLTNLTELDLSGN----------EELSNLTNLESLDLSGNQLTDLPEELANL---TNLKELDLSNNQL 148
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 299-366 2.38e-03

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. 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. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. 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 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: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 37.37  E-value: 2.38e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30017449 299 AQVGERAIVHCdSKTGNGNTDFIWVGPDNRLlepDKDMGNFrVFYNGSLVIENPGFEDAGVYSCIAMN 366
Cdd:cd20978  13 VKGGQDVTLPC-QVTGVPQPKITWLHNGKPL---QGPMERA-TVEDGTLTIINVQPEDTGYYGCVATN 75
LRR_8 pfam13855
Leucine rich repeat;
164-229 2.51e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 36.35  E-value: 2.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30017449   164 SHLQKLYLSGNFLTQFPMDLYTGrfkLADLTFLDVSYNRIPSIPMHHinLVPGRQLRGIYLHGNPF 229
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKG---LSNLKVLDLSNNLLTTLSPGA--FSGLPSLRYLDLSGNRL 61
LRR_9 pfam14580
Leucine-rich repeat;
72-153 2.78e-03

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 38.98  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449    72 LDLSYNRIGLLDA-DWIPvsfvKLSTLILRHNNITSISTGSFSTTPNLKCLDLSSNRLKSVKSAT-FQELKALEVLLLYN 149
Cdd:pfam14580  47 IDFSDNEIRKLDGfPLLR----RLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLQELGDLDpLASLKKLTFLSLLR 122


                  ....
gi 30017449   150 NHIS 153
Cdd:pfam14580 123 NPVT 126
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 54-201 3.86e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 40.22  E-value: 3.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449   54 TNKNLS-KVPGNLFRLIKRLDLSYNRIglldADWIPV---SFVKLSTLILRHNNITSISTGSFSTTPNLKCLDLSSNRLK 129
Cdd:PLN00113 126 SNNNFTgSIPRGSIPNLETLDLSNNML----SGEIPNdigSFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLV 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017449  130 SVKSATFQELKALEVLLL-YNN-------------HISYLD----------PAAFGGLSHLQKLYLSGNFLT-QFPMDLy 184
Cdd:PLN00113 202 GQIPRELGQMKSLKWIYLgYNNlsgeipyeiggltSLNHLDlvynnltgpiPSSLGNLKNLQYLFLYQNKLSgPIPPSI- 280

                        170
                 ....*....|....*..
gi 30017449  185 tgrFKLADLTFLDVSYN 201
Cdd:PLN00113 281 ---FSLQKLISLDLSDN 294
 
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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