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Conserved domains on  [gi|1632519236|ref|NP_001357228|]
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amphoterin-induced protein 2 precursor [Homo sapiens]

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];
51-230 2.98e-19

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 89.99  E-value: 2.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236  51 IVSCTNKNLSKVPGNLFRL--IKRLDLSYNRIGLLDSEwIPvSFAKLNTLILRHNNITSISTgSFSTTPNLKCLDLSSNK 128
Cdd:COG4886   117 SLDLSGNQLTDLPEELANLtnLKELDLSNNQLTDLPEP-LG-NLTNLKSLDLSNNQLTDLPE-ELGNLTNLKELDLSNNQ 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236 129 LKTVKNAVFQELKVLEVLLlYNNHISYLdPSAFGGLSQLQKLYLSGNFLTQFPmDLyvgrFKLAELMFLDVSYNRIPSMP 208
Cdd:COG4886   194 ITDLPEPLGNLTNLEELDL-SGNQLTDL-PEPLANLTNLETLDLSNNQLTDLP-EL----GNLTNLEELDLSNNQLTDLP 266

                         170       180
                  ....*....|....*....|..
gi 1632519236 209 mhhiNLVPGKQLRGIYLHGNPF 230
Cdd:COG4886   267 ----PLANLTNLKTLDLSNNQL 284
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 298-380 2.45e-08

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: 51.35  E-value: 2.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236  298 HEAQVGERLMVHCDSkTGNANTDFIWVGPDNRLLEPDKEMENFYVFHNGSLVIESPRFEDAGVYSCIAMNKQRLLNETVD 377
Cdd:smart00410   4 VTVKEGESVTLSCEA-SGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82


                   ...
gi 1632519236  378 VTI 380
Cdd:smart00410  83 LTV 85
LRRCT super family cl47026
Leucine rich repeat C-terminal domain;
228-283 1.08e-03

Leucine rich repeat C-terminal domain;


The actual alignment was detected with superfamily member smart00082:

Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 37.02  E-value: 1.08e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1632519236  228 NPFVCDCSLYSLLVFWyrRHFSSVMDFkNDYTCrlWSDSRHSRQVLLLQDSFMNCS 283
Cdd:smart00082   1 NPFICDCELRWLLRWL--QANEHLQDP-VDLRC--ASPSSLRGPLLELLHSEFKCP 51
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-230 2.98e-19

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 89.99  E-value: 2.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236  51 IVSCTNKNLSKVPGNLFRL--IKRLDLSYNRIGLLDSEwIPvSFAKLNTLILRHNNITSISTgSFSTTPNLKCLDLSSNK 128
Cdd:COG4886   117 SLDLSGNQLTDLPEELANLtnLKELDLSNNQLTDLPEP-LG-NLTNLKSLDLSNNQLTDLPE-ELGNLTNLKELDLSNNQ 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236 129 LKTVKNAVFQELKVLEVLLlYNNHISYLdPSAFGGLSQLQKLYLSGNFLTQFPmDLyvgrFKLAELMFLDVSYNRIPSMP 208
Cdd:COG4886   194 ITDLPEPLGNLTNLEELDL-SGNQLTDL-PEPLANLTNLETLDLSNNQLTDLP-EL----GNLTNLEELDLSNNQLTDLP 266

                         170       180
                  ....*....|....*....|..
gi 1632519236 209 mhhiNLVPGKQLRGIYLHGNPF 230
Cdd:COG4886   267 ----PLANLTNLKTLDLSNNQL 284
LRR_8 pfam13855
Leucine rich repeat;
94-175 8.87e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 60.23  E-value: 8.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236  94 KLNTLILRHNNITSISTGSFSTTPNLKCLDLSSNKLKTvknavfqelkvlevlllynnhisyLDPSAFGGLSQLQKLYLS 173
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTT------------------------LSPGAFSGLPSLRYLDLS 57


                  ..
gi 1632519236 174 GN 175
Cdd:pfam13855  58 GN 59
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 298-380 2.45e-08

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: 51.35  E-value: 2.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236  298 HEAQVGERLMVHCDSkTGNANTDFIWVGPDNRLLEPDKEMENFYVFHNGSLVIESPRFEDAGVYSCIAMNKQRLLNETVD 377
Cdd:smart00410   4 VTVKEGESVTLSCEA-SGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82


                   ...
gi 1632519236  378 VTI 380
Cdd:smart00410  83 LTV 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 298-367 6.16e-07

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: 47.19  E-value: 6.16e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236 298 HEAQVGERLMVHCDSKTGNANTDFIWVGPDNRLLEPDKEMENFYVFHNGSLVIESPRFEDAGVYSCIAMN 367
Cdd:pfam00047   6 VTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNN 75
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 301-372 8.74e-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: 47.16  E-value: 8.74e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1632519236 301 QVGERLMVHCDSkTGNANTDFIWV----GPDNRLLEPDKEMENFYVFHNGSLVIESPRFEDAGVYSCIAMNKQRLL 372
Cdd:cd05765    13 KVGETASFHCDV-TGRPQPEITWEkqvpGKENLIMRPNHVRGNVVVTNIGQLVIYNAQPQDAGLYTCTARNSGGLL 87
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 92-230 2.40e-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: 48.63  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236  92 FAKLNTLILRHNNITSIstGSFSTTPNLKCLDLSSNKLKTVKNAVF---------QelkvlevlllyNNHISYLDPsaFG 162
Cdd:cd21340     1 LKRITHLYLNDKNITKI--DNLSLCKNLKVLYLYDNKITKIENLEFltnlthlylQ-----------NNQIEKIEN--LE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236 163 GLSQLQKLYLSGNF------LTQFPM--DLYVGRFKLAE-----------------LMFLDVSYNRIPSM----PMHHI- 212
Cdd:cd21340    66 NLVNLKKLYLGGNRisvvegLENLTNleELHIENQRLPPgekltfdprslaalsnsLRVLNISGNNIDSLeplaPLRNLe 145

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1632519236 213 ----------------NLVPG-KQLRGIYLHGNPF 230
Cdd:cd21340   146 qldasnnqisdleellDLLSSwPSLRELDLTGNPV 180
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
52-208 4.46e-06

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 49.31  E-value: 4.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236  52 VSCTNKNLSKVPGNLFRLIKRLDLSYNRIGLLdSEWIPvsfAKLNTLILRHNNITSIStgsfSTTPN-LKCLDLSSNKLK 130
Cdd:PRK15370  225 LYANSNQLTSIPATLPDTIQEMELSINRITEL-PERLP---SALQSLDLFHNKISCLP----ENLPEeLRYLSVYDNSIR 296

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1632519236 131 TVKNavfQELKVLEVLLLYNNHISYLDPSAFGGLSQLQKlylSGNFLTQFPMDLyvgrfkLAELMFLDVSYNRIPSMP 208
Cdd:PRK15370  297 TLPA---HLPSGITHLNVQSNSLTALPETLPPGLKTLEA---GENALTSLPASL------PPELQVLDVSKNQITVLP 362
LRRCT smart00082
Leucine rich repeat C-terminal domain;
228-283 1.08e-03

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 37.02  E-value: 1.08e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1632519236  228 NPFVCDCSLYSLLVFWyrRHFSSVMDFkNDYTCrlWSDSRHSRQVLLLQDSFMNCS 283
Cdd:smart00082   1 NPFICDCELRWLLRWL--QANEHLQDP-VDLRC--ASPSSLRGPLLELLHSEFKCP 51
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-230 2.98e-19

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 89.99  E-value: 2.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236  51 IVSCTNKNLSKVPGNLFRL--IKRLDLSYNRIGLLDSEwIPvSFAKLNTLILRHNNITSISTgSFSTTPNLKCLDLSSNK 128
Cdd:COG4886   117 SLDLSGNQLTDLPEELANLtnLKELDLSNNQLTDLPEP-LG-NLTNLKSLDLSNNQLTDLPE-ELGNLTNLKELDLSNNQ 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236 129 LKTVKNAVFQELKVLEVLLlYNNHISYLdPSAFGGLSQLQKLYLSGNFLTQFPmDLyvgrFKLAELMFLDVSYNRIPSMP 208
Cdd:COG4886   194 ITDLPEPLGNLTNLEELDL-SGNQLTDL-PEPLANLTNLETLDLSNNQLTDLP-EL----GNLTNLEELDLSNNQLTDLP 266

                         170       180
                  ....*....|....*....|..
gi 1632519236 209 mhhiNLVPGKQLRGIYLHGNPF 230
Cdd:COG4886   267 ----PLANLTNLKTLDLSNNQL 284
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-207 6.31e-15

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 76.90  E-value: 6.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236  51 IVSCTNKNLSKVPGNLFRL--IKRLDLSYNRIGLLDSEWIpvSFAKLNTLILRHNNITSISTgSFSTTPNLKCLDLSSNK 128
Cdd:COG4886   140 ELDLSNNQLTDLPEPLGNLtnLKSLDLSNNQLTDLPEELG--NLTNLKELDLSNNQITDLPE-PLGNLTNLEELDLSGNQ 216

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1632519236 129 LKTVKNAVFQELKVLEVLLlYNNHISYLdpSAFGGLSQLQKLYLSGNFLTQFPMDLyvgrfKLAELMFLDVSYNRIPSM 207
Cdd:COG4886   217 LTDLPEPLANLTNLETLDL-SNNQLTDL--PELGNLTNLEELDLSNNQLTDLPPLA-----NLTNLKTLDLSNNQLTDL 287
LRR_8 pfam13855
Leucine rich repeat;
94-175 8.87e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 60.23  E-value: 8.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236  94 KLNTLILRHNNITSISTGSFSTTPNLKCLDLSSNKLKTvknavfqelkvlevlllynnhisyLDPSAFGGLSQLQKLYLS 173
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTT------------------------LSPGAFSGLPSLRYLDLS 57


                  ..
gi 1632519236 174 GN 175
Cdd:pfam13855  58 GN 59
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
55-230 9.50e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 60.72  E-value: 9.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236  55 TNKNLSKVPGNLFRLIKRLDLSYNRIGLLDSEWIPVSFAKLNTLILRHNNITSISTGSFSTTPNLKCLDLSSNKLktvkn 134
Cdd:COG4886    34 LLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEE----- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236 135 avFQELKVLEVLLLYNNHISYLdPSAFGGLSQLQKLYLSGNFLTQFPMDLyvgrFKLAELMFLDVSYNRIPSMPMHHINL 214
Cdd:COG4886   109 --LSNLTNLESLDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDLPEPL----GNLTNLKSLDLSNNQLTDLPEELGNL 181

                         170
                  ....*....|....*.
gi 1632519236 215 vpgKQLRGIYLHGNPF 230
Cdd:COG4886   182 ---TNLKELDLSNNQI 194
LRR_8 pfam13855
Leucine rich repeat;
68-129 2.35e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 50.60  E-value: 2.35e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1632519236  68 RLIKRLDLSYNRIGLLDSEWIpVSFAKLNTLILRHNNITSISTGSFSTTPNLKCLDLSSNKL 129
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAF-KGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 298-380 2.45e-08

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: 51.35  E-value: 2.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236  298 HEAQVGERLMVHCDSkTGNANTDFIWVGPDNRLLEPDKEMENFYVFHNGSLVIESPRFEDAGVYSCIAMNKQRLLNETVD 377
Cdd:smart00410   4 VTVKEGESVTLSCEA-SGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82


                   ...
gi 1632519236  378 VTI 380
Cdd:smart00410  83 LTV 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 298-367 6.16e-07

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: 47.19  E-value: 6.16e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236 298 HEAQVGERLMVHCDSKTGNANTDFIWVGPDNRLLEPDKEMENFYVFHNGSLVIESPRFEDAGVYSCIAMN 367
Cdd:pfam00047   6 VTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNN 75
LRR_8 pfam13855
Leucine rich repeat;
150-204 8.67e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 45.98  E-value: 8.67e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1632519236 150 NNHISYLDPSAFGGLSQLQKLYLSGNFLTQFPMDLYVGrfkLAELMFLDVSYNRI 204
Cdd:pfam13855  10 NNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSG---LPSLRYLDLSGNRL 61
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 301-372 8.74e-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: 47.16  E-value: 8.74e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1632519236 301 QVGERLMVHCDSkTGNANTDFIWV----GPDNRLLEPDKEMENFYVFHNGSLVIESPRFEDAGVYSCIAMNKQRLL 372
Cdd:cd05765    13 KVGETASFHCDV-TGRPQPEITWEkqvpGKENLIMRPNHVRGNVVVTNIGQLVIYNAQPQDAGLYTCTARNSGGLL 87
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 298-367 1.16e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 46.40  E-value: 1.16e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236 298 HEAQVGERLMVHCDSkTGNANTDFIWVgPDNRLLEPDKEMENFYVFHNGSLVIESPRFEDAGVYSCIAMN 367
Cdd:pfam13927  11 VTVREGETVTLTCEA-TGSPPPTITWY-KNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 92-230 2.40e-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: 48.63  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236  92 FAKLNTLILRHNNITSIstGSFSTTPNLKCLDLSSNKLKTVKNAVF---------QelkvlevlllyNNHISYLDPsaFG 162
Cdd:cd21340     1 LKRITHLYLNDKNITKI--DNLSLCKNLKVLYLYDNKITKIENLEFltnlthlylQ-----------NNQIEKIEN--LE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236 163 GLSQLQKLYLSGNF------LTQFPM--DLYVGRFKLAE-----------------LMFLDVSYNRIPSM----PMHHI- 212
Cdd:cd21340    66 NLVNLKKLYLGGNRisvvegLENLTNleELHIENQRLPPgekltfdprslaalsnsLRVLNISGNNIDSLeplaPLRNLe 145

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1632519236 213 ----------------NLVPG-KQLRGIYLHGNPF 230
Cdd:cd21340   146 qldasnnqisdleellDLLSSwPSLRELDLTGNPV 180
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 306-368 4.31e-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: 44.63  E-value: 4.31e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1632519236 306 LMVHCDSkTGNANTDFIWVGpDNRLLEPDKEMENFYVFHNGSLVIESPRFEDAGVYSCIAMNK 368
Cdd:cd00096     1 VTLTCSA-SGNPPPTITWYK-NGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNS 61
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
52-208 4.46e-06

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 49.31  E-value: 4.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236  52 VSCTNKNLSKVPGNLFRLIKRLDLSYNRIGLLdSEWIPvsfAKLNTLILRHNNITSIStgsfSTTPN-LKCLDLSSNKLK 130
Cdd:PRK15370  225 LYANSNQLTSIPATLPDTIQEMELSINRITEL-PERLP---SALQSLDLFHNKISCLP----ENLPEeLRYLSVYDNSIR 296

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1632519236 131 TVKNavfQELKVLEVLLLYNNHISYLDPSAFGGLSQLQKlylSGNFLTQFPMDLyvgrfkLAELMFLDVSYNRIPSMP 208
Cdd:PRK15370  297 TLPA---HLPSGITHLNVQSNSLTALPETLPPGLKTLEA---GENALTSLPASL------PPELQVLDVSKNQITVLP 362
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
58-158 5.71e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.78  E-value: 5.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236  58 NLSKVPGNLFRL--IKRLDLSYNRIglldsEWIPV--SFAKLNTLILRHNNITSIStgSFSTTPNLKCLDLSSNKLKTVK 133
Cdd:COG4886   216 QLTDLPEPLANLtnLETLDLSNNQL-----TDLPElgNLTNLEELDLSNNQLTDLP--PLANLTNLKTLDLSNNQLTDLK 288

                          90       100
                  ....*....|....*....|....*
gi 1632519236 134 NAVFQELKVLEVLLLYNNHISYLDP 158
Cdd:COG4886   289 LKELELLLGLNSLLLLLLLLNLLEL 313
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 342-369 8.30e-05

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: 41.40  E-value: 8.30e-05
                          10        20
                  ....*....|....*....|....*....
gi 1632519236 342 VFHNGSLVIES-PRFEDAGVYSCIAMNKQ 369
Cdd:cd20958    49 VFPNGTLVIENvQRSSDEGEYTCTARNQQ 77
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 297-382 1.76e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 40.57  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236 297 IHEAQVGERLMVHCDSKTGNANTDFIWVGPDNRL-LEPDKEMENFYVFHNGSLVIESPRFEDAGVYSCIAMNKqrLLNET 375
Cdd:cd05750     8 SQTVQEGSKLVLKCEATSENPSPRYRWFKDGKELnRKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENI--LGKDT 85


                  ....*..
gi 1632519236 376 VDVTINV 382
Cdd:cd05750    86 VTGNVTV 92
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 94-129 3.26e-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: 3.26e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1632519236  94 KLNTLILRHNNITSIStgSFSTTPNLKCLDLSSNKL 129
Cdd:pfam12799   2 NLEVLDLSNNQITDIP--PLAKLPNLETLDLSGNNK 35
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 42-228 5.32e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 42.91  E-value: 5.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236  42 PTACICATDIVSCTN-----------KNLS-KVPGNLFRL--IKRLDLSYNRIGLLDSEWIPVSFAKLNTLILRHNNIT- 106
Cdd:PLN00113   53 SSADVCLWQGITCNNssrvvsidlsgKNISgKISSAIFRLpyIQTINLSNNQLSGPIPDDIFTTSSSLRYLNLSNNNFTg 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236 107 SISTGSFsttPNLKCLDLSsnklktvknavfqelkvlevlllyNNHISYLDPSAFGGLSQLQKLYLSGNFLT-QFPmdLY 185
Cdd:PLN00113  133 SIPRGSI---PNLETLDLS------------------------NNMLSGEIPNDIGSFSSLKVLDLGGNVLVgKIP--NS 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1632519236 186 VGrfKLAELMFLDVSYNR----IPSmpmhhiNLVPGKQLRGIYLHGN 228
Cdd:PLN00113  184 LT--NLTSLEFLTLASNQlvgqIPR------ELGQMKSLKWIYLGYN 222
LRRCT smart00082
Leucine rich repeat C-terminal domain;
228-283 1.08e-03

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 37.02  E-value: 1.08e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1632519236  228 NPFVCDCSLYSLLVFWyrRHFSSVMDFkNDYTCrlWSDSRHSRQVLLLQDSFMNCS 283
Cdd:smart00082   1 NPFICDCELRWLLRWL--QANEHLQDP-VDLRC--ASPSSLRGPLLELLHSEFKCP 51
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 303-380 1.43e-03

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: 37.84  E-value: 1.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1632519236 303 GERLMVHCDSKtGNANTDFIWVGPDNRLLEPDKEMenfYVFHNGSLVIESPRFEDAGVYSCIAMNKQRLLNETVDVTI 380
Cdd:cd05764    15 GQRATLRCKAR-GDPEPAIHWISPEGKLISNSSRT---LVYDNGTLDILITTVKDTGAFTCIASNPAGEATARVELHI 88
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 300-367 2.19e-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: 2.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1632519236 300 AQVGERLMVHCdSKTGNANTDFIWVGPDNRLlepDKEMENfYVFHNGSLVIESPRFEDAGVYSCIAMN 367
Cdd:cd20978    13 VKGGQDVTLPC-QVTGVPQPKITWLHNGKPL---QGPMER-ATVEDGTLTIINVQPEDTGYYGCVATN 75
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 299-367 2.30e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. 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: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 37.38  E-value: 2.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1632519236 299 EAQVGERLMVHCDSKTGNANTDFIWVGPDNRLLEPDkemENFYVFHNGSLVIESPRFEDAGVYSCIAMN 367
Cdd:cd05724     8 QVAVGEMAVLECSPPRGHPEPTVSWRKDGQPLNLDN---ERVRIVDDGNLLIAEARKSDEGTYKCVATN 73
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 70-177 2.78e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 40.60  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632519236  70 IKRLDLSYNRIglldSEWIPVSFAKLNTLI---LRHNNITSISTGSFSTTPNLKCLDLSSNKLKTVKNAVFQELKVLEVL 146
Cdd:PLN00113  477 LENLDLSRNQF----SGAVPRKLGSLSELMqlkLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQL 552

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1632519236 147 LLYNNHISYLDPSAFGGLSQLQKLYLSGNFL 177
Cdd:PLN00113  553 DLSQNQLSGEIPKNLGNVESLVQVNISHNHL 583
 
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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