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Conserved domains on  [gi|24584026|ref|NP_609610|]
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uncharacterized protein Dmel_CG16974, isoform A [Drosophila melanogaster]

Protein Classification

LRR and Ig domain-containing protein( domain architecture ID 11469616)

LRR and Ig 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];
230-531 1.61e-26

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 113.88  E-value: 1.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  230 KVLEMSGNRLSNCSLlNLQYMKQLQELHLDRSELTYLPqRFLGELSELRMLNLSQNLLTELPRDIfvGALK-LERLYLSG 308
Cdd:COG4886  116 ESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDLP-EPLGNLTNLKSLDLSNNQLTDLPEEL--GNLTnLKELDLSN 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  309 NRLSVLPFMLFQTAAdLQVLDLSDNRLLSFPDNfFARNGQLRQLHLQRNQLKSIGkhSLYSLRELRQLDLSQNSLSVIDr 388
Cdd:COG4886  192 NQITDLPEPLGNLTN-LEELDLSGNQLTDLPEP-LANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNNQLTDLP- 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  389 kAFESLDHLLALNVSGNNLTLLSSIIFQSLHALRQLDLSRNQFK---QLPSGLFQRQRSLVLLRIDETPIEQFSNWISRY 465
Cdd:COG4886  267 -PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNlleLLILLLLLTTLLLLLLLLKGLLVTLTTLALSLS 345
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24584026  466 DESLVDPQVLHRLRYLSVQQNRKLTYLPATLFANTPNIRELLLAENGLLQLPTQISGLSRLQRLSV 531
Cdd:COG4886  346 LLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAV 411
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
714-761 9.88e-09

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.


The actual alignment was detected with superfamily member cd04969:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 89  Bit Score: 53.62  E-value: 9.88e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 24584026  714 SLNWTRQNSLV--GRRVVLVENGSLLVHNISRIDSGLYTCYAFNVMGKAS 761
Cdd:cd04969   33 TISWSKGTELLtnSSRICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKAN 82
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
230-531 1.61e-26

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 113.88  E-value: 1.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  230 KVLEMSGNRLSNCSLlNLQYMKQLQELHLDRSELTYLPqRFLGELSELRMLNLSQNLLTELPRDIfvGALK-LERLYLSG 308
Cdd:COG4886  116 ESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDLP-EPLGNLTNLKSLDLSNNQLTDLPEEL--GNLTnLKELDLSN 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  309 NRLSVLPFMLFQTAAdLQVLDLSDNRLLSFPDNfFARNGQLRQLHLQRNQLKSIGkhSLYSLRELRQLDLSQNSLSVIDr 388
Cdd:COG4886  192 NQITDLPEPLGNLTN-LEELDLSGNQLTDLPEP-LANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNNQLTDLP- 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  389 kAFESLDHLLALNVSGNNLTLLSSIIFQSLHALRQLDLSRNQFK---QLPSGLFQRQRSLVLLRIDETPIEQFSNWISRY 465
Cdd:COG4886  267 -PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNlleLLILLLLLTTLLLLLLLLKGLLVTLTTLALSLS 345
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24584026  466 DESLVDPQVLHRLRYLSVQQNRKLTYLPATLFANTPNIRELLLAENGLLQLPTQISGLSRLQRLSV 531
Cdd:COG4886  346 LLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAV 411
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
215-450 3.31e-14

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 77.97  E-value: 3.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   215 LECLHW-------AIPLAVR---RVKVLEMSGNRLSNCSLLNLQYMKQLQELHLDRSELT-YLPQRFLGELSELRMLNLS 283
Cdd:PLN00113  310 LEILHLfsnnftgKIPVALTslpRLQVLQLWSNKFSGEIPKNLGKHNNLTVLDLSTNNLTgEIPEGLCSSGNLFKLILFS 389
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   284 QNLLTELPRDIfvGALK-LERLYLSGNRLS--------VLPFMLFQTAAD----------------LQVLDLSDNRLL-S 337
Cdd:PLN00113  390 NSLEGEIPKSL--GACRsLRRVRLQDNSFSgelpseftKLPLVYFLDISNnnlqgrinsrkwdmpsLQMLSLARNKFFgG 467
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   338 FPDNFfaRNGQLRQLHLQRNQLKSIGKHSLYSLRELRQLDLSQNSLSVIDRKAFESLDHLLALNVSGNNLTLLSSIIFQS 417
Cdd:PLN00113  468 LPDSF--GSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSE 545
                         250       260       270
                  ....*....|....*....|....*....|....
gi 24584026   418 LHALRQLDLSRNQFK-QLPSGLfQRQRSLVLLRI 450
Cdd:PLN00113  546 MPVLSQLDLSQNQLSgEIPKNL-GNVESLVQVNI 578
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
304-470 5.10e-14

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: 72.51  E-value: 5.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  304 LYLSGNRLSVLPfmLFQTAADLQVLDLSDNRLLSFPDNFFARNgqLRQLHLQRNQLKSIGkhSLYSLRELRQLDLSQNSL 383
Cdd:cd21340    7 LYLNDKNITKID--NLSLCKNLKVLYLYDNKITKIENLEFLTN--LTHLYLQNNQIEKIE--NLENLVNLKKLYLGGNRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  384 SVIdrKAFESLDHL-------------------------LA-----LNVSGNNLTLLSSiiFQSLHALRQLDLSRNQFKQ 433
Cdd:cd21340   81 SVV--EGLENLTNLeelhienqrlppgekltfdprslaaLSnslrvLNISGNNIDSLEP--LAPLRNLEQLDASNNQISD 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 24584026  434 LP--SGLFQRQRSLVLLRIDETPIEQfsnwISRYDESLV 470
Cdd:cd21340  157 LEelLDLLSSWPSLRELDLTGNPVCK----KPKYRDKII 191
LRR_8 pfam13855
Leucine rich repeat;
371-431 4.96e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 62.16  E-value: 4.96e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584026    371 RELRQLDLSQNSLSVIDRKAFESLDHLLALNVSGNNLTLLSSIIFQSLHALRQLDLSRNQF 431
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
714-761 9.88e-09

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 53.62  E-value: 9.88e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 24584026  714 SLNWTRQNSLV--GRRVVLVENGSLLVHNISRIDSGLYTCYAFNVMGKAS 761
Cdd:cd04969   33 TISWSKGTELLtnSSRICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKAN 82
I-set pfam07679
Immunoglobulin I-set domain;
649-766 5.94e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 43.01  E-value: 5.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026    649 STAKLECQISGSPVPDIIWVTprnkilrhhadpdkrpiiidskedahqppsaqelaalmDESYIQSlnwtrqnslvGRRV 728
Cdd:pfam07679   16 ESARFTCTVTGTPDPEVSWFK--------------------------------------DGQPLRS----------SDRF 47
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 24584026    729 VLVENG---SLLVHNISRIDSGLYTCYAFNVMGKASAGLRL 766
Cdd:pfam07679   48 KVTYEGgtyTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
649-768 8.50e-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: 42.49  E-value: 8.50e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026     649 STAKLECQISGSPVPDIIWVTPRNKILrhhadpdkrpiiidskedahqppsaqelaalmdeSYIQSLNWTRQNSlvgrrv 728
Cdd:smart00410   10 ESVTLSCEASGSPPPEVTWYKQGGKLL----------------------------------AESGRFSVSRSGS------ 49
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 24584026     729 vlveNGSLLVHNISRIDSGLYTCYAFNVMGKASAGLRLYI 768
Cdd:smart00410   50 ----TSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
LRR smart00370
Leucine-rich repeats, outliers;
418-440 5.42e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 35.41  E-value: 5.42e-03
                            10        20
                    ....*....|....*....|...
gi 24584026     418 LHALRQLDLSRNQFKQLPSGLFQ 440
Cdd:smart00370    1 LPNLRELDLSNNQLSSLPPGAFQ 23
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
230-531 1.61e-26

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 113.88  E-value: 1.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  230 KVLEMSGNRLSNCSLlNLQYMKQLQELHLDRSELTYLPqRFLGELSELRMLNLSQNLLTELPRDIfvGALK-LERLYLSG 308
Cdd:COG4886  116 ESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDLP-EPLGNLTNLKSLDLSNNQLTDLPEEL--GNLTnLKELDLSN 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  309 NRLSVLPFMLFQTAAdLQVLDLSDNRLLSFPDNfFARNGQLRQLHLQRNQLKSIGkhSLYSLRELRQLDLSQNSLSVIDr 388
Cdd:COG4886  192 NQITDLPEPLGNLTN-LEELDLSGNQLTDLPEP-LANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNNQLTDLP- 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  389 kAFESLDHLLALNVSGNNLTLLSSIIFQSLHALRQLDLSRNQFK---QLPSGLFQRQRSLVLLRIDETPIEQFSNWISRY 465
Cdd:COG4886  267 -PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNlleLLILLLLLTTLLLLLLLLKGLLVTLTTLALSLS 345
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24584026  466 DESLVDPQVLHRLRYLSVQQNRKLTYLPATLFANTPNIRELLLAENGLLQLPTQISGLSRLQRLSV 531
Cdd:COG4886  346 LLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAV 411
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
246-436 4.68e-26

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 112.72  E-value: 4.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  246 NLQYMKQLQELHLDRSEltylpqrFLGELSELRMLNLSQNLLTELPRDIfvGALK-LERLYLSGNRLSVLPFMLFQTAAd 324
Cdd:COG4886   91 DLGDLTNLTELDLSGNE-------ELSNLTNLESLDLSGNQLTDLPEEL--ANLTnLKELDLSNNQLTDLPEPLGNLTN- 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  325 LQVLDLSDNRLLSFPDnFFARNGQLRQLHLQRNQLKSIGKhSLYSLRELRQLDLSQNSLSVIDrKAFESLDHLLALNVSG 404
Cdd:COG4886  161 LKSLDLSNNQLTDLPE-ELGNLTNLKELDLSNNQITDLPE-PLGNLTNLEELDLSGNQLTDLP-EPLANLTNLETLDLSN 237
                        170       180       190
                 ....*....|....*....|....*....|..
gi 24584026  405 NNLTLLSSIifQSLHALRQLDLSRNQFKQLPS 436
Cdd:COG4886  238 NQLTDLPEL--GNLTNLEELDLSNNQLTDLPP 267
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
139-511 7.85e-25

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 108.87  E-value: 7.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  139 NQELLSQRSSHINYNQLMLAHVPADRSNPLKLPQLESLREFSWQSSELKDETLMELFTRQP-RSFEYMERLNLAENRLEC 217
Cdd:COG4886   48 LLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEElSNLTNLESLDLSGNQLTD 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  218 LHWAIPlAVRRVKVLEMSGNRLSncSL-LNLQYMKQLQELHLDRSELTYLPqRFLGELSELRMLNLSQNLLTELPRDIfv 296
Cdd:COG4886  128 LPEELA-NLTNLKELDLSNNQLT--DLpEPLGNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNNQITDLPEPL-- 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  297 GALK-LERLYLSGNRLSVLPFMLFQTAAdLQVLDLSDNRLLSFPDnfFARNGQLRQLHLQRNQLKSIGKhsLYSLRELRQ 375
Cdd:COG4886  202 GNLTnLEELDLSGNQLTDLPEPLANLTN-LETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDLPP--LANLTNLKT 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  376 LDLSQNSLSVIDRKAFESLDHLLALNVSGNNLTLLSSIIFQSLHALRQLDLSRNQFKQLPSGLFQRQRSLVLLRIDETPI 455
Cdd:COG4886  277 LDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLL 356
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 24584026  456 EQFSNWISRYDESLVDPQVLHRLRYLSVQQNRKLTYLPATLFANTPNIRELLLAEN 511
Cdd:COG4886  357 NLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAVN 412
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
232-558 1.23e-23

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 105.40  E-value: 1.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  232 LEMSGNRLSNCSLLNLQYMKQLQELHLDRSELTYLPQRFLGELSELRMLNLSQNLLTELPRDIFVGALKLERLYLSGNRL 311
Cdd:COG4886    5 LLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  312 SVLPFMLFQTAADLQVLDLSDNRLLSFPDNffarngqLRQLHLQRNQLKSIGKhSLYSLRELRQLDLSQNSLSVIDrKAF 391
Cdd:COG4886   85 LLLGLTDLGDLTNLTELDLSGNEELSNLTN-------LESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDLP-EPL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  392 ESLDHLLALNVSGNNLTLLSSIIFQsLHALRQLDLSRNQFKQLPSGLFQrqrslvllridetpieqfsnwisrydeslvd 471
Cdd:COG4886  156 GNLTNLKSLDLSNNQLTDLPEELGN-LTNLKELDLSNNQITDLPEPLGN------------------------------- 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  472 pqvLHRLRYLSVQQNrKLTYLPATLfANTPNIRELLLAENGLLQLPtQISGLSRLQRLSVRGNSLGSLPEnIKELRQLHY 551
Cdd:COG4886  204 ---LTNLEELDLSGN-QLTDLPEPL-ANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKT 276

                 ....*..
gi 24584026  552 LNILGNE 558
Cdd:COG4886  277 LDLSNNQ 283
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
215-450 3.31e-14

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 77.97  E-value: 3.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   215 LECLHW-------AIPLAVR---RVKVLEMSGNRLSNCSLLNLQYMKQLQELHLDRSELT-YLPQRFLGELSELRMLNLS 283
Cdd:PLN00113  310 LEILHLfsnnftgKIPVALTslpRLQVLQLWSNKFSGEIPKNLGKHNNLTVLDLSTNNLTgEIPEGLCSSGNLFKLILFS 389
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   284 QNLLTELPRDIfvGALK-LERLYLSGNRLS--------VLPFMLFQTAAD----------------LQVLDLSDNRLL-S 337
Cdd:PLN00113  390 NSLEGEIPKSL--GACRsLRRVRLQDNSFSgelpseftKLPLVYFLDISNnnlqgrinsrkwdmpsLQMLSLARNKFFgG 467
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   338 FPDNFfaRNGQLRQLHLQRNQLKSIGKHSLYSLRELRQLDLSQNSLSVIDRKAFESLDHLLALNVSGNNLTLLSSIIFQS 417
Cdd:PLN00113  468 LPDSF--GSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSE 545
                         250       260       270
                  ....*....|....*....|....*....|....
gi 24584026   418 LHALRQLDLSRNQFK-QLPSGLfQRQRSLVLLRI 450
Cdd:PLN00113  546 MPVLSQLDLSQNQLSgEIPKNL-GNVESLVQVNI 578
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
304-470 5.10e-14

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: 72.51  E-value: 5.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  304 LYLSGNRLSVLPfmLFQTAADLQVLDLSDNRLLSFPDNFFARNgqLRQLHLQRNQLKSIGkhSLYSLRELRQLDLSQNSL 383
Cdd:cd21340    7 LYLNDKNITKID--NLSLCKNLKVLYLYDNKITKIENLEFLTN--LTHLYLQNNQIEKIE--NLENLVNLKKLYLGGNRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  384 SVIdrKAFESLDHL-------------------------LA-----LNVSGNNLTLLSSiiFQSLHALRQLDLSRNQFKQ 433
Cdd:cd21340   81 SVV--EGLENLTNLeelhienqrlppgekltfdprslaaLSnslrvLNISGNNIDSLEP--LAPLRNLEQLDASNNQISD 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 24584026  434 LP--SGLFQRQRSLVLLRIDETPIEQfsnwISRYDESLV 470
Cdd:cd21340  157 LEelLDLLSSWPSLRELDLTGNPVCK----KPKYRDKII 191
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
251-547 2.84e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 74.35  E-value: 2.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   251 KQLQELHLDRSELTYLPQRFLGELSElrmLNLSQNLLTELPRDIfvgALKLERLYLSGNRLSVLPFMLfqtAADLQVLDL 330
Cdd:PRK15370  199 EQITTLILDNNELKSLPENLQGNIKT---LYANSNQLTSIPATL---PDTIQEMELSINRITELPERL---PSALQSLDL 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   331 SDNRLLSFPDNFfarngqlrqlhlqrnqlksigkhslysLRELRQLDLSQNSLSVIDRKAFESLDHllaLNVSGNNLTLL 410
Cdd:PRK15370  270 FHNKISCLPENL---------------------------PEELRYLSVYDNSIRTLPAHLPSGITH---LNVQSNSLTAL 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   411 SSIIFQSLHALRQLDlsrNQFKQLPSGLfqrqrslvllridetPIEqfsnwisrydeslvdpqvlhrLRYLSVQQNRkLT 490
Cdd:PRK15370  320 PETLPPGLKTLEAGE---NALTSLPASL---------------PPE---------------------LQVLDVSKNQ-IT 359
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24584026   491 YLPATLfanTPNIRELLLAENGLLQLPTQISglSRLQRLSVRGNSLGSLPENIKELR 547
Cdd:PRK15370  360 VLPETL---PPTITTLDVSRNALTNLPENLP--AALQIMQASRNNLVRLPESLPHFR 411
LRR_8 pfam13855
Leucine rich repeat;
371-431 4.96e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 62.16  E-value: 4.96e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584026    371 RELRQLDLSQNSLSVIDRKAFESLDHLLALNVSGNNLTLLSSIIFQSLHALRQLDLSRNQF 431
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
348-407 4.05e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.46  E-value: 4.05e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026    348 QLRQLHLQRNQLKSIGKHSLYSLRELRQLDLSQNSLSVIDRKAFESLDHLLALNVSGNNL 407
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
227-425 7.91e-11

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: 63.27  E-value: 7.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  227 RRVKVLEMSGNRLSNCSLLNLqyMKQLQELHLDRSELTYLPQrfLGELSELRMLNLSQNLLTELPRdiFVGALKLERLYL 306
Cdd:cd21340    2 KRITHLYLNDKNITKIDNLSL--CKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLYL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  307 SGNRLSVLPFmlFQTAADLQVLDLSDNRL-----LSF-PDNFFARNGQLRQLHLQRNQLKSIgkHSLYSLRELRQLDLSQ 380
Cdd:cd21340   76 GGNRISVVEG--LENLTNLEELHIENQRLppgekLTFdPRSLAALSNSLRVLNISGNNIDSL--EPLAPLRNLEQLDASN 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24584026  381 NSLSVIDR--KAFESLDHLLALNVSGNNLTLLS----SIIFQSlHALRQLD 425
Cdd:cd21340  152 NQISDLEEllDLLSSWPSLRELDLTGNPVCKKPkyrdKIILAS-KSLEVLD 201
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
246-433 3.04e-10

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: 63.14  E-value: 3.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  246 NLQYMKQLQELHLDRSELTYLPQRFLGEL---SELRMLNLSQNLLTELPRDIFVGALK-----LERLYLSGNRLSVLPFM 317
Cdd:cd00116   76 GLTKGCGLQELDLSDNALGPDGCGVLESLlrsSSLQELKLNNNGLGDRGLRLLAKGLKdlppaLEKLVLGRNRLEGASCE 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  318 ----LFQTAADLQVLDLSDNRLLS------FPDnfFARNGQLRQLHLQRNQLKSIG----KHSLYSLRELRQLDLSQNSL 383
Cdd:cd00116  156 alakALRANRDLKELNLANNGIGDagiralAEG--LKANCNLEVLDLNNNGLTDEGasalAETLASLKSLEVLNLGDNNL 233
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 24584026  384 SVIDRKAFES-----LDHLLALNVSGNNLTLLSSIIF-QSLHA---LRQLDLSRNQFKQ 433
Cdd:cd00116  234 TDAGAAALASallspNISLLTLSLSCNDITDDGAKDLaEVLAEkesLLELDLRGNKFGE 292
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
228-560 3.50e-10

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 64.48  E-value: 3.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   228 RVKVLEMSGNRLS---NCSLLNLQYmkqLQELHLDRSELTY-LPQRFLGELSELRMLNLSQNLLT-ELPRDIFVGalkLE 302
Cdd:PLN00113   70 RVVSIDLSGKNISgkiSSAIFRLPY---IQTINLSNNQLSGpIPDDIFTTSSSLRYLNLSNNNFTgSIPRGSIPN---LE 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   303 RLYLSGNRLSVLPFMLFQTAADLQVLDLSDNRLLSFPDNFFARNGQLRQLHLQRNQLKSIGKHSLYSLRELRQLDLSQNS 382
Cdd:PLN00113  144 TLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVGQIPRELGQMKSLKWIYLGYNN 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   383 LS---VIDRKAFESLDHllaLNVSGNNLTLLSSIIFQSLHALRQLDLSRNQFK-QLPSGLFQRQRSLVLLRID-----ET 453
Cdd:PLN00113  224 LSgeiPYEIGGLTSLNH---LDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDnslsgEI 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   454 P-----------IEQFSN----WISRYDESLVDPQVL------------------HRLRYLSVQQNRKLTYLPATLfANT 500
Cdd:PLN00113  301 PelviqlqnleiLHLFSNnftgKIPVALTSLPRLQVLqlwsnkfsgeipknlgkhNNLTVLDLSTNNLTGEIPEGL-CSS 379
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584026   501 PNIRELLLAENGLL-QLPTQISGLSRLQRLSVRGNSL-GSLPENIKELRQLHYLNILGNEYQ 560
Cdd:PLN00113  380 GNLFKLILFSNSLEgEIPKSLGACRSLRRVRLQDNSFsGELPSEFTKLPLVYFLDISNNNLQ 441
LRR_8 pfam13855
Leucine rich repeat;
325-383 3.59e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 56.76  E-value: 3.59e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24584026    325 LQVLDLSDNRLLSFPDNFFARNGQLRQLHLQRNQLKSIGKHSLYSLRELRQLDLSQNSL 383
Cdd:pfam13855    3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
232-558 7.20e-10

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 63.71  E-value: 7.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   232 LEMSGNRLSNCSLLNLQYMKQLQELHLDRSELTYLPQRFLGELSELRMLNLSQNLLT-ELPRDIfvGALK-LERLYLSGN 309
Cdd:PLN00113  145 LDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVgQIPREL--GQMKsLKWIYLGYN 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   310 RLS-VLPFMLFQTAAdLQVLDLSDNRLL-SFPDNFfarnGQLRQLH---LQRNQLKSIGKHSLYSLRELRQLDLSQNSLS 384
Cdd:PLN00113  223 NLSgEIPYEIGGLTS-LNHLDLVYNNLTgPIPSSL----GNLKNLQylfLYQNKLSGPIPPSIFSLQKLISLDLSDNSLS 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   385 ------VIDRKAFESLdHLLAlnvsgNNLTLLSSIIFQSLHALRQLDLSRNQFK-QLPSGLFQRQRSLVL--------LR 449
Cdd:PLN00113  298 geipelVIQLQNLEIL-HLFS-----NNFTGKIPVALTSLPRLQVLQLWSNKFSgEIPKNLGKHNNLTVLdlstnnltGE 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   450 IDETPIEQ--------FSNWI-SRYDESLVDPQVLHRLR----YLSVQQNRKLTYLPATLFAN----------------T 500
Cdd:PLN00113  372 IPEGLCSSgnlfklilFSNSLeGEIPKSLGACRSLRRVRlqdnSFSGELPSEFTKLPLVYFLDisnnnlqgrinsrkwdM 451
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   501 PNIRELLLAENGLL-QLPtQISGLSRLQRLSVRGNSL-GSLPENIKELRQLHYLNILGNE 558
Cdd:PLN00113  452 PSLQMLSLARNKFFgGLP-DSFGSKRLENLDLSRNQFsGAVPRKLGSLSELMQLKLSENK 510
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
299-543 3.14e-09

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 61.25  E-value: 3.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   299 LKLERLylsgnRLSVLPFMLfqtAADLQVLDLSDNRLLSFPDNFfarNGQLRQLHLQRNQLKSIGKHSLYSLRELrqlDL 378
Cdd:PRK15370  183 LRLKIL-----GLTTIPACI---PEQITTLILDNNELKSLPENL---QGNIKTLYANSNQLTSIPATLPDTIQEM---EL 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   379 SQNSLSVIDRKAFESLDhllALNVSGNNLTLLSSIIFQSLhalRQLDLSRNQFKQLPSGLfqrQRSLVLLRIdetpieqF 458
Cdd:PRK15370  249 SINRITELPERLPSALQ---SLDLFHNKISCLPENLPEEL---RYLSVYDNSIRTLPAHL---PSGITHLNV-------Q 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   459 SNWISRYDESLvdPQVLHRLrylsVQQNRKLTYLPATLfanTPNIRELLLAENGLLQLPTQISglSRLQRLSVRGNSLGS 538
Cdd:PRK15370  313 SNSLTALPETL--PPGLKTL----EAGENALTSLPASL---PPELQVLDVSKNQITVLPETLP--PTITTLDVSRNALTN 381

                  ....*
gi 24584026   539 LPENI 543
Cdd:PRK15370  382 LPENL 386
LRR_8 pfam13855
Leucine rich repeat;
252-311 5.50e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 53.30  E-value: 5.50e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026    252 QLQELHLDRSELTYLPQRFLGELSELRMLNLSQNLLTELPRDIFVGALKLERLYLSGNRL 311
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
714-761 9.88e-09

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 53.62  E-value: 9.88e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 24584026  714 SLNWTRQNSLV--GRRVVLVENGSLLVHNISRIDSGLYTCYAFNVMGKAS 761
Cdd:cd04969   33 TISWSKGTELLtnSSRICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKAN 82
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
385-557 1.16e-08

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 59.71  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   385 VIDRKAFESLDHLL-----ALNVSGNNLTLLSSIIFQSLhalRQLDLSRNQFKQLPSGLFQRQRSLVLlridetpieqFS 459
Cdd:PRK15370  205 ILDNNELKSLPENLqgnikTLYANSNQLTSIPATLPDTI---QEMELSINRITELPERLPSALQSLDL----------FH 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   460 NWISRYDESLVDpqvlhRLRYLSVQ--------------------QNRKLTYLPATLfanTPNIRELLLAENGLLQLPTQ 519
Cdd:PRK15370  272 NKISCLPENLPE-----ELRYLSVYdnsirtlpahlpsgithlnvQSNSLTALPETL---PPGLKTLEAGENALTSLPAS 343
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 24584026   520 ISglSRLQRLSVRGNSLGSLPENIKELRQLHYL--NILGN 557
Cdd:PRK15370  344 LP--PELQVLDVSKNQITVLPETLPPTITTLDVsrNALTN 381
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
269-527 3.96e-08

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: 56.59  E-value: 3.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  269 RFLGELSELRMLNLSQNLLTELP-RDIFvGALK----LERLYLSGNRLSVLPFML------FQTAADLQVLDLSDNRLL- 336
Cdd:cd00116   17 ELLPKLLCLQVLRLEGNTLGEEAaKALA-SALRpqpsLKELCLSLNETGRIPRGLqsllqgLTKGCGLQELDLSDNALGp 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  337 ----SFPDnfFARNGQLRQLHLQRNQL-KSIGKHSLYSLRE----LRQLDLSQNSLSVID----RKAFESLDHLLALNVS 403
Cdd:cd00116   96 dgcgVLES--LLRSSSLQELKLNNNGLgDRGLRLLAKGLKDlppaLEKLVLGRNRLEGAScealAKALRANRDLKELNLA 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  404 GNNLT--LLSSI--IFQSLHALRQLDLSRNQF-----KQLpSGLFQRQRSLVLLRIDETPIeqfSNW-ISRYDESLvdPQ 473
Cdd:cd00116  174 NNGIGdaGIRALaeGLKANCNLEVLDLNNNGLtdegaSAL-AETLASLKSLEVLNLGDNNL---TDAgAAALASAL--LS 247
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 24584026  474 VLHRLRYLSVQQNrKLTYLPATLFA----NTPNIRELLLAENGLLQLPTQISGLSRLQ 527
Cdd:cd00116  248 PNISLLTLSLSCN-DITDDGAKDLAevlaEKESLLELDLRGNKFGEEGAQLLAESLLE 304
LRR_8 pfam13855
Leucine rich repeat;
275-335 1.26e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 49.45  E-value: 1.26e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584026    275 SELRMLNLSQNLLTELPRDIFVGALKLERLYLSGNRLSVLPFMLFQTAADLQVLDLSDNRL 335
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
300-359 1.81e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 49.06  E-value: 1.81e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026    300 KLERLYLSGNRLSVLPFMLFQTAADLQVLDLSDNRLLSFPDNFFARNGQLRQLHLQRNQL 359
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
256-557 2.69e-07

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 55.17  E-value: 2.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   256 LHLDRSELTYLPQRFLGELSELRmlnLSQNLLTELPrdifvgAL--KLERLYLSGNRLSVLPFMlfqtAADLQVLDLSDN 333
Cdd:PRK15387  206 LNVGESGLTTLPDCLPAHITTLV---IPDNNLTSLP------ALppELRTLEVSGNQLTSLPVL----PPGLLELSIFSN 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   334 RLLSFPdnffARNGQLRQLHLQRNQLKSIGKHSlyslRELRQLDLSQNSLSVIDRKAFEsLDHLLALNvsgNNLTLLSSI 413
Cdd:PRK15387  273 PLTHLP----ALPSGLCKLWIFGNQLTSLPVLP----PGLQELSVSDNQLASLPALPSE-LCKLWAYN---NQLTSLPTL 340
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   414 IfqslHALRQLDLSRNQFKQLPSglfqrqrslvllrideTPIEQFSNWIsrYDESLVD-PQVLHRLRYLSVQQNRkLTYL 492
Cdd:PRK15387  341 P----SGLQELSVSDNQLASLPT----------------LPSELYKLWA--YNNRLTSlPALPSGLKELIVSGNR-LTSL 397
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584026   493 PATlfanTPNIRELLLAENGLLQLPTQISGLsrlQRLSVRGNSLGSLPENIKELRQLHYLNILGN 557
Cdd:PRK15387  398 PVL----PSELKELMVSGNRLTSLPMLPSGL---LSLSVYRNQLTRLPESLIHLSSETTVNLEGN 455
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
232-540 6.53e-07

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 54.08  E-value: 6.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   232 LEMSGNRLSNCSLLNLQYMKQLQELHLDRSELTYLPQRFLGELSELRMLNLSQNLLT-ELPRDIfvgalklerlylsGNR 310
Cdd:PLN00113  289 LDLSDNSLSGEIPELVIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLWSNKFSgEIPKNL-------------GKH 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   311 lsvlpfmlfqtaADLQVLDLSDNRLLSFPDNFFARNGQLRQLHLQRNQLKSIGKHSLYSLRELRQLDLSQNSLSVIDRKA 390
Cdd:PLN00113  356 ------------NNLTVLDLSTNNLTGEIPEGLCSSGNLFKLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSGELPSE 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   391 FESLDHLLALNVSGNNLT-----------------LLSSIIFQSL------HALRQLDLSRNQFKQLPSGLFQRQRSLVL 447
Cdd:PLN00113  424 FTKLPLVYFLDISNNNLQgrinsrkwdmpslqmlsLARNKFFGGLpdsfgsKRLENLDLSRNQFSGAVPRKLGSLSELMQ 503
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   448 LRIDETPIeqfsnwisrydeSLVDPQVL---HRLRYLSVQQNRKLTYLPATlFANTPNIRELLLAENGLL-QLPTQISGL 523
Cdd:PLN00113  504 LKLSENKL------------SGEIPDELsscKKLVSLDLSHNQLSGQIPAS-FSEMPVLSQLDLSQNQLSgEIPKNLGNV 570
                         330
                  ....*....|....*...
gi 24584026   524 SRLQRLSVRGNSL-GSLP 540
Cdd:PLN00113  571 ESLVQVNISHNHLhGSLP 588
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
221-440 2.71e-06

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 51.70  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   221 AIPLAVRRVKVLEMSGNRLSNCSLLNlqymKQLQELHLDRSELTYLPQR---------FLGELSE-------LRMLNLSQ 284
Cdd:PRK15387  236 SLPALPPELRTLEVSGNQLTSLPVLP----PGLLELSIFSNPLTHLPALpsglcklwiFGNQLTSlpvlppgLQELSVSD 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   285 NLLTELPrdifvgALKLE--RLYLSGNRLSVLPFMlfqtAADLQVLDLSDNRLLSFPdnffARNGQLRQLHLQRNQLKSI 362
Cdd:PRK15387  312 NQLASLP------ALPSElcKLWAYNNQLTSLPTL----PSGLQELSVSDNQLASLP----TLPSELYKLWAYNNRLTSL 377
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24584026   363 GkhSLYSlrELRQLDLSQNSLSVIDRKAFEsldhLLALNVSGNNLTLLSSIIfqslHALRQLDLSRNQFKQLPSGLFQ 440
Cdd:PRK15387  378 P--ALPS--GLKELIVSGNRLTSLPVLPSE----LKELMVSGNRLTSLPMLP----SGLLSLSVYRNQLTRLPESLIH 443
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
715-762 3.10e-06

Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409438  Cd Length: 89  Bit Score: 46.53  E-value: 3.10e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 24584026  715 LNWTRQNSLV--GRRVVLVENGSLLVHNISRIDSGLYTCYAFNVMGKASA 762
Cdd:cd05852   34 FSWSKGTELLvnNSRISIWDDGSLEILNITKLDEGSYTCFAENNRGKANS 83
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
456-557 3.46e-06

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 51.62  E-value: 3.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026   456 EQFSNWISRYDESLVDPQVLH-RLRYLSVQQNrKLTYLPATLfantPN-IRELLLAENGLLQLPTQISglSRLQRLSVRG 533
Cdd:PRK15370  199 EQITTLILDNNELKSLPENLQgNIKTLYANSN-QLTSIPATL----PDtIQEMELSINRITELPERLP--SALQSLDLFH 271
                          90       100
                  ....*....|....*....|....
gi 24584026   534 NSLGSLPENIKElrQLHYLNILGN 557
Cdd:PRK15370  272 NKISCLPENLPE--ELRYLSVYDN 293
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
651-768 3.95e-06

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). 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: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 46.33  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  651 AKLECQISGSPVPDIIWvtprnKILRHHADPDKRPIIidskedahqppsaqelaaLMDESyiqslnwtrqnslvGRRvvl 730
Cdd:cd05744   18 CRFDCKVSGLPTPDLFW-----QLNGKPVRPDSAHKM------------------LVREN--------------GRH--- 57
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 24584026  731 vengSLLVHNISRIDSGLYTCYAFNVMGKASAGLRLYI 768
Cdd:cd05744   58 ----SLIIEPVTKRDAGIYTCIARNRAGENSFNAELVV 91
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
714-760 2.48e-05

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: 44.16  E-value: 2.48e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 24584026  714 SLNWTRQNSLV--GRRVVLVENGSLLVHNISRIDSGLYTCYAFNVMGKA 760
Cdd:cd20968   30 SVSWIKGDDLIkeNNRIAVLESGSLRIHNVQKEDAGQYRCVAKNSLGIA 78
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
712-766 4.78e-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: 43.32  E-value: 4.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 24584026  712 IQSLNWTRQNSL--VGRRVVLVENGSLLVHNISR-IDSGLYTCYAFNVMG-KASAGLRL 766
Cdd:cd20958   29 ISSITWEKDGRRlpLNHRQRVFPNGTLVIENVQRsSDEGEYTCTARNQQGqSASRSVFV 87
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
649-762 5.79e-05

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of 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, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -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, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -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 Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 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. 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


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 42.87  E-value: 5.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  649 STAKLECQISGSPVPDIIWVtprnkilrhhadpdkrpiiidskEDAHQPPSAQElaalmdesyiqslnwtrqnslvgrRV 728
Cdd:cd20952   15 GTVVLNCQATGEPVPTISWL-----------------------KDGVPLLGKDE------------------------RI 47
                         90       100       110
                 ....*....|....*....|....*....|....
gi 24584026  729 VLVENGSLLVHNISRIDSGLYTCYAFNVMGKASA 762
Cdd:cd20952   48 TTLENGSLQIKGAEKSDTGEYTCVALNLSGEATW 81
I-set pfam07679
Immunoglobulin I-set domain;
649-766 5.94e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 43.01  E-value: 5.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026    649 STAKLECQISGSPVPDIIWVTprnkilrhhadpdkrpiiidskedahqppsaqelaalmDESYIQSlnwtrqnslvGRRV 728
Cdd:pfam07679   16 ESARFTCTVTGTPDPEVSWFK--------------------------------------DGQPLRS----------SDRF 47
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 24584026    729 VLVENG---SLLVHNISRIDSGLYTCYAFNVMGKASAGLRL 766
Cdd:pfam07679   48 KVTYEGgtyTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
649-766 7.46e-05

Third 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 third 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 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, 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, and 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 Slit2 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: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 42.38  E-value: 7.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  649 STAKLECQISGSPVPDIIWvtprnkilrhhadpdkrpiiidSKEDAHQPpsaqelaalmdesyiqslnwtrqnslVGRRV 728
Cdd:cd05725   13 DSAEFQCEVGGDPVPTVRW----------------------RKEDGELP--------------------------KGRYE 44
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 24584026  729 VLVENgSLLVHNISRIDSGLYTCYAFNVMGKASAGLRL 766
Cdd:cd05725   45 ILDDH-SLKIRKVTAGDMGSYTCVAENMVGKIEASATL 81
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
649-768 8.50e-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: 42.49  E-value: 8.50e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026     649 STAKLECQISGSPVPDIIWVTPRNKILrhhadpdkrpiiidskedahqppsaqelaalmdeSYIQSLNWTRQNSlvgrrv 728
Cdd:smart00410   10 ESVTLSCEASGSPPPEVTWYKQGGKLL----------------------------------AESGRFSVSRSGS------ 49
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 24584026     729 vlveNGSLLVHNISRIDSGLYTCYAFNVMGKASAGLRLYI 768
Cdd:smart00410   50 ----TSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
634-766 1.13e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. 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: 409473  Cd Length: 92  Bit Score: 42.06  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  634 PTVVQfsEPKMHKLLS--TAKLECQISGSPVPDIIWvTPRNKILRHHADpdkrpiiidskedahqppsaqelaalmdesy 711
Cdd:cd05892    1 PMFIQ--KPQNKKVLEgdPVRLECQISAIPPPQIFW-KKNNEMLQYNTD------------------------------- 46
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 24584026  712 iqslnwtrqnslvgrRVVLVENGS----LLVHNISRIDSGLYTCYAFNVMGKASAGLRL 766
Cdd:cd05892   47 ---------------RISLYQDNCgricLLIQNANKKDAGWYTVSAVNEAGVVSCNARL 90
LRR_8 pfam13855
Leucine rich repeat;
396-455 1.26e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.97  E-value: 1.26e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026    396 HLLALNVSGNNLTLLSSIIFQSLHALRQLDLSRNQFKQLPSGLFQRQRSLVLLRIDETPI 455
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
651-762 1.52e-04

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: 41.16  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  651 AKLECQISGSPVPDIIWVTPRNKIlrhhadpdkrpiiidskedahqppsaqelaalmdesyiqslnwtrQNSLVGRRVVL 730
Cdd:cd00096    1 VTLTCSASGNPPPTITWYKNGKPL---------------------------------------------PPSSRDSRRSE 35
                         90       100       110
                 ....*....|....*....|....*....|...
gi 24584026  731 VENGSLLVHNISRIDSGLYTCYAFN-VMGKASA 762
Cdd:cd00096   36 LGNGTLTISNVTLEDSGTYTCVASNsAGGSASA 68
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
227-397 3.19e-04

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 44.78  E-value: 3.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  227 RRVKVLEMSGNRLSNCSLL----NLQYMKQLQELHLDRSELTYLPQRFLGEL----SELRMLNLSQNLLTELPRDIFVGA 298
Cdd:COG5238  264 TTVETLYLSGNQIGAEGAIalakALQGNTTLTSLDLSVNRIGDEGAIALAEGlqgnKTLHTLNLAYNGIGAQGAIALAKA 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  299 LK----LERLYLSGNRLSVlpfmlfQTAADLQvldlsdnrllsfpdNFFARNGQLRQLHLQRNQLKSIGKHSLYSLRE-- 372
Cdd:COG5238  344 LQenttLHSLDLSDNQIGD------EGAIALA--------------KYLEGNTTLRELNLGKNNIGKQGAEALIDALQtn 403
                        170       180
                 ....*....|....*....|....*..
gi 24584026  373 -LRQLDLSQNSLSV-IDRKAFESLDHL 397
Cdd:COG5238  404 rLHTLILDGNLIGAeAQQRLEQLLERI 430
LRR_8 pfam13855
Leucine rich repeat;
227-287 7.85e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 38.66  E-value: 7.85e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584026    227 RRVKVLEMSGNRLSNCSLLNLQYMKQLQELHLDRSELTYLPQRFLGELSELRMLNLSQNLL 287
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
351-557 9.04e-04

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: 43.11  E-value: 9.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  351 QLHLQRNQLKSIG-KHSLYSLRELRQLDLSQNSLSVIDRKA-FESLDH---LLALNVSGNNLTLLSSII------FQSLH 419
Cdd:cd00116    2 QLSLKGELLKTERaTELLPKLLCLQVLRLEGNTLGEEAAKAlASALRPqpsLKELCLSLNETGRIPRGLqsllqgLTKGC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584026  420 ALRQLDLSRNQFKQLPSGLFQRQRSLVLLRidETPIEQFSNWISRYD---ESLVDPQvlHRLRYLsVQQNRKLTYLPAT- 495
Cdd:cd00116   82 GLQELDLSDNALGPDGCGVLESLLRSSSLQ--ELKLNNNGLGDRGLRllaKGLKDLP--PALEKL-VLGRNRLEGASCEa 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584026  496 ---LFANTPNIRELLLAENGLLQ--LPTQISGL---SRLQRLSVRGNSLGS-----LPENIKELRQLHYLNILGN 557
Cdd:cd00116  157 lakALRANRDLKELNLANNGIGDagIRALAEGLkanCNLEVLDLNNNGLTDegasaLAETLASLKSLEVLNLGDN 231
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
723-768 2.42e-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: 38.15  E-value: 2.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 24584026  723 LVGRRVVLVENGSLLVHNISRIDSGLYTCYAFNVMG-KASAGLRLYI 768
Cdd:cd05724   41 LDNERVRIVDDGNLLIAEARKSDEGTYKCVATNMVGeRESRAARLSV 87
LRR smart00370
Leucine-rich repeats, outliers;
418-440 5.42e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 35.41  E-value: 5.42e-03
                            10        20
                    ....*....|....*....|...
gi 24584026     418 LHALRQLDLSRNQFKQLPSGLFQ 440
Cdd:smart00370    1 LPNLRELDLSNNQLSSLPPGAFQ 23
LRR_TYP smart00369
Leucine-rich repeats, typical (most populated) subfamily;
418-440 5.42e-03

Leucine-rich repeats, typical (most populated) subfamily;


Pssm-ID: 197687 [Multi-domain]  Cd Length: 24  Bit Score: 35.41  E-value: 5.42e-03
                            10        20
                    ....*....|....*....|...
gi 24584026     418 LHALRQLDLSRNQFKQLPSGLFQ 440
Cdd:smart00369    1 LPNLRELDLSNNQLSSLPPGAFQ 23
LRR_8 pfam13855
Leucine rich repeat;
477-536 9.03e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 35.96  E-value: 9.03e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584026    477 RLRYLSVQQNRkLTYLPATLFANTPNIRELLLAENGLLQL-PTQISGLSRLQRLSVRGNSL 536
Cdd:pfam13855    2 NLRSLDLSNNR-LTSLDDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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