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Conserved domains on  [gi|2554604|dbj|BAA22848|]
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ISLR [Homo sapiens]

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];
50-182 4.08e-20

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 91.92  E-value: 4.08e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604   50 ANVTTLSLSANRLPGLPEgAFREVPLLQSLWLAHNEIRTVAAgALASLSHLKSLDLSHNLISDFAwSDLHNLSALQLLKM 129
Cdd:COG4886 113 TNLESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDL 189

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 2554604  130 DSNELTFIPrDAFRSLRALRSLQLNHNRLHTLAEgTFTPLTALSHLQINENPF 182
Cdd:COG4886 190 SNNQITDLP-EPLGNLTNLEELDLSGNQLTDLPE-PLANLTNLETLDLSNNQL 240
PCC super family cl28216
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 153-227 3.52e-10

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


The actual alignment was detected with superfamily member TIGR00864:

Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 62.41  E-value: 3.52e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2554604     153 LNHNRLHTLAEGTFTPLTALSHLQINENPFDCTCGIVWLKTWALTTAVSIPEQDNIACTSPHVLKGTPLSRLPPL 227
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLL 76
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 239-340 2.55e-08

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 pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 51.10  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604    239 QPSQDgAELRPGFVLALHCDVDGQPAPQLHWHiqipsgiveitspnvgtdgraLPGTPVASSQpRFQAFANG---SLLIP 315
Cdd:pfam07679   5 QKPKD-VEVQEGESARFTCTVTGTPDPEVSWF---------------------KDGQPLRSSD-RFKVTYEGgtyTLTIS 61

                          90       100
                  ....*....|....*....|....*
gi 2554604    316 DFGKLEEGTYSCLATNELGSAESSV 340
Cdd:pfam07679  62 NVQPDDSGKYTCVATNSAGEAEASA 86
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
50-182 4.08e-20

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 91.92  E-value: 4.08e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604   50 ANVTTLSLSANRLPGLPEgAFREVPLLQSLWLAHNEIRTVAAgALASLSHLKSLDLSHNLISDFAwSDLHNLSALQLLKM 129
Cdd:COG4886 113 TNLESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDL 189

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 2554604  130 DSNELTFIPrDAFRSLRALRSLQLNHNRLHTLAEgTFTPLTALSHLQINENPF 182
Cdd:COG4886 190 SNNQITDLP-EPLGNLTNLEELDLSGNQLTDLPE-PLANLTNLETLDLSNNQL 240
LRR_8 pfam13855
Leucine rich repeat;
98-158 8.54e-14

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 65.62  E-value: 8.54e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2554604     98 SHLKSLDLSHNLISDFAWSDLHNLSALQLLKMDSNELTFIPRDAFRSLRALRSLQLNHNRL 158
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 153-227 3.52e-10

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 62.41  E-value: 3.52e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2554604     153 LNHNRLHTLAEGTFTPLTALSHLQINENPFDCTCGIVWLKTWALTTAVSIPEQDNIACTSPHVLKGTPLSRLPPL 227
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLL 76
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 52-180 4.38e-10

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 61.79  E-value: 4.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604    52 VTTLSLSANRLPGLPEGAFREVPLLQSLWLAHNEIrtvaAGALASLS---HLKSLDLSHNLISDFAWSDLHNLSALQLLK 128
Cdd:PLN00113 430 VYFLDISNNNLQGRINSRKWDMPSLQMLSLARNKF----FGGLPDSFgskRLENLDLSRNQFSGAVPRKLGSLSELMQLK 505

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 2554604   129 MDSNELTFIPRDAFRSLRALRSLQLNHNRLHTLAEGTFTPLTALSHLQINEN 180
Cdd:PLN00113 506 LSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQLDLSQN 557
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 74-183 1.18e-08

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 55.18  E-value: 1.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604   74 PLLQSLWLAHNEIRTVaaGALASLSHLKSLDLSHNLISdfAWSDLHNLSALQLLKMD------SNELTFIPrdafRSLRA 147
Cdd:cd21340  46 TNLTHLYLQNNQIEKI--ENLENLVNLKKLYLGGNRIS--VVEGLENLTNLEELHIEnqrlppGEKLTFDP----RSLAA 117

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 2554604  148 L-RSLQ-LN--HNRLHTLAEgtFTPLTALSHLQINENPFD 183
Cdd:cd21340 118 LsNSLRvLNisGNNIDSLEP--LAPLRNLEQLDASNNQIS 155
I-set pfam07679
Immunoglobulin I-set domain;
239-340 2.55e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 51.10  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604    239 QPSQDgAELRPGFVLALHCDVDGQPAPQLHWHiqipsgiveitspnvgtdgraLPGTPVASSQpRFQAFANG---SLLIP 315
Cdd:pfam07679   5 QKPKD-VEVQEGESARFTCTVTGTPDPEVSWF---------------------KDGQPLRSSD-RFKVTYEGgtyTLTIS 61

                          90       100
                  ....*....|....*....|....*
gi 2554604    316 DFGKLEEGTYSCLATNELGSAESSV 340
Cdd:pfam07679  62 NVQPDDSGKYTCVATNSAGEAEASA 86
LRRCT smart00082
Leucine rich repeat C-terminal domain;
180-228 2.80e-07

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 47.04  E-value: 2.80e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2554604     180 NPFDCTCGIVWLKTWaLTTAVSIPEQDNIACTSPHVLKGtPLSRLPPLP 228
Cdd:smart00082   1 NPFICDCELRWLLRW-LQANEHLQDPVDLRCASPSSLRG-PLLELLHSE 47
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 253-340 5.79e-07

Seventh 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 seventh 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: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 47.31  E-value: 5.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  253 LALHCDVDGQPAPQLHWHiqipsgiveitspnvgtdgRALPGTPVA----SSQPRFQAFANGSLLIPDFGKLEEGTYSCL 328
Cdd:cd20954  19 VMLHCQADGFPTPTVTWK-------------------KATGSTPGEykdlLYDPNVRILPNGTLVFGHVQKENEGHYLCE 79

                        90
                ....*....|..
gi 2554604  329 ATNELGSAESSV 340
Cdd:cd20954  80 AKNGIGSGLSKV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 248-342 2.58e-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: 2.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604     248 RPGFVLALHCDVDGQPAPQLHWHIQIPSGIVEitspnvgtdgralpgtpvassQPRFQAFANG---SLLIPDFGKLEEGT 324
Cdd:smart00410   7 KEGESVTLSCEASGSPPPEVTWYKQGGKLLAE---------------------SGRFSVSRSGstsTLTISNVTPEDSGT 65

                           90
                   ....*....|....*...
gi 2554604     325 YSCLATNELGSAESSVDV 342
Cdd:smart00410  66 YTCAATNSSGSASSGTTL 83
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
50-182 4.08e-20

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 91.92  E-value: 4.08e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604   50 ANVTTLSLSANRLPGLPEgAFREVPLLQSLWLAHNEIRTVAAgALASLSHLKSLDLSHNLISDFAwSDLHNLSALQLLKM 129
Cdd:COG4886 113 TNLESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDL 189

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 2554604  130 DSNELTFIPrDAFRSLRALRSLQLNHNRLHTLAEgTFTPLTALSHLQINENPF 182
Cdd:COG4886 190 SNNQITDLP-EPLGNLTNLEELDLSGNQLTDLPE-PLANLTNLETLDLSNNQL 240
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-182 3.08e-17

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 83.06  E-value: 3.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604   51 NVTTLSLSANRLPGLPEgAFREVPLLQSLWLAHNEIRTVAAgALASLSHLKSLDLSHNLISDFAWsdLHNLSALQLLKMD 130
Cdd:COG4886 183 NLKELDLSNNQITDLPE-PLGNLTNLEELDLSGNQLTDLPE-PLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLS 258

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 2554604  131 SNELTFIPRDAfrSLRALRSLQLNHNRLHTLAEGTFTPLTALSHLQINENPF 182
Cdd:COG4886 259 NNQLTDLPPLA--NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLL 308
LRR_8 pfam13855
Leucine rich repeat;
98-158 8.54e-14

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 65.62  E-value: 8.54e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2554604     98 SHLKSLDLSHNLISDFAWSDLHNLSALQLLKMDSNELTFIPRDAFRSLRALRSLQLNHNRL 158
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
51-110 1.41e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 62.16  E-value: 1.41e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604     51 NVTTLSLSANRLPGLPEGAFREVPLLQSLWLAHNEIRTVAAGALASLSHLKSLDLSHNLI 110
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
50-182 1.79e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 68.42  E-value: 1.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604   50 ANVTTLSLSANRLPGLPEGAFREVPLLQSLWLAHNEirtvaagALASLSHLKSLDLSHNLISDFAWSdLHNLSALQLLKM 129
Cdd:COG4886  72 LLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE-------ELSNLTNLESLDLSGNQLTDLPEE-LANLTNLKELDL 143

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 2554604  130 DSNELTFIPrDAFRSLRALRSLQLNHNRLHTLAEGtFTPLTALSHLQINENPF 182
Cdd:COG4886 144 SNNQLTDLP-EPLGNLTNLKSLDLSNNQLTDLPEE-LGNLTNLKELDLSNNQI 194
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
35-208 3.74e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 67.65  E-value: 3.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604   35 DCAYRDLESVPPGF--PANVTTLSLSANRLPGLPEgAFREVPLLQSLWLAHNEIRTVAAgaLASLSHLKSLDLSHNLISD 112
Cdd:COG4886 188 DLSNNQITDLPEPLgnLTNLEELDLSGNQLTDLPE-PLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTD 264

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  113 FawSDLHNLSALQLLKMDSNELTFIPRDAFRSLRALRSLQLNHNRLHTLAEGTFTPLTALSHLQINENPFDCTCGIVWLK 192
Cdd:COG4886 265 L--PPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLAL 342

                       170
                ....*....|....*.
gi 2554604  193 TWALTTAVSIPEQDNI 208
Cdd:COG4886 343 SLSLLALLTLLLLLNL 358
LRR_8 pfam13855
Leucine rich repeat;
74-134 9.66e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.85  E-value: 9.66e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2554604     74 PLLQSLWLAHNEIRTVAAGALASLSHLKSLDLSHNLISDFAWSDLHNLSALQLLKMDSNEL 134
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
124-182 1.62e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 56.38  E-value: 1.62e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2554604    124 LQLLKMDSNELTFIPRDAFRSLRALRSLQLNHNRLHTLAEGTFTPLTALSHLQINENPF 182
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 153-227 3.52e-10

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 62.41  E-value: 3.52e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2554604     153 LNHNRLHTLAEGTFTPLTALSHLQINENPFDCTCGIVWLKTWALTTAVSIPEQDNIACTSPHVLKGTPLSRLPPL 227
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPEAALCAGPGALAGQPLLGIPLL 76
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 52-180 4.38e-10

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 61.79  E-value: 4.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604    52 VTTLSLSANRLPGLPEGAFREVPLLQSLWLAHNEIrtvaAGALASLS---HLKSLDLSHNLISDFAWSDLHNLSALQLLK 128
Cdd:PLN00113 430 VYFLDISNNNLQGRINSRKWDMPSLQMLSLARNKF----FGGLPDSFgskRLENLDLSRNQFSGAVPRKLGSLSELMQLK 505

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 2554604   129 MDSNELTFIPRDAFRSLRALRSLQLNHNRLHTLAEGTFTPLTALSHLQINEN 180
Cdd:PLN00113 506 LSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQLDLSQN 557
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 74-183 1.18e-08

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 55.18  E-value: 1.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604   74 PLLQSLWLAHNEIRTVaaGALASLSHLKSLDLSHNLISdfAWSDLHNLSALQLLKMD------SNELTFIPrdafRSLRA 147
Cdd:cd21340  46 TNLTHLYLQNNQIEKI--ENLENLVNLKKLYLGGNRIS--VVEGLENLTNLEELHIEnqrlppGEKLTFDP----RSLAA 117

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 2554604  148 L-RSLQ-LN--HNRLHTLAEgtFTPLTALSHLQINENPFD 183
Cdd:cd21340 118 LsNSLRvLNisGNNIDSLEP--LAPLRNLEQLDASNNQIS 155
I-set pfam07679
Immunoglobulin I-set domain;
239-340 2.55e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 51.10  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604    239 QPSQDgAELRPGFVLALHCDVDGQPAPQLHWHiqipsgiveitspnvgtdgraLPGTPVASSQpRFQAFANG---SLLIP 315
Cdd:pfam07679   5 QKPKD-VEVQEGESARFTCTVTGTPDPEVSWF---------------------KDGQPLRSSD-RFKVTYEGgtyTLTIS 61

                          90       100
                  ....*....|....*....|....*
gi 2554604    316 DFGKLEEGTYSCLATNELGSAESSV 340
Cdd:pfam07679  62 NVQPDDSGKYTCVATNSAGEAEASA 86
LRRCT smart00082
Leucine rich repeat C-terminal domain;
180-228 2.80e-07

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 47.04  E-value: 2.80e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2554604     180 NPFDCTCGIVWLKTWaLTTAVSIPEQDNIACTSPHVLKGtPLSRLPPLP 228
Cdd:smart00082   1 NPFICDCELRWLLRW-LQANEHLQDPVDLRCASPSSLRG-PLLELLHSE 47
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 253-340 5.79e-07

Seventh 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 seventh 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: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 47.31  E-value: 5.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  253 LALHCDVDGQPAPQLHWHiqipsgiveitspnvgtdgRALPGTPVA----SSQPRFQAFANGSLLIPDFGKLEEGTYSCL 328
Cdd:cd20954  19 VMLHCQADGFPTPTVTWK-------------------KATGSTPGEykdlLYDPNVRILPNGTLVFGHVQKENEGHYLCE 79

                        90
                ....*....|..
gi 2554604  329 ATNELGSAESSV 340
Cdd:cd20954  80 AKNGIGSGLSKV 91
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 253-342 1.27e-06

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: 46.41  E-value: 1.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  253 LALHCDVDGQPAPQLHWHiqipsgiveitspnvgTDGRALPgtpvasSQPRFQAFANGSLLIPD-FGKLEEGTYSCLATN 331
Cdd:cd20958  18 LRLHCPVAGYPISSITWE----------------KDGRRLP------LNHRQRVFPNGTLVIENvQRSSDEGEYTCTARN 75

                        90
                ....*....|..
gi 2554604  332 ELG-SAESSVDV 342
Cdd:cd20958  76 QQGqSASRSVFV 87
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 255-339 1.31e-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: 45.78  E-value: 1.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  255 LHCDVDGQPAPQLHWHIqipsgiveitspnvgtDGRALPGTPVassQPRFQAFANGSLLIPDFGKLEEGTYSCLATNELG 334
Cdd:cd00096   3 LTCSASGNPPPTITWYK----------------NGKPLPPSSR---DSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63


                ....*
gi 2554604  335 SAESS 339
Cdd:cd00096  64 GSASA 68
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
 239-335 2.07e-06

First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409387  Cd Length: 97  Bit Score: 45.93  E-value: 2.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  239 QPSqDGAELRpGFVLALHCDVDGQPAPQLHWHiqipsgiveitspnvgTDGRALPgtpvASSQPRFQAFANGSLLIPDF- 317
Cdd:cd05722   7 EPS-DIVAMR-GGPVVLNCSAESDPPPKIEWK----------------KDGVLLN----LVSDERRQQLPNGSLLITSVv 64

                        90       100
                ....*....|....*....|...
gi 2554604  318 ----GKLEEGTYSCLATNE-LGS 335
Cdd:cd05722  65 hskhNKPDEGFYQCVAQNEsLGS 87
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 51-159 2.54e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 49.85  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604    51 NVTTLSLSANRLPGLPEGAFREVPLLQSLWLAHNEIRTVAAGALASLSHLKSLDLSHNLISDFAWSDLHNLSALQLLKMD 130
Cdd:PLN00113 476 RLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQLDLS 555

                         90       100       110
                 ....*....|....*....|....*....|
gi 2554604   131 SNELTF-IPRDAFRsLRALRSLQLNHNRLH 159
Cdd:PLN00113 556 QNQLSGeIPKNLGN-VESLVQVNISHNHLH 584
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 55-180 2.63e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 49.85  E-value: 2.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604    55 LSLSANRLPG-LPEGAfreVPLLQSLWLAHNEIRTVAAGALASLSHLKSLDLSHNLISDFAWSDLHNLSALQLLKMDSNE 133
Cdd:PLN00113 123 LNLSNNNFTGsIPRGS---IPNLETLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQ 199

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 2554604   134 LTF-IPRDAFRsLRALRSLQLNHNRLHTLAEGTFTPLTALSHLQINEN 180
Cdd:PLN00113 200 LVGqIPRELGQ-MKSLKWIYLGYNNLSGEIPYEIGGLTSLNHLDLVYN 246
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 246-342 5.19e-06

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. 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 titin Z1z2 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: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 44.50  E-value: 5.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  246 ELRPGFVLALHCDVDGQPAPQLHWHiqipsgiveitspnvgTDGRALpgtpvaSSQPRFQAFANG---SLLIPDFGKLEE 322
Cdd:cd20972  12 EVAEGSKVRLECRVTGNPTPVVRWF----------------CEGKEL------QNSPDIQIHQEGdlhSLIIAEAFEEDT 69

                        90       100
                ....*....|....*....|
gi 2554604  323 GTYSCLATNELGSAESSVDV 342
Cdd:cd20972  70 GRYSCLATNSVGSDTTSAEI 89
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 294-340 1.27e-05

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: 43.54  E-value: 1.27e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 2554604  294 GTPVASSQPRFQAFANGSLLIPDFGKLEEGTYSCLATNELGSAESSV 340
Cdd:cd05724  36 GQPLNLDNERVRIVDDGNLLIAEARKSDEGTYKCVATNMVGERESRA 82
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 232-340 1.87e-05

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 43.00  E-value: 1.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  232 PSVQLsyQPSQDGAELRPGFVLALHCDVDGQPAPQLHWHIQipsgiveitspnvgtdgralpGTPVASSQPRFQAFANGS 311
Cdd:cd05730   2 PTIRA--RQSEVNATANLGQSVTLACDADGFPEPTMTWTKD---------------------GEPIESGEEKYSFNEDGS 58

                        90       100       110
                ....*....|....*....|....*....|
gi 2554604  312 -LLIPDFGKLEEGTYSCLATNELGSAESSV 340
Cdd:cd05730  59 eMTILDVDKLDEAEYTCIAENKAGEQEAEI 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 248-342 2.58e-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: 2.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604     248 RPGFVLALHCDVDGQPAPQLHWHIQIPSGIVEitspnvgtdgralpgtpvassQPRFQAFANG---SLLIPDFGKLEEGT 324
Cdd:smart00410   7 KEGESVTLSCEASGSPPPEVTWYKQGGKLLAE---------------------SGRFSVSRSGstsTLTISNVTPEDSGT 65

                           90
                   ....*....|....*...
gi 2554604     325 YSCLATNELGSAESSVDV 342
Cdd:smart00410  66 YTCAATNSSGSASSGTTL 83
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 254-342 3.72e-05

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: 42.08  E-value: 3.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  254 ALHCDVDGQPAPQLHWhiqipsgiveitspnVGTDGRALPGTPvassqpRFQAFANGSLLIPDFGKLEEGTYSCLATNEL 333
Cdd:cd05764  19 TLRCKARGDPEPAIHW---------------ISPEGKLISNSS------RTLVYDNGTLDILITTVKDTGAFTCIASNPA 77


                ....*....
gi 2554604  334 GSAESSVDV 342
Cdd:cd05764  78 GEATARVEL 86
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 294-339 4.36e-05

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: 42.06  E-value: 4.36e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 2554604  294 GTPVASSQPRFQAFANGSLLIPDFGKLEEGTYSCLATNELGSAESS 339
Cdd:cd04969  39 GTELLTNSSRICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKANST 84
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 247-340 4.48e-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: 41.71  E-value: 4.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  247 LRPGFVLALHCDVDGQPAPQLHWHIQipsgiveitspnvgtdgralpGTPVASSQPRFQAFANGSLLIPDFGKLEEGTYS 326
Cdd:cd20952  11 VAVGGTVVLNCQATGEPVPTISWLKD---------------------GVPLLGKDERITTLENGSLQIKGAEKSDTGEYT 69

                        90
                ....*....|....
gi 2554604  327 CLATNELGSAESSV 340
Cdd:cd20952  70 CVALNLSGEATWSA 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 255-331 5.01e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 41.40  E-value: 5.01e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2554604    255 LHCDVDGQPAPQLHWHIqipsgiveitspnvgtDGRALPGTPvasSQPRFQAFANGSLLIPDFGKLEEGTYSCLATN 331
Cdd:pfam13927  21 LTCEATGSPPPTITWYK----------------NGEPISSGS---TRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 39-181 5.28e-05

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 45.04  E-value: 5.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604   39 RDLESVPPGFPANV--TTLSLSANRL-PGLPEG--AFREVPLLQSLWLAHNEI-----RTVAAGALASLSHLKSLDLSHN 108
Cdd:cd00116  68 RGLQSLLQGLTKGCglQELDLSDNALgPDGCGVleSLLRSSSLQELKLNNNGLgdrglRLLAKGLKDLPPALEKLVLGRN 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  109 LISD---FAWSD-LHNLSALQLLKMDSNELTF--IPR--DAFRSLRALRSLQLNHNRLHTLA----EGTFTPLTALSHLQ 176
Cdd:cd00116 148 RLEGascEALAKaLRANRDLKELNLANNGIGDagIRAlaEGLKANCNLEVLDLNNNGLTDEGasalAETLASLKSLEVLN 227


                ....*
gi 2554604  177 INENP 181
Cdd:cd00116 228 LGDNN 232
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 255-342 9.04e-05

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: 40.84  E-value: 9.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  255 LHCDVDGQPAPQLHWhiqipsgiveitSPNvgtdgralpGTPVASSQPRFQaFANGSLLIPDFGKLEEGTYSCLATNELG 334
Cdd:cd20978  21 LPCQVTGVPQPKITW------------LHN---------GKPLQGPMERAT-VEDGTLTIINVQPEDTGYYGCVATNEIG 78


                ....*...
gi 2554604  335 SAESSVDV 342
Cdd:cd20978  79 DIYTETLL 86
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
32-180 9.11e-05

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 44.69  E-value: 9.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604    32 QIADCAYRDLESVPPGFPANVTTLSLSANRLPGLPEGAFREvplLQSLWLAHNEIRTVAAGALASLSHLKSLDLSHNLIS 111
Cdd:PRK15370 244 QEMELSINRITELPERLPSALQSLDLFHNKISCLPENLPEE---LRYLSVYDNSIRTLPAHLPSGITHLNVQSNSLTALP 320

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604   112 DFAWSDLHNLSAlqllkmDSNELTFIPrdafRSL-RALRSLQLNHNRLHTLAEgTFTPltALSHLQINEN 180
Cdd:PRK15370 321 ETLPPGLKTLEA------GENALTSLP----ASLpPELQVLDVSKNQITVLPE-TLPP--TITTLDVSRN 377
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 74-113 9.13e-05

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 39.54  E-value: 9.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2554604     74 PLLQSLWLAHNEIRTVaaGALASLSHLKSLDLSHN-LISDF 113
Cdd:pfam12799   1 PNLEVLDLSNNQITDI--PPLAKLPNLETLDLSGNnKITDL 39
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 76-156 9.28e-05

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 43.62  E-value: 9.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604   76 LQSLWLAHNEIRTVAAgaLASLSHLKSLDLSHNLISDFawsdlhnlsalqllkmdsNELTfiprDAFRSLRALRSLQLNH 155
Cdd:cd21340 122 LRVLNISGNNIDSLEP--LAPLRNLEQLDASNNQISDL------------------EELL----DLLSSWPSLRELDLTG 177


                .
gi 2554604  156 N 156
Cdd:cd21340 178 N 178
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
 239-335 1.11e-04

Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.


Pssm-ID: 409397 [Multi-domain]  Cd Length: 97  Bit Score: 40.94  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  239 QPS-QDGAElrpGFVLALHCDVDGQPAPQLHWHIqipsgiveitspnvgTDGRALPG-TPVASSQPRFQAFANGSLLIPD 316
Cdd:cd05734   7 QPNdQDGIY---GKAVVLNCSADGYPPPTIVWKH---------------SKGSGVPQfQHIVPLNGRIQLLSNGSLLIKH 68

                        90
                ....*....|....*....
gi 2554604  317 FGKLEEGTYSCLATNELGS 335
Cdd:cd05734  69 VLEEDSGYYLCKVSNDVGA 87
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 51-161 1.28e-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: 44.01  E-value: 1.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604   51 NVTTLSLSANRLPGlpEGAFREVPLLQ------SLWLAHNEIRTVAAGALA----SLSHLKSLDLSHNLISDfawsdlHN 120
Cdd:COG5238 293 TLTSLDLSVNRIGD--EGAIALAEGLQgnktlhTLNLAYNGIGAQGAIALAkalqENTTLHSLDLSDNQIGD------EG 364

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 2554604  121 LSAL-QLLKMDSNELTF------IPRDAFRSLRALrslqLNHNRLHTL 161
Cdd:COG5238 365 AIALaKYLEGNTTLRELnlgknnIGKQGAEALIDA----LQTNRLHTL 408
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 255-339 1.72e-04

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: 40.17  E-value: 1.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  255 LHCDVDGQPAPQLHWHIqipsgiveitspnvgtDGRALpgTPVASSQPRFQAFANGSLLIPDFGKLEEGTYSCLATNELG 334
Cdd:cd05744  20 FDCKVSGLPTPDLFWQL----------------NGKPV--RPDSAHKMLVRENGRHSLIIEPVTKRDAGIYTCIARNRAG 81


                ....*
gi 2554604  335 SAESS 339
Cdd:cd05744  82 ENSFN 86
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 254-342 3.23e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. 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 this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus 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: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 39.54  E-value: 3.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  254 ALHCDVDGQPAPQLHWhiqipsgiveitspnvgtdgrALPGTPVASSQPRFQAFAN-GSLLIPDFGKLEEGTYSCLATNE 332
Cdd:cd20976  20 VAQCSARGKPVPRITW---------------------IRNAQPLQYAADRSTCEAGvGELHIQDVLPEDHGTYTCLAKNA 78

                        90
                ....*....|
gi 2554604  333 LGSAESSVDV 342
Cdd:cd20976  79 AGQVSCSAWV 88
LRR_8 pfam13855
Leucine rich repeat;
146-180 3.57e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 38.27  E-value: 3.57e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2554604    146 RALRSLQLNHNRLHTLAEGTFTPLTALSHLQINEN 180
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNN 35
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 46-158 3.97e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 42.91  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604    46 PGFPANVTTL---SLSANRLPGlpeGAFREVPLLQSL---WLAHNEIRTVAAGALASLSHLKSLDLSHNLISDFAWSDLH 119
Cdd:PLN00113 181 PNSLTNLTSLeflTLASNQLVG---QIPRELGQMKSLkwiYLGYNNLSGEIPYEIGGLTSLNHLDLVYNNLTGPIPSSLG 257

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 2554604   120 NLSALQLLKMDSNELTF-IPRDAFrSLRALRSLQLNHNRL 158
Cdd:PLN00113 258 NLKNLQYLFLYQNKLSGpIPPSIF-SLQKLISLDLSDNSL 296
PLN03150 PLN03150
hypothetical protein; Provisional
 76-135 1.20e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 41.34  E-value: 1.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604    76 LQSLWLAHNEIRTVAAGALASLSHLKSLDLSHNLISDFAWSDLHNLSALQLLKMDSNELT 135
Cdd:PLN03150 444 LQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLS 503
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 48-193 1.22e-03

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 40.80  E-value: 1.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604   48 FPANVT--TLSLSANRLpgLPEG------AFREVPLLQSLWLAHNEIRTVAAGALA-SLSHLKSL---DLSHNLISDFAW 115
Cdd:cd00116 161 LRANRDlkELNLANNGI--GDAGiralaeGLKANCNLEVLDLNNNGLTDEGASALAeTLASLKSLevlNLGDNNLTDAGA 238

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  116 SDLHN-----LSALQLLKMDSNELTfipRDAFRSLR-------ALRSLQLNHNRLhtLAEGTFtpLTALSHLQinenpFD 183
Cdd:cd00116 239 AALASallspNISLLTLSLSCNDIT---DDGAKDLAevlaekeSLLELDLRGNKF--GEEGAQ--LLAESLLE-----PG 306

                       170
                ....*....|
gi 2554604  184 CTCGIVWLKT 193
Cdd:cd00116 307 NELESLWVKD 316
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 246-342 1.67e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 37.39  E-value: 1.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  246 ELRpGFVLALHCDVDGQPAPQLHWhiqipsgiVEITSPnvgtdgraLPgtpvaSSQPRFQAFaNGSLLIPDFGKLEEGTY 325
Cdd:cd05731   7 VLR-GGVLLLECIAEGLPTPDIRW--------IKLGGE--------LP-----KGRTKFENF-NKTLKIENVSEADSGEY 63

                        90
                ....*....|....*..
gi 2554604  326 SCLATNELGSAESSVDV 342
Cdd:cd05731  64 QCTASNTMGSARHTISV 80
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 255-342 1.72e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. 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 telokin Ig domain 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: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 37.55  E-value: 1.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  255 LHCDVDGQPAPQLHWHiqipsgiveitspnvgTDGRalpgtPVASSQpRFQAFANG----SLLIPDFGKLEEGTYSCLAT 330
Cdd:cd20973  17 FDCKVEGYPDPEVKWM----------------KDDN-----PIVESR-RFQIDQDEdglcSLIISDVCGDDSGKYTCKAV 74

                        90
                ....*....|..
gi 2554604  331 NELGSAESSVDV 342
Cdd:cd20973  75 NSLGEATCSAEL 86
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 55-158 2.58e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 40.22  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604    55 LSLSANRLPGLPEGAFREVPLLQSLWLAHNEIRTVAAGALASLSHLKSLDLSHNLISDFAWSDLHNLSALQLLKMDSNEL 134
Cdd:PLN00113 241 LDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFSNNF 320

                         90       100
                 ....*....|....*....|....*
gi 2554604   135 T-FIPRdAFRSLRALRSLQLNHNRL 158
Cdd:PLN00113 321 TgKIPV-ALTSLPRLQVLQLWSNKF 344
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
 294-339 3.47e-03

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: 36.52  E-value: 3.47e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 2554604  294 GTPVASSQPRFQAFANGSLLIPDFGKLEEGTYSCLATNELGSAESS 339
Cdd:cd05852  39 GTELLVNNSRISIWDDGSLEILNITKLDEGSYTCFAENNRGKANST 84
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here ...
 245-349 5.83e-03

Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here are composed of the second immunoglobulin (Ig)-like domain in protein tyrosine kinase (PTK) 7, also known as CCK4. PTK7 is a subfamily of the receptor protein tyrosine kinase family, and is referred to as an RPTK-like molecule. RPTKs transduce extracellular signals across the cell membrane and play important roles in regulating cell proliferation, migration, and differentiation. PTK7 is organized as an extracellular portion having seven Ig-like domains, a single transmembrane region, and a cytoplasmic tyrosine kinase-like domain. PTK7 is considered a pseudokinase as it has several unusual residues in some of the highly conserved tyrosine kinase (TK) motifs; it is predicted to lack TK activity. PTK7 may function as a cell-adhesion molecule. PTK7 mRNA is expressed at high levels in placenta, melanocytes, liver, lung, pancreas, and kidney. PTK7 is overexpressed in several cancers, including melanoma and colon cancer lines.


Pssm-ID: 409417  Cd Length: 95  Bit Score: 36.06  E-value: 5.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554604  245 AELRPGFVLALHCDVDGQPAPQLHWHiqipsgiveitspnvgTDGRALP---GTPVASSQPRfqafangSLLIPDFGKLE 321
Cdd:cd05760  11 AEIQPSSRVTLRCHIDGHPRPTYQWF----------------RDGTPLSdgqGNYSVSSKER-------TLTLRSAGPDD 67

                        90       100
                ....*....|....*....|....*...
gi 2554604  322 EGTYSCLATNELGSAESSVDVALATPGE 349
Cdd:cd05760  68 SGLYYCCAHNAFGSVCSSQNFTLSIIDE 95
 
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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