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Conserved domains on  [gi|1950411589|ref|XP_038246359|]
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LOW QUALITY PROTEIN: leucine-rich repeat-containing protein 24 [Dermochelys coriacea]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 257-352 5.69e-16

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 72.60  E-value: 5.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 257 PPVVQVEPLEATARLGDDLRV*CQASGYPQP*VSWRKVAHVGQDLPRRRQaagrnggaagarrrgsas*SDTGSGMLFLN 336
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSR------------------SLSGSNSTLTIS 62

                          90
                  ....*....|....*.
gi 1950411589 337 NITVAHAGKYECEASN 352
Cdd:pfam13927  63 NVTRSDAGTYTCVASN 78
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
39-161 1.81e-14

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 75.36  E-value: 1.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589  39 LKEIPASIHPST--QTIFLQDNSITQIHQqDLAVLRGLQYLYMQNNTISALePGAFRSQEHLLELALNGNRIHLLNSSIf 116
Cdd:COG4886   125 LTDLPEELANLTnlKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDL-PEELGNLTNLKELDLSNNQITDLPEPL- 201

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1950411589 117 KGLEHLRVLYLAGNQITKlLDFTFCDLQRLQELHLQENSIVALEE 161
Cdd:COG4886   202 GNLTNLEELDLSGNQLTD-LPEPLANLTNLETLDLSNNQLTDLPE 245
PCC super family cl28216
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 178-249 7.12e-08

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: 55.47  E-value: 7.12e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950411589  178 NNLRTISRAALRPLVSLQVLRLTENPWRCDCALHWLGAWIKEEGQRLLSSldKKIMCSEPPRLAYQ*LLDIS 249
Cdd:TIGR00864    5 NKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQP--EAALCAGPGALAGQPLLGIP 74
LRRNT smart00013
Leucine rich repeat N-terminal domain;
20-51 6.43e-03

Leucine rich repeat N-terminal domain;


:

Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 34.60  E-value: 6.43e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1950411589   20 GCPTTCRCYSMTVECGSLGLKEIPASIHPSTQ 51
Cdd:smart00013   1 ACPAPCNCSGTAVDCSGRGLTEVPLDLPPDTT 32
 
Name Accession Description Interval E-value
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 257-352 5.69e-16

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 72.60  E-value: 5.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 257 PPVVQVEPLEATARLGDDLRV*CQASGYPQP*VSWRKVAHVGQDLPRRRQaagrnggaagarrrgsas*SDTGSGMLFLN 336
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSR------------------SLSGSNSTLTIS 62

                          90
                  ....*....|....*.
gi 1950411589 337 NITVAHAGKYECEASN 352
Cdd:pfam13927  63 NVTRSDAGTYTCVASN 78
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
39-161 1.81e-14

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 75.36  E-value: 1.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589  39 LKEIPASIHPST--QTIFLQDNSITQIHQqDLAVLRGLQYLYMQNNTISALePGAFRSQEHLLELALNGNRIHLLNSSIf 116
Cdd:COG4886   125 LTDLPEELANLTnlKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDL-PEELGNLTNLKELDLSNNQITDLPEPL- 201

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1950411589 117 KGLEHLRVLYLAGNQITKlLDFTFCDLQRLQELHLQENSIVALEE 161
Cdd:COG4886   202 GNLTNLEELDLSGNQLTD-LPEPLANLTNLETLDLSNNQLTDLPE 245
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 53-202 2.25e-13

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: 69.43  E-value: 2.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589  53 IFLQDNSITQIHqqDLAVLRGLQYLYMQNNTISALEpgAFRSQEHLLELALNGNRIhllnSSI--FKGLEHLRVLYLAGN 130
Cdd:cd21340     7 LYLNDKNITKID--NLSLCKNLKVLYLYDNKITKIE--NLEFLTNLTHLYLQNNQI----EKIenLENLVNLKKLYLGGN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 131 QITKL--LDftfcDLQRLQELHLqENSIVALEEQALAGLSSLALLDL-------SKNNLRTISraALRPLVSLQVLRLTE 201
Cdd:cd21340    79 RISVVegLE----NLTNLEELHI-ENQRLPPGEKLTFDPRSLAALSNslrvlniSGNNIDSLE--PLAPLRNLEQLDASN 151


                  .
gi 1950411589 202 N 202
Cdd:cd21340   152 N 152
LRR_8 pfam13855
Leucine rich repeat;
72-132 1.59e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.46  E-value: 1.59e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950411589  72 RGLQYLYMQNNTISALEPGAFRSQEHLLELALNGNRIHLLNSSIFKGLEHLRVLYLAGNQI 132
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 264-365 1.93e-10

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: 57.13  E-value: 1.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589  264 PLEATARLGDDLRV*CQASGYPQP*VSWRKVAHVGQDLPRRRQAAGrnggaagarrrgsas*sDTGSGMLFLNNITVAHA 343
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSR-----------------SGSTSTLTISNVTPEDS 63

                           90       100
                   ....*....|....*....|..
gi 1950411589  344 GKYECEASNPGGTARVLFHLMV 365
Cdd:smart00410  64 GTYTCAATNSSGSASSGTTLTV 85
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 257-352 2.04e-08

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: 51.93  E-value: 2.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 257 PPVVQVEPLEATARLGDDLRV*CQASGYPQP*VSWRKVahVGQDLPRRRQAAGRNGGAAGarrrgsas*sdtGSGMLFLN 336
Cdd:cd20954     1 PPRWIVEPVDANVAAGQDVMLHCQADGFPTPTVTWKKA--TGSTPGEYKDLLYDPNVRIL------------PNGTLVFG 66

                          90
                  ....*....|....*.
gi 1950411589 337 NITVAHAGKYECEASN 352
Cdd:cd20954    67 HVQKENEGHYLCEAKN 82
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 178-249 7.12e-08

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: 55.47  E-value: 7.12e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950411589  178 NNLRTISRAALRPLVSLQVLRLTENPWRCDCALHWLGAWIKEEGQRLLSSldKKIMCSEPPRLAYQ*LLDIS 249
Cdd:TIGR00864    5 NKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQP--EAALCAGPGALAGQPLLGIP 74
LRRCT smart00082
Leucine rich repeat C-terminal domain;
202-255 1.11e-06

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 45.50  E-value: 1.11e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1950411589  202 NPWRCDCALHWLGAWIkEEGQRLLSSLDkkIMCSEPPRLAYQ*LLDISGNSLIC 255
Cdd:smart00082   1 NPFICDCELRWLLRWL-QANEHLQDPVD--LRCASPSSLRGP-LLELLHSEFKC 50
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
37-257 2.51e-03

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 40.84  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589  37 LGLKEIPASIHPSTQTIFLQDNSITQIHQQdlavLRG-LQYLYMQNNTISALePGAFRSQEHLLELALngNRIHLLNSSI 115
Cdd:PRK15370  188 LGLTTIPACIPEQITTLILDNNELKSLPEN----LQGnIKTLYANSNQLTSI-PATLPDTIQEMELSI--NRITELPERL 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 116 FKGLEHLRVLYlagNQITKLLDfTFCDlqRLQELHLQENSIVALEEQalagLSSLALLDLSKNNLRTISRAALRPlvSLQ 195
Cdd:PRK15370  261 PSALQSLDLFH---NKISCLPE-NLPE--ELRYLSVYDNSIRTLPAH----LPSGITHLNVQSNSLTALPETLPP--GLK 328

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1950411589 196 VLRLTENpwrcdcALHWLGAWIKEEGQRLLSSLDKKIMCSE--PPRLayq*LLDISGNSLICIP 257
Cdd:PRK15370  329 TLEAGEN------ALTSLPASLPPELQVLDVSKNQITVLPEtlPPTI---TTLDVSRNALTNLP 383
LRRNT smart00013
Leucine rich repeat N-terminal domain;
20-51 6.43e-03

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 34.60  E-value: 6.43e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1950411589   20 GCPTTCRCYSMTVECGSLGLKEIPASIHPSTQ 51
Cdd:smart00013   1 ACPAPCNCSGTAVDCSGRGLTEVPLDLPPDTT 32
 
Name Accession Description Interval E-value
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 257-352 5.69e-16

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 72.60  E-value: 5.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 257 PPVVQVEPLEATARLGDDLRV*CQASGYPQP*VSWRKVAHVGQDLPRRRQaagrnggaagarrrgsas*SDTGSGMLFLN 336
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSR------------------SLSGSNSTLTIS 62

                          90
                  ....*....|....*.
gi 1950411589 337 NITVAHAGKYECEASN 352
Cdd:pfam13927  63 NVTRSDAGTYTCVASN 78
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
39-161 1.81e-14

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 75.36  E-value: 1.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589  39 LKEIPASIHPST--QTIFLQDNSITQIHQqDLAVLRGLQYLYMQNNTISALePGAFRSQEHLLELALNGNRIHLLNSSIf 116
Cdd:COG4886   125 LTDLPEELANLTnlKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDL-PEELGNLTNLKELDLSNNQITDLPEPL- 201

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1950411589 117 KGLEHLRVLYLAGNQITKlLDFTFCDLQRLQELHLQENSIVALEE 161
Cdd:COG4886   202 GNLTNLEELDLSGNQLTD-LPEPLANLTNLETLDLSNNQLTDLPE 245
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-266 4.80e-14

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 74.20  E-value: 4.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589  51 QTIFLQDNSITQIhQQDLAVLRGLQYLYMQNNTISALePGAFRSQEHLLELALNGNRIHLLNSSIfKGLEHLRVLYLAGN 130
Cdd:COG4886   116 ESLDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDL-PEPLGNLTNLKSLDLSNNQLTDLPEEL-GNLTNLKELDLSNN 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 131 QITKLlDFTFCDLQRLQELHLQENSIVALEEqalaglsslalldlsknnlrtisraALRPLVSLQVLRLTENPwrcdcal 210
Cdd:COG4886   193 QITDL-PEPLGNLTNLEELDLSGNQLTDLPE-------------------------PLANLTNLETLDLSNNQ------- 239

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1950411589 211 hwlgawIKEegqrlLSSLdkkimcSEPPRLAYq*lLDISGNSLICIPPVVQVEPLE 266
Cdd:COG4886   240 ------LTD-----LPEL------GNLTNLEE---LDLSNNQLTDLPPLANLTNLK 275
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 53-202 2.25e-13

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: 69.43  E-value: 2.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589  53 IFLQDNSITQIHqqDLAVLRGLQYLYMQNNTISALEpgAFRSQEHLLELALNGNRIhllnSSI--FKGLEHLRVLYLAGN 130
Cdd:cd21340     7 LYLNDKNITKID--NLSLCKNLKVLYLYDNKITKIE--NLEFLTNLTHLYLQNNQI----EKIenLENLVNLKKLYLGGN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 131 QITKL--LDftfcDLQRLQELHLqENSIVALEEQALAGLSSLALLDL-------SKNNLRTISraALRPLVSLQVLRLTE 201
Cdd:cd21340    79 RISVVegLE----NLTNLEELHI-ENQRLPPGEKLTFDPRSLAALSNslrvlniSGNNIDSLE--PLAPLRNLEQLDASN 151


                  .
gi 1950411589 202 N 202
Cdd:cd21340   152 N 152
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
39-202 7.52e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 67.27  E-value: 7.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589  39 LKEIPASIHPST--QTIFLQDNSITQIhQQDLAVLRGLQYLYMQNNTISALePGAFRSQEHLLELALNGNRIHLLNSSIf 116
Cdd:COG4886   148 LTDLPEPLGNLTnlKSLDLSNNQLTDL-PEELGNLTNLKELDLSNNQITDL-PEPLGNLTNLEELDLSGNQLTDLPEPL- 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 117 KGLEHLRVLYLAGNQITKLLDFTfcDLQRLQELHLQENSIVALEEqaLAGLSSLALLDLSKNNLRTISRAALRPLVSLQV 196
Cdd:COG4886   225 ANLTNLETLDLSNNQLTDLPELG--NLTNLEELDLSNNQLTDLPP--LANLTNLKTLDLSNNQLTDLKLKELELLLGLNS 300


                  ....*.
gi 1950411589 197 LRLTEN 202
Cdd:COG4886   301 LLLLLL 306
LRR_8 pfam13855
Leucine rich repeat;
72-132 1.59e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.46  E-value: 1.59e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950411589  72 RGLQYLYMQNNTISALEPGAFRSQEHLLELALNGNRIHLLNSSIFKGLEHLRVLYLAGNQI 132
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 264-365 1.93e-10

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: 57.13  E-value: 1.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589  264 PLEATARLGDDLRV*CQASGYPQP*VSWRKVAHVGQDLPRRRQAAGrnggaagarrrgsas*sDTGSGMLFLNNITVAHA 343
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSR-----------------SGSTSTLTISNVTPEDS 63

                           90       100
                   ....*....|....*....|..
gi 1950411589  344 GKYECEASNPGGTARVLFHLMV 365
Cdd:smart00410  64 GTYTCAATNSSGSASSGTTLTV 85
LRR_8 pfam13855
Leucine rich repeat;
97-156 4.26e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 55.61  E-value: 4.26e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589  97 HLLELALNGNRIHLLNSSIFKGLEHLRVLYLAGNQITKLLDFTFCDLQRLQELHLQENSI 156
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
I-set pfam07679
Immunoglobulin I-set domain;
258-365 3.05e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 54.19  E-value: 3.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 258 PVVQVEPLEATARLGDDLRV*CQASGYPQP*VSWRKvahVGQDLP--RRRQaagrnggaagarrrgsaS*SDTGSGMLFL 335
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFK---DGQPLRssDRFK-----------------VTYEGGTYTLTI 60

                          90       100       110
                  ....*....|....*....|....*....|
gi 1950411589 336 NNITVAHAGKYECEASNPGGTARVLFHLMV 365
Cdd:pfam07679  61 SNVQPDDSGKYTCVATNSAGEAEASAELTV 90
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 257-352 2.04e-08

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: 51.93  E-value: 2.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 257 PPVVQVEPLEATARLGDDLRV*CQASGYPQP*VSWRKVahVGQDLPRRRQAAGRNGGAAGarrrgsas*sdtGSGMLFLN 336
Cdd:cd20954     1 PPRWIVEPVDANVAAGQDVMLHCQADGFPTPTVTWKKA--TGSTPGEYKDLLYDPNVRIL------------PNGTLVFG 66

                          90
                  ....*....|....*.
gi 1950411589 337 NITVAHAGKYECEASN 352
Cdd:cd20954    67 HVQKENEGHYLCEAKN 82
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 275-358 2.11e-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.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 51.18  E-value: 2.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 275 LRV*CQASGYPQP*VSWRKVahvGQDLPrrrqaagrnggaagaRRRGSAS*SDTGSGMLFLNNITVAHAGKYECEASNPG 354
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKN---GKPLP---------------PSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSA 62


                  ....
gi 1950411589 355 GTAR 358
Cdd:cd00096    63 GGSA 66
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 272-365 3.37e-08

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: 50.87  E-value: 3.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 272 GDDLRV*CQASGYPQP*VSWRKVahvGQDLPRRRqaagrnggaagarrrgsaS*SDTGSGMLFLNNITVAHAGKYECEAS 351
Cdd:cd05731    10 GGVLLLECIAEGLPTPDIRWIKL---GGELPKGR------------------TKFENFNKTLKIENVSEADSGEYQCTAS 68

                          90
                  ....*....|....
gi 1950411589 352 NPGGTARVLFHLMV 365
Cdd:cd05731    69 NTMGSARHTISVTV 82
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 38-156 5.90e-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: 53.25  E-value: 5.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589  38 GLKEIPASIH-PSTQTIFLQDNSITQIhqQDLAVLRGLQYLYMQNNTISALEPgaFRSQEHLLELALNGNRI-------- 108
Cdd:cd21340    13 NITKIDNLSLcKNLKVLYLYDNKITKI--ENLEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLGGNRIsvveglen 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 109 -------HL---------------------------LN------SSI--FKGLEHLRVLYLAGNQITKLLDF--TFCDLQ 144
Cdd:cd21340    89 ltnleelHIenqrlppgekltfdprslaalsnslrvLNisgnniDSLepLAPLRNLEQLDASNNQISDLEELldLLSSWP 168

                         170
                  ....*....|..
gi 1950411589 145 RLQELHLQENSI 156
Cdd:cd21340   169 SLRELDLTGNPV 180
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 178-249 7.12e-08

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: 55.47  E-value: 7.12e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950411589  178 NNLRTISRAALRPLVSLQVLRLTENPWRCDCALHWLGAWIKEEGQRLLSSldKKIMCSEPPRLAYQ*LLDIS 249
Cdd:TIGR00864    5 NKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQP--EAALCAGPGALAGQPLLGIP 74
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
 269-365 1.99e-07

First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domain A168 within the A-band segment of human cardiac titin. 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 structures of the titin-A168169 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: 409563  Cd Length: 93  Bit Score: 49.01  E-value: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 269 ARLGDDLRV*CQASGYPQP*VSWRKVAHVGQDlprrrqaagrnggaagaRRRGSAS*SDTGSGMLFLNNITV-AHAGKYE 347
Cdd:cd20971    13 VRYQSNATLVCKVTGHPKPIVKWYRQGKEIIA-----------------DGLKYRIQEFKGGYHQLIIASVTdDDATVYQ 75

                          90
                  ....*....|....*...
gi 1950411589 348 CEASNPGGTARVLFHLMV 365
Cdd:cd20971    76 VRATNQGGSVSGTASLEV 93
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
39-257 3.55e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 52.63  E-value: 3.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589  39 LKEIPASIHPST--QTIFLQDNSITQIHQqDLAVLRGLQYLYMQNNTISALePGAFRSQEHLLELALNGNRI-------- 108
Cdd:COG4886   171 LTDLPEELGNLTnlKELDLSNNQITDLPE-PLGNLTNLEELDLSGNQLTDL-PEPLANLTNLETLDLSNNQLtdlpelgn 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 109 ------------HLLNSSIFKGLEHLRVLYLAGNQITKLldftfcDLQRLQELHLQENSIVALEEQALAGLSSLALLDLS 176
Cdd:COG4886   249 ltnleeldlsnnQLTDLPPLANLTNLKTLDLSNNQLTDL------KLKELELLLGLNSLLLLLLLLNLLELLILLLLLTT 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 177 KNNLRTISRAALRPLVSLQVLRLTENPWRCDCALHWLGAWIKEEGQRLLSSLDKKIMCSEPPRLAYQ*LLDISGNSLICI 256
Cdd:COG4886   323 LLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLL 402


                  .
gi 1950411589 257 P 257
Cdd:COG4886   403 L 403
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 259-359 6.97e-07

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: 47.11  E-value: 6.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 259 VVQVEPLEATARLGDDLRV*CQASGYPQP*VSWRKVAH--VGQDlPRRRQAAgrnggaagarrrgsas*sdtgSGMLFLN 336
Cdd:cd20952     1 IILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVplLGKD-ERITTLE---------------------NGSLQIK 58

                          90       100
                  ....*....|....*....|...
gi 1950411589 337 NITVAHAGKYECEASNPGGTARV 359
Cdd:cd20952    59 GAEKSDTGEYTCVALNLSGEATW 81
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 272-365 9.74e-07

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 46.47  E-value: 9.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 272 GDDLRV*CQASGYPQP*VSWRKVahvGQDLP--RRRQAAgrnggaagarrrgsas*sdtGSGMLFLNNITVAHAGKYECE 349
Cdd:cd05745     2 GQTVDFLCEAQGYPQPVIAWTKG---GSQLSvdRRHLVL--------------------SSGTLRISRVALHDQGQYECQ 58

                          90
                  ....*....|....*.
gi 1950411589 350 ASNPGGTARVLFHLMV 365
Cdd:cd05745    59 AVNIVGSQRTVAQLTV 74
LRRCT smart00082
Leucine rich repeat C-terminal domain;
202-255 1.11e-06

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 45.50  E-value: 1.11e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1950411589  202 NPWRCDCALHWLGAWIkEEGQRLLSSLDkkIMCSEPPRLAYQ*LLDISGNSLIC 255
Cdd:smart00082   1 NPFICDCELRWLLRWL-QANEHLQDPVD--LRCASPSSLRGP-LLELLHSEFKC 50
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 258-365 1.51e-06

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


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 46.39  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 258 PVVQVEPLEATARLGDDLRV*CQASGYPQP*VSWRKVAHVGQDLPRRRQAAGRNGGAagarrrgsas*sdTGSGMLFLNN 337
Cdd:cd05765     1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEKQVPGKENLIMRPNHVRGNVVV-------------TNIGQLVIYN 67

                          90       100
                  ....*....|....*....|....*...
gi 1950411589 338 ITVAHAGKYECEASNPGGTARVLFHLMV 365
Cdd:cd05765    68 AQPQDAGLYTCTARNSGGLLRANFPLSV 95
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 263-357 4.39e-06

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 45.13  E-value: 4.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 263 EPLEATARLGDDLRV*CQASGYPQP*VSWRKVAHVGQDLPRRRqaagrnggaagarrrgsas*SDTGSG-MLFLNNITVA 341
Cdd:cd04978     5 EPPSLVLSPGETGELICEAEGNPQPTITWRLNGVPIEPAPEDM--------------------RRTVDGrTLIFSNLQPN 64

                          90
                  ....*....|....*.
gi 1950411589 342 HAGKYECEASNPGGTA 357
Cdd:cd04978    65 DTAVYQCNASNVHGYL 80
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 264-356 4.43e-06

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup 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. 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. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin 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. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 45.30  E-value: 4.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 264 PLEATARLGDDLRV*CQASGYPQP*VSWRKVAhvGQDLPRRRQAAGRNGgaagarrrgsas*sdTGSGMLFLNNITVAHA 343
Cdd:cd05763     6 PHDITIRAGSTARLECAATGHPTPQIAWQKDG--GTDFPAARERRMHVM---------------PEDDVFFIVDVKIEDT 68

                          90
                  ....*....|...
gi 1950411589 344 GKYECEASNPGGT 356
Cdd:cd05763    69 GVYSCTAQNSAGS 81
LRR_8 pfam13855
Leucine rich repeat;
121-203 4.82e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 44.05  E-value: 4.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 121 HLRVLYLAGNQITKLLDFTFCDLQRLQELHLQENsivaleeqalaglsslalldlsknNLRTISRAALRPLVSLQVLRLT 200
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNN------------------------LLTTLSPGAFSGLPSLRYLDLS 57


                  ...
gi 1950411589 201 ENP 203
Cdd:pfam13855  58 GNR 60
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 258-368 2.37e-05

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 43.02  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 258 PVVQVEPLEATARLGDDLRV*CQASGYPQP*VSWRKVAH-VGQDLPRRrqaagrnggaagarrrgsAS*SDTGSgMLFLN 336
Cdd:cd05736     1 PVIRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMdINPKLSKQ------------------LTLIANGS-ELHIS 61

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1950411589 337 NITVAHAGKYECEASNPGGTARVLFHLMVNRS 368
Cdd:cd05736    62 NVRYEDTGAYTCIAKNEGGVDEDISSLFVEDS 93
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 257-365 3.91e-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: 42.38  E-value: 3.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 257 PPVVQVEPLEATARLGDDLRV*CQASGYPQP*VSWrkvAHVGQDLPRRRqaagrnggaagarrrgsaS*SDTGSGMLFLN 336
Cdd:cd20978     1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITW---LHNGKPLQGPM------------------ERATVEDGTLTII 59

                          90       100
                  ....*....|....*....|....*....
gi 1950411589 337 NITVAHAGKYECEASNPGGTARVLFHLMV 365
Cdd:cd20978    60 NVQPEDTGYYGCVATNEIGDIYTETLLHV 88
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 257-365 4.40e-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: 42.23  E-value: 4.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 257 PPVVQVEPLE--ATARLGDDLRV*CQASGYPQP*VSWRKVAHVGQDLPRRrqaagrnggaagarrrgsAS*SDTGSGMLF 334
Cdd:cd05730     1 PPTIRARQSEvnATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEK------------------YSFNEDGSEMTI 62

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1950411589 335 LNnITVAHAGKYECEASNPGGTARVLFHLMV 365
Cdd:cd05730    63 LD-VDKLDEAEYTCIAENKAGEQEAEIHLKV 92
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 258-357 4.82e-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: 4.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 258 PVVQVEPleatARLGDDLRV*CQASGYPQP*VSWRKvahvGQDLPRRRQAAGRnggaagarrrgsas*sdTGSGMLFLNN 337
Cdd:cd04969     7 PVKKKIL----AAKGGDVIIECKPKASPKPTISWSK----GTELLTNSSRICI-----------------LPDGSLKIKN 61

                          90       100
                  ....*....|....*....|
gi 1950411589 338 ITVAHAGKYECEASNPGGTA 357
Cdd:cd04969    62 VTKSDEGKYTCFAVNFFGKA 81
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 257-355 7.37e-05

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third 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. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 41.38  E-value: 7.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 257 PPVVQVEPLEATARLGDDLRV*CQASGYPQP*VSWRKVAhvGQDLPRRRQAagrnggaagarrrgsas*sdTGSGMLFLN 336
Cdd:cd04968     1 PSIKVRFPADTYALKGQTVTLECFALGNPVPQIKWRKVD--GSPSSQWEIT--------------------TSEPVLEIP 58

                          90
                  ....*....|....*....
gi 1950411589 337 NITVAHAGKYECEASNPGG 355
Cdd:cd04968    59 NVQFEDEGTYECEAENSRG 77
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 258-352 9.92e-05

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). 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: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 41.34  E-value: 9.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 258 PVVQV--EPLEATARLGDDLRV*CQASGYPQP*VSWRKVAHVGQDLPRRRQAAgrnggaagarrrgsas*sdtGSG-MLF 334
Cdd:cd20970     1 PVISTpqPSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVR--------------------ENGtTLT 60

                          90
                  ....*....|....*...
gi 1950411589 335 LNNITVAHAGKYECEASN 352
Cdd:cd20970    61 IRNIRRSDMGIYLCIASN 78
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 264-356 1.26e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 40.66  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 264 PLEATARLGDDLRV*CQASGYPQP*VSWRKvahVGQDLPRRRQAAGRnggaagarrrgsas*sdtgSGMLFLNNITVAHA 343
Cdd:cd05728     6 ISDTEADIGSSLRWECKASGNPRPAYRWLK---NGQPLASENRIEVE-------------------AGDLRITKLSLSDS 63

                          90
                  ....*....|...
gi 1950411589 344 GKYECEASNPGGT 356
Cdd:cd05728    64 GMYQCVAENKHGT 76
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 257-365 2.19e-04

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


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 40.24  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 257 PPVV-QVEPLEATArlGDDLRV*CQASGYPQP*VSWRKvahVGQDLP-RRRQAAGRnggaagarrrgsas*sdtgSGMLF 334
Cdd:cd20958     1 PPFIrPMGNLTAVA--GQTLRLHCPVAGYPISSITWEK---DGRRLPlNHRQRVFP-------------------NGTLV 56

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1950411589 335 LNNITVAH-AGKYECEASNPGG-TARVLFHLMV 365
Cdd:cd20958    57 IENVQRSSdEGEYTCTARNQQGqSASRSVFVKV 89
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
 257-355 3.78e-04

Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third 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. This group belongs to the I-set of IgSF domains.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 39.62  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 257 PPVVQVEPLEATARLGDDLRV*CQASGYPQP*VSWRKVAhvgQDLPRRRQaagrnggaagarrrgsas*SDTGSGMLFLN 336
Cdd:cd05851     1 PADINVKFKDTYALKGQNVTLECFALGNPVPVIRWRKIL---EPMPATAE-------------------ISMSGAVLKIF 58

                          90
                  ....*....|....*....
gi 1950411589 337 NITVAHAGKYECEASNPGG 355
Cdd:cd05851    59 NIQPEDEGTYECEAENIKG 77
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
 257-355 6.22e-04

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth 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. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 39.04  E-value: 6.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 257 PPVVQVEplEATARLGDDLRV*CQASGYPQP*VSWRKVAHV----GQDLPRRrqaagrnggaagarrrgSAS*SDTGSGM 332
Cdd:cd05732     3 PKITYLE--NQTAVELEQITLTCEAEGDPIPEITWRRATRGisfeEGDLDGR-----------------IVVRGHARVSS 63

                          90       100
                  ....*....|....*....|...
gi 1950411589 333 LFLNNITVAHAGKYECEASNPGG 355
Cdd:cd05732    64 LTLKDVQLTDAGRYDCEASNRIG 86
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 262-355 8.92e-04

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 38.33  E-value: 8.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 262 VEPLEATARLGDDLRV*CQAS-GYPQP*VSWRKVahvGQDLPRRRQAAGRNGgaagarrrgsas*sDTGSGMLFLNNITV 340
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAStGSPGPDVTWSKE---GGTLIESLKVKHDNG--------------RTTQSSLLISNVTK 63

                          90
                  ....*....|....*
gi 1950411589 341 AHAGKYECEASNPGG 355
Cdd:pfam00047  64 EDAGTYTCVVNNPGG 78
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 275-359 1.02e-03

Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the fourth immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted, and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143223  Cd Length: 69  Bit Score: 37.93  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 275 LRV*CQASGYPQP*VSWRKVA---------HVGQDlprrrqaagrnggaagarrrgsas*sdtgsGMLFLNNITVAHAGK 345
Cdd:cd05746     1 VQIPCSAQGDPEPTITWNKDGvqvtesgkfHISPE------------------------------GYLAIRDVGVADQGR 50

                          90
                  ....*....|....
gi 1950411589 346 YECEASNPGGTARV 359
Cdd:cd05746    51 YECVARNTIGYASV 64
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
 272-355 1.87e-03

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 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.


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 37.57  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 272 GDDLRV*CQASGYPQP*VSWR----KVAHVGQDlPRRRqaagrnggaagarrrgsas*sdTGSGMLFLNNITVAHAGKYE 347
Cdd:cd05867    14 GETARLDCQVEGIPTPNITWSingaPIEGTDPD-PRRH----------------------VSSGALILTDVQPSDTAVYQ 70


                  ....*...
gi 1950411589 348 CEASNPGG 355
Cdd:cd05867    71 CEARNRHG 78
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
37-257 2.51e-03

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 40.84  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589  37 LGLKEIPASIHPSTQTIFLQDNSITQIHQQdlavLRG-LQYLYMQNNTISALePGAFRSQEHLLELALngNRIHLLNSSI 115
Cdd:PRK15370  188 LGLTTIPACIPEQITTLILDNNELKSLPEN----LQGnIKTLYANSNQLTSI-PATLPDTIQEMELSI--NRITELPERL 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 116 FKGLEHLRVLYlagNQITKLLDfTFCDlqRLQELHLQENSIVALEEQalagLSSLALLDLSKNNLRTISRAALRPlvSLQ 195
Cdd:PRK15370  261 PSALQSLDLFH---NKISCLPE-NLPE--ELRYLSVYDNSIRTLPAH----LPSGITHLNVQSNSLTALPETLPP--GLK 328

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1950411589 196 VLRLTENpwrcdcALHWLGAWIKEEGQRLLSSLDKKIMCSE--PPRLayq*LLDISGNSLICIP 257
Cdd:PRK15370  329 TLEAGEN------ALTSLPASLPPELQVLDVSKNQITVLPEtlPPTI---TTLDVSRNALTNLP 383
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
 277-356 3.05e-03

Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains and a cytoplasmic portion having two tandem phosphatase domains.


Pssm-ID: 409400 [Multi-domain]  Cd Length: 91  Bit Score: 36.91  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 277 V*CQASGYPQP*VSWRKvahvgQDLPrrrqaagrnggaaGARRRGSAS*SDTGSGMLFLNNITVAHAGKYECEASNPGGT 356
Cdd:cd05738    19 MLCAASGNPDPEISWFK-----DFLP-------------VDTATSNGRIKQLRSGALQIENSEESDQGKYECVATNSAGT 80
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 263-357 4.28e-03

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: 36.22  E-value: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 263 EPLEATARLGDDLRV*CQASGYPQP*VSWRKvahVGQDLPRRRqaagrnggaagarrrgsAS*SDTGSgmLFLNNITVAH 342
Cdd:cd05725     3 RPQNQVVLVDDSAEFQCEVGGDPVPTVRWRK---EDGELPKGR-----------------YEILDDHS--LKIRKVTAGD 60

                          90
                  ....*....|....*
gi 1950411589 343 AGKYECEASNPGGTA 357
Cdd:cd05725    61 MGSYTCVAENMVGKI 75
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 272-357 4.41e-03

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: 36.70  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 272 GDDLRV*CQASGYPQP*VSWRKVAHVGQDLPRrrqaagrnggaagarrrGSAS*SDTGSGMLFLNNITVAHAGKYECEAS 351
Cdd:cd05744    15 GRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSA-----------------HKMLVRENGRHSLIIEPVTKRDAGIYTCIAR 77


                  ....*.
gi 1950411589 352 NPGGTA 357
Cdd:cd05744    78 NRAGEN 83
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 271-355 4.69e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 36.38  E-value: 4.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 271 LGDDLRV*CQASGYPQP*VSWRK------VAHVGQdlPRRRQAAgrnggaagarrrgsas*sdtgsgmLFLNNITVAHAG 344
Cdd:cd05856    18 VGSSVRLKCVASGNPRPDITWLKdnkpltPPEIGE--NKKKKWT------------------------LSLKNLKPEDSG 71

                          90
                  ....*....|.
gi 1950411589 345 KYECEASNPGG 355
Cdd:cd05856    72 KYTCHVSNRAG 82
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 258-358 4.85e-03

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) 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, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), 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 Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 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.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 36.76  E-value: 4.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 258 PVVQVEPLEATARLGDDLRV*CQASGYPQP*VSWRKvahVGQDLPRRRQaagrnggaagaRRRGSAS*SDTGSgMLFLNN 337
Cdd:cd07693     1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLK---NGQPLETDKD-----------DPRSHRIVLPSGS-LFFLRV 65

                          90       100
                  ....*....|....*....|....*
gi 1950411589 338 I----TVAHAGKYECEASNPGGTAR 358
Cdd:cd07693    66 VhgrkGRSDEGVYVCVAHNSLGEAV 90
LRRNT smart00013
Leucine rich repeat N-terminal domain;
20-51 6.43e-03

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 34.60  E-value: 6.43e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1950411589   20 GCPTTCRCYSMTVECGSLGLKEIPASIHPSTQ 51
Cdd:smart00013   1 ACPAPCNCSGTAVDCSGRGLTEVPLDLPPDTT 32
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 264-357 7.26e-03

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


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 36.07  E-value: 7.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 264 PLEATARLGDDLRV*CQASGYPQP*VSWRKvahvGQDLPRRRQAAGRNGgaagarrrgsas*sdtgSGMLFLNNITVAHA 343
Cdd:cd20968     6 PTNVTIIEGLKAVLPCTTMGNPKPSVSWIK----GDDLIKENNRIAVLE-----------------SGSLRIHNVQKEDA 64

                          90
                  ....*....|....
gi 1950411589 344 GKYECEASNPGGTA 357
Cdd:cd20968    65 GQYRCVAKNSLGIA 78
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 121-157 7.61e-03

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: 34.53  E-value: 7.61e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1950411589 121 HLRVLYLAGNQITKLldFTFCDLQRLQELHLQENSIV 157
Cdd:pfam12799   2 NLEVLDLSNNQITDI--PPLAKLPNLETLDLSGNNKI 36
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 268-365 9.30e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 35.26  E-value: 9.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950411589 268 TARLGDDLRV*CQASGYPQP*VSWRKvahVGQDL--PRRRQaagrnggaagarrrgsas*SDTGSGM--LFLNNITVAHA 343
Cdd:cd05748     3 VVRAGESLRLDIPIKGRPTPTVTWSK---DGQPLkeTGRVQ-------------------IETTASStsLVIKNAKRSDS 60

                          90       100
                  ....*....|....*....|..
gi 1950411589 344 GKYECEASNPGGTARVLFHLMV 365
Cdd:cd05748    61 GKYTLTLKNSAGEKSATINVKV 82
 
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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