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Conserved domains on  [gi|564363844|ref|XP_006243182|]
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leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
417-508 3.06e-54

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. 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 Lingo-1 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: 409561  Cd Length: 92  Bit Score: 179.51  E-value: 3.06e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 417 RAHIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANA 496
Cdd:cd20969    1 RAAIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANA 80
                         90
                 ....*....|..
gi 564363844 497 GGNDSMPAHLHV 508
Cdd:cd20969   81 GGNDSMPAHLHV 92
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
65-365 2.16e-23

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 103.09  E-value: 2.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  65 TETRLLDLGKNRIKTLNQDEFASFPHLEELELNENivsavepGAFNNLFNLRTLGLRSNRLKLIPLGvFTGLSNLTKLDI 144
Cdd:COG4886   72 LLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPEE-LANLTNLKELDL 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 145 SENKIVILLDYmFQDLYNLKSLEVGDNDLVYIShRAFSGLNSLEQLTLEKCNLTSIPtEALSHLHGLIVLRLRHLNINAI 224
Cdd:COG4886  144 SNNQLTDLPEP-LGNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNNQITDLP-EPLGNLTNLEELDLSGNQLTDL 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 225 rdysfkrlyrlkvleishwpyldtmtPNCLYGL-NLTSLSITHCNLTAVPYLAvrHLVYLRFLNLSYNPIGTIEGSMlhe 303
Cdd:COG4886  221 --------------------------PEPLANLtNLETLDLSNNQLTDLPELG--NLTNLEELDLSNNQLTDLPPLA--- 269
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564363844 304 llrlqeiqlvggqlavvepyafrGLNYLRVLNVSGNQLTTLEESAFHSVGNLETLILDSNPL 365
Cdd:COG4886  270 -----------------------NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLL 308
PCC super family cl28216
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
335-415 2.46e-06

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: 50.85  E-value: 2.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844   335 NVSGNQLTTLEESAFHSVGNLETLILDSNPLACDCRLLWVFRRRWRLNFNRQQP---TCATPEFVQGKEFKDFPdvLLP- 410
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPeaaLCAGPGALAGQPLLGIP--LLDs 78

                   ....*....
gi 564363844   411 ----NYFTC 415
Cdd:TIGR00864   79 gcdeEYVAC 87
LRRNT smart00013
Leucine rich repeat N-terminal domain;
35-69 7.63e-03

Leucine rich repeat N-terminal domain;


:

Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 34.22  E-value: 7.63e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 564363844    35 GCPPRCECSaqDRAVLCHRKRFVAVPEGIPTETRL 69
Cdd:smart00013   1 ACPAPCNCS--GTAVDCSGRGLTEVPLDLPPDTTL 33
 
Name Accession Description Interval E-value
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
417-508 3.06e-54

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. 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 Lingo-1 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: 409561  Cd Length: 92  Bit Score: 179.51  E-value: 3.06e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 417 RAHIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANA 496
Cdd:cd20969    1 RAAIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANA 80
                         90
                 ....*....|..
gi 564363844 497 GGNDSMPAHLHV 508
Cdd:cd20969   81 GGNDSMPAHLHV 92
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
65-365 2.16e-23

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 103.09  E-value: 2.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  65 TETRLLDLGKNRIKTLNQDEFASFPHLEELELNENivsavepGAFNNLFNLRTLGLRSNRLKLIPLGvFTGLSNLTKLDI 144
Cdd:COG4886   72 LLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPEE-LANLTNLKELDL 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 145 SENKIVILLDYmFQDLYNLKSLEVGDNDLVYIShRAFSGLNSLEQLTLEKCNLTSIPtEALSHLHGLIVLRLRHLNINAI 224
Cdd:COG4886  144 SNNQLTDLPEP-LGNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNNQITDLP-EPLGNLTNLEELDLSGNQLTDL 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 225 rdysfkrlyrlkvleishwpyldtmtPNCLYGL-NLTSLSITHCNLTAVPYLAvrHLVYLRFLNLSYNPIGTIEGSMlhe 303
Cdd:COG4886  221 --------------------------PEPLANLtNLETLDLSNNQLTDLPELG--NLTNLEELDLSNNQLTDLPPLA--- 269
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564363844 304 llrlqeiqlvggqlavvepyafrGLNYLRVLNVSGNQLTTLEESAFHSVGNLETLILDSNPL 365
Cdd:COG4886  270 -----------------------NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLL 308
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
426-508 8.93e-15

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: 69.84  E-value: 8.93e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844   426 QQVFVDEGHTVQFVCRADGDPPPAILWLspRKHLVSAKSNGRLTVFPDG---TLEVRYAQVQDNGTYLCIAANAGGNDSM 502
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWY--KQGGKLLAESGRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSASS 79

                   ....*.
gi 564363844   503 PAHLHV 508
Cdd:smart00410  80 GTTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
426-495 2.42e-13

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 65.66  E-value: 2.42e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  426 QQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAAN 495
Cdd:pfam13927   9 SSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
LRR_8 pfam13855
Leucine rich repeat;
114-173 8.05e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 60.62  E-value: 8.05e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  114 NLRTLGLRSNRLKLIPLGVFTGLSNLTKLDISENKIVILLDYMFQDLYNLKSLEVGDNDL 173
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
184-365 7.26e-11

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 62.11  E-value: 7.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 184 LNSLEQLTLEKCNLTSIptEALSHLHGLIVLRLRHLNINAIRDysfkrlyrlkvleishwpyLDTMTpnclyglNLTSLS 263
Cdd:cd21340    1 LKRITHLYLNDKNITKI--DNLSLCKNLKVLYLYDNKITKIEN-------------------LEFLT-------NLTHLY 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 264 ITHCNLTAVPYLAvrHLVYLRFLNLSYNPIGTIEGsmLHELLRLQEIQLVGGQLAVVEPYAF--RGLNY----LRVLNVS 337
Cdd:cd21340   53 LQNNQIEKIENLE--NLVNLKKLYLGGNRISVVEG--LENLTNLEELHIENQRLPPGEKLTFdpRSLAAlsnsLRVLNIS 128
                        170       180
                 ....*....|....*....|....*...
gi 564363844 338 GNQLTTLEEsaFHSVGNLETLILDSNPL 365
Cdd:cd21340  129 GNNIDSLEP--LAPLRNLEQLDASNNQI 154
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
70-384 9.53e-11

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 64.87  E-value: 9.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  70 LDL-GKNRIKTLNQDEFaSFPHLEELELNENIVSAVEPGA-FNNLFNLRTLGLRSNRLK-LIPLGvftGLSNLTKLDISE 146
Cdd:PLN00113  74 IDLsGKNISGKISSAIF-RLPYIQTINLSNNQLSGPIPDDiFTTSSSLRYLNLSNNNFTgSIPRG---SIPNLETLDLSN 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 147 NkivILLDYMFQDL---YNLKSLEVGDNDLVYISHRAFSGLNSLEQLTLEKCNLT-SIPTEaLSHLHGLIVLRLRHLNIN 222
Cdd:PLN00113 150 N---MLSGEIPNDIgsfSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVgQIPRE-LGQMKSLKWIYLGYNNLS 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 223 AIRDYSFKRLYRLKVLEISH--------------------WPYLDTMT---PNCLYGL-NLTSLSITHCNLTA-VPYLaV 277
Cdd:PLN00113 226 GEIPYEIGGLTSLNHLDLVYnnltgpipsslgnlknlqylFLYQNKLSgpiPPSIFSLqKLISLDLSDNSLSGeIPEL-V 304
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 278 RHLVYLRFLNL-SYNPIGTIEGSmLHELLRLQEIQLVGGQLAVVEPYAFRGLNYLRVLNVSGNQLTTLEESAFHSVGNLE 356
Cdd:PLN00113 305 IQLQNLEILHLfSNNFTGKIPVA-LTSLPRLQVLQLWSNKFSGEIPKNLGKHNNLTVLDLSTNNLTGEIPEGLCSSGNLF 383
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 564363844 357 TLILDSNPLA-------CDCRLLwvfrRRWRLNFN 384
Cdd:PLN00113 384 KLILFSNSLEgeipkslGACRSL----RRVRLQDN 414
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
335-415 2.46e-06

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: 50.85  E-value: 2.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844   335 NVSGNQLTTLEESAFHSVGNLETLILDSNPLACDCRLLWVFRRRWRLNFNRQQP---TCATPEFVQGKEFKDFPdvLLP- 410
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPeaaLCAGPGALAGQPLLGIP--LLDs 78

                   ....*....
gi 564363844   411 ----NYFTC 415
Cdd:TIGR00864   79 gcdeEYVAC 87
LRRCT smart00082
Leucine rich repeat C-terminal domain;
363-399 1.60e-03

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 36.64  E-value: 1.60e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 564363844   363 NPLACDCRLLWvFRRRWRLNF---NRQQPTCATPEFVQGK 399
Cdd:smart00082   1 NPFICDCELRW-LLRWLQANEhlqDPVDLRCASPSSLRGP 39
LRRNT smart00013
Leucine rich repeat N-terminal domain;
35-69 7.63e-03

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 34.22  E-value: 7.63e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 564363844    35 GCPPRCECSaqDRAVLCHRKRFVAVPEGIPTETRL 69
Cdd:smart00013   1 ACPAPCNCS--GTAVDCSGRGLTEVPLDLPPDTTL 33
 
Name Accession Description Interval E-value
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
417-508 3.06e-54

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. 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 Lingo-1 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: 409561  Cd Length: 92  Bit Score: 179.51  E-value: 3.06e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 417 RAHIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANA 496
Cdd:cd20969    1 RAAIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANA 80
                         90
                 ....*....|..
gi 564363844 497 GGNDSMPAHLHV 508
Cdd:cd20969   81 GGNDSMPAHLHV 92
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
65-365 2.16e-23

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 103.09  E-value: 2.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  65 TETRLLDLGKNRIKTLNQDEFASFPHLEELELNENivsavepGAFNNLFNLRTLGLRSNRLKLIPLGvFTGLSNLTKLDI 144
Cdd:COG4886   72 LLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPEE-LANLTNLKELDL 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 145 SENKIVILLDYmFQDLYNLKSLEVGDNDLVYIShRAFSGLNSLEQLTLEKCNLTSIPtEALSHLHGLIVLRLRHLNINAI 224
Cdd:COG4886  144 SNNQLTDLPEP-LGNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNNQITDLP-EPLGNLTNLEELDLSGNQLTDL 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 225 rdysfkrlyrlkvleishwpyldtmtPNCLYGL-NLTSLSITHCNLTAVPYLAvrHLVYLRFLNLSYNPIGTIEGSMlhe 303
Cdd:COG4886  221 --------------------------PEPLANLtNLETLDLSNNQLTDLPELG--NLTNLEELDLSNNQLTDLPPLA--- 269
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564363844 304 llrlqeiqlvggqlavvepyafrGLNYLRVLNVSGNQLTTLEESAFHSVGNLETLILDSNPL 365
Cdd:COG4886  270 -----------------------NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLL 308
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
56-365 1.49e-21

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 97.31  E-value: 1.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  56 FVAVPEGIPTETRLLDLGKNRIKTLNQDEFASFPHLEELELNENIVSAVEPGAFNNLFNLRTLGLRSNRLkliplgvFTG 135
Cdd:COG4886   39 LLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEE-------LSN 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 136 LSNLTKLDISENKIViLLDYMFQDLYNLKSLEVGDNDLVYIShRAFSGLNSLEQLTLEKCNLTSIPtEALSHLHGLIVLR 215
Cdd:COG4886  112 LTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQLTDLP-EPLGNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELD 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 216 LRHLNINAIrdysfkrlyrlkvleishwpyldtmtPNCLYGL-NLTSLSITHCNLTAVPyLAVRHLVYLRFLNLSYNPIG 294
Cdd:COG4886  189 LSNNQITDL--------------------------PEPLGNLtNLEELDLSGNQLTDLP-EPLANLTNLETLDLSNNQLT 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564363844 295 TIEgsmlhellrlqeiqlvggqlavvepyAFRGLNYLRVLNVSGNQLTTLEESAfhSVGNLETLILDSNPL 365
Cdd:COG4886  242 DLP--------------------------ELGNLTNLEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQL 284
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
69-365 1.65e-19

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 91.15  E-value: 1.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  69 LLDLGKNRIKTLNQDEFASFPHLEELELNENIVSAVEPGAFNNLFNLRTLGLRSNRLKLIPLGVFTGLSN--LTKLDISE 146
Cdd:COG4886    2 LLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLllLLLLSLLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 147 NKIVILLDYMFQDLYNLKSLEVGDNDlvyishrAFSGLNSLEQLTLEKCNLTSIPtEALSHLHGLIVLRLRHLNINAIRD 226
Cdd:COG4886   82 LSLLLLGLTDLGDLTNLTELDLSGNE-------ELSNLTNLESLDLSGNQLTDLP-EELANLTNLKELDLSNNQLTDLPE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 227 ysfkrlyrlkvlEISHWPyldtmtpnclyglNLTSLSITHCNLTAVPyLAVRHLVYLRFLNLSYNPIGTIEGSmLHELLR 306
Cdd:COG4886  154 ------------PLGNLT-------------NLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNNQITDLPEP-LGNLTN 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564363844 307 LQEIQLVGGQLAVVePYAFRGLNYLRVLNVSGNQLTTLEEsaFHSVGNLETLILDSNPL 365
Cdd:COG4886  207 LEELDLSGNQLTDL-PEPLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQL 262
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
423-508 2.81e-19

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: 82.52  E-value: 2.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 423 RKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSngRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSM 502
Cdd:cd05764    5 RHTHELRVLEGQRATLRCKARGDPEPAIHWISPEGKLISNSS--RTLVYDNGTLDILITTVKDTGAFTCIASNPAGEATA 82

                 ....*.
gi 564363844 503 PAHLHV 508
Cdd:cd05764   83 RVELHI 88
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
426-508 8.93e-15

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: 69.84  E-value: 8.93e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844   426 QQVFVDEGHTVQFVCRADGDPPPAILWLspRKHLVSAKSNGRLTVFPDG---TLEVRYAQVQDNGTYLCIAANAGGNDSM 502
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWY--KQGGKLLAESGRFSVSRSGstsTLTISNVTPEDSGTYTCAATNSSGSASS 79

                   ....*.
gi 564363844   503 PAHLHV 508
Cdd:smart00410  80 GTTLTV 85
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
420-508 1.59e-13

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: 66.37  E-value: 1.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 420 IRDRKAQQVfVDEGHTVQFVCRADGDPPPAILWLSpRKHLVSAKsNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGN 499
Cdd:cd20952    2 ILQGPQNQT-VAVGGTVVLNCQATGEPVPTISWLK-DGVPLLGK-DERITTLENGSLQIKGAEKSDTGEYTCVALNLSGE 78

                 ....*....
gi 564363844 500 DSMPAHLHV 508
Cdd:cd20952   79 ATWSAVLDV 87
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
426-495 2.42e-13

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 65.66  E-value: 2.42e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  426 QQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAAN 495
Cdd:pfam13927   9 SSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
I-set pfam07679
Immunoglobulin I-set domain;
422-508 1.40e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.82  E-value: 1.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  422 DRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLvsaKSNGRLTVFPDG---TLEVRYAQVQDNGTYLCIAANAGG 498
Cdd:pfam07679   4 TQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPL---RSSDRFKVTYEGgtyTLTISNVQPDDSGKYTCVATNSAG 80
                          90
                  ....*....|
gi 564363844  499 NDSMPAHLHV 508
Cdd:pfam07679  81 EAEASAELTV 90
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
420-508 3.82e-12

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: 62.41  E-value: 3.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 420 IRDRKAQQVFVDEghTVQFVCRADGDPPPAILWLSPRKHLvsakSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGN 499
Cdd:cd05725    1 VKRPQNQVVLVDD--SAEFQCEVGGDPVPTVRWRKEDGEL----PKGRYEILDDHSLKIRKVTAGDMGSYTCVAENMVGK 74

                 ....*....
gi 564363844 500 DSMPAHLHV 508
Cdd:cd05725   75 IEASATLTV 83
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
436-501 7.84e-12

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: 60.81  E-value: 7.84e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564363844 436 VQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAAN-AGGNDS 501
Cdd:cd00096    1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNsAGGSAS 67
LRR_8 pfam13855
Leucine rich repeat;
114-173 8.05e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 60.62  E-value: 8.05e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  114 NLRTLGLRSNRLKLIPLGVFTGLSNLTKLDISENKIVILLDYMFQDLYNLKSLEVGDNDL 173
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
420-509 2.32e-11

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: 60.41  E-value: 2.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 420 IRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAAN-AGG 498
Cdd:cd05738    1 IIDMGPQLKVVEKARTATMLCAASGNPDPEISWFKDFLPVDTATSNGRIKQLRSGALQIENSEESDQGKYECVATNsAGT 80
                         90
                 ....*....|.
gi 564363844 499 NDSMPAHLHVR 509
Cdd:cd05738   81 RYSAPANLYVR 91
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
424-508 5.89e-11

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth 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: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 59.20  E-value: 5.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 424 KAQQVFVDEGHTVQFVCRADGDPPPAILW--------LSPRKhlvSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAAN 495
Cdd:cd05726    5 KPRDQVVALGRTVTFQCETKGNPQPAIFWqkegsqnlLFPYQ---PPQPSSRFSVSPTGDLTITNVQRSDVGYYICQALN 81
                         90
                 ....*....|...
gi 564363844 496 AGGNDSMPAHLHV 508
Cdd:cd05726   82 VAGSILAKAQLEV 94
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
184-365 7.26e-11

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 62.11  E-value: 7.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 184 LNSLEQLTLEKCNLTSIptEALSHLHGLIVLRLRHLNINAIRDysfkrlyrlkvleishwpyLDTMTpnclyglNLTSLS 263
Cdd:cd21340    1 LKRITHLYLNDKNITKI--DNLSLCKNLKVLYLYDNKITKIEN-------------------LEFLT-------NLTHLY 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 264 ITHCNLTAVPYLAvrHLVYLRFLNLSYNPIGTIEGsmLHELLRLQEIQLVGGQLAVVEPYAF--RGLNY----LRVLNVS 337
Cdd:cd21340   53 LQNNQIEKIENLE--NLVNLKKLYLGGNRISVVEG--LENLTNLEELHIENQRLPPGEKLTFdpRSLAAlsnsLRVLNIS 128
                        170       180
                 ....*....|....*....|....*...
gi 564363844 338 GNQLTTLEEsaFHSVGNLETLILDSNPL 365
Cdd:cd21340  129 GNNIDSLEP--LAPLRNLEQLDASNNQI 154
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
70-384 9.53e-11

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 64.87  E-value: 9.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  70 LDL-GKNRIKTLNQDEFaSFPHLEELELNENIVSAVEPGA-FNNLFNLRTLGLRSNRLK-LIPLGvftGLSNLTKLDISE 146
Cdd:PLN00113  74 IDLsGKNISGKISSAIF-RLPYIQTINLSNNQLSGPIPDDiFTTSSSLRYLNLSNNNFTgSIPRG---SIPNLETLDLSN 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 147 NkivILLDYMFQDL---YNLKSLEVGDNDLVYISHRAFSGLNSLEQLTLEKCNLT-SIPTEaLSHLHGLIVLRLRHLNIN 222
Cdd:PLN00113 150 N---MLSGEIPNDIgsfSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVgQIPRE-LGQMKSLKWIYLGYNNLS 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 223 AIRDYSFKRLYRLKVLEISH--------------------WPYLDTMT---PNCLYGL-NLTSLSITHCNLTA-VPYLaV 277
Cdd:PLN00113 226 GEIPYEIGGLTSLNHLDLVYnnltgpipsslgnlknlqylFLYQNKLSgpiPPSIFSLqKLISLDLSDNSLSGeIPEL-V 304
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 278 RHLVYLRFLNL-SYNPIGTIEGSmLHELLRLQEIQLVGGQLAVVEPYAFRGLNYLRVLNVSGNQLTTLEESAFHSVGNLE 356
Cdd:PLN00113 305 IQLQNLEILHLfSNNFTGKIPVA-LTSLPRLQVLQLWSNKFSGEIPKNLGKHNNLTVLDLSTNNLTGEIPEGLCSSGNLF 383
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 564363844 357 TLILDSNPLA-------CDCRLLwvfrRRWRLNFN 384
Cdd:PLN00113 384 KLILFSNSLEgeipkslGACRSL----RRVRLQDN 414
LRR_8 pfam13855
Leucine rich repeat;
89-149 9.73e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 57.53  E-value: 9.73e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564363844   89 PHLEELELNENIVSAVEPGAFNNLFNLRTLGLRSNRLKLIPLGVFTGLSNLTKLDISENKI 149
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
306-365 1.73e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 56.76  E-value: 1.73e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  306 RLQEIQLVGGQLAVVEPYAFRGLNYLRVLNVSGNQLTTLEESAFHSVGNLETLILDSNPL 365
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
427-508 4.04e-10

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: 56.63  E-value: 4.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 427 QVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSakSNGRLTvFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHL 506
Cdd:cd20978   10 NVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQG--PMERAT-VEDGTLTIINVQPEDTGYYGCVATNEIGDIYTETLL 86

                 ..
gi 564363844 507 HV 508
Cdd:cd20978   87 HV 88
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
428-508 4.79e-10

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: 56.75  E-value: 4.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 428 VFVDEGHTVQFVCRADGDPPPAILWLspRKHLVSAKSNGRLTVFPDGT-LEVRYAQVQDNGTYLCIAAN-AGGNDSMPAH 505
Cdd:cd20970   12 VTAREGENATFMCRAEGSPEPEISWT--RNGNLIIEFNTRYIVRENGTtLTIRNIRRSDMGIYLCIASNgVPGSVEKRIT 89

                 ...
gi 564363844 506 LHV 508
Cdd:cd20970   90 LQV 92
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
83-241 5.18e-10

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 59.80  E-value: 5.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  83 DEFASFPHLEELELNENIVSAVEpgAFNNLFNLRTLGLRSNRLKLIPlgVFTGLSNLTKLDISENKIVILldymfQDLYN 162
Cdd:cd21340   18 DNLSLCKNLKVLYLYDNKITKIE--NLEFLTNLTHLYLQNNQIEKIE--NLENLVNLKKLYLGGNRISVV-----EGLEN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 163 LKSLEvgdnDLvYISH-------------RAFSGL-NSLEQLTLEKCNLTSIptEALSHLHGLIVLRLRHLNINAIRD-- 226
Cdd:cd21340   89 LTNLE----EL-HIENqrlppgekltfdpRSLAALsNSLRVLNISGNNIDSL--EPLAPLRNLEQLDASNNQISDLEEll 161
                        170
                 ....*....|....*
gi 564363844 227 YSFKRLYRLKVLEIS 241
Cdd:cd21340  162 DLLSSWPSLRELDLT 176
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
432-508 6.87e-10

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: 55.71  E-value: 6.87e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564363844 432 EGHTVQFVCRADGDPPPAILWLSPRKHLvsaKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 508
Cdd:cd05745    1 EGQTVDFLCEAQGYPQPVIAWTKGGSQL---SVDRRHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
424-498 2.60e-09

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; 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 and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. 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: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 54.67  E-value: 2.60e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564363844 424 KAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGG 498
Cdd:cd05747    9 KPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEG 83
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
436-501 4.08e-09

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: 53.34  E-value: 4.08e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564363844 436 VQFVCRADGDPPPAILWlspRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDS 501
Cdd:cd05746    1 VQIPCSAQGDPEPTITW---NKDGVQVTESGKFHISPEGYLAIRDVGVADQGRYECVARNTIGYAS 63
IgI_NCAM-1 cd05869
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members ...
436-508 1.11e-08

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule 1(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. 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: 143277 [Multi-domain]  Cd Length: 97  Bit Score: 53.06  E-value: 1.11e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564363844 436 VQFVCRADGDPPPAILWLSPRKHLVSAKS--NGRLTVFPD---GTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 508
Cdd:cd05869   20 ITLTCEASGDPIPSITWRTSTRNISSEEKtlDGHIVVRSHarvSSLTLKYIQYTDAGEYLCTASNTIGQDSQSMYLEV 97
LRR_8 pfam13855
Leucine rich repeat;
68-125 1.32e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 51.37  E-value: 1.32e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564363844   68 RLLDLGKNRIKTLNQDEFASFPHLEELELNENIVSAVEPGAFNNLFNLRTLGLRSNRL 125
Cdd:pfam13855   4 RSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
433-508 2.03e-08

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: 52.11  E-value: 2.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 433 GHTVQFVCRADGDPPPAILWLSPR-----KHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGND-SMPAHL 506
Cdd:cd05734   16 GKAVVLNCSADGYPPPTIVWKHSKgsgvpQFQHIVPLNGRIQLLSNGSLLIKHVLEEDSGYYLCKVSNDVGADiSKSMYL 95

                 ..
gi 564363844 507 HV 508
Cdd:cd05734   96 TV 97
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
440-508 4.32e-08

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: 50.92  E-value: 4.32e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564363844 440 CRADGDPPPAILWlspRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 508
Cdd:cd04969   24 CKPKASPKPTISW---SKGTELLTNSSRICILPDGSLKIKNVTKSDEGKYTCFAVNFFGKANSTGSLSV 89
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
430-498 8.74e-08

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: 50.24  E-value: 8.74e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564363844 430 VDEGHTVQFVCRADGDPPPAILW--LSPRKHLVSAKSN---GRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGG 498
Cdd:cd05765   12 VKVGETASFHCDVTGRPQPEITWekQVPGKENLIMRPNhvrGNVVVTNIGQLVIYNAQPQDAGLYTCTARNSGG 85
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
432-508 2.11e-07

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: 49.06  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 432 EGHTVQFVCRADGDPPPAILW-LSPRKHLVSAKS-NGRLTVFPD---GTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHL 506
Cdd:cd05732   15 ELEQITLTCEAEGDPIPEITWrRATRGISFEEGDlDGRIVVRGHarvSSLTLKDVQLTDAGRYDCEASNRIGGDQQSMYL 94

                 ..
gi 564363844 507 HV 508
Cdd:cd05732   95 EV 96
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
75-188 2.16e-07

BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 49.85  E-value: 2.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844   75 NRIKTLNQDEFASFPHLEELELNENIVSaVEPGAFNNlFNLRTLGLRSNrLKLIPLGVFTGLSNLTKLDISENkIVILLD 154
Cdd:pfam13306  20 SSLTSIGEYAFSNCTSLKSITLPSSLTS-IGSYAFYN-CSLTSITIPSS-LTSIGEYAFSNCSNLKSITLPSN-LTSIGS 95
                          90       100       110
                  ....*....|....*....|....*....|....
gi 564363844  155 YMFQDLyNLKSLEVGDNdLVYISHRAFSGLNSLE 188
Cdd:pfam13306  96 YAFSNC-SLKSITIPSS-VTTIGSYAFSNCSNLK 127
IgI_Perlecan_like cd05754
Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of ...
426-507 3.01e-07

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. 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: 409412  Cd Length: 85  Bit Score: 48.32  E-value: 3.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 426 QQVFVDEGHTVQFVCRA-DGDPPPAILWlsprkhlvsAKSNGRLtvfP------DGTLEVRYAQVQDNGTYLCIAANAGG 498
Cdd:cd05754    9 RSQEVRPGADVSFICRAkSKSPAYTLVW---------TRVNGTL---PsramdfNGILTIRNVQLSDAGTYVCTGSNMLD 76

                 ....*....
gi 564363844 499 NDSMPAHLH 507
Cdd:cd05754   77 TDEATATLY 85
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
428-508 3.81e-07

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: 48.70  E-value: 3.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 428 VFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRL--TVFPDGTL------EVRYAQvQDNGTYLCIAANAGGN 499
Cdd:cd07693   10 LIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKDDPRShrIVLPSGSLfflrvvHGRKGR-SDEGVYVCVAHNSLGE 88
                         90
                 ....*....|
gi 564363844 500 D-SMPAHLHV 508
Cdd:cd07693   89 AvSRNASLEV 98
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
423-509 5.57e-07

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: 47.83  E-value: 5.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 423 RKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDgTLEVRYAQVQDNGTYLCIAANAGGNDSM 502
Cdd:cd04978    4 IEPPSLVLSPGETGELICEAEGNPQPTITWRLNGVPIEPAPEDMRRTVDGR-TLIFSNLQPNDTAVYQCNASNVHGYLLA 82

                 ....*..
gi 564363844 503 PAHLHVR 509
Cdd:cd04978   83 NAFLHVL 89
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
423-508 6.18e-07

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: 47.58  E-value: 6.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 423 RKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSA-----KSNGRLTvfpdgTLEVRYAQVQDNGTYLCIAANAG 497
Cdd:cd20972    6 QKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSpdiqiHQEGDLH-----SLIIAEAFEEDTGRYSCLATNSV 80
                         90
                 ....*....|.
gi 564363844 498 GNDSMPAHLHV 508
Cdd:cd20972   81 GSDTTSAEIFV 91
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
433-498 2.12e-06

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 45.94  E-value: 2.12e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564363844 433 GHTVQFVCRADGDPPPAILWL--------SPRKHLVSakSNGRltvfpdGTLEVRYAQVQDNGTYLCIAANAGG 498
Cdd:cd05743    1 GETVEFTCVATGVPTPIINWRlnwghvpdSARVSITS--EGGY------GTLTIRDVKESDQGAYTCEAINTRG 66
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
430-497 2.33e-06

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third 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. 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. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 45.99  E-value: 2.33e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564363844 430 VDEGHTVQFVCRADGDPPPAILWLSPRKHLVsakSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAG 497
Cdd:cd20957   13 VDFGRTAVFNCSVTGNPIHTVLWMKDGKPLG---HSSRVQILSEDVLVIPSVKREDKGMYQCFVRNDG 77
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
335-415 2.46e-06

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: 50.85  E-value: 2.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844   335 NVSGNQLTTLEESAFHSVGNLETLILDSNPLACDCRLLWVFRRRWRLNFNRQQP---TCATPEFVQGKEFKDFPdvLLP- 410
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPeaaLCAGPGALAGQPLLGIP--LLDs 78

                   ....*....
gi 564363844   411 ----NYFTC 415
Cdd:TIGR00864   79 gcdeEYVAC 87
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
104-236 2.49e-06

BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 46.77  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  104 VEPGAFNNLfNLRTLGLRSNrLKLIPLGVFTGLSNLTKLDISENkIVILLDYMFQDLyNLKSLEVGDNdLVYISHRAFSG 183
Cdd:pfam13306   3 IGSYAFYNC-SLTSITIPSS-LTSIGEYAFSNCTSLKSITLPSS-LTSIGSYAFYNC-SLTSITIPSS-LTSIGEYAFSN 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564363844  184 LNSLEQLTLEKcNLTSIPTEALSHLHglivlrLRHLNINA----IRDYSFKRLYRLK 236
Cdd:pfam13306  78 CSNLKSITLPS-NLTSIGSYAFSNCS------LKSITIPSsvttIGSYAFSNCSNLK 127
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
430-508 2.61e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; 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. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 46.00  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 430 VDEGHTVQFVCRADGDPPPAILWLSPRKHLvsaKSNGRLtvfpdGTLEVRYAQVQ---------DNGTYLCIAANAGGND 500
Cdd:cd05857   16 VPAANTVKFRCPAAGNPTPTMRWLKNGKEF---KQEHRI-----GGYKVRNQHWSlimesvvpsDKGNYTCVVENEYGSI 87

                 ....*...
gi 564363844 501 SMPAHLHV 508
Cdd:cd05857   88 NHTYHLDV 95
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
60-260 2.91e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.93  E-value: 2.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  60 PEGIPTETRL--LDLGKNRIKTLnqDEFASFPHLEELELNENIVSAVEPGAfnNLFNLRTLGLRSNRLKLIPLGVFTGLS 137
Cdd:COG4886  221 PEPLANLTNLetLDLSNNQLTDL--PELGNLTNLEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQLTDLKLKELELLL 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 138 NLTKLDISENKIVILLdymfqDLYNLKSLEVGDNDLVYISHRAFSGLNSLEQLTLEKCNLTSIPTEALSHLHGLIVLRLR 217
Cdd:COG4886  297 GLNSLLLLLLLLNLLE-----LLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGL 371
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 564363844 218 HLNINAIRDYSFKRLYRLKVLEISHWPYLDTMTPNCLYGLNLT 260
Cdd:COG4886  372 LGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAVNTE 414
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
426-502 3.82e-06

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: 45.26  E-value: 3.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  426 QQVFVDEGHTVQFVCRA-DGDPPPAILWLSPRKHLVSA----KSNGRLTVFpdgTLEVRYAQVQDNGTYLCIAANAGGND 500
Cdd:pfam00047   4 PTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESlkvkHDNGRTTQS---SLLISNVTKEDAGTYTCVVNNPGGSA 80

                  ..
gi 564363844  501 SM 502
Cdd:pfam00047  81 TL 82
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
70-379 4.14e-06

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: 48.89  E-value: 4.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  70 LDLGKNRIKTLNQDE-FASFPHLEELELNENIVSAVE-PGAFNNL---FNLRTLGLRSNRLKLIPLGV------FTGLSN 138
Cdd:cd00116    3 LSLKGELLKTERATElLPKLLCLQVLRLEGNTLGEEAaKALASALrpqPSLKELCLSLNETGRIPRGLqsllqgLTKGCG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 139 LTKLDISENKIVILLDYMFQDLYNLKSLEVGD--NDLVYISHRAFS--GLNS----LEQLTLEKCNLTSIPTEALSHLhg 210
Cdd:cd00116   83 LQELDLSDNALGPDGCGVLESLLRSSSLQELKlnNNGLGDRGLRLLakGLKDlppaLEKLVLGRNRLEGASCEALAKA-- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 211 LIVLR-LRHLNI--NAIRDYSFKRLYRlkvleishwpyldTMTPNC-LYGLNLTSLSITHCNLTAVPyLAVRHLVYLRFL 286
Cdd:cd00116  161 LRANRdLKELNLanNGIGDAGIRALAE-------------GLKANCnLEVLDLNNNGLTDEGASALA-ETLASLKSLEVL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 287 NLSYNPIG-----TIEGSMLHELLRLQEIQLVG------GQLAVVEPYAFRGLnyLRVLNVSGNQLTtlEESAFhsvgnL 355
Cdd:cd00116  227 NLGDNNLTdagaaALASALLSPNISLLTLSLSCnditddGAKDLAEVLAEKES--LLELDLRGNKFG--EEGAQ-----L 297
                        330       340
                 ....*....|....*....|....
gi 564363844 356 ETLILDSNplACDCRLLWVFRRRW 379
Cdd:cd00116  298 LAESLLEP--GNELESLWVKDDSF 319
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
433-508 5.40e-06

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: 44.85  E-value: 5.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 433 GHTVQFVCRADGDPPPAILW------LSPRKHLVSAksngrltvfpDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHL 506
Cdd:cd04968   16 GQTVTLECFALGNPVPQIKWrkvdgsPSSQWEITTS----------EPVLEIPNVQFEDEGTYECEAENSRGKDTVQGRI 85

                 ..
gi 564363844 507 HV 508
Cdd:cd04968   86 IV 87
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
432-508 9.68e-06

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. 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: 409474  Cd Length: 92  Bit Score: 44.32  E-value: 9.68e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564363844 432 EGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGT--LEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 508
Cdd:cd05893   14 EGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRDLDGTcsLHTTASTLDDDGNYTIMAANPQGRISCTGRLMV 92
IgI_1_NCAM-1_like cd04977
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar ...
427-501 1.01e-05

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, 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 of neural cell adhesion molecule NCAM-1. NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-nonNCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. 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). 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: 409366  Cd Length: 95  Bit Score: 44.55  E-value: 1.01e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564363844 427 QVFVDEGHTVQFVCRADGDPPpAILWLSPRKHLVSAKSNGRLTVFPDG---TLEVRYAQVQDNGTYLCIAANAGGNDS 501
Cdd:cd04977    9 YAEISVGESKFFLCKVSGDAK-NINWVSPNGEKVLTKHGNLKVVNHGSvlsSLTIYNANINDAGIYKCVATNGKGTES 85
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
426-500 1.01e-05

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar proteins; The members here are composed of the immunoglobulin (Ig) variable domain of the alpha chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta polypeptide chains with variable (V) and constant (C) regions. This group represents the variable domain of the alpha chain of TCRs and also includes the variable domain of delta chains of TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409372 [Multi-domain]  Cd Length: 109  Bit Score: 44.57  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 426 QQVFVDEGHTVQFVCRADGDPPPAILWLS--PRKHLVS---------AKSNGRLTVFPD-----GTLEVRYAQVQDNGTY 489
Cdd:cd04983    6 QSLSVQEGENVTLNCNYSTSTFYYLFWYRqyPGQGPQFliyissdsgNKKKGRFSATLDksrksSSLHISAAQLSDSAVY 85
                         90
                 ....*....|.
gi 564363844 490 LCIAANAGGND 500
Cdd:cd04983   86 FCALSESGGTG 96
LRR_5 pfam13306
BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich ...
162-276 1.14e-05

BspA type Leucine rich repeat region (6 copies); This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.


Pssm-ID: 463839 [Multi-domain]  Cd Length: 127  Bit Score: 45.23  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  162 NLKSLEVGDNdLVYISHRAFSGLNSLEQLTLEKcNLTSIPTEALSHLHglivlrLRHLNINA----IRDYSFKRLYRLKV 237
Cdd:pfam13306  12 SLTSITIPSS-LTSIGEYAFSNCTSLKSITLPS-SLTSIGSYAFYNCS------LTSITIPSsltsIGEYAFSNCSNLKS 83
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 564363844  238 LEIShwPYLDTMTPNCLYGLNLTSLSIThCNLTAVPYLA 276
Cdd:pfam13306  84 ITLP--SNLTSIGSYAFSNCSLKSITIP-SSVTTIGSYA 119
LRR_8 pfam13855
Leucine rich repeat;
162-218 1.18e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 43.28  E-value: 1.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564363844  162 NLKSLEVGDNDLVYISHRAFSGLNSLEQLTLEKCNLTSIPTEALSHLHGLIVLRLRH 218
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSG 58
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
423-508 1.33e-05

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: 44.02  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 423 RKAQQVFVDEGHTVQFVCRADGDPPPAILWLSpRKHLVSAKSNGRLTVFPDG--TLEVRYAQVQDNGTYLCIAANAGGND 500
Cdd:cd05744    5 QAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQL-NGKPVRPDSAHKMLVRENGrhSLIIEPVTKRDAGIYTCIARNRAGEN 83

                 ....*...
gi 564363844 501 SMPAHLHV 508
Cdd:cd05744   84 SFNAELVV 91
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
433-509 1.35e-05

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


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 43.71  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 433 GHTVQFVCRADGDPPPAILWLSPRKHLvsaKSNGRLTVFPDGTLEVRyaQVQ---DNGTYLCIAANAGGNdSMPAHLHVR 509
Cdd:cd20958   15 GQTLRLHCPVAGYPISSITWEKDGRRL---PLNHRQRVFPNGTLVIE--NVQrssDEGEYTCTARNQQGQ-SASRSVFVK 88
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
444-508 1.37e-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: 43.93  E-value: 1.37e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564363844 444 GDPPPAILWLSPRKHLVSakSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAAN-AGGNDSMPAHLHV 508
Cdd:cd05724   24 GHPEPTVSWRKDGQPLNL--DNERVRIVDDGNLLIAEARKSDEGTYKCVATNmVGERESRAARLSV 87
LRR_8 pfam13855
Leucine rich repeat;
283-341 1.73e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 42.51  E-value: 1.73e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564363844  283 LRFLNLSYNPIGTIEGSMLHELLRLQEIQLVGGQLAVVEPYAFRGLNYLRVLNVSGNQL 341
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
425-508 1.75e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 43.15  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  425 AQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLvsaKSNGRLTvfpdgtleVRYAQVQDNGTYLCIAAN-AGGNDSMP 503
Cdd:pfam13895   6 PSPTVVTEGEPVTLTCSAPGNPPPSYTWYKDGSAI---SSSPNFF--------TLSVSAEDSGTYTCVARNgRGGKVSNP 74

                  ....*
gi 564363844  504 AHLHV 508
Cdd:pfam13895  75 VELTV 79
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
430-498 2.21e-05

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: 43.46  E-value: 2.21e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564363844 430 VDEGHTVQFVCRADGDPPPAILWlspRKHLVSA-------KSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGG 498
Cdd:cd20954   13 VAAGQDVMLHCQADGFPTPTVTW---KKATGSTpgeykdlLYDPNVRILPNGTLVFGHVQKENEGHYLCEAKNGIG 85
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
433-498 2.83e-05

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: 42.92  E-value: 2.83e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564363844 433 GHTVQFVCRADGDPPPAILWLsprkhlvsaKSNGRLTVFPDG-------TLEVRYAQVQDNGTYLCIAANAGG 498
Cdd:cd05856   19 GSSVRLKCVASGNPRPDITWL---------KDNKPLTPPEIGenkkkkwTLSLKNLKPEDSGKYTCHVSNRAG 82
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
440-508 3.06e-05

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


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 43.00  E-value: 3.06e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 440 CRADGDPPPAILWLsprKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGND-SMPAHLHV 508
Cdd:cd20968   21 CTTMGNPKPSVSWI---KGDDLIKENNRIAVLESGSLRIHNVQKEDAGQYRCVAKNSLGIAySKPVTIEV 87
IgI_3_FGFR cd04974
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
433-507 3.28e-05

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. 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: 409363  Cd Length: 102  Bit Score: 43.18  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 433 GHTVQFVCRADGDPPPAILWLsprKHLvsaKSNGRlTVFPDG-------------------TLEVRYAQVQDNGTYLCIA 493
Cdd:cd04974   16 GSDVEFHCKVYSDAQPHIQWL---KHV---EVNGS-KYGPDGlpyvtvlkvagvnttgeenTLTISNVTFDDAGEYICLA 88
                         90
                 ....*....|....
gi 564363844 494 ANAGGNDSMPAHLH 507
Cdd:cd04974   89 GNSIGLSFHSAWLT 102
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
423-508 3.66e-05

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: 42.59  E-value: 3.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 423 RKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLvsaKSNGRLTVfPDGTLEVRYAQVQDNGTYLCIAANAGGNDSM 502
Cdd:cd05728    4 KVISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPL---ASENRIEV-EAGDLRITKLSLSDSGMYQCVAENKHGTIYA 79

                 ....*.
gi 564363844 503 PAHLHV 508
Cdd:cd05728   80 SAELAV 85
IgI_2_Dscam cd20953
Second immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
423-508 6.12e-05

Second 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 second immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. 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: 409545  Cd Length: 95  Bit Score: 42.14  E-value: 6.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 423 RKAQQVFVDEGHTVQFVCRADGDPPPAILWL-----SPRKHLVsaKSNGRLTVFpDGTLEVRYAQVQDNGTYLCIAANAG 497
Cdd:cd20953    8 SKSQPLTVSSASSIALLCPAQGYPAPSFRWYkfiegTTRKQAV--VLNDRVKQV-SGTLIIKDAVVEDSGKYLCVVNNSV 84
                         90
                 ....*....|.
gi 564363844 498 GNDSMPAHLHV 508
Cdd:cd20953   85 GGESVETVLTV 95
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
432-508 7.11e-05

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: 41.85  E-value: 7.11e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564363844 432 EGHTVQFVCRADGDPPPAILWLSPRKHLvsAKSNGRLTVFPD-GTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 508
Cdd:cd20976   15 EGQDFVAQCSARGKPVPRITWIRNAQPL--QYAADRSTCEAGvGELHIQDVLPEDHGTYTCLAKNAAGQVSCSAWVTV 90
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
433-508 8.27e-05

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: 41.84  E-value: 8.27e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564363844 433 GHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFP-DGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 508
Cdd:cd05763   14 GSTARLECAATGHPTPQIAWQKDGGTDFPAARERRMHVMPeDDVFFIVDVKIEDTGVYSCTAQNSAGSISANATLTV 90
LRR_8 pfam13855
Leucine rich repeat;
186-242 9.74e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.59  E-value: 9.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564363844  186 SLEQLTLEKCNLTSIPTEALSHLHGLIVLRLRHLNINAIRDYSFKRLYRLKVLEISH 242
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSG 58
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
424-509 9.77e-05

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: 41.55  E-value: 9.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 424 KAQQVFVDEGHTVQFVCRADGDPPPAILWlspRKHLVSAKSNGRLTVfPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMP 503
Cdd:cd05851    7 KFKDTYALKGQNVTLECFALGNPVPVIRW---RKILEPMPATAEISM-SGAVLKIFNIQPEDEGTYECEAENIKGKDKHQ 82

                 ....*.
gi 564363844 504 AHLHVR 509
Cdd:cd05851   83 ARVYVQ 88
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
37-210 1.05e-04

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 45.46  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  37 PPRCECSAQDRAVLCHRkrFVAVPEGIPTETRLLDLGKNRIKTLNQDEFASFPHLEELELNENIVSAVEPgafnnlFNLR 116
Cdd:PRK15370 257 PERLPSALQSLDLFHNK--ISCLPENLPEELRYLSVYDNSIRTLPAHLPSGITHLNVQSNSLTALPETLP------PGLK 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 117 TLGLRSNRLKLIPLGVFTGLSNltkLDISENKIVILLDYMFQDLYNLkslevgdndlvYISHRAFSGL-----NSLEQLT 191
Cdd:PRK15370 329 TLEAGENALTSLPASLPPELQV---LDVSKNQITVLPETLPPTITTL-----------DVSRNALTNLpenlpAALQIMQ 394
                        170
                 ....*....|....*....
gi 564363844 192 LEKCNLTSIPtEALSHLHG 210
Cdd:PRK15370 395 ASRNNLVRLP-ESLPHFRG 412
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
70-183 1.32e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 45.22  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844  70 LDLGKNRIKTLNQDEFASFPHLEELELNENIVSAVEPGAFNNLFNLRTLGLRSNRLK-LIPLGvFTGLSNLTKLDISENK 148
Cdd:PLN00113 480 LDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSgQIPAS-FSEMPVLSQLDLSQNQ 558
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 564363844 149 iviLLDYMFQDLYNLKSLEvgdndLVYISHRAFSG 183
Cdd:PLN00113 559 ---LSGEIPKNLGNVESLV-----QVNISHNHLHG 585
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
433-500 1.35e-04

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: 41.09  E-value: 1.35e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564363844 433 GHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNgRLTVFPDGT-LEVRYAQVQDNGTYLCIAANAGGND 500
Cdd:cd05736   15 GVEASLRCHAEGIPLPRVQWLKNGMDINPKLSK-QLTLIANGSeLHISNVRYEDTGAYTCIAKNEGGVD 82
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
424-498 3.14e-04

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. 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. The Ig-like domain of the Twitchin is a member of the I-set 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. 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.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 40.01  E-value: 3.14e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564363844 424 KAQQVFVDEGHTVQFVCRADGDPPPAILW-LSPRKHLVSAKSNGRLTVFPDGTLEVRYAQvQDNGTYLCIAANAGG 498
Cdd:cd20949    5 NAYVTTVKEGQSATILCEVKGEPQPNVTWhFNGQPISASVADMSKYRILADGLLINKVTQ-DDTGEYTCRAYQVNS 79
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
420-508 3.44e-04

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: 39.92  E-value: 3.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 420 IRDRKAQ-QVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSngRLTVFPDGT-LEVRYAQVQDNGTYLCIAANAG 497
Cdd:cd05730    4 IRARQSEvNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEE--KYSFNEDGSeMTILDVDKLDEAEYTCIAENKA 81
                         90
                 ....*....|.
gi 564363844 498 GNDSMPAHLHV 508
Cdd:cd05730   82 GEQEAEIHLKV 92
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
433-508 3.93e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; 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. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). 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: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 39.90  E-value: 3.93e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564363844 433 GHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDG-TLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 508
Cdd:cd05729   19 ANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGwSLIIERAIPRDKGKYTCIVENEYGSINHTYDVDV 95
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
424-508 4.21e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 39.75  E-value: 4.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 424 KAQQVFVDEGHTVQFVCRADGDPPPAILWlsPRKHLVSAKSNGRLTVFPDGT----LEVRYAQVQDNGTYLCIAANAGGN 499
Cdd:cd05892    6 KPQNKKVLEGDPVRLECQISAIPPPQIFW--KKNNEMLQYNTDRISLYQDNCgricLLIQNANKKDAGWYTVSAVNEAGV 83

                 ....*....
gi 564363844 500 DSMPAHLHV 508
Cdd:cd05892   84 VSCNARLDV 92
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
433-509 5.94e-04

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: 38.93  E-value: 5.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 433 GHTVQFVCRADGDPPPAILWLsprkhlvsaKSNGRL----TVFPD--GTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHL 506
Cdd:cd05731   10 GGVLLLECIAEGLPTPDIRWI---------KLGGELpkgrTKFENfnKTLKIENVSEADSGEYQCTASNTMGSARHTISV 80

                 ...
gi 564363844 507 HVR 509
Cdd:cd05731   81 TVE 83
LRR_9 pfam14580
Leucine-rich repeat;
70-180 6.75e-04

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 40.90  E-value: 6.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844   70 LDLGKNRIKTLnqDEFASFPHLEELELNENIVSAVEPGAFNNLFNLRTLGLRSNRL-KLIPLGVFTGLSNLTKLDISENK 148
Cdd:pfam14580  47 IDFSDNEIRKL--DGFPLLRRLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLqELGDLDPLASLKKLTFLSLLRNP 124
                          90       100       110
                  ....*....|....*....|....*....|..
gi 564363844  149 IVILLDYMFQDLYNLKSLEVGDNDLVYISHRA 180
Cdd:pfam14580 125 VTNKPHYRLYVIYKVPQLRLLDFRKVKQKERQ 156
IgI_1_Titin-A168_like cd20971
First immunoglobulin-like domains A168 within the A-band segment of human cardiac titin, and ...
415-505 1.09e-03

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: 38.60  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 415 CRRAHIRDRKAQQvfvdeGHTVQFVCRADGDPPPAILWL---SP----RKHLVSAKSNGRLTVFPDGTLEVRYAqvqdnG 487
Cdd:cd20971    3 HFKEELRNLNVRY-----QSNATLVCKVTGHPKPIVKWYrqgKEiiadGLKYRIQEFKGGYHQLIIASVTDDDA-----T 72
                         90
                 ....*....|....*...
gi 564363844 488 TYLCIAANAGGNDSMPAH 505
Cdd:cd20971   73 VYQVRATNQGGSVSGTAS 90
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
433-508 1.19e-03

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination. 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: 409444  Cd Length: 105  Bit Score: 38.79  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 433 GHTVQFVCRADGDPPPAILWLsprKHLvsaKSNGRlTVFPDGT--------------------LEVRYAQVQDNGTYLCI 492
Cdd:cd05858   16 GTDAEFVCKVYSDAQPHIQWL---KHV---EKNGS-KYGPDGLpyvevlktagvnttdkeievLYLRNVTFEDAGEYTCL 88
                         90
                 ....*....|....*.
gi 564363844 493 AANAGGNDSMPAHLHV 508
Cdd:cd05858   89 AGNSIGISHHSAWLTV 104
LRRCT smart00082
Leucine rich repeat C-terminal domain;
363-399 1.60e-03

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 36.64  E-value: 1.60e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 564363844   363 NPLACDCRLLWvFRRRWRLNF---NRQQPTCATPEFVQGK 399
Cdd:smart00082   1 NPFICDCELRW-LLRWLQANEhlqDPVDLRCASPSSLRGP 39
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
423-509 1.61e-03

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band 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. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. 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 Ig I1 domain of the titin I-band 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, 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: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 38.17  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 423 RKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDG---TLEVRYAQVQDNGTYLCIAANAGGN 499
Cdd:cd20951    5 IRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESEYgvhVLHIRRVTVEDSAVYSAVAKNIHGE 84
                         90
                 ....*....|
gi 564363844 500 DSMPAHLHVR 509
Cdd:cd20951   85 ASSSASVVVE 94
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
426-498 1.80e-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: 37.67  E-value: 1.80e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564363844 426 QQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSaksNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGG 498
Cdd:cd05852   10 KKILAAKGGRVIIECKPKAAPKPKFSWSKGTELLVN---NSRISIWDDGSLEILNITKLDEGSYTCFAENNRG 79
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
430-508 2.08e-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: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 430 VDEGHTVQFVCRADGDPPPAILWLsprKHLVSAKSNGRLTVFPDG----TLEVRYAQVQDNGTYLCIAANAGGNDSMPAH 505
Cdd:cd20973    9 VVEGSAARFDCKVEGYPDPEVKWM---KDDNPIVESRRFQIDQDEdglcSLIISDVCGDDSGKYTCKAVNSLGEATCSAE 85

                 ...
gi 564363844 506 LHV 508
Cdd:cd20973   86 LTV 88
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
423-508 3.76e-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: 36.80  E-value: 3.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564363844 423 RKAQQVFVDEGHTVQFVCRADGDPPPAILW-----------LSPRKHLVSaksngrltvfpdGTLEVRYAQVQDNGTYLC 491
Cdd:cd05867    4 RRPQSHLYGPGETARLDCQVEGIPTPNITWsingapiegtdPDPRRHVSS------------GALILTDVQPSDTAVYQC 71
                         90
                 ....*....|....*..
gi 564363844 492 IAANAGGNDSMPAHLHV 508
Cdd:cd05867   72 EARNRHGNLLANAHVHV 88
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
114-150 5.59e-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: 34.91  E-value: 5.59e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 564363844  114 NLRTLGLRSNRLKLIPLgvFTGLSNLTKLDISENKIV 150
Cdd:pfam12799   2 NLEVLDLSNNQITDIPP--LAKLPNLETLDLSGNNKI 36
LRRNT smart00013
Leucine rich repeat N-terminal domain;
35-69 7.63e-03

Leucine rich repeat N-terminal domain;


Pssm-ID: 214470 [Multi-domain]  Cd Length: 33  Bit Score: 34.22  E-value: 7.63e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 564363844    35 GCPPRCECSaqDRAVLCHRKRFVAVPEGIPTETRL 69
Cdd:smart00013   1 ACPAPCNCS--GTAVDCSGRGLTEVPLDLPPDTTL 33
 
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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