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Conserved domains on  [gi|148237004|ref|NP_001081296|]
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neural cell adhesion molecule 1-A precursor [Xenopus laevis]

Protein Classification

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List of domain hits

Name Accession Description Interval E-value
Ig super family cl11960
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
301-396 2.57e-55

Immunoglobulin domain; 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, 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.


The actual alignment was detected with superfamily member cd05869:

Pssm-ID: 325142  Cd Length: 97  Bit Score: 189.04  E-value: 2.57e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  301 AKPKITYVENKTAVEL-DEITLTCEASGDPIPSITWRTAVRNISSEATTLDGHIVVKEHIRMSALTLKDIQYTDAGEYFC 379
Cdd:cd05869     1 AKPKITYVENQTAMELeEQITLTCEASGDPIPSITWRTSTRNISSEEKTLDGHIVVRSHARVSSLTLKYIQYTDAGEYLC 80
                          90
                  ....*....|....*..
gi 148237004  380 IASNPIGVDMQAMYFEV 396
Cdd:cd05869    81 TASNTIGQDSQSMYLEV 97
Ig super family cl11960
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
20-112 1.03e-52

Immunoglobulin domain; 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, 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.


The actual alignment was detected with superfamily member cd05865:

Pssm-ID: 325142  Cd Length: 96  Bit Score: 181.37  E-value: 1.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   20 LEVNIVPDQGEISLGESKFFLCQVSGEA--TDISWYSPTGEKLVT-QQQISVVRSDDYTSTLTIYNASSQDAGIYKCVAS 96
Cdd:cd05865     1 LQVDIVPSQGEISVGESKFFLCQVAGEAkdKDISWFSPNGEKLTPnQQRISVVRNDDYSSTLTIYNANIDDAGIYKCVVS 80
                          90
                  ....*....|....*.
gi 148237004   97 NEAEGESEGTVNLKIY 112
Cdd:cd05865    81 NEDEGESEATVNVKIF 96
Ig super family cl11960
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
208-302 4.54e-50

Immunoglobulin domain; 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, 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.


The actual alignment was detected with superfamily member cd05730:

Pssm-ID: 325142  Cd Length: 95  Bit Score: 173.96  E-value: 4.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  208 PPTIQARQLRVNATANMAESVVLSCDADGFPDPEISWLKKGEPIEDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQ 287
Cdd:cd05730     1 PPTIRARQSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAENK 80
                          90
                  ....*....|....*
gi 148237004  288 AGEAEATILLKVYAK 302
Cdd:cd05730    81 AGEQEAEIHLKVFAK 95
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
400-477 2.56e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


:

Pssm-ID: 316449  Cd Length: 76  Bit Score: 65.60  E-value: 2.56e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237004   400 PKIRG-PVVVYTWEGNPVNITCEVFAHPRAAVTWFRDGQLLPSSnfsnIKIYSGPTSSSLEVNPDSENDFGNYNCTAIN 477
Cdd:pfam13927    2 PVITVsPSSVVVLEGESVTLTCEATGGPPPTITWYKNGKPGPTS----SRISLSGSNSTLTISNVTREDSGTYTCVASN 76
IG smart00409
Immunoglobulin;
121-187 2.56e-10

Immunoglobulin;


:

Pssm-ID: 214652  Cd Length: 85  Bit Score: 59.83  E-value: 2.56e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004    121 PTPQEFKEGEDAVIICDVSSSIPSIITWRHKGKDVIFKKDvRFVVLANN---YLQIRGIKKTDEGTYRCE 187
Cdd:smart00409    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESG-RFSVSRSGstsTLTISNVTPEDSGTYTCA 69
fn3 pfam00041
Fibronectin type III domain;
596-679 1.19e-09

Fibronectin type III domain;


:

Pssm-ID: 306538  Cd Length: 85  Bit Score: 57.81  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   596 SAPKLVGHLSEDGNSIKVDILKQDDGGSPIRHYLVNYRALNALEWKPEMRVPSNSHHVMLKALEWNVDYEVIVVAENQQG 675
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ....
gi 148237004   676 KSKP 679
Cdd:pfam00041   81 EGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
492-589 4.98e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020  Cd Length: 93  Bit Score: 53.27  E-value: 4.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  492 DTPSSPAIRKVEpySSTVMIVFDEPDSTGGvPILKYKAEWRVIGHEKWHTkyYDAKEVNAESIiTVMGLKPETSYMVKLS 571
Cdd:cd00063     2 SPPTNLRVTDVT--STSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKE--VEVTPGSETSY-TLTGLKPGTEYEFRVR 75
                          90
                  ....*....|....*...
gi 148237004  572 AMNGKGLGDSTPSQEFTT 589
Cdd:cd00063    76 AVNGGGESPPSESVTVTT 93
Atrophin-1 super family cl26464
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
864-1048 1.69e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 331285  Cd Length: 3151  Bit Score: 49.17  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  864 QATPSKAEAPTTSSPPPTSSPKVAPLVDLSDTP----TNNPSKVVANQAGPLNPSAATSAAEPPTVIIKPVTTVPPNAAS 939
Cdd:PHA03247 2670 LGRAAQASSPPQRPRRRAARPTVGSLTSLADPPppppTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA 2749
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  940 PPPTPEPKQVKQEQSGTKSPEKEEAQPSTVknPTEATKDESASLSNTKPlqdedfqidggtfKTPEIDLAKDVFAALGTA 1019
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAPPAAPAAGP--PRRLTRPAVASLSESRE-------------SLPSPWDPADPPAAVLAP 2814
                         170       180
                  ....*....|....*....|....*....
gi 148237004 1020 TPTAVASGKASELVSSTAdTSVPLDSAKT 1048
Cdd:PHA03247 2815 AAALPPAASPAGPLPPPT-SAQPTAPPPP 2842
 
Name Accession Description Interval E-value
Ig_NCAM-1 cd05869
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig_NCAM-1: ...
301-396 2.57e-55

Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig_NCAM-1: immunoglobulin (Ig)-like domain similar to the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM). 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: 143277  Cd Length: 97  Bit Score: 189.04  E-value: 2.57e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  301 AKPKITYVENKTAVEL-DEITLTCEASGDPIPSITWRTAVRNISSEATTLDGHIVVKEHIRMSALTLKDIQYTDAGEYFC 379
Cdd:cd05869     1 AKPKITYVENQTAMELeEQITLTCEASGDPIPSITWRTSTRNISSEEKTLDGHIVVRSHARVSSLTLKYIQYTDAGEYLC 80
                          90
                  ....*....|....*..
gi 148237004  380 IASNPIGVDMQAMYFEV 396
Cdd:cd05869    81 TASNTIGQDSQSMYLEV 97
Ig1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1; Ig1_NCAM-1: ...
20-112 1.03e-52

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1; Ig1_NCAM-1: 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.


Pssm-ID: 143273  Cd Length: 96  Bit Score: 181.37  E-value: 1.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   20 LEVNIVPDQGEISLGESKFFLCQVSGEA--TDISWYSPTGEKLVT-QQQISVVRSDDYTSTLTIYNASSQDAGIYKCVAS 96
Cdd:cd05865     1 LQVDIVPSQGEISVGESKFFLCQVAGEAkdKDISWFSPNGEKLTPnQQRISVVRNDDYSSTLTIYNANIDDAGIYKCVVS 80
                          90
                  ....*....|....*.
gi 148237004   97 NEAEGESEGTVNLKIY 112
Cdd:cd05865    81 NEDEGESEATVNVKIF 96
Ig3_NCAM-1_like cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); ...
208-302 4.54e-50

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig3_NCAM-1_like: domain similar to the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM). 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  Cd Length: 95  Bit Score: 173.96  E-value: 4.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  208 PPTIQARQLRVNATANMAESVVLSCDADGFPDPEISWLKKGEPIEDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQ 287
Cdd:cd05730     1 PPTIRARQSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAENK 80
                          90
                  ....*....|....*
gi 148237004  288 AGEAEATILLKVYAK 302
Cdd:cd05730    81 AGEQEAEIHLKVFAK 95
I-set pfam07679
Immunoglobulin I-set domain;
219-299 9.60e-19

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 84.23  E-value: 9.60e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   219 NATANMAESVVLSCDADGFPDPEISWLKKGEPI-EDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQAGEAEATILL 297
Cdd:pfam07679    9 DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLrSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88

                   ..
gi 148237004   298 KV 299
Cdd:pfam07679   89 TV 90
I-set pfam07679
Immunoglobulin I-set domain;
24-111 1.36e-16

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 78.07  E-value: 1.36e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004    24 IVPDQGEISLGESKFFLCQVSGEAT-DISWYSptGEKLVTQQQISVVRSDDYTSTLTIYNASSQDAGIYKCVASNEAeGE 102
Cdd:pfam07679    5 QKPKDVEVQEGESARFTCTVTGTPDpEVSWFK--DGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA-GE 81

                   ....*....
gi 148237004   103 SEGTVNLKI 111
Cdd:pfam07679   82 AEASAELTV 90
IG smart00409
Immunoglobulin;
226-299 4.66e-16

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 76.39  E-value: 4.66e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148237004    226 ESVVLSCDADGFPDPEISWLKKG--EPIEDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:smart00409   10 ESVTLSCEASGSPPPEVTWYKQGgkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IG smart00409
Immunoglobulin;
26-111 2.17e-13

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 68.69  E-value: 2.17e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004     26 PDQGEISLGESKFFLCQVSGEATD-ISWYSPTGEKLVTQQQISVVRSDDyTSTLTIYNASSQDAGIYKCVASNEAeGESE 104
Cdd:smart00409    1 PPSVTVKEGESVTLSCEASGSPPPeVTWYKQGGKLLAESGRFSVSRSGS-TSTLTISNVTPEDSGTYTCAATNSS-GSAS 78

                    ....*..
gi 148237004    105 GTVNLKI 111
Cdd:smart00409   79 SGTTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
400-477 2.56e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 65.60  E-value: 2.56e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237004   400 PKIRG-PVVVYTWEGNPVNITCEVFAHPRAAVTWFRDGQLLPSSnfsnIKIYSGPTSSSLEVNPDSENDFGNYNCTAIN 477
Cdd:pfam13927    2 PVITVsPSSVVVLEGESVTLTCEATGGPPPTITWYKNGKPGPTS----SRISLSGSNSTLTISNVTREDSGTYTCVASN 76
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
405-488 4.94e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653  Cd Length: 85  Bit Score: 64.83  E-value: 4.94e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004    405 PVVVYTWEGNPVNITCEVFAHPRAAVTWFRDGQLLPSSNfSNIKIYSGPTSSSLEVNPDSENDFGNYNCTAINTIGHEFS 484
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAES-GRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79

                    ....
gi 148237004    485 EFIL 488
Cdd:smart00410   80 GTTL 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
302-383 3.37e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 62.13  E-value: 3.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   302 KPKITYVENKTAVEL-DEITLTCEASGDPIPSITWRtavRNisseATTLDGHIVVKEHIRMSALTLKDIQYTDAGEYFCI 380
Cdd:pfam13927    1 KPVITVSPSSVVVLEgESVTLTCEATGGPPPTITWY---KN----GKPGPTSSRISLSGSNSTLTISNVTREDSGTYTCV 73

                   ...
gi 148237004   381 ASN 383
Cdd:pfam13927   74 ASN 76
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
309-388 2.22e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653  Cd Length: 85  Bit Score: 59.83  E-value: 2.22e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004    309 ENKTAVELDEITLTCEASGDPIPSITWRtavRNISSEATTlDGHIVVKEHIRMSALTLKDIQYTDAGEYFCIASNPIGVD 388
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWY---KQGGKLLAE-SGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSA 77
IG smart00409
Immunoglobulin;
121-187 2.56e-10

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 59.83  E-value: 2.56e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004    121 PTPQEFKEGEDAVIICDVSSSIPSIITWRHKGKDVIFKKDvRFVVLANN---YLQIRGIKKTDEGTYRCE 187
Cdd:smart00409    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESG-RFSVSRSGstsTLTISNVTPEDSGTYTCA 69
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
416-486 1.17e-09

Immunoglobulin domain; 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, 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.


Pssm-ID: 319273  Cd Length: 70  Bit Score: 57.64  E-value: 1.17e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148237004  416 VNITCEVFAHPRAAVTWFRDGQLLPSSNFSNIKIYSGptSSSLEVNPDSENDFGNYNCTAINTIGHEFSEF 486
Cdd:cd00096     1 VTLTCSASGNPPPTITWLKNGKPLPSSSRFRRRSSGG--NGTLTISNVTPEDSGTYTCVASNSAGSASASV 69
fn3 pfam00041
Fibronectin type III domain;
596-679 1.19e-09

Fibronectin type III domain;


Pssm-ID: 306538  Cd Length: 85  Bit Score: 57.81  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   596 SAPKLVGHLSEDGNSIKVDILKQDDGGSPIRHYLVNYRALNALEWKPEMRVPSNSHHVMLKALEWNVDYEVIVVAENQQG 675
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ....
gi 148237004   676 KSKP 679
Cdd:pfam00041   81 EGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
492-589 4.98e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020  Cd Length: 93  Bit Score: 53.27  E-value: 4.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  492 DTPSSPAIRKVEpySSTVMIVFDEPDSTGGvPILKYKAEWRVIGHEKWHTkyYDAKEVNAESIiTVMGLKPETSYMVKLS 571
Cdd:cd00063     2 SPPTNLRVTDVT--STSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKE--VEVTPGSETSY-TLTGLKPGTEYEFRVR 75
                          90
                  ....*....|....*...
gi 148237004  572 AMNGKGLGDSTPSQEFTT 589
Cdd:cd00063    76 AVNGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
595-680 1.13e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020  Cd Length: 93  Bit Score: 52.11  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  595 PSAPKLVGHLSEDGNSIKVDILKQDDGGSPIRHYLVNYRALNALEWKPEMRVPSNSHHVMLKALEWNVDYEVIVVAENQQ 674
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                  ....*.
gi 148237004  675 GKSKPA 680
Cdd:cd00063    81 GESPPS 86
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
121-187 1.69e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 51.35  E-value: 1.69e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148237004   121 PTPQEFKEGEDAVIICDVSSSIPSIITWRHKGKDVIFKKDVRFvVLANNYLQIRGIKKTDEGTYRCE 187
Cdd:pfam13927    8 PSSVVVLEGESVTLTCEATGGPPPTITWYKNGKPGPTSSRISL-SGSNSTLTISNVTREDSGTYTCV 73
PHA02785 PHA02785
IL-beta-binding protein; Provisional
73-284 4.09e-07

IL-beta-binding protein; Provisional


Pssm-ID: 165149  Cd Length: 326  Bit Score: 53.10  E-value: 4.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   73 DYTSTLTIYNASSQDAGIYKCVASNEAEGE-----------SEGTVNLKIYqkltfknaptPQEFKEGEDAVIICD---- 137
Cdd:PHA02785   79 DNGSNMLILNPTQSDSGIYICITKNETYCDmmslnltivsvSESNIDLISY----------PQIVNERSTGEMVCPnina 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  138 -VSSSIPSIITWRHKGKdvifKKDVRFVVLANNYLQIRGIKKTDEGTYRCEGRILARGEInyKDIQVIVN-------VPP 209
Cdd:PHA02785  149 fIASNVNADIIWSGHRR----LRNKRLKQRTPGIITIEDVRKNDAGYYTCVLKYIYGDKT--YNVTRIVKlevrdriIPP 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  210 TIqarQLRVNATANMAESVVLSCDADGFP---DPEISWLKKG----EPIEDGEEKIS-----FNEDQ-----SEMTIHHV 272
Cdd:PHA02785  223 TM---QLPEGVVTSIGSNLTIACRVSLRPpttDADVFWISNGmyyeEDDEDGDGRISvankiYTTDKrrvitSRLNINPV 299
                         250
                  ....*....|..
gi 148237004  273 EKDDEAEYSCIA 284
Cdd:PHA02785  300 KEEDATTFTCMA 311
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
132-187 5.20e-06

Immunoglobulin domain; 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, 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.


Pssm-ID: 319273  Cd Length: 70  Bit Score: 46.85  E-value: 5.20e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148237004  132 AVIICDVSSSIPSIITWRHKGKDVIFKKDVRFVVLANNY-LQIRGIKKTDEGTYRCE 187
Cdd:cd00096     1 VTLTCSASGNPPPTITWLKNGKPLPSSSRFRRRSSGGNGtLTISNVTPEDSGTYTCV 57
PHA03247 PHA03247
large tegument protein UL36; Provisional
864-1048 1.69e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021  Cd Length: 3151  Bit Score: 49.17  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  864 QATPSKAEAPTTSSPPPTSSPKVAPLVDLSDTP----TNNPSKVVANQAGPLNPSAATSAAEPPTVIIKPVTTVPPNAAS 939
Cdd:PHA03247 2670 LGRAAQASSPPQRPRRRAARPTVGSLTSLADPPppppTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA 2749
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  940 PPPTPEPKQVKQEQSGTKSPEKEEAQPSTVknPTEATKDESASLSNTKPlqdedfqidggtfKTPEIDLAKDVFAALGTA 1019
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAPPAAPAAGP--PRRLTRPAVASLSESRE-------------SLPSPWDPADPPAAVLAP 2814
                         170       180
                  ....*....|....*....|....*....
gi 148237004 1020 TPTAVASGKASELVSSTAdTSVPLDSAKT 1048
Cdd:PHA03247 2815 AAALPPAASPAGPLPPPT-SAQPTAPPPP 2842
fn3 pfam00041
Fibronectin type III domain;
495-582 2.47e-05

Fibronectin type III domain;


Pssm-ID: 306538  Cd Length: 85  Bit Score: 45.10  E-value: 2.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   495 SSPAIRKVEPYSSTVMIVFDEPDSTGGVPILKYKAEWRVIGHEKWHTKYydaKEVNAESIITVMGLKPETSYMVKLSAMN 574
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEI---TVPGTTTSVTLTGLKPGTEYEVRVQAVN 77

                   ....*...
gi 148237004   575 GKGLGDST 582
Cdd:pfam00041   78 GGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
494-579 5.89e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495  Cd Length: 83  Bit Score: 43.76  E-value: 5.89e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004    494 PSSPAIRKVEPYSST-VMIVFDEPDSTGGV-PILKYKAEWRVIGHEkWHTkyydAKEVNAESIITVMGLKPETSYMVKLS 571
Cdd:smart00060    1 PSPPSNLRVTDVTSTsVTLSWEPPPDDGITgYIVGYRVEYREEGSE-WKE----VNVTPSSTSYTLTGLKPGTEYEFRVR 75

                    ....*...
gi 148237004    572 AMNGKGLG 579
Cdd:smart00060   76 AVNGAGEG 83
AflR pfam08493
Aflatoxin regulatory protein; This domain is found in the aflatoxin regulatory protein (AflR) ...
892-1041 1.91e-04

Aflatoxin regulatory protein; This domain is found in the aflatoxin regulatory protein (AflR) which is involved in the regulation of the biosynthesis of aflatoxin in the fungal genus Aspergillus. It occurs together with the fungal Zn(2)-Cys(6) binuclear cluster domain (pfam00172).


Pssm-ID: 285666  Cd Length: 275  Bit Score: 44.61  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   892 LSDTPTNNPSKVVANQAGPLNPSAATSAAEPPTVIIKPVTTVPPNAASPPPTPEPkqVKQEQSGTKSPEKEEAQPSTVKN 971
Cdd:pfam08493    7 TTISPPANTGANTTSSVLPSNPVTSGQSQTPLNAPITPNPTSSVSAIFSHPSPKP--CIETQGQTPDLWGSILSPSASFT 84
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148237004   972 PTEAtkDESASLSNTKPLQDEDFQIDGGT--FKTPEIDLAKDVFAALGTATPTA------VASGKASELVSSTADTSV 1041
Cdd:pfam08493   85 PDVS--SLSGSLTSMPTDVGSLFASPMGLplFDTCDIDSLPPEAAGEHPLFPTSalssppNARASPSSDTTSTTDNHP 160
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
595-677 1.92e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495  Cd Length: 83  Bit Score: 42.22  E-value: 1.92e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004    595 PSAPKLVGHLSEDGNSIKV--DILKQDDGGSPIRHYLVNYRALNAlEWKpEMRVPSNSHHVMLKALEWNVDYEVIVVAEN 672
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLswEPPPDDGITGYIVGYRVEYREEGS-EWK-EVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 148237004    673 QQGKS 677
Cdd:smart00060   79 GAGEG 83
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
73-205 5.60e-04

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173  Cd Length: 227  Bit Score: 42.59  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   73 DYTSTLTIYNASSQDAGIYKCVASNEAEGEsEGTVnlkiyqKLTFKNAPTPQEFKEGEDAVIICDVSSSIPS-----IIT 147
Cdd:PHA02826   95 DRSENLWIGNVINIDEGIYICTISSGNICE-ESTI------RLTFDSGTINYQFNSGKDSKLHCYGTDGISStfkdyTLT 167
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148237004  148 WRHKGkDVIFKKDvRFVVLANNY-LQIRGIKKTDEGTYRCEGRIlARGEINY---KDIQVIV 205
Cdd:PHA02826  168 WYKNG-NIVLYTD-RIQLRNNNStLVIKSATHDDSGIYTCNLRF-NKNSNNYnitKEYKVTI 226
 
Name Accession Description Interval E-value
Ig_NCAM-1 cd05869
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig_NCAM-1: ...
301-396 2.57e-55

Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig_NCAM-1: immunoglobulin (Ig)-like domain similar to the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM). 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: 143277  Cd Length: 97  Bit Score: 189.04  E-value: 2.57e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  301 AKPKITYVENKTAVEL-DEITLTCEASGDPIPSITWRTAVRNISSEATTLDGHIVVKEHIRMSALTLKDIQYTDAGEYFC 379
Cdd:cd05869     1 AKPKITYVENQTAMELeEQITLTCEASGDPIPSITWRTSTRNISSEEKTLDGHIVVRSHARVSSLTLKYIQYTDAGEYLC 80
                          90
                  ....*....|....*..
gi 148237004  380 IASNPIGVDMQAMYFEV 396
Cdd:cd05869    81 TASNTIGQDSQSMYLEV 97
Ig1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1; Ig1_NCAM-1: ...
20-112 1.03e-52

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1; Ig1_NCAM-1: 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.


Pssm-ID: 143273  Cd Length: 96  Bit Score: 181.37  E-value: 1.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   20 LEVNIVPDQGEISLGESKFFLCQVSGEA--TDISWYSPTGEKLVT-QQQISVVRSDDYTSTLTIYNASSQDAGIYKCVAS 96
Cdd:cd05865     1 LQVDIVPSQGEISVGESKFFLCQVAGEAkdKDISWFSPNGEKLTPnQQRISVVRNDDYSSTLTIYNANIDDAGIYKCVVS 80
                          90
                  ....*....|....*.
gi 148237004   97 NEAEGESEGTVNLKIY 112
Cdd:cd05865    81 NEDEGESEATVNVKIF 96
Ig_NCAM-1_like cd05732
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM) and similar ...
301-396 7.15e-52

Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM) and similar proteins; Ig_NCAM-1 like: domain similar to the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM). 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).


Pssm-ID: 143209  Cd Length: 96  Bit Score: 179.26  E-value: 7.15e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  301 AKPKITYVENKTAVELDEITLTCEASGDPIPSITWRTAVRNISSEATTLDGHIVVKEHIRMSALTLKDIQYTDAGEYFCI 380
Cdd:cd05732     1 VQPKITYLENQTAVELEQITLTCEAEGDPIPEITWRRATRNFSEGDKSLDGRIVVRGHARVSSLTLKDVQLTDAGRYDCE 80
                          90
                  ....*....|....*.
gi 148237004  381 ASNPIGVDMQAMYFEV 396
Cdd:cd05732    81 ASNRIGGDQQSMYLEV 96
Ig3_NCAM-1_like cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); ...
208-302 4.54e-50

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig3_NCAM-1_like: domain similar to the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM). 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  Cd Length: 95  Bit Score: 173.96  E-value: 4.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  208 PPTIQARQLRVNATANMAESVVLSCDADGFPDPEISWLKKGEPIEDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQ 287
Cdd:cd05730     1 PPTIRARQSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAENK 80
                          90
                  ....*....|....*
gi 148237004  288 AGEAEATILLKVYAK 302
Cdd:cd05730    81 AGEQEAEIHLKVFAK 95
Ig1_NCAM-1_like cd04977
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1 and similar ...
20-111 5.93e-35

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1 and similar proteins; Ig1_NCAM-1 like: 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).


Pssm-ID: 319283  Cd Length: 93  Bit Score: 131.22  E-value: 5.93e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   20 LEVNIVPDQGEISLGESKFFLCQVSGEATDISWYSPTGEKLVT-QQQISVVRSDDYTSTLTIYNASSQDAGIYKCVASNE 98
Cdd:cd04977     1 LQVKIIPSYAEISVGESKFFLCKVSGDAKNINWVSPNGEKVLTkHGNLKVVNHGSVLSSLTIYNANINDAGIYKCVATNG 80
                          90
                  ....*....|...
gi 148237004   99 AEGESEGTVNLKI 111
Cdd:cd04977    81 KGTESEATVKLDI 93
Ig1_NCAM-2 cd05866
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; Ig1_NCAM-2: ...
20-112 5.49e-23

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; Ig1_NCAM-2: first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2 (OCAM/mamFas II, RNCAM). NCAM-2 is organized similarly to NCAM-1, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule.


Pssm-ID: 143274  Cd Length: 92  Bit Score: 96.64  E-value: 5.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   20 LEVNIVPDQGEISLGESKFFLCQVSGEATDISWYSPTGEKLVTQQQIsVVRSDDYTSTLTIYNASSQDAGIYKCVASnEA 99
Cdd:cd05866     1 LQVSISLSKVELSVGESKFFTCTAIGEPESIDWYNPQGEKIVSSQRV-VVQKEGVRSRLTIYNANIEDAGIYRCQAT-DA 78
                          90
                  ....*....|....
gi 148237004  100 EGES-EGTVNLKIY 112
Cdd:cd05866    79 KGQTqEATVVLEIY 92
I-set pfam07679
Immunoglobulin I-set domain;
219-299 9.60e-19

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 84.23  E-value: 9.60e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   219 NATANMAESVVLSCDADGFPDPEISWLKKGEPI-EDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQAGEAEATILL 297
Cdd:pfam07679    9 DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLrSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88

                   ..
gi 148237004   298 KV 299
Cdd:pfam07679   89 TV 90
Ig_NCAM-2 cd05870
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM ...
302-396 6.48e-17

Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM); Ig_NCAM-2: immunoglobulin (Ig)-like domain similar to the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is organized similarly to NCAM , including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule.


Pssm-ID: 143278  Cd Length: 98  Bit Score: 79.25  E-value: 6.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  302 KPKITYVENKTAVELDEITLTCEASGDPIPSITWRTAVRNIS-SEA-TTLDGHIVVKEHIRMSALTLKDIQYTDAGEYFC 379
Cdd:cd05870     2 QPHIIQLKNETTVENGAATLSCKAEGEPIPEITWKRASDGHTfSEGdKSPDGRIEVKGQHGESSLHIKDVKLSDSGRYDC 81
                          90
                  ....*....|....*..
gi 148237004  380 IASNPIGVDMQAMYFEV 396
Cdd:cd05870    82 EAASRIGGHQKSMYLDI 98
I-set pfam07679
Immunoglobulin I-set domain;
24-111 1.36e-16

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 78.07  E-value: 1.36e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004    24 IVPDQGEISLGESKFFLCQVSGEAT-DISWYSptGEKLVTQQQISVVRSDDYTSTLTIYNASSQDAGIYKCVASNEAeGE 102
Cdd:pfam07679    5 QKPKDVEVQEGESARFTCTVTGTPDpEVSWFK--DGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA-GE 81

                   ....*....
gi 148237004   103 SEGTVNLKI 111
Cdd:pfam07679   82 AEASAELTV 90
IG smart00409
Immunoglobulin;
226-299 4.66e-16

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 76.39  E-value: 4.66e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148237004    226 ESVVLSCDADGFPDPEISWLKKG--EPIEDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:smart00409   10 ESVTLSCEASGSPPPEVTWYKQGgkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
226-299 4.66e-16

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653  Cd Length: 85  Bit Score: 76.39  E-value: 4.66e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148237004    226 ESVVLSCDADGFPDPEISWLKKG--EPIEDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:smart00410   10 ESVTLSCEASGSPPPEVTWYKQGgkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IGc2 smart00408
Immunoglobulin C-2 Type;
226-289 8.30e-16

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 75.14  E-value: 8.30e-16
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148237004    226 ESVVLSCDADGFPDPEISWLKKGEPIEDGeekISFNEDQSEMTIHHVEKDDEAEYSCIANNQAG 289
Cdd:smart00408    3 QSVTLTCPAEGNPVPNITWLKDGKPLPES---NRFVASGSTLTIKSVSLEDSGLYTCVAENSAG 63
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
228-295 3.85e-15

Immunoglobulin domain; 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, 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.


Pssm-ID: 319273  Cd Length: 70  Bit Score: 73.43  E-value: 3.85e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237004  228 VVLSCDADGFPDPEISWLKKGEPI-EDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQAGEAEATI 295
Cdd:cd00096     1 VTLTCSASGNPPPTITWLKNGKPLpSSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSASASV 69
IG smart00409
Immunoglobulin;
26-111 2.17e-13

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 68.69  E-value: 2.17e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004     26 PDQGEISLGESKFFLCQVSGEATD-ISWYSPTGEKLVTQQQISVVRSDDyTSTLTIYNASSQDAGIYKCVASNEAeGESE 104
Cdd:smart00409    1 PPSVTVKEGESVTLSCEASGSPPPeVTWYKQGGKLLAESGRFSVSRSGS-TSTLTISNVTPEDSGTYTCAATNSS-GSAS 78

                    ....*..
gi 148237004    105 GTVNLKI 111
Cdd:smart00409   79 SGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
26-111 2.17e-13

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653  Cd Length: 85  Bit Score: 68.69  E-value: 2.17e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004     26 PDQGEISLGESKFFLCQVSGEATD-ISWYSPTGEKLVTQQQISVVRSDDyTSTLTIYNASSQDAGIYKCVASNEAeGESE 104
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPeVTWYKQGGKLLAESGRFSVSRSGS-TSTLTISNVTPEDSGTYTCAATNSS-GSAS 78

                    ....*..
gi 148237004    105 GTVNLKI 111
Cdd:smart00410   79 SGTTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
400-477 2.56e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 65.60  E-value: 2.56e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237004   400 PKIRG-PVVVYTWEGNPVNITCEVFAHPRAAVTWFRDGQLLPSSnfsnIKIYSGPTSSSLEVNPDSENDFGNYNCTAIN 477
Cdd:pfam13927    2 PVITVsPSSVVVLEGESVTLTCEATGGPPPTITWYKNGKPGPTS----SRISLSGSNSTLTISNVTREDSGTYTCVASN 76
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
208-286 4.40e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 64.83  E-value: 4.40e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237004   208 PPTIQARQLRVNATANmaESVVLSCDADGFPDPEISWLKKGEPiEDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANN 286
Cdd:pfam13927    1 KPVITVSPSSVVVLEG--ESVTLTCEATGGPPPTITWYKNGKP-GPTSSRISLSGSNSTLTISNVTREDSGTYTCVASN 76
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
405-488 4.94e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653  Cd Length: 85  Bit Score: 64.83  E-value: 4.94e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004    405 PVVVYTWEGNPVNITCEVFAHPRAAVTWFRDGQLLPSSNfSNIKIYSGPTSSSLEVNPDSENDFGNYNCTAINTIGHEFS 484
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAES-GRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79

                    ....
gi 148237004    485 EFIL 488
Cdd:smart00410   80 GTTL 83
IG smart00409
Immunoglobulin;
405-488 4.94e-12

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 64.83  E-value: 4.94e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004    405 PVVVYTWEGNPVNITCEVFAHPRAAVTWFRDGQLLPSSNfSNIKIYSGPTSSSLEVNPDSENDFGNYNCTAINTIGHEFS 484
Cdd:smart00409    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAES-GRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79

                    ....
gi 148237004    485 EFIL 488
Cdd:smart00409   80 GTTL 83
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
302-383 3.37e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 62.13  E-value: 3.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   302 KPKITYVENKTAVEL-DEITLTCEASGDPIPSITWRtavRNisseATTLDGHIVVKEHIRMSALTLKDIQYTDAGEYFCI 380
Cdd:pfam13927    1 KPVITVSPSSVVVLEgESVTLTCEATGGPPPTITWY---KN----GKPGPTSSRISLSGSNSTLTISNVTREDSGTYTCV 73

                   ...
gi 148237004   381 ASN 383
Cdd:pfam13927   74 ASN 76
Ig2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig2_Robo: domain ...
226-292 4.67e-11

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig2_Robo: domain similar to 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 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.


Pssm-ID: 143201  Cd Length: 86  Bit Score: 62.03  E-value: 4.67e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148237004  226 ESVVLSCDAD-GFPDPEISWLKKGEPIEDGEEKISFNEDQSEMtIHHVEKDDEAEYSCIANNQAGEAE 292
Cdd:cd05724    12 EMAVLECSPPrGHPEPTVSWRKDGQPLNLDNERVRIVDDGNLL-IAEARKSDEGTYKCVATNMVGERE 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
309-388 2.22e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653  Cd Length: 85  Bit Score: 59.83  E-value: 2.22e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004    309 ENKTAVELDEITLTCEASGDPIPSITWRtavRNISSEATTlDGHIVVKEHIRMSALTLKDIQYTDAGEYFCIASNPIGVD 388
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWY---KQGGKLLAE-SGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSA 77
IG smart00409
Immunoglobulin;
309-388 2.22e-10

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 59.83  E-value: 2.22e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004    309 ENKTAVELDEITLTCEASGDPIPSITWRtavRNISSEATTlDGHIVVKEHIRMSALTLKDIQYTDAGEYFCIASNPIGVD 388
Cdd:smart00409    2 PSVTVKEGESVTLSCEASGSPPPEVTWY---KQGGKLLAE-SGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSA 77
IG smart00409
Immunoglobulin;
121-187 2.56e-10

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 59.83  E-value: 2.56e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004    121 PTPQEFKEGEDAVIICDVSSSIPSIITWRHKGKDVIFKKDvRFVVLANN---YLQIRGIKKTDEGTYRCE 187
Cdd:smart00409    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESG-RFSVSRSGstsTLTISNVTPEDSGTYTCA 69
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
121-187 2.56e-10

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653  Cd Length: 85  Bit Score: 59.83  E-value: 2.56e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004    121 PTPQEFKEGEDAVIICDVSSSIPSIITWRHKGKDVIFKKDvRFVVLANN---YLQIRGIKKTDEGTYRCE 187
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESG-RFSVSRSGstsTLTISNVTPEDSGTYTCA 69
IGc2 smart00408
Immunoglobulin C-2 Type;
317-386 2.60e-10

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 59.34  E-value: 2.60e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004    317 DEITLTCEASGDPIPSITWRTavrnissEATTLDGHIVVKEHIrmSALTLKDIQYTDAGEYFCIASNPIG 386
Cdd:smart00408    3 QSVTLTCPAEGNPVPNITWLK-------DGKPLPESNRFVASG--STLTIKSVSLEDSGLYTCVAENSAG 63
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
319-388 3.28e-10

Immunoglobulin domain; 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, 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.


Pssm-ID: 319273  Cd Length: 70  Bit Score: 59.18  E-value: 3.28e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  319 ITLTCEASGDPIPSITWRTAVRNISSEATTLDGHIVVKehirmSALTLKDIQYTDAGEYFCIASNPIGVD 388
Cdd:cd00096     1 VTLTCSASGNPPPTITWLKNGKPLPSSSRFRRRSSGGN-----GTLTISNVTPEDSGTYTCVASNSAGSA 65
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
416-486 1.17e-09

Immunoglobulin domain; 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, 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.


Pssm-ID: 319273  Cd Length: 70  Bit Score: 57.64  E-value: 1.17e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148237004  416 VNITCEVFAHPRAAVTWFRDGQLLPSSNFSNIKIYSGptSSSLEVNPDSENDFGNYNCTAINTIGHEFSEF 486
Cdd:cd00096     1 VTLTCSASGNPPPTITWLKNGKPLPSSSRFRRRSSGG--NGTLTISNVTPEDSGTYTCVASNSAGSASASV 69
fn3 pfam00041
Fibronectin type III domain;
596-679 1.19e-09

Fibronectin type III domain;


Pssm-ID: 306538  Cd Length: 85  Bit Score: 57.81  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   596 SAPKLVGHLSEDGNSIKVDILKQDDGGSPIRHYLVNYRALNALEWKPEMRVPSNSHHVMLKALEWNVDYEVIVVAENQQG 675
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

                   ....
gi 148237004   676 KSKP 679
Cdd:pfam00041   81 EGPP 84
Ig_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: ...
221-297 1.67e-09

Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: domain similar to the M5, fifth immunoglobulin (Ig)-like domain from the human titin C terminus. 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.


Pssm-ID: 143224  Cd Length: 92  Bit Score: 57.75  E-value: 1.67e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148237004  221 TANMAESVVLSCDADGFPDPEISWLKKGEPIEDGEE-KISFNEDQSEMTIHHVEKDDEAEYSCIANNQAGEAEATILL 297
Cdd:cd05747    14 TVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRhQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQFTL 91
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
405-488 2.62e-09

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: 278476  Cd Length: 86  Bit Score: 56.82  E-value: 2.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   405 PVVVYTWEGNPVNITCEV-FAHPRAAVTWFRDGQLLPSSNFSNIKIYSGpTSSSLEVNPDSENDFGNYNCTAINTIGHEF 483
Cdd:pfam00047    3 PPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKVKHDNGRT-TQSSLLISNVTKEDAGTYTCVVNNPGGPAT 81

                   ....*
gi 148237004   484 SEFIL 488
Cdd:pfam00047   82 LSTSL 86
IGc2 smart00408
Immunoglobulin C-2 Type;
412-480 3.90e-09

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 55.88  E-value: 3.90e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237004    412 EGNPVNITCEVFAHPRAAVTWFRDGQLLPSSNfsnikiYSGPTSSSLEVNPDSENDFGNYNCTAINTIG 480
Cdd:smart00408    1 EGQSVTLTCPAEGNPVPNITWLKDGKPLPESN------RFVASGSTLTIKSVSLEDSGLYTCVAENSAG 63
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: ...
228-299 6.80e-09

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: domain similar to 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, or 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: 319298  Cd Length: 71  Bit Score: 55.13  E-value: 6.80e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148237004  228 VVLSCDADGFPDPEISWLKKGEPIEDGeeKISFNEDQSEMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:cd05731     1 LLLECIAEGLPTPDIRWIKLGGELPKG--RTKFENFNKTLKIENVSEADSGEYQCTASNTMGSARHTISVTV 70
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7, also known as CCK4; ...
228-291 1.12e-08

Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7, also known as CCK4; Ig2_PTK7: domain similar to the second immunoglobulin (Ig)-like domain in protein tyrosine kinase (PTK) 7, also known as CCK4. PTK7 is a subfamily of the receptor protein tyrosine kinase family, and is referred to as an RPTK-like molecule. RPTKs transduce extracellular signals across the cell membrane, and play important roles in regulating cell proliferation, migration, and differentiation. PTK7 is organized as an extracellular portion having seven Ig-like domains, a single transmembrane region, and a cytoplasmic tyrosine kinase-like domain. PTK7 is considered a pseudokinase as it has several unusual residues in some of the highly conserved tyrosine kinase (TK) motifs; it is predicted to lack TK activity. PTK7 may function as a cell-adhesion molecule. PTK7 mRNA is expressed at high levels in placenta, melanocytes, liver, lung, pancreas, and kidney. PTK7 is overexpressed in several cancers, including melanoma and colon cancer lines.


Pssm-ID: 143237  Cd Length: 77  Bit Score: 54.92  E-value: 1.12e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148237004  228 VVLSCDADGFPDPEISWLKKGEPIEDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQAGEA 291
Cdd:cd05760     1 VTLRCHIDGHPRPTYQWFRDGTPLSDGQGNYSVSSKERTLTLRSAGPDDSGLYYCCAHNAFGSV 64
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
39-108 1.13e-08

Immunoglobulin domain; 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, 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.


Pssm-ID: 319273  Cd Length: 70  Bit Score: 54.56  E-value: 1.13e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148237004   39 FLCQVSGEAT-DISWYspTGEKLVTQQQISVVRSDDYTSTLTIYNASSQDAGIYKCVASNEAeGESEGTVN 108
Cdd:cd00096     3 LTCSASGNPPpTITWL--KNGKPLPSSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSA-GSASASVT 70
I-set pfam07679
Immunoglobulin I-set domain;
303-388 3.12e-08

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 53.80  E-value: 3.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   303 PKITYV-ENKTAVELDEITLTCEASGDPIPSITWRTAVRNISSeattlDGHIVVKEHIRMSALTLKDIQYTDAGEYFCIA 381
Cdd:pfam07679    1 PKFTQKpKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRS-----SDRFKVTYEGGTYTLTISNVQPDDSGKYTCVA 75

                   ....*..
gi 148237004   382 SNPIGVD 388
Cdd:pfam07679   76 TNSAGEA 82
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
492-589 4.98e-08

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020  Cd Length: 93  Bit Score: 53.27  E-value: 4.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  492 DTPSSPAIRKVEpySSTVMIVFDEPDSTGGvPILKYKAEWRVIGHEKWHTkyYDAKEVNAESIiTVMGLKPETSYMVKLS 571
Cdd:cd00063     2 SPPTNLRVTDVT--STSVTLSWTPPEDDGG-PITGYVVEYREKGSGDWKE--VEVTPGSETSY-TLTGLKPGTEYEFRVR 75
                          90
                  ....*....|....*...
gi 148237004  572 AMNGKGLGDSTPSQEFTT 589
Cdd:cd00063    76 AVNGGGESPPSESVTVTT 93
Ig2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5 and similar proteins; ...
230-289 5.00e-08

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5 and similar proteins; Ig2_Follistatin_like: domain similar to 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: 143213  Cd Length: 76  Bit Score: 53.00  E-value: 5.00e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148237004  230 LSCDADGFPDPEISWLKKGEPI-EDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQAG 289
Cdd:cd05736     3 LRCHAEGIPLPRLTWLKNGMDItPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEAG 63
IGc2 smart00408
Immunoglobulin C-2 Type;
128-189 7.32e-08

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 52.02  E-value: 7.32e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148237004    128 EGEDAVIICDVSSSIPSIITWRHKGKDVifkKDVRFVVLANNYLQIRGIKKTDEGTYRCEGR 189
Cdd:smart00408    1 EGQSVTLTCPAEGNPVPNITWLKDGKPL---PESNRFVASGSTLTIKSVSLEDSGLYTCVAE 59
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; Ig4_Peroxidasin: the fourth ...
319-390 7.33e-08

Fourth immunoglobulin (Ig)-like domain of peroxidasin; Ig4_Peroxidasin: 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: 52.18  E-value: 7.33e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148237004  319 ITLTCEASGDPIPSITWrtavrNISSEATTLDGHIVVKEHirmSALTLKDIQYTDAGEYFCIASNPIG---VDMQ 390
Cdd:cd05746     1 VQIPCSAQGDPEPTITW-----NKDGVQVTESGKFHISPE---GYLAIRDVGVADQGRYECVARNTIGyasVSMV 67
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
21-97 8.72e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 52.12  E-value: 8.72e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148237004    21 EVNIVPDQGEISLGESKFFLCQVSGEAT-DISWYSPTGEklvtQQQISVVRSDDYTSTLTIYNASSQDAGIYKCVASN 97
Cdd:pfam13927    3 VITVSPSSVVVLEGESVTLTCEATGGPPpTITWYKNGKP----GPTSSRISLSGSNSTLTISNVTREDSGTYTCVASN 76
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
595-680 1.13e-07

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020  Cd Length: 93  Bit Score: 52.11  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  595 PSAPKLVGHLSEDGNSIKVDILKQDDGGSPIRHYLVNYRALNALEWKPEMRVPSNSHHVMLKALEWNVDYEVIVVAENQQ 674
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                  ....*.
gi 148237004  675 GKSKPA 680
Cdd:cd00063    81 GESPPS 86
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
121-187 1.69e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 316449  Cd Length: 76  Bit Score: 51.35  E-value: 1.69e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148237004   121 PTPQEFKEGEDAVIICDVSSSIPSIITWRHKGKDVIFKKDVRFvVLANNYLQIRGIKKTDEGTYRCE 187
Cdd:pfam13927    8 PSSVVVLEGESVTLTCEATGGPPPTITWYKNGKPGPTSSRISL-SGSNSTLTISNVTREDSGTYTCV 73
Ig2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
227-294 1.73e-07

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); Ig2_FGFRL1-like: 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: 143264  Cd Length: 82  Bit Score: 51.37  E-value: 1.73e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148237004  227 SVVLSCDADGFPDPEISWLKKGEPI---EDGEEKisfnEDQSEMTIHHVEKDDEAEYSCIANNQAGEAEAT 294
Cdd:cd05856    11 SVRLKCVASGNPRPDITWLKDNKPLtptEIGESR----KKKWTLSLKNLKPEDSGKYTCHVSNRAGEINAT 77
Ig3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; Ig3_Contactin-1: Third Ig domain of the ...
319-397 2.62e-07

Third immunoglobulin (Ig) domain of contactin-1; Ig3_Contactin-1: Third 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: 143259  Cd Length: 88  Bit Score: 50.79  E-value: 2.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  319 ITLTCEASGDPIPSITWRTAVRNISSEAttldghivvkeHIRMSALTLK--DIQYTDAGEYFCIASNPIGVDMQAMYFEV 396
Cdd:cd05851    19 VTLECFALGNPVPVIRWRKILEPMPATA-----------EISMSGAVLKifNIQPEDEGTYECEAENIKGKDKHQARVYV 87

                  .
gi 148237004  397 Q 397
Cdd:cd05851    88 Q 88
PHA02785 PHA02785
IL-beta-binding protein; Provisional
73-284 4.09e-07

IL-beta-binding protein; Provisional


Pssm-ID: 165149  Cd Length: 326  Bit Score: 53.10  E-value: 4.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   73 DYTSTLTIYNASSQDAGIYKCVASNEAEGE-----------SEGTVNLKIYqkltfknaptPQEFKEGEDAVIICD---- 137
Cdd:PHA02785   79 DNGSNMLILNPTQSDSGIYICITKNETYCDmmslnltivsvSESNIDLISY----------PQIVNERSTGEMVCPnina 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  138 -VSSSIPSIITWRHKGKdvifKKDVRFVVLANNYLQIRGIKKTDEGTYRCEGRILARGEInyKDIQVIVN-------VPP 209
Cdd:PHA02785  149 fIASNVNADIIWSGHRR----LRNKRLKQRTPGIITIEDVRKNDAGYYTCVLKYIYGDKT--YNVTRIVKlevrdriIPP 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  210 TIqarQLRVNATANMAESVVLSCDADGFP---DPEISWLKKG----EPIEDGEEKIS-----FNEDQ-----SEMTIHHV 272
Cdd:PHA02785  223 TM---QLPEGVVTSIGSNLTIACRVSLRPpttDADVFWISNGmyyeEDDEDGDGRISvankiYTTDKrrvitSRLNINPV 299
                         250
                  ....*....|..
gi 148237004  273 EKDDEAEYSCIA 284
Cdd:PHA02785  300 KEEDATTFTCMA 311
Ig3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar ...
228-299 5.01e-07

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar to 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, -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.


Pssm-ID: 143202  Cd Length: 69  Bit Score: 49.71  E-value: 5.01e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148237004  228 VVLSCDADGFPDPEISWLKkgepiEDGEEKISFNE--DQSEMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:cd05725     1 VEFQCEVGGDPVPTVLWRK-----EDGELPKGRAEilDDKSLKIRNVTAGDEGSYTCEAENMVGKIEASASLTV 69
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
399-484 6.50e-07

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 316418  Cd Length: 78  Bit Score: 49.68  E-value: 6.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   399 APKIRGPVVVYtWEGNPVNITCEVFAHPRAAVTWFRDGQLLPSS-NFSNIKiysgptssslevnpdSENDFGNYNCTAIN 477
Cdd:pfam13895    1 KPVLTPSPTVV-TEGEPVTLTCSAPGNPPANYTWYKGGEALNSSpNFISSV---------------SAEDSGTYTCVARN 64

                   ....*..
gi 148237004   478 TIGHEFS 484
Cdd:pfam13895   65 GRGGKVS 71
I-set pfam07679
Immunoglobulin I-set domain;
412-488 8.44e-07

Immunoglobulin I-set domain;


Pssm-ID: 254352  Cd Length: 90  Bit Score: 49.56  E-value: 8.44e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148237004   412 EGNPVNITCEVFAHPRAAVTWFRDGQLLPSSNFSNIKiYSGPTsSSLEVNPDSENDFGNYNCTAINTIGHEFSEFIL 488
Cdd:pfam07679   14 EGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVT-YEGGT-YTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; Ig5_Contactin_like: Fifth Ig domain of ...
227-299 9.52e-07

Fifth immunoglobulin (Ig) domain of contactin; Ig5_Contactin_like: Fifth 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 act ivity 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: 319278  Cd Length: 73  Bit Score: 48.98  E-value: 9.52e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148237004  227 SVVLSCDADGFPDPEISWLKKGEPIEDGEeKISFNEDQSeMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:cd04969     3 DVIIECKPKASPKPTISWSKGTELLTNSS-RICILPDGS-LKIKNVSKSDEGKYTCFAVNFFGKANSTGSLSV 73
Ig2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F, ...
232-298 1.89e-06

Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR; Ig2_RPTP_IIa_LAR_like: domain similar to 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: 319301  Cd Length: 74  Bit Score: 48.12  E-value: 1.89e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  232 CDADGFPDPEISWLKKGEPIEDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQAG---EAEATILLK 298
Cdd:cd05738     5 CAASGNPDPEITWFKDFLPVDTTSNGRIKQLRSGALQIENSEESDQGKYECVATNSAGtrySAPANLYVR 74
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; Ig4_Peroxidasin: the fourth ...
228-297 2.15e-06

Fourth immunoglobulin (Ig)-like domain of peroxidasin; Ig4_Peroxidasin: 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: 47.95  E-value: 2.15e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148237004  228 VVLSCDADGFPDPEISWLKKGEPI-EDGEEKISfneDQSEMTIHHVEKDDEAEYSCIANNQAGEAEATILL 297
Cdd:cd05746     1 VQIPCSAQGDPEPTITWNKDGVQVtESGKFHIS---PEGYLAIRDVGVADQGRYECVARNTIGYASVSMVL 68
Ig_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: ...
405-488 2.43e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: domain similar to the M5, fifth immunoglobulin (Ig)-like domain from the human titin C terminus. 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.


Pssm-ID: 143224  Cd Length: 92  Bit Score: 48.12  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  405 PVVVYTWEGNPVNITCEVFAHPRAAVTWFRDGQLLPSSnfSNIKIYSGPTSSSLEVNPDSENDFGNYNCTAINTIGHEFS 484
Cdd:cd05747    10 PRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSS--QRHQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEA 87

                  ....
gi 148237004  485 EFIL 488
Cdd:cd05747    88 QFTL 91
Ig3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; Ig3_Contactin_like: Third Ig domain of ...
319-389 2.99e-06

Third immunoglobulin (Ig) domain of contactin; Ig3_Contactin_like: Third 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 act ivity 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: 319277  Cd Length: 88  Bit Score: 47.93  E-value: 2.99e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148237004  319 ITLTCEASGDPIPSITWRTAVRNISSEATTLDGHIVVKehirmsaltLKDIQYTDAGEYFCIASNPIGVDM 389
Cdd:cd04968    19 VTLECFALGNPVPQIKWRKVDGSPSSQWTTSTSEPVLE---------IPNVQFEDEGTYECEAENSRGKDT 80
Ig2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; Ig2_FGFR: ...
225-299 3.25e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; Ig2_FGFR: 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, -2, -3, -4). 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: 143265  Cd Length: 85  Bit Score: 47.55  E-value: 3.25e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148237004  225 AESVVLSCDADGFPDPEISWLKKGEPIEdGEEKI---SFNEDQSEMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:cd05857     9 ANTVKFRCPAAGNPTPTMRWLKNGKEFK-QEHRIggyKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDV 85
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
226-299 4.93e-06

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); Ig4_L1-NrCAM_like: 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: 319284  Cd Length: 76  Bit Score: 47.07  E-value: 4.93e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148237004  226 ESVVLSCDADGFPDPEISWLKKGEPIEDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:cd04978     2 ETGELICEAEGNPQPTITWRLNGVPIEPAPEDMRRTVDGRTLIFSNLQPNDTAVYQCNASNVHGYLLANAFLHV 75
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
132-187 5.20e-06

Immunoglobulin domain; 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, 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.


Pssm-ID: 319273  Cd Length: 70  Bit Score: 46.85  E-value: 5.20e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 148237004  132 AVIICDVSSSIPSIITWRHKGKDVIFKKDVRFVVLANNY-LQIRGIKKTDEGTYRCE 187
Cdd:cd00096     1 VTLTCSASGNPPPTITWLKNGKPLPSSSRFRRRSSGGNGtLTISNVTPEDSGTYTCV 57
Ig2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor and similar ...
225-299 6.06e-06

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor and similar proteins; Ig2_FGFR_like: domain similar to 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, -2, -3, -4). 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: 319297  Cd Length: 85  Bit Score: 46.83  E-value: 6.06e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148237004  225 AESVVLSCDADGFPDPEISWLKKGEPI-EDGEEKISFNEDQS-EMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:cd05729     9 NTKVRLECGARGNPTPNITWLKDGKQKwKINVIRPTRVEEKGwVLIIRRAIPRDTGKYTCIVSNQYGTINHTYDVKV 85
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: ...
321-386 6.26e-06

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: domain similar to 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, or 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: 319298  Cd Length: 71  Bit Score: 46.65  E-value: 6.26e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148237004  321 LTCEASGDPIPSITWRTAVRNISSEATTLDGHivvkehirMSALTLKDIQYTDAGEYFCIASNPIG 386
Cdd:cd05731     3 LECIAEGLPTPDIRWIKLGGELPKGRTKFENF--------NKTLKIENVSEADSGEYQCTASNTMG 60
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); Ig_C5_MyBP_C: the ...
236-299 8.39e-06

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); Ig_C5_MyBP_C: the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP_C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP_C exist and are included in this group: cardiac(c), and fast and slow skeletal muscle (s) MyBP_C. cMYBP_C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 143302  Cd Length: 86  Bit Score: 46.38  E-value: 8.39e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148237004  236 GFPDPEISWLKKGEPIEDGEEKISFNE--DQSEMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:cd05894    21 GEPAPTVTWSRGDKAFTETEGRVRVESykDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86
Ig4_NrCAM cd05868
Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); Ig4_ ...
226-299 9.61e-06

Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); Ig4_ NrCAM: fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule). NrCAM 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. NrCAM is primarily expressed in the nervous system.


Pssm-ID: 143276  Cd Length: 76  Bit Score: 46.14  E-value: 9.61e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148237004  226 ESVVLSCDADGFPDPEISWLKKGEPIEDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:cd05868     2 EDGTLICRANGNPKPSISWLTNGVPIEIAPTDPSRKVDGDTIIFSKVQERSSAVYQCNASNEYGYLLANAFVNV 75
Ig_Palladin_C cd05893
C-terminal immunoglobulin (Ig)-like domain of palladin; Ig_Palladin_C: C-terminal ...
228-299 1.00e-05

C-terminal immunoglobulin (Ig)-like domain of palladin; Ig_Palladin_C: 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 (DIP, 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.


Pssm-ID: 143301  Cd Length: 75  Bit Score: 45.82  E-value: 1.00e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148237004  228 VVLSCDADGFPDPEISWLKKGEPIEDGEEKISFNEDQSE---MTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:cd05893     1 VRLECRVSGVPHPQIFWKKENESLTHNTDRVSMHQDNCGyicLLIQGATKEDAGWYTVSAKNEAGIVSCTARLDV 75
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
24-97 1.08e-05

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: 278476  Cd Length: 86  Bit Score: 46.03  E-value: 1.08e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148237004    24 IVPDQGEISLGESKFFLCQVSG--EATDISWYSpTGEKLVTQQQISVVRSDDYTSTLTIYNASSQDAGIYKCVASN 97
Cdd:pfam00047    1 SAPPTVTVLEGDSATLTCSASTgsPGPDVTWSK-EGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNN 75
IgC_MHC_I_alpha3 cd07698
Class I major histocompatibility complex (MHC) alpha chain immunoglobulin domain; ...
207-282 1.35e-05

Class I major histocompatibility complex (MHC) alpha chain immunoglobulin domain; IgC_MHC_I_alpha3; Immunoglobulin (Ig) domain of major histocompatibility complex (MHC) class I alpha chain. Class I MHC proteins bind antigenic peptide fragments and present them to CD8+ T lymphocytes. Class I molecules consist of a transmembrane alpha chain and a small chain called the beta2 microglobulin. The alpha chain contains three extracellular domains, two of which fold together to form the peptide-binding cleft (alpha1 and alpha2), and one which has an Ig fold (alpha3). Peptide binding to class I molecules occurs in the endoplasmic reticulum (ER) and involves both chaperones and dedicated factors to assist in peptide loading. Class I MHC molecules are expressed on most nucleated cells.


Pssm-ID: 143322  Cd Length: 93  Bit Score: 45.74  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  207 VPPTIqarqlRVNATANMAESVVLSCDADGF-PDP-EISWLKKGEPIEDGEEK--ISFNED---QSEMTIhHVEKDDEAE 279
Cdd:cd07698     1 VPPEV-----RVTRKRAPDGSLTLSCHATGFyPRDiEVTWLRDGEDSVDDVESgeILPNGDgtyQLWVTL-EVPPEDKAR 74

                  ...
gi 148237004  280 YSC 282
Cdd:cd07698    75 YSC 77
Ig_2 cd05764
Subgroup of the immunoglobulin (Ig) superfamily; Ig_2: subgroup of the immunoglobulin (Ig) ...
226-299 1.67e-05

Subgroup of the immunoglobulin (Ig) superfamily; Ig_2: 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. 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.


Pssm-ID: 143241  Cd Length: 74  Bit Score: 45.17  E-value: 1.67e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148237004  226 ESVVLSCDADGFPDPEISWLK-KGEPIEDGEEKISFNEDQSEMTIHHVEkdDEAEYSCIANNQAGEAEATILLKV 299
Cdd:cd05764     2 QRATLRCKARGDPEPAIHWISpDGKLISNSSRTLVYDNGTLDILITTVK--DTGSFTCIASNAAGEATATVELHI 74
PHA03247 PHA03247
large tegument protein UL36; Provisional
864-1048 1.69e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021  Cd Length: 3151  Bit Score: 49.17  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  864 QATPSKAEAPTTSSPPPTSSPKVAPLVDLSDTP----TNNPSKVVANQAGPLNPSAATSAAEPPTVIIKPVTTVPPNAAS 939
Cdd:PHA03247 2670 LGRAAQASSPPQRPRRRAARPTVGSLTSLADPPppppTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA 2749
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  940 PPPTPEPKQVKQEQSGTKSPEKEEAQPSTVknPTEATKDESASLSNTKPlqdedfqidggtfKTPEIDLAKDVFAALGTA 1019
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAPPAAPAAGP--PRRLTRPAVASLSESRE-------------SLPSPWDPADPPAAVLAP 2814
                         170       180
                  ....*....|....*....|....*....
gi 148237004 1020 TPTAVASGKASELVSSTAdTSVPLDSAKT 1048
Cdd:PHA03247 2815 AAALPPAASPAGPLPPPT-SAQPTAPPPP 2842
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2 and similar proteins; ...
219-299 2.04e-05

Fourth Ig domain of the neural cell adhesion molecule contactin-2 and similar proteins; Ig4_Contactin-2-like: 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 (aliases 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  Cd Length: 85  Bit Score: 45.28  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  219 NATANMAESVVLSCDADGFPDPEISWLKKGEPIEDgEEKISFneDQSEMTIHHVEKDDEAEYSCIANNQAGEAEATILLK 298
Cdd:cd05728     8 DTEADIGSSLRWECKASGNPRPAYRWLKNGQPLAS-ENRIEV--EAGDLRITKLSLSDSGMYQCVAENKHGTIYASAELA 84

                  .
gi 148237004  299 V 299
Cdd:cd05728    85 V 85
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar domains; Ig_Titin_like: immunoglobulin ...
236-299 2.11e-05

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


Pssm-ID: 319305  Cd Length: 74  Bit Score: 44.90  E-value: 2.11e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148237004  236 GFPDPEISWLKKGEPIE-DGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:cd05748    10 GRPTPTVTWSKDGQPLKlSGRVQIETTATSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATVNVKV 74
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
209-293 2.41e-05

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.


Pssm-ID: 311910  Cd Length: 89  Bit Score: 45.09  E-value: 2.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   209 PTIQARQLRVNataNMAESVVLSC-DADGFPDPEISWLKKGEPIEDGEEKISFNED------QSEMTIHHVEKDDEAEYS 281
Cdd:pfam08205    1 PEIEPPASLLE---GEGPEVVATCsSAGGKPAPRITWYLNGKPLEAAETSSEQDPEsglytvTSTLKLVPSRSDHGQSLT 77
                           90
                   ....*....|..
gi 148237004   282 CIANNQAGEAEA 293
Cdd:pfam08205   78 CQVSYPALRGPQ 89
fn3 pfam00041
Fibronectin type III domain;
495-582 2.47e-05

Fibronectin type III domain;


Pssm-ID: 306538  Cd Length: 85  Bit Score: 45.10  E-value: 2.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   495 SSPAIRKVEPYSSTVMIVFDEPDSTGGVPILKYKAEWRVIGHEKWHTKYydaKEVNAESIITVMGLKPETSYMVKLSAMN 574
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEI---TVPGTTTSVTLTGLKPGTEYEVRVQAVN 77

                   ....*...
gi 148237004   575 GKGLGDST 582
Cdd:pfam00041   78 GGGEGPPS 85
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; Ig5_Contactin-1: fifth Ig domain of the ...
228-299 2.64e-05

Fifth immunoglobulin (Ig) domain of contactin-1; Ig5_Contactin-1: fifth 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: 143260  Cd Length: 73  Bit Score: 44.63  E-value: 2.64e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148237004  228 VVLSCDADGFPDPEISWLKKGEPIEDGEeKISFNEDQSeMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:cd05852     4 VIIECKPKAAPKPKFSWSKGTELLVNNS-RISIWDDGS-LEILNITKLDEGSYTCFAENNRGKANSTGVLSV 73
Ig1_Robo cd07693
First immunoglobulin (Ig)-like domain in Robo (roundabout) receptors and similar proteins; ...
208-291 2.74e-05

First immunoglobulin (Ig)-like domain in Robo (roundabout) receptors and similar proteins; Ig1_Robo: domain similar to the first 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, -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.


Pssm-ID: 143317  Cd Length: 100  Bit Score: 44.84  E-value: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  208 PPTIQARQLRVNATANmaESVVLSCDADGFPDPEISWLKKGEPIEdgeekISFNEDQSEMT------------IHHVE-K 274
Cdd:cd07693     1 PPRIVEHPSDLIVSKG--DPATLNCKAEGRPTPTIQWLKNGQPLE-----TDKDDPRSHRIvlpsgslfflrvVHGRKgR 73
                          90
                  ....*....|....*..
gi 148237004  275 DDEAEYSCIANNQAGEA 291
Cdd:cd07693    74 SDEGVYVCVAHNSLGEA 90
Ig_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2); ...
405-482 2.89e-05

C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2); Ig_M-protein_C: the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains, and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 44.90  E-value: 2.89e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148237004  405 PVVVYTWEGNPVNITCEVFAHPRAAVTWFRDGQLLPSSNFSNIKIYSGpTSSSLEVNPDSENDFGNYNCTAINTIGHE 482
Cdd:cd05891     8 PDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSEHYSVKLEQG-KYASLTIKGVTSEDSGKYSINVKNKYGGE 84
Ig3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar ...
319-386 4.17e-05

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar to 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, -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.


Pssm-ID: 143202  Cd Length: 69  Bit Score: 43.93  E-value: 4.17e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237004  319 ITLTCEASGDPIPSITWRTAVRNIS-SEATTLDGHivvkehirmsALTLKDIQYTDAGEYFCIASNPIG 386
Cdd:cd05725     1 VEFQCEVGGDPVPTVLWRKEDGELPkGRAEILDDK----------SLKIRNVTAGDEGSYTCEAENMVG 59
Ig_Myomesin_like_C cd05737
C-temrinal immunoglobulin (Ig)-like domain of myomesin and M-protein; Ig_Myomesin_like_C: ...
402-486 4.25e-05

C-temrinal immunoglobulin (Ig)-like domain of myomesin and M-protein; Ig_Myomesin_like_C: domain similar to the C-temrinal immunoglobulin (Ig)-like domain of myomesin and M-protein. Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 44.12  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  402 IRG-PVVVYTWEGNPVNITCEVFAHPRAAVTWFRDGQLLPSSNFSNIKIYSGPTsSSLEVNPDSENDFGNYNCTAINTIG 480
Cdd:cd05737     4 LGGlPDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRT-VYFTINGVSSEDSGKYGLVVKNKYG 82

                  ....*.
gi 148237004  481 HEFSEF 486
Cdd:cd05737    83 SETSDV 88
Ig_NCAM-2 cd05870
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM ...
215-299 5.11e-05

Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM); Ig_NCAM-2: immunoglobulin (Ig)-like domain similar to the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is organized similarly to NCAM , including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule.


Pssm-ID: 143278  Cd Length: 98  Bit Score: 44.20  E-value: 5.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  215 QLRvNATANMAESVVLSCDADGFPDPEISW--------LKKGEPIEDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANN 286
Cdd:cd05870     7 QLK-NETTVENGAATLSCKAEGEPIPEITWkrasdghtFSEGDKSPDGRIEVKGQHGESSLHIKDVKLSDSGRYDCEAAS 85
                          90
                  ....*....|...
gi 148237004  287 QAGEAEATILLKV 299
Cdd:cd05870    86 RIGGHQKSMYLDI 98
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM: ...
228-294 5.26e-05

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM: 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, 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, or 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: 143284  Cd Length: 71  Bit Score: 43.76  E-value: 5.26e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148237004  228 VVLSCDADGFPDPEISWLKKGEPIEDGEEKISFNedQSEMTIHHVEKDDEAEYSCIANNQAGEAEAT 294
Cdd:cd05876     1 LVLECIAEGLPTPEVHWDRIDGPLSPNRTKKLNN--NKTLQLDNVLESDDGEYVCTAENSEGSARHH 65
Ig2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig2_Robo: domain ...
425-485 5.40e-05

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig2_Robo: domain similar to 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 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.


Pssm-ID: 143201  Cd Length: 86  Bit Score: 43.92  E-value: 5.40e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148237004  425 HPRAAVTWFRDGQLLPSSNfSNIKIYSGptsSSLEVNPDSENDFGNYNCTAINTIGHEFSE 485
Cdd:cd05724    24 HPEPTVSWRKDGQPLNLDN-ERVRIVDD---GNLLIAEARKSDEGTYKCVATNMVGERESA 80
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
494-579 5.89e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495  Cd Length: 83  Bit Score: 43.76  E-value: 5.89e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004    494 PSSPAIRKVEPYSST-VMIVFDEPDSTGGV-PILKYKAEWRVIGHEkWHTkyydAKEVNAESIITVMGLKPETSYMVKLS 571
Cdd:smart00060    1 PSPPSNLRVTDVTSTsVTLSWEPPPDDGITgYIVGYRVEYREEGSE-WKE----VNVTPSSTSYTLTGLKPGTEYEFRVR 75

                    ....*...
gi 148237004    572 AMNGKGLG 579
Cdd:smart00060   76 AVNGAGEG 83
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
120-189 6.88e-05

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: 278476  Cd Length: 86  Bit Score: 43.72  E-value: 6.88e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148237004   120 APTPQEFKEGEDAVIICDVSSSIPS-IITWRHKGKdviFKKDVRFVVLANNY-----LQIRGIKKTDEGTYRCEGR 189
Cdd:pfam00047    2 APPTVTVLEGDSATLTCSASTGSPGpDVTWSKEGG---TLIESLKVKHDNGRttqssLLISNVTKEDAGTYTCVVN 74
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
317-388 7.95e-05

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: 278476  Cd Length: 86  Bit Score: 43.34  E-value: 7.95e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148237004   317 DEITLTCEAS-GDPIPSITWRtavRNISSEATTLDGHIVVKEHIRMSaLTLKDIQYTDAGEYFCIASNPIGVD 388
Cdd:pfam00047   12 DSATLTCSAStGSPGPDVTWS---KEGGTLIESLKVKHDNGRTTQSS-LLISNVTKEDAGTYTCVVNNPGGPA 80
IgV cd00099
Immunoglobulin variable domain (IgV); IgV: Immunoglobulin variable domain (IgV). Members of ...
32-96 9.48e-05

Immunoglobulin variable domain (IgV); IgV: Immunoglobulin variable domain (IgV). Members of the IgV family are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 319275  Cd Length: 103  Bit Score: 43.16  E-value: 9.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   32 SLGESKFFLCQVSGE--ATDISWY---SPTGEKLVTQQQ----------ISVVRSDDYTS-TLTIYNASSQDAGIYKCVA 95
Cdd:cd00099     4 STGESVTLNCVLSGSfsLYSISWYrqkPGKQPQFLISGSstgkpgipgrFSGTRNGGSSSfSLTISNLRPEDSGTYYCAV 83

                  .
gi 148237004   96 S 96
Cdd:cd00099    84 S 84
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7, also known as CCK4; ...
416-492 1.08e-04

Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7, also known as CCK4; Ig2_PTK7: domain similar to the second immunoglobulin (Ig)-like domain in protein tyrosine kinase (PTK) 7, also known as CCK4. PTK7 is a subfamily of the receptor protein tyrosine kinase family, and is referred to as an RPTK-like molecule. RPTKs transduce extracellular signals across the cell membrane, and play important roles in regulating cell proliferation, migration, and differentiation. PTK7 is organized as an extracellular portion having seven Ig-like domains, a single transmembrane region, and a cytoplasmic tyrosine kinase-like domain. PTK7 is considered a pseudokinase as it has several unusual residues in some of the highly conserved tyrosine kinase (TK) motifs; it is predicted to lack TK activity. PTK7 may function as a cell-adhesion molecule. PTK7 mRNA is expressed at high levels in placenta, melanocytes, liver, lung, pancreas, and kidney. PTK7 is overexpressed in several cancers, including melanoma and colon cancer lines.


Pssm-ID: 143237  Cd Length: 77  Bit Score: 42.98  E-value: 1.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237004  416 VNITCEVFAHPRAAVTWFRDGQLLPSSNfSNIKIYSgpTSSSLEVNPDSENDFGNYNCTAINTIGHEFSE--FILVQAD 492
Cdd:cd05760     1 VTLRCHIDGHPRPTYQWFRDGTPLSDGQ-GNYSVSS--KERTLTLRSAGPDDSGLYYCCAHNAFGSVCSSqnFTLSIID 76
Ig2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5 and similar proteins; ...
320-388 1.11e-04

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5 and similar proteins; Ig2_Follistatin_like: domain similar to 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: 143213  Cd Length: 76  Bit Score: 42.98  E-value: 1.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148237004  320 TLTCEASGDPIPSITWRTAVRNIS---SEATTLDGHivvkehirMSALTLKDIQYTDAGEYFCIASNPIGVD 388
Cdd:cd05736     2 SLRCHAEGIPLPRLTWLKNGMDITpklSKQLTLIAN--------GSELHISNVRYEDTGAYTCIAKNEAGVD 65
PRK14960 PRK14960
DNA polymerase III subunits gamma and tau; Provisional
907-1078 1.39e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237868  Cd Length: 702  Bit Score: 45.81  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  907 QAGPLNPSAATSAAEPPTVIIKPVTTVPPNAASPPPTPEPKQ---VKQEQSGTKSPEKEEAQPSTVKNPT--EATKDESA 981
Cdd:PRK14960  385 QAQTAQEITPVSAVQPVEVISQPAMVEPEPEPEPEPEPEPEPepePEPEPEPEPEPEPQPNQDLMVFDPNhhELIGLESA 464
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  982 SLSNTKPLQDEDFqidggtFKTPEIDLAK-DVFAALGTATPTAVASGKASELV-SSTADTSVPLDSAKTEKTQ--VEEKS 1057
Cdd:PRK14960  465 VVQETVSVLEEDF------IPVPEQKLVQvQAETQVKQIEPEPASTAEPIGLFeASSAEFSLAQDTSAYDLVSepVIEQQ 538
                         170       180
                  ....*....|....*....|.
gi 148237004 1058 KPEEIDVKGTPAEVKtVPNEA 1078
Cdd:PRK14960  539 SLVQAEIVETVAVVK-EPNAT 558
Ig2_KIRREL3-like cd05759
Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known ...
415-477 1.76e-04

Second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2); Ig2_KIRREL3-like: domain similar to the second immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (Neph1), Kirrel2 (Neph3), and Drosophila RST (irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development.


Pssm-ID: 143236  Cd Length: 82  Bit Score: 42.43  E-value: 1.76e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148237004  415 PVNITCEVF-AHPRAAVTWFRDGQLLPSSNFSNIKIYSG---PTSSSLEVNPDSENDFGNYNCTAIN 477
Cdd:cd05759     1 PYNLTCRARgAKPAAEIIWFRDGEVLDGATYSKELLKDGkreTTVSTLPITPSDHDTGRTFTCRARN 67
Ig2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
319-386 1.84e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); Ig2_FGFRL1-like: 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: 143264  Cd Length: 82  Bit Score: 42.13  E-value: 1.84e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148237004  319 ITLTCEASGDPIPSITWRTavrnisseattlDGHIVVKEHIRMS-----ALTLKDIQYTDAGEYFCIASNPIG 386
Cdd:cd05856    12 VRLKCVASGNPRPDITWLK------------DNKPLTPTEIGESrkkkwTLSLKNLKPEDSGKYTCHVSNRAG 72
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
320-386 1.89e-04

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); Ig4_L1-NrCAM_like: 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: 319284  Cd Length: 76  Bit Score: 42.06  E-value: 1.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148237004  320 TLTCEASGDPIPSITWRTAVRNIssEATTLDGHIVVkehiRMSALTLKDIQYTDAGEYFCIASNPIG 386
Cdd:cd04978     5 ELICEAEGNPQPTITWRLNGVPI--EPAPEDMRRTV----DGRTLIFSNLQPNDTAVYQCNASNVHG 65
AflR pfam08493
Aflatoxin regulatory protein; This domain is found in the aflatoxin regulatory protein (AflR) ...
892-1041 1.91e-04

Aflatoxin regulatory protein; This domain is found in the aflatoxin regulatory protein (AflR) which is involved in the regulation of the biosynthesis of aflatoxin in the fungal genus Aspergillus. It occurs together with the fungal Zn(2)-Cys(6) binuclear cluster domain (pfam00172).


Pssm-ID: 285666  Cd Length: 275  Bit Score: 44.61  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   892 LSDTPTNNPSKVVANQAGPLNPSAATSAAEPPTVIIKPVTTVPPNAASPPPTPEPkqVKQEQSGTKSPEKEEAQPSTVKN 971
Cdd:pfam08493    7 TTISPPANTGANTTSSVLPSNPVTSGQSQTPLNAPITPNPTSSVSAIFSHPSPKP--CIETQGQTPDLWGSILSPSASFT 84
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148237004   972 PTEAtkDESASLSNTKPLQDEDFQIDGGT--FKTPEIDLAKDVFAALGTATPTA------VASGKASELVSSTADTSV 1041
Cdd:pfam08493   85 PDVS--SLSGSLTSMPTDVGSLFASPMGLplFDTCDIDSLPPEAAGEHPLFPTSalssppNARASPSSDTTSTTDNHP 160
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
595-677 1.92e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495  Cd Length: 83  Bit Score: 42.22  E-value: 1.92e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004    595 PSAPKLVGHLSEDGNSIKV--DILKQDDGGSPIRHYLVNYRALNAlEWKpEMRVPSNSHHVMLKALEWNVDYEVIVVAEN 672
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLswEPPPDDGITGYIVGYRVEYREEGS-EWK-EVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ....*
gi 148237004    673 QQGKS 677
Cdd:smart00060   79 GAGEG 83
PRK12323 PRK12323
DNA polymerase III subunits gamma and tau; Provisional
848-1040 2.02e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237057  Cd Length: 700  Bit Score: 45.25  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  848 APPPTTAPDSNTIQSIQATPSKAEAPTTSSPPPTSSPKVAPLVDLSDTPTNNPSKvVANQAGPLNPSAAtsAAEPPTVII 927
Cdd:PRK12323  380 APVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALA-AARQASARGPGGA--PAPAPAPAA 456
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  928 KPVTTVPPNAASPPPTP---EPKQVKQEQSGTKSPEKE-----EAQPSTVKNPTEATKDESASLSNTKPLQDEDFQIDGG 999
Cdd:PRK12323  457 APAAAARPAAAGPRPVAaaaAAAPARAAPAAAPAPADDdpppwEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDD 536
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 148237004 1000 TFKTPEIDLAKDVFAALGTATPTAVASGKASELVSSTADTS 1040
Cdd:PRK12323  537 AFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMF 577
Ig_3 cd05765
Subgroup of the immunoglobulin (Ig) superfamily; Ig_3: subgroup of the immunoglobulin (Ig) ...
34-99 2.07e-04

Subgroup of the immunoglobulin (Ig) superfamily; Ig_3: 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. 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.


Pssm-ID: 143242  Cd Length: 81  Bit Score: 42.14  E-value: 2.07e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148237004   34 GESKFFLCQVSGEAT-DISW--YSPTGEKLV---TQQQISVVRSDdyTSTLTIYNASSQDAGIYKCVASNEA 99
Cdd:cd05765     1 GETASFHCDVTGRPPpEITWekQVHGKENLImrpNHVRGNVVVTN--IGQLVIYNAQPQDAGLYTCTARNSG 70
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig4_L1-CAM_like: ...
321-386 2.14e-04

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig4_L1-CAM_like: 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, or 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: 143275  Cd Length: 76  Bit Score: 41.79  E-value: 2.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148237004  321 LTCEASGDPIPSITWRtaVRNISSEATTLDGhivvKEHIRMSALTLKDIQYTDAGEYFCIASNPIG 386
Cdd:cd05867     6 LDCQVEGIPTPNITWS--INGAPIEGTDPDP----RRHVSSGALILTDVQPSDTAVYQCEARNRHG 65
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins (NRGs); Ig_Pro_neuregulin: immunoglobulin (Ig) ...
420-480 2.28e-04

Immunoglobulin (Ig)-like domain in neuregulins (NRGs); Ig_Pro_neuregulin: immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules, which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG1, -2, -3, and -4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions; for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors; in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms, which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and -3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 143227  Cd Length: 75  Bit Score: 41.75  E-value: 2.28e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148237004  420 CEVFA-HPRAAVTWFRDGQLLPSSN-FSNIKIYSGPTSSSLEVNPDSENDFGNYNCTAINTIG 480
Cdd:cd05750     5 CEATSeYPSLRFKWFKDGKELNRKNkPRNIKIRNKKKNSELQINKAKLADSGEYTCVVENILG 67
Ig_2 cd05764
Subgroup of the immunoglobulin (Ig) superfamily; Ig_2: subgroup of the immunoglobulin (Ig) ...
41-111 2.62e-04

Subgroup of the immunoglobulin (Ig) superfamily; Ig_2: 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. 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.


Pssm-ID: 143241  Cd Length: 74  Bit Score: 41.70  E-value: 2.62e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148237004   41 CQVSGE-ATDISWYSPTGeKLVTQQQISVVRSDdytSTLTIYNASSQDAGIYKCVASNEAeGESEGTVNLKI 111
Cdd:cd05764     8 CKARGDpEPAIHWISPDG-KLISNSSRTLVYDN---GTLDILITTVKDTGSFTCIASNAA-GEATATVELHI 74
Ig_1 cd05763
Subgroup of the immunoglobulin (Ig) superfamily; Ig_1: subgroup of the immunoglobulin (Ig) ...
230-299 2.69e-04

Subgroup of the immunoglobulin (Ig) superfamily; Ig_1: 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. 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.


Pssm-ID: 143240  Cd Length: 75  Bit Score: 41.84  E-value: 2.69e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148237004  230 LSCDADGFPDPEISWLKKGE---PIEDgEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:cd05763     3 LECAATGHPTPQIAWQKDGGtdfPAAR-ERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNTAGSISANATLTV 74
Ig_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: ...
26-109 2.95e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: domain similar to the M5, fifth immunoglobulin (Ig)-like domain from the human titin C terminus. 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.


Pssm-ID: 143224  Cd Length: 92  Bit Score: 41.57  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   26 PDQGEISLGESKFFLCQVSGE-ATDISWYSpTGEKLVTQQQISVVRSdDYTSTLTIYNASSQDAGIYKCVASNeAEGESE 104
Cdd:cd05747    10 PRSLTVSEGESARFSCDVDGEpAPTVTWMR-EGQIIVSSQRHQITST-EYKSTFEISKVQMSDEGNYTVVVEN-SEGKQE 86

                  ....*
gi 148237004  105 GTVNL 109
Cdd:cd05747    87 AQFTL 91
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2 and similar proteins; ...
25-98 3.18e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2 and similar proteins; Ig4_Contactin-2-like: 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 (aliases 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  Cd Length: 85  Bit Score: 41.43  E-value: 3.18e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148237004   25 VPDQGEISLGESKFFLCQVSGEATDISWYSPTGEKLVTQQQISVVrsddyTSTLTIYNASSQDAGIYKCVASNE 98
Cdd:cd05728     5 VISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVE-----AGDLRITKLSLSDSGMYQCVAENK 73
IGc2 smart00408
Immunoglobulin C-2 Type;
34-99 3.39e-04

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 41.24  E-value: 3.39e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148237004     34 GESKFFLCQVSGEAT-DISWYSPtGEKLVTQQQISVVRSddytsTLTIYNASSQDAGIYKCVASNEA 99
Cdd:smart00408    2 GQSVTLTCPAEGNPVpNITWLKD-GKPLPESNRFVASGS-----TLTIKSVSLEDSGLYTCVAENSA 62
Ig3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; Ig3_Contactin-1: Third Ig domain of the ...
222-289 3.60e-04

Third immunoglobulin (Ig) domain of contactin-1; Ig3_Contactin-1: Third 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: 143259  Cd Length: 88  Bit Score: 41.55  E-value: 3.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148237004  222 ANMAESVVLSCDADGFPDPEISWLKKGEPIEDGEEkISFNedQSEMTIHHVEKDDEAEYSCIANNQAG 289
Cdd:cd05851    13 ALKGQNVTLECFALGNPVPVIRWRKILEPMPATAE-ISMS--GAVLKIFNIQPEDEGTYECEAENIKG 77
Ig4_Neogenin cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig4_Neogenin: fourth ...
228-297 4.31e-04

Fourth immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig4_Neogenin: fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC, which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain.


Pssm-ID: 212460  Cd Length: 71  Bit Score: 41.10  E-value: 4.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  228 VVLSCDADGFPDPEISWLKKGEPIEDgEEKISFNEDQSEMTIHHVeKDDEAEYSCIANNQAGEAEATILL 297
Cdd:cd05723     2 IVFECEVTGKPTPTVKWVKNGDMVIP-SDYFKIVKEHNLQVLGLV-KSDEGFYQCIAENDVGNVQAGAQL 69
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: ...
41-97 4.31e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: domain similar to 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, or 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: 319298  Cd Length: 71  Bit Score: 40.88  E-value: 4.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 148237004   41 CQVSGEAT-DISWYSPTGEKLVTQQQIsvvrsDDYTSTLTIYNASSQDAGIYKCVASN 97
Cdd:cd05731     5 CIAEGLPTpDIRWIKLGGELPKGRTKF-----ENFNKTLKIENVSEADSGEYQCTASN 57
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig4_L1-CAM_like: ...
226-289 4.82e-04

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig4_L1-CAM_like: 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, or 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: 143275  Cd Length: 76  Bit Score: 41.02  E-value: 4.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148237004  226 ESVVLSCDADGFPDPEISWLKKGEPIEDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQAG 289
Cdd:cd05867     2 ETARLDCQVEGIPTPNITWSINGAPIEGTDPDPRRHVSSGALILTDVQPSDTAVYQCEARNRHG 65
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
319-386 4.82e-04

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar domains; Ig_Perlecan_like: the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar domains. 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: 40.94  E-value: 4.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148237004  319 ITLTCEASGDPIPSITWRTAVRNISSEAttldgHIVVKEHIRMSALTLKDIQYTDAGEYFCIASNPIG 386
Cdd:cd05743     4 VEFTCVATGVPTPIINWRLNWGHVPDSA-----RVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRG 66
Ig3_FGFR-2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); ...
319-396 4.95e-04

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); Ig3_FGFR-2-like; domain similar to 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.


Pssm-ID: 143266  Cd Length: 90  Bit Score: 41.07  E-value: 4.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  319 ITLTCEASGDPIPSITWRTAVRNISSEATTlDGHIVVK---------EHIRMSALTLKDIQYTDAGEYFCIASNPIGVDM 389
Cdd:cd05858     4 VEFVCKVYSDAQPHIQWLKHVEKNGSKYGP-DGLPYVTvlktagvntTDKEMEVLYLRNVTFEDAGEYTCLAGNSIGISH 82

                  ....*..
gi 148237004  390 QAMYFEV 396
Cdd:cd05858    83 HSAWLTV 89
Ig1_NCAM-2 cd05866
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; Ig1_NCAM-2: ...
223-300 5.09e-04

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; Ig1_NCAM-2: first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2 (OCAM/mamFas II, RNCAM). NCAM-2 is organized similarly to NCAM-1, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule.


Pssm-ID: 143274  Cd Length: 92  Bit Score: 40.78  E-value: 5.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  223 NMAESVVLSCDADGFPDpEISWLK-KGEPIEDGEEKISFNED-QSEMTIHHVEKDDEAEYSCIANNQAGEA-EATILLKV 299
Cdd:cd05866    13 SVGESKFFTCTAIGEPE-SIDWYNpQGEKIVSSQRVVVQKEGvRSRLTIYNANIEDAGIYRCQATDAKGQTqEATVVLEI 91

                  .
gi 148237004  300 Y 300
Cdd:cd05866    92 Y 92
Ig2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F, ...
320-386 5.18e-04

Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR; Ig2_RPTP_IIa_LAR_like: domain similar to 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: 319301  Cd Length: 74  Bit Score: 40.80  E-value: 5.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148237004  320 TLTCEASGDPIPSITWrtaVRNISSEATTLDGHIvvkEHIRMSALTLKDIQYTDAGEYFCIASNPIG 386
Cdd:cd05738     2 TMLCAASGNPDPEITW---FKDFLPVDTTSNGRI---KQLRSGALQIENSEESDQGKYECVATNSAG 62
Ig3_NCAM-1_like cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); ...
33-114 5.36e-04

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig3_NCAM-1_like: domain similar to the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM). 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  Cd Length: 95  Bit Score: 40.69  E-value: 5.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   33 LGESKFFLCQVSGEATDISWYSPTGEKLVTQQQISVVRSDdyTSTLTIYNASSQDAGIYKCVASNEAeGESEGTVNLKIY 112
Cdd:cd05730    17 LGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSFNED--GSEMTILDVDKLDEAEYTCIAENKA-GEQEAEIHLKVF 93

                  ..
gi 148237004  113 QK 114
Cdd:cd05730    94 AK 95
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
73-205 5.60e-04

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173  Cd Length: 227  Bit Score: 42.59  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   73 DYTSTLTIYNASSQDAGIYKCVASNEAEGEsEGTVnlkiyqKLTFKNAPTPQEFKEGEDAVIICDVSSSIPS-----IIT 147
Cdd:PHA02826   95 DRSENLWIGNVINIDEGIYICTISSGNICE-ESTI------RLTFDSGTINYQFNSGKDSKLHCYGTDGISStfkdyTLT 167
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148237004  148 WRHKGkDVIFKKDvRFVVLANNY-LQIRGIKKTDEGTYRCEGRIlARGEINY---KDIQVIV 205
Cdd:PHA02826  168 WYKNG-NIVLYTD-RIQLRNNNStLVIKSATHDDSGIYTCNLRF-NKNSNNYnitKEYKVTI 226
Ig_L1-CAM_like cd05733
Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; ...
228-291 6.00e-04

Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; Ig_L1-CAM_like: domain similar to the first 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, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains NrCAM [Ng(neuronglia)CAM-related cell adhesion molecule], which is primarily expressed in the nervous system, and human neurofascin.


Pssm-ID: 319299  Cd Length: 77  Bit Score: 40.50  E-value: 6.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237004  228 VVLSCDADGFPDPEISWLKKGEPIE-DGEEKISFNEDQSEMTIH----HVEKDDEAEYSCIANNQAGEA 291
Cdd:cd05733     1 IVLKCEAKGNPPPTFSWTKDGKHFDpEKDPSVSMKRDSGTFVISnhngNAAKDYQGKYRCYASNELGTA 69
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2 and similar proteins; ...
420-480 6.16e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2 and similar proteins; Ig4_Contactin-2-like: 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 (aliases 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  Cd Length: 85  Bit Score: 40.66  E-value: 6.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148237004  420 CEVFAHPRAAVTWFRDGQLLPSSNfsNIKIYSGPTSSSLEVNPDSendfGNYNCTAINTIG 480
Cdd:cd05728    21 CKASGNPRPAYRWLKNGQPLASEN--RIEVEAGDLRITKLSLSDS----GMYQCVAENKHG 75
Ig2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F, ...
418-484 6.26e-04

Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR; Ig2_RPTP_IIa_LAR_like: domain similar to 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: 319301  Cd Length: 74  Bit Score: 40.42  E-value: 6.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148237004  418 ITCEVFAHPRAAVTWFRDgqLLPSSNFSNIKIySGPTSSSLEVNPDSENDFGNYNCTAINTIGHEFS 484
Cdd:cd05738     3 MLCAASGNPDPEITWFKD--FLPVDTTSNGRI-KQLRSGALQIENSEESDQGKYECVATNSAGTRYS 66
Ig_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; Ig_Myotilin_C: C-terminal ...
228-299 7.32e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; Ig_Myotilin_C: 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 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.


Pssm-ID: 143300  Cd Length: 75  Bit Score: 40.32  E-value: 7.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148237004  228 VVLSCDADGFPDPEISWLKKGEPIEDGEEKISFNEDQS---EMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:cd05892     1 VKLECQISAIPPPKIFWKRNNEMVQYNTDRISLYQDNSgrvTLLIKNVNKKDAGWYTVSAVNEAGVATCHARLDV 75
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins (NRGs); Ig_Pro_neuregulin: immunoglobulin (Ig) ...
229-294 8.43e-04

Immunoglobulin (Ig)-like domain in neuregulins (NRGs); Ig_Pro_neuregulin: immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules, which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG1, -2, -3, and -4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions; for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors; in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms, which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and -3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 143227  Cd Length: 75  Bit Score: 40.20  E-value: 8.43e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148237004  229 VLSCDADG-FPDPEISWLKKGEPIEDGEE----KISFNEDQSEMTIHHVEKDDEAEYSCIANNQAGEAEAT 294
Cdd:cd05750     2 VLKCEATSeYPSLRFKWFKDGKELNRKNKprniKIRNKKKNSELQINKAKLADSGEYTCVVENILGNDTVT 72
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
226-286 8.81e-04

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


Pssm-ID: 278476  Cd Length: 86  Bit Score: 40.25  E-value: 8.81e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148237004   226 ESVVLSCDADGF-PDPEISWLKKGEPIEDGEEKISFNED--QSEMTIHHVEKDDEAEYSCIANN 286
Cdd:pfam00047   12 DSATLTCSASTGsPGPDVTWSKEGGTLIESLKVKHDNGRttQSSLLISNVTKEDAGTYTCVVNN 75
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
302-397 8.90e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 316418  Cd Length: 78  Bit Score: 40.05  E-value: 8.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   302 KPKITyVENKTAVELDEITLTCEASGDPIPSITWRtavrnisseattLDGHIVVKEHIrmsalTLKDIQYTDAGEYFCIA 381
Cdd:pfam13895    1 KPVLT-PSPTVVTEGEPVTLTCSAPGNPPANYTWY------------KGGEALNSSPN-----FISSVSAEDSGTYTCVA 62
                           90
                   ....*....|....*.
gi 148237004   382 SNPiGVDMQAMYFEVQ 397
Cdd:pfam13895   63 RNG-RGGKVSNPVELT 77
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
226-289 9.04e-04

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar domains; Ig_Perlecan_like: the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar domains. 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: 40.17  E-value: 9.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148237004  226 ESVVLSCDADGFPDPEISWLKKGEPIEDGEEKISFNED-QSEMTIHHVEKDDEAEYSCIANNQAG 289
Cdd:cd05743     2 ETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGgYGTLTIRDVKESDQGAYTCEAINTRG 66
Ig_2 cd05764
Subgroup of the immunoglobulin (Ig) superfamily; Ig_2: subgroup of the immunoglobulin (Ig) ...
320-386 1.04e-03

Subgroup of the immunoglobulin (Ig) superfamily; Ig_2: 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. 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.


Pssm-ID: 143241  Cd Length: 74  Bit Score: 39.78  E-value: 1.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148237004  320 TLTCEASGDPIPSITWRT--------AVRNISSEATTLDGHIVvkehirmsalTLKdiqytDAGEYFCIASNPIG 386
Cdd:cd05764     5 TLRCKARGDPEPAIHWISpdgklisnSSRTLVYDNGTLDILIT----------TVK-----DTGSFTCIASNAAG 64
Ig4_PDGFR cd05859
Fourth immunoglobulin (Ig)-like domain of platelet-derived growth factor receptor (PDGFR); ...
219-299 1.05e-03

Fourth immunoglobulin (Ig)-like domain of platelet-derived growth factor receptor (PDGFR); IG4_PDGFR: The fourth immunoglobulin (Ig)-like domain of platelet-derived growth factor receptor (PDGFR) alpha and beta. PDGF is a potent mitogen for connective tissue cells. PDGF-stimulated processes are mediated by three different PDGFs (PDGF-A,-B, and C). PDGFR alpha binds to all three PDGFs, whereas the PDGFR beta binds only to PDGF-B. PDGF alpha is organized as an extracellular component having five Ig-like domains, a transmembrane segment, and a cytoplasmic portion having protein tyrosine kinase activity. In mice, PDGFR alpha and PDGFR beta are essential for normal development.


Pssm-ID: 143267  Cd Length: 101  Bit Score: 39.85  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  219 NATANMAESVVLSCDADGFPDPEISWLKKGEP-------IEDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQAGEA 291
Cdd:cd05859    12 LEFANLHEVKEFVVEVEAYPPPQIRWLKDNRTlienlteITTSEHNVQETRYVSKLKLIRAKEEDSGLYTALAQNEDAVK 91

                  ....*...
gi 148237004  292 EATILLKV 299
Cdd:cd05859    92 SYTFALQI 99
Ig_Myomesin_like_C cd05737
C-temrinal immunoglobulin (Ig)-like domain of myomesin and M-protein; Ig_Myomesin_like_C: ...
220-299 1.14e-03

C-temrinal immunoglobulin (Ig)-like domain of myomesin and M-protein; Ig_Myomesin_like_C: domain similar to the C-temrinal immunoglobulin (Ig)-like domain of myomesin and M-protein. Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 39.88  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  220 ATANMAESVVLSCDADGFPDPEISWLKKGEPIEDGEEKISFNEDQSE--MTIHHVEKDDEAEYSCIANNQAGEAEATILL 297
Cdd:cd05737    11 VTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLDHCNLKVEAGRTvyFTINGVSSEDSGKYGLVVKNKYGSETSDVTV 90

                  ..
gi 148237004  298 KV 299
Cdd:cd05737    91 SV 92
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
747-1075 1.14e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904  Cd Length: 886  Bit Score: 42.98  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   747 AGPGAKGKDIEEGKAAFSKDESKEPIVEVRTEEERT--PNHDGSNQIEPNETTPLTE----PEHPAAVEDMLPSVTT--V 818
Cdd:pfam05109  394 SGLGTAPKTLIITRTATNATTTTHKVIFSKAPESTTtsPTLNTTGFAAPNTTTGLPSsthvPTNLTAPASTGPTVSTadV 473
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   819 TTNSDTITETFATAQNSPTSETTTLTSSTAPPPTTAPDSNTIQSIQAT-PSKAEAPTTSSPPPTSSPKVAPLVDLSdTPT 897
Cdd:pfam05109  474 TSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATsPTPAVTTPTPNATSPTLGKTSPTSAVT-TPT 552
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   898 NNPSKVVANQAGPL-NPSAATSAAEPPTviiKPVTTVPPNAASPP---PTPEPKQVKQEQSGTKSPEKEEAQPstvKNPT 973
Cdd:pfam05109  553 PNATSPTPAVTTPTpNATIPTLGKTSPT---SAVTTPTPNATSPTvgeTSPQANTTNHTLGGTSSTPVVTSPP---KNAT 626
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   974 EA--------TKDESASLSNTKPLQDEDFQIDGGTFKTPEIDLAKDVFAALGTATPTAVASGKASELVSSTADTSVP-LD 1044
Cdd:pfam05109  627 SAvttgqhniTSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPgTT 706
                          330       340       350
                   ....*....|....*....|....*....|..
gi 148237004  1045 SAKTEKTQVEEKSKPEEIDV-KGTPAEVKTVP 1075
Cdd:pfam05109  707 SQASGPGNSSTSTKPGEVNVtKGTPPKNATSP 738
Ig_L1-CAM_like cd05733
Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; ...
319-389 1.19e-03

Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; Ig_L1-CAM_like: domain similar to the first 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, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains NrCAM [Ng(neuronglia)CAM-related cell adhesion molecule], which is primarily expressed in the nervous system, and human neurofascin.


Pssm-ID: 319299  Cd Length: 77  Bit Score: 39.73  E-value: 1.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148237004  319 ITLTCEASGDPIPSITWrtaVRNISSEATTLDGHIVVKEHIRMSALTLKDIQYTDA--GEYFCIASNPIGVDM 389
Cdd:cd05733     1 IVLKCEAKGNPPPTFSW---TKDGKHFDPEKDPSVSMKRDSGTFVISNHNGNAAKDyqGKYRCYASNELGTAI 70
Ig1_Neogenin cd05722
First immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig1_Neogenin: first ...
218-286 1.20e-03

First immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig1_Neogenin: first immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC, which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain.


Pssm-ID: 143199  Cd Length: 95  Bit Score: 39.77  E-value: 1.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148237004  218 VNATANMAESVVLSCDADGFPDPEISWLKKGEPIEDGEEKISFNEDQSEMTIHHVE-----KDDEAEYSCIANN 286
Cdd:cd05722     7 SDIVAVRGGPVVLNCSAEGEPPPKIEWKKDGVLLNLVSDERRQQLPNGSLLITSVVhskhnKPDEGFYQCVAQN 80
Ig_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: ...
293-386 1.34e-03

Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: domain similar to the M5, fifth immunoglobulin (Ig)-like domain from the human titin C terminus. 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.


Pssm-ID: 143224  Cd Length: 92  Bit Score: 39.65  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  293 ATILlkvyAKPK-ITYVENKTAveldeiTLTCEASGDPIPSITWRTAVRNISSEATtldgHIVVKEHIRmSALTLKDIQY 371
Cdd:cd05747     4 ATIL----TKPRsLTVSEGESA------RFSCDVDGEPAPTVTWMREGQIIVSSQR----HQITSTEYK-STFEISKVQM 68
                          90
                  ....*....|....*
gi 148237004  372 TDAGEYFCIASNPIG 386
Cdd:cd05747    69 SDEGNYTVVVENSEG 83
Ig1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; Ig1_Contactin-5: First Ig domain of the ...
318-387 1.35e-03

First immunoglobulin (Ig) domain of contactin-5; Ig1_Contactin-5: First Ig domain of the neural cell adhesion molecule contactin-5. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains, anchored to the membrane by glycosylphosphatidylinositol. The different contactins show different expression patterns in the central nervous system. In rats, a lack of contactin-5 (NB-2) results in an impairment of the neuronal activity in the auditory system. Contactin-5 is expressed specifically in the postnatal nervous system, peaking at about 3 weeks postnatal. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala; lower levels of expression have been detected in the corpus callosum, caudate nucleus, and spinal cord.


Pssm-ID: 143256  Cd Length: 94  Bit Score: 39.53  E-value: 1.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148237004  318 EITLTCEASGDPIPSITWRTAVRNISSEA----TTLDGHIVVKEHIRMsaltlkdiqyTDAGEYFCIASNPIGV 387
Cdd:cd05848    21 KVILNCEARGNPVPTYRWLRNGTEIDTESdyrySLIDGNLIISNPSEV----------KDSGRYQCLATNSIGS 84
Ig_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; Ig_Myotilin_like_C: ...
228-299 1.41e-03

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; Ig_Myotilin_like_C: 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: all three bind 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).


Pssm-ID: 319304  Cd Length: 75  Bit Score: 39.51  E-value: 1.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148237004  228 VVLSCDADGFPDPEISWLKKGEPIEDGEEKISFNEDQS---EMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:cd05744     1 VKLECQVLAIPPPQIFWKKENEMLQFNTDRISLYQDNHgriCLLIKDVTKEDAGWYTVSAKNEAGITSCNARLDV 75
PRK13335 PRK13335
superantigen-like protein; Reviewed
818-962 1.42e-03

superantigen-like protein; Reviewed


Pssm-ID: 139494  Cd Length: 356  Bit Score: 42.04  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  818 VTTNSDTITETFATAQNSPTSETTTLTSSTA-----------PPPTTAPDSNTIQSIQATPSKAEAPTTSSPPPTSSPKV 886
Cdd:PRK13335   16 LTTGAITVTTQSVKAEKIQSTKVDKVPTLKAerlaminitagANSATTQAANTRQERTPKLEKAPNTNEEKTSASKIEKI 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148237004  887 aplvdlSDTPTNNPSKvvANQAGPLNPSAATSAAEPPTVIIKPVTTVPPNAASPPPTPEPKQVKQEQSGTKSPEKE 962
Cdd:PRK13335   96 ------SQPKQEEQKS--LNISATPAPKQEQSQTTTESTTPKTKVTTPPSTNTPQPMQSTKSDTPQSPTIKQAQTD 163
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
900-1041 1.46e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865  Cd Length: 618  Bit Score: 42.39  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  900 PSKVVANQAGPLNPSAATSAAEPPTV-IIKPVTTVPPNAASPPPTPEPKQVkqeQSGTKSPEKEEAQPSTVKNPTEATKD 978
Cdd:PRK14951  371 EAAAPAEKKTPARPEAAAPAAAPVAQaAAAPAPAAAPAAAASAPAAPPAAA---PPAPVAAPAAAAPAAAPAAAPAAVAL 447
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237004  979 ESASlsnTKPLQDEDFQIDGGTFKTPEIDLAKDVFAALGTATPTAVAS------GKASELVSSTADTSV 1041
Cdd:PRK14951  448 APAP---PAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEegdvwhATVQQLAAAEAITAL 513
Ig1_Neogenin cd05722
First immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig1_Neogenin: first ...
129-196 1.51e-03

First immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig1_Neogenin: first immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC, which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain.


Pssm-ID: 143199  Cd Length: 95  Bit Score: 39.38  E-value: 1.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148237004  129 GEDAVIICDVSSSIPSIITWRHKGKDVIFKKDVRFVVLANNYLQIRGIK-----KTDEGTYRCEGRILARGEI 196
Cdd:cd05722    14 GGPVVLNCSAEGEPPPKIEWKKDGVLLNLVSDERRQQLPNGSLLITSVVhskhnKPDEGFYQCVAQNDSLGSI 86
PHA03247 PHA03247
large tegument protein UL36; Provisional
848-944 1.53e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021  Cd Length: 3151  Bit Score: 42.62  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  848 APPPTTAPDSNTIQSIQATPSKAEAPTTSSPPPTSSPKVAPLV-DLSDTPTnnpskVVANQAGPLNPSAATSAAEPPTVI 926
Cdd:PHA03247 2759 RPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPwDPADPPA-----AVLAPAAALPPAASPAGPLPPPTS 2833
                          90
                  ....*....|....*...
gi 148237004  927 IKPVTTVPPNAASPPPTP 944
Cdd:PHA03247 2834 AQPTAPPPPPGPPPPSLP 2851
PHA03247 PHA03247
large tegument protein UL36; Provisional
849-1032 1.56e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021  Cd Length: 3151  Bit Score: 42.62  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  849 PPPTTAPDSNTIQSIQATP-------SKAEAPTTSSPPPTSSPKVAPLVDLSDTPTNNPskvvANQAGPLNPS--AATSA 919
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPlppgpaaARQASPALPAAPAPPAVPAGPATPGGPARPARP----PTTAGPPAPAppAAPAA 2777
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  920 AEPPTVIIKPVTTVPPNAASPPPTPEPKQVKQEQSGTKSPEKEEAQPSTVKNPTeaTKDESASLSNTKPLQDEDFQIDGG 999
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP--TSAQPTAPPPPPGPPPPSLPLGGS 2855
                         170       180       190
                  ....*....|....*....|....*....|...
gi 148237004 1000 TfkTPEIDLAKDVFAALGTATPTAVASGKASEL 1032
Cdd:PHA03247 2856 V--APGGDVRRRPPSRSPAAKPAAPARPPVRRL 2886
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
849-1059 1.65e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748  Cd Length: 576  Bit Score: 42.22  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  849 PPPTTAPdsntiqsIQATPSKAEAPTTSSPPPTSSPKVAPLVDL-SDTPTNNPSKVVANQAGPLNPSAATSAAEPPTvii 927
Cdd:PLN03209  382 PPTSPIP-------TPPSSSPASSKSVDAVAKPAEPDVVPSPGSaSNVPEVEPAQVEAKKTRPLSPYARYEDLKPPT--- 451
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  928 kpvttvppnaaSPPPTPEPKQVKQEQSGTKSPEKEEAQPstvknPTEATKDESASLSNTKPLQDEDFQIDGGTFKTPeid 1007
Cdd:PLN03209  452 -----------SPSPTAPTGVSPSVSSTSSVPAVPDTAP-----ATAATDAAAPPPANMRPLSPYAVYDDLKPPTSP--- 512
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 148237004 1008 lakdvfaalgTATPTAVASGKASELVSSTADTSVPLDSAKTEKTQVEEKSKP 1059
Cdd:PLN03209  513 ----------SPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQPKPRP 554
Ig1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; Ig1_Contactin: First Ig domain of contactins. ...
318-386 1.67e-03

First immunoglobulin (Ig) domain of contactin; Ig1_Contactin: First 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: 319276  Cd Length: 91  Bit Score: 39.12  E-value: 1.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148237004  318 EITLTCEASGDPIPSITWR---TAVRNISSEATTL-DGHIVVKEHIRMSaltlkdiqytDAGEYFCIASNPIG 386
Cdd:cd04967    21 KVALNCRARANPPPTYRWKmngTEIKLEPDSRYSLvGGNLVISNPSKAK----------DAGHYQCLATNTVG 83
Ig_TrkABC_d4 cd04972
Fourth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB and TrkC; TrkABC_d4: the ...
226-299 1.79e-03

Fourth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB and TrkC; TrkABC_d4: the fourth domain of Trk receptors TrkA, TrkB and TrkC, an immunoglobulin (Ig)-like domain which binds to neurotrophin. The Trk family of receptors are tyrosine kinase receptors. They are activated by dimerization, leading to autophosphorylation of intracellular tyrosine residues, and triggering the signal transduction pathway. TrkA, TrkB, and TrkC share significant sequence homology and domain organization. The first three domains are leucine-rich domains. The fourth and fifth domains are Ig-like domains playing a part in ligand binding. TrkA, B, and C mediate the trophic effects of the neurotrophin Nerve growth factor (NGF) family. TrkA is recognized by NGF. TrKB is recognized by brain-derived neurotrophic factor (BDNF) and neurotrophin (NT)-4. TrkC is recognized by NT-3. NT-3 is promiscuous as in some cell systems it activates TrkA and TrkB receptors. TrkA is a receptor found in all major NGF targets, including the sympathetic, trigeminal, and dorsal root ganglia, cholinergic neurons of the basal forebrain and the striatum. TrKB transcripts are found throughout multiple structures of the central and peripheral nervous systems. The TrkC gene is expressed throughout the mammalian nervous system.


Pssm-ID: 143173  Cd Length: 90  Bit Score: 39.04  E-value: 1.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148237004  226 ESVVLSCDADGFPDPEISWLK-KGEPIEDGEEKISFNEDQSEMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:cd04972    16 GTATIRCTAEGSPLPKVEWIIaGLIVIQTRTDTLETTVDIYNLQLSNITSETQTTVTCTAENPVGQANVSVQVTV 90
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); Ig_DSCAM: ...
319-394 1.82e-03

Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); Ig_DSCAM: 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 mental retardation 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: 143211  Cd Length: 79  Bit Score: 39.14  E-value: 1.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237004  319 ITLTCEASGDPIPSITWRTAVRNISSEAT---TLDGHIVVkehIRMSALTLKDIQYTDAGEYFCIASNPIGVDMQAMYF 394
Cdd:cd05734     1 VTLNCSAEGYPPPTIVWKHSKGRGHPQHThtcCLAGRIQL---LSNGSLLIKHVLEEDSGYYLCKVSNDVGADASKSMV 76
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: the third ...
323-396 1.85e-03

Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: 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  Cd Length: 74  Bit Score: 39.15  E-value: 1.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148237004  323 CEASGDPIPSITWRTAVRNISseattldghiVVKEHIRMSALTLK--DIQYTDAGEYFCIASNPIGVDMQAMYFEV 396
Cdd:cd05745     9 CEAQGYPQPVIAWTKGGSQLS----------VDRRHLVLSSGTLRisRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: the third ...
226-299 1.95e-03

Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: 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  Cd Length: 74  Bit Score: 39.15  E-value: 1.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148237004  226 ESVVLSCDADGFPDPEISWLKKGEPIEDGEEKISFNedQSEMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:cd05745     3 QTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLS--SGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
Ig3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; Ig3_Contactin_like: Third Ig domain of ...
209-289 2.00e-03

Third immunoglobulin (Ig) domain of contactin; Ig3_Contactin_like: Third 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 act ivity 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: 319277  Cd Length: 88  Bit Score: 39.07  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  209 PTIQARQLRvNATANMAESVVLSCDADGFPDPEISWLKKgepieDGEEKISFNEDQSEMTIH--HVEKDDEAEYSCIANN 286
Cdd:cd04968     1 PSIKVRFPA-DTYALKGQTVTLECFALGNPVPQIKWRKV-----DGSPSSQWTTSTSEPVLEipNVQFEDEGTYECEAEN 74

                  ...
gi 148237004  287 QAG 289
Cdd:cd04968    75 SRG 77
Ig_3 cd05765
Subgroup of the immunoglobulin (Ig) superfamily; Ig_3: subgroup of the immunoglobulin (Ig) ...
317-387 2.14e-03

Subgroup of the immunoglobulin (Ig) superfamily; Ig_3: 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. 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.


Pssm-ID: 143242  Cd Length: 81  Bit Score: 39.06  E-value: 2.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148237004  317 DEITLTCEASGDPIPSITWRTAV---RNISSEATTLDGHIVVKEhirMSALTLKDIQYTDAGEYFCIASNPIGV 387
Cdd:cd05765     2 ETASFHCDVTGRPPPEITWEKQVhgkENLIMRPNHVRGNVVVTN---IGQLVIYNAQPQDAGLYTCTARNSGGL 72
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
32-111 2.15e-03

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 311561  Cd Length: 109  Bit Score: 39.00  E-value: 2.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004    32 SLGESKFFLCQVSG----EATDISW---------------YSPTGEKLVTQQQISVVRSDDYTS-TLTIYNASSQDAGIY 91
Cdd:pfam07686    9 AEGGSVTLPCTYSSsmseASYYIYWyrqppgggpeeliayYSNGYEEGKKKGRFSLRGDPSRSDfSLTIQNLTPSDSGTY 88
                           90       100
                   ....*....|....*....|
gi 148237004    92 KCVASNEAEGESEGTVNLKI 111
Cdd:pfam07686   89 FCAVIPSGEGVFGSGTRLTV 108
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; Ig4_Peroxidasin: the fourth ...
416-488 2.28e-03

Fourth immunoglobulin (Ig)-like domain of peroxidasin; Ig4_Peroxidasin: 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: 38.70  E-value: 2.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148237004  416 VNITCEVFAHPRAAVTWFRDG-QLLPSSNFSnikIYSGPTSSSLEVNPDsenDFGNYNCTAINTIGHEFSEFIL 488
Cdd:cd05746     1 VQIPCSAQGDPEPTITWNKDGvQVTESGKFH---ISPEGYLAIRDVGVA---DQGRYECVARNTIGYASVSMVL 68
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
804-979 3.18e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138  Cd Length: 647  Bit Score: 41.39  E-value: 3.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  804 HPAAVEDMLPSVTTVTTNSDTITETFATAQNSPTSETTTLTSSTAPPPTTAPDSNTIQSiQATPSKAEAPTTSSPPPTSS 883
Cdd:PRK07994  360 HPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPET-TSQLLAARQQLQRAQGATKA 438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  884 PKVAPLVDLSDTPTNNPSKVVAnqagPLNPSAATSAAEPPTVIIKPVTTVPPNAASPPPTPEPKQVKQeqsgtkSPEKEE 963
Cdd:PRK07994  439 KKSEPAAASRARPVNSALERLA----SVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKK------ALEHEK 508
                         170
                  ....*....|....*.
gi 148237004  964 AQPSTVKNPTEATKDE 979
Cdd:PRK07994  509 TPELAAKLAAEAIERD 524
Ig1_Contactin-2 cd05850
First immunoglobulin (Ig) domain of contactin-2; Ig1_Contactin-2: First Ig domain of the ...
117-186 3.58e-03

First immunoglobulin (Ig) domain of contactin-2; Ig1_Contactin-2: First Ig domain of the neural cell adhesion molecule contactin-2-like. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. It may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. 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. 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-2 is also expressed in retinal amacrine cells in the developing chick retina, corresponding to the period of formation and maturation of AC processes.


Pssm-ID: 143258  Cd Length: 94  Bit Score: 38.38  E-value: 3.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148237004  117 FKNAPTPQEFKEG---EDAVIICDVSSSIPSIITWRHKGKDVIFKKDVRFVVLANNYLQIRGIKKTDEGTYRC 186
Cdd:cd05850     4 FEEQPSSLLFPEGspeEKVTLGCRARASPPATYRWKMNGTEIKFAPESRYTLVAGNLVINNPQKARDAGSYQC 76
Ig_NCAM-1 cd05869
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig_NCAM-1: ...
21-97 3.63e-03

Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig_NCAM-1: immunoglobulin (Ig)-like domain similar to the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM). 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: 143277  Cd Length: 97  Bit Score: 38.42  E-value: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   21 EVNIVPDQGEISLGESKFFLCQVSGEAT-DISWysPTGEKLVTQQQIS-----VVRSDDYTSTLTIYNASSQDAGIYKCV 94
Cdd:cd05869     4 KITYVENQTAMELEEQITLTCEASGDPIpSITW--RTSTRNISSEEKTldghiVVRSHARVSSLTLKYIQYTDAGEYLCT 81

                  ...
gi 148237004   95 ASN 97
Cdd:cd05869    82 ASN 84
Ig_3 cd05765
Subgroup of the immunoglobulin (Ig) superfamily; Ig_3: subgroup of the immunoglobulin (Ig) ...
226-299 3.71e-03

Subgroup of the immunoglobulin (Ig) superfamily; Ig_3: 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. 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.


Pssm-ID: 143242  Cd Length: 81  Bit Score: 38.29  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  226 ESVVLSCDADGFPDPEISWLKKgepiEDGEEKISFNEDQ----------SEMTIHHVEKDDEAEYSCIANNQAGEAEATI 295
Cdd:cd05765     2 ETASFHCDVTGRPPPEITWEKQ----VHGKENLIMRPNHvrgnvvvtniGQLVIYNAQPQDAGLYTCTARNSGGLLRANF 77

                  ....
gi 148237004  296 LLKV 299
Cdd:cd05765    78 PLSV 81
PHA03247 PHA03247
large tegument protein UL36; Provisional
793-972 3.85e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021  Cd Length: 3151  Bit Score: 41.46  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  793 PNETTPLTEPEHPAAVEDMLPSVTTVTTNSDTITETfATAQNSPTSETTTLTSSTAPPPTTAPDSNTIQSIQATPSKAEA 872
Cdd:PHA03247 2751 PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRP-AVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP 2829
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  873 PTTSSP-PPTSSPK------------VAPLVDLSDTPTNNPSkvVANQAGPLNPSAATSAAEPPTVIIKPVtTVPPNAAS 939
Cdd:PHA03247 2830 PPTSAQpTAPPPPPgppppslplggsVAPGGDVRRRPPSRSP--AAKPAAPARPPVRRLARPAVSRSTESF-ALPPDQPE 2906
                         170       180       190
                  ....*....|....*....|....*....|...
gi 148237004  940 PPPTPEPKQVKQEQSGTKSPEKEEAQPSTVKNP 972
Cdd:PHA03247 2907 RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
121-186 3.90e-03

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 311561  Cd Length: 109  Bit Score: 38.23  E-value: 3.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004   121 PTPQEFKEGEDAVIICDVSSSIPSI---ITW--------------RHKGKDVIFKKDVRFVVLANN-----YLQIRGIKK 178
Cdd:pfam07686    3 PRSVTVAEGGSVTLPCTYSSSMSEAsyyIYWyrqppgggpeeliaYYSNGYEEGKKKGRFSLRGDPsrsdfSLTIQNLTP 82

                   ....*...
gi 148237004   179 TDEGTYRC 186
Cdd:pfam07686   83 SDSGTYFC 90
IgC cd00098
Immunoglobulin Constant (IgC) domain; Members of the IgC family are components of ...
411-473 4.09e-03

Immunoglobulin Constant (IgC) domain; Members of the IgC family are components of immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and Major Histocompatibility Complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, and the IgC domain is involved in oligomerization and molecular interactions.


Pssm-ID: 319274  Cd Length: 95  Bit Score: 38.19  E-value: 4.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148237004  411 WEGNPVNITCEV--FAHPRAAVTWFRDGQLLPSSNFSNIKIYSGP----TSSSLEVNPDSENDFGNYNC 473
Cdd:cd00098    11 KLGGTVTLVCLVsgFYPKDITVTWLKNGKEVTSGVSTTPPTKNSDgtfsVTSYLTVPPSDWDEGTTYTC 79
Ig1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; Ig1_Contactin-5: First Ig domain of the ...
228-289 4.55e-03

First immunoglobulin (Ig) domain of contactin-5; Ig1_Contactin-5: First Ig domain of the neural cell adhesion molecule contactin-5. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains, anchored to the membrane by glycosylphosphatidylinositol. The different contactins show different expression patterns in the central nervous system. In rats, a lack of contactin-5 (NB-2) results in an impairment of the neuronal activity in the auditory system. Contactin-5 is expressed specifically in the postnatal nervous system, peaking at about 3 weeks postnatal. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala; lower levels of expression have been detected in the corpus callosum, caudate nucleus, and spinal cord.


Pssm-ID: 143256  Cd Length: 94  Bit Score: 37.99  E-value: 4.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148237004  228 VVLSCDADGFPDPEISWLKKGEPIeDGEEKISFNEDQSEMTIHHV-EKDDEAEYSCIANNQAG 289
Cdd:cd05848    22 VILNCEARGNPVPTYRWLRNGTEI-DTESDYRYSLIDGNLIISNPsEVKDSGRYQCLATNSIG 83
IgV cd00099
Immunoglobulin variable domain (IgV); IgV: Immunoglobulin variable domain (IgV). Members of ...
126-186 4.78e-03

Immunoglobulin variable domain (IgV); IgV: Immunoglobulin variable domain (IgV). Members of the IgV family are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 319275  Cd Length: 103  Bit Score: 37.76  E-value: 4.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  126 FKEGEDAVIICDVSSSIPS----------------IITWRHKGKDVIFKkdvRFVVLANN-----YLQIRGIKKTDEGTY 184
Cdd:cd00099     3 VSTGESVTLNCVLSGSFSLysiswyrqkpgkqpqfLISGSSTGKPGIPG---RFSGTRNGgsssfSLTISNLRPEDSGTY 79

                  ..
gi 148237004  185 RC 186
Cdd:cd00099    80 YC 81
Ig_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2); ...
230-299 5.21e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2); Ig_M-protein_C: the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains, and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 37.58  E-value: 5.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148237004  230 LSCDADGFPDPEISWLKKGEPIEDGEE-KISFNEDQ-SEMTIHHVEKDDEAEYSCIANNQAGEAEATILLKV 299
Cdd:cd05891    21 LTCTVFGNPDPEVIWFKNDQDIELSEHySVKLEQGKyASLTIKGVTSEDSGKYSINVKNKYGGETVDVTVSV 92
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; Ig5_Contactin_like: Fifth Ig domain of ...
413-489 6.75e-03

Fifth immunoglobulin (Ig) domain of contactin; Ig5_Contactin_like: Fifth 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 act ivity 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: 319278  Cd Length: 73  Bit Score: 37.43  E-value: 6.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148237004  413 GNPVNITCEVFAHPRAAVTWFRDGQLLPSSnfSNIKIYSgptSSSLEVNPDSENDFGNYNCTAINTIGHEFSEFILV 489
Cdd:cd04969     1 GGDVIIECKPKASPKPTISWSKGTELLTNS--SRICILP---DGSLKIKNVSKSDEGKYTCFAVNFFGKANSTGSLS 72
C1-set pfam07654
Immunoglobulin C1-set domain;
413-466 7.15e-03

Immunoglobulin C1-set domain;


Pssm-ID: 311543  Cd Length: 89  Bit Score: 37.25  E-value: 7.15e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148237004   413 GNPVNITCEV--FaHPRA-AVTWFRDGQLLPSSNFSNIKIYSGP----TSSSLEVNPDSEN 466
Cdd:pfam07654   16 GKPNTLTCLVtgF-YPPDiTVTWLKNGQEVTEGVTSTTLPQNGDwtyqLSSYLTVTPSDWE 75
Ig4_Neogenin cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig4_Neogenin: fourth ...
131-186 7.40e-03

Fourth immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig4_Neogenin: fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC, which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain.


Pssm-ID: 212460  Cd Length: 71  Bit Score: 37.25  E-value: 7.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148237004  131 DAVIICDVSSSIPSIITWRHKGkDVIFKKDVrFVVLANNYLQIRGIKKTDEGTYRC 186
Cdd:cd05723     1 DIVFECEVTGKPTPTVKWVKNG-DMVIPSDY-FKIVKEHNLQVLGLVKSDEGFYQC 54
PHA03369 PHA03369
capsid maturational protease; Provisional
850-970 7.88e-03

capsid maturational protease; Provisional


Pssm-ID: 223061  Cd Length: 663  Bit Score: 39.98  E-value: 7.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  850 PPTTAPDSNTIQSIQATPSKAEAPTTSSPPPTSSPKVAPLVDLSDTPTNNP------SKVVANQAGPLNpSAATSAAEPP 923
Cdd:PHA03369  530 PNCSADAAAPATKRARPETKTELEAVVRFPYQIRNMESPAFVHSFTSTTLAaaagqgSDTAEALAGAIE-TLLTQASAQP 608
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 148237004  924 TVIIKPVTTVPPNAASPPPTPEPKQVKQEQSGTKSPEKEEAQPSTVK 970
Cdd:PHA03369  609 AGLSLPAPAVPVNASTPASTPPPLAPQEPPQPGTSAPSLETSLPQQK 655
PHA03247 PHA03247
large tegument protein UL36; Provisional
793-966 8.09e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021  Cd Length: 3151  Bit Score: 40.31  E-value: 8.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  793 PNETTPLTEPEHPAAVedmlPSVTTVTTNSDT-------ITETFATAQNSPTSETTTLTSSTAPPPTTAPDSNTIQSIQA 865
Cdd:PHA03247 2674 AQASSPPQRPRRRAAR----PTVGSLTSLADPppppptpEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA 2749
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148237004  866 TPSKAEAPTTSSPPPTSSPKVAPLVDLSDTPTNNPSKVVANQAGPLNPS-AATSAAEPPTVIIKPVTTVPPNAASPPPTP 944
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLpSPWDPADPPAAVLAPAAALPPAASPAGPLP 2829
                         170       180
                  ....*....|....*....|..
gi 148237004  945 EPKQVKQEQSGTKSPEKEEAQP 966
Cdd:PHA03247 2830 PPTSAQPTAPPPPPGPPPPSLP 2851
Ig1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; Ig1_Contactin: First Ig domain of contactins. ...
416-480 8.75e-03

First immunoglobulin (Ig) domain of contactin; Ig1_Contactin: First 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: 319276  Cd Length: 91  Bit Score: 37.19  E-value: 8.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148237004  416 VNITCEVFAHPRAAVTWFRDG---QLLPSSNFSNIkiysgpTSSSLEVNPDSENDFGNYNCTAINTIG 480
Cdd:cd04967    22 VALNCRARANPPPTYRWKMNGteiKLEPDSRYSLV------GGNLVISNPSKAKDAGHYQCLATNTVG 83
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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