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Conserved domains on  [gi|386769894|ref|NP_001246094|]
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Leukocyte-antigen-related-like, isoform D [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1378-1615 1.81e-177

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


:

Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 536.21  E-value: 1.81e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1378 EHNKSKNRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRL 1457
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1458 EERTRIKCDQYWPTRGTETYGQIFVTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRR 1537
Cdd:cd14553    81 EERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894 1538 CRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAIIC 1615
Cdd:cd14553   161 VKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAVTC 238
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1664-1901 5.92e-173

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


:

Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 524.01  E-value: 5.92e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1664 ANLPCNKHKNRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVML 1743
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1744 TKLKEMGREKCFQYWPHERSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDF 1823
Cdd:cd14554    81 TKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894 1824 IGQVHKTKEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAAL 1901
Cdd:cd14554   161 IGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
IgI_3_RPTP_IIa_LAR_like cd05739
Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F ...
 219-301 4.98e-46

Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F (also known as LAR), type IIa; member of the I-set of IgSF domains; The members here are composed of the third 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. Included in this group is Drosophila LAR (DLAR).


:

Pssm-ID: 409401  Cd Length: 82  Bit Score: 160.45  E-value: 4.98e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  219 SRPPeTISEVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPIGRNVLQLINIQESANYTCIAASTLGQIDSVSVV 298
Cdd:cd05739     1 SIPP-SNHEVMPGGSVNLTCVAVGAPMPYVKWMKGGEELTKEDEMPVGRNVLELTNIYESANYTCVAISSLGMIEATAQV 79


                  ...
gi 386769894  299 KVQ 301
Cdd:cd05739    80 TVK 82
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
285-702 2.23e-23

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 107.40  E-value: 2.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  285 AASTLGQIDSVSVVKVQSLPTAPTDVQISEVTATSVRLEWSYKGPEDLQYYVIQYKPKNANQAFSEISGIITMYYVVRAL 364
Cdd:COG3401    11 AGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  365 SPYTEYEFYVIAVNNIGRGPPSAPATC---TTGETKMESAPRNVQVRTLSSSTMVITWEPPETPNGQVTGYKVYYTTNSN 441
Cdd:COG3401    91 ATGLTTLTGSGSVGGATNTGLTSSDEVpspAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  442 QPEASWNSQMVDNSELTTVSELT-------PHAIYTVRVQAYTSMGAGPMSTPVQVKAQQGVPSQPSNFRATDIGETAVT 514
Cdd:COG3401   171 SPDTSATAAVATTSLTVTSTTLVdgggdiePGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVT 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  515 LQWTKptHSSENIVHYELYWNDTYANQAhhKRISNSEA--YTLDGLYPDTLYYIWLAARSQRG-EGATTPPIPVRTKQYV 591
Cdd:COG3401   251 LSWDP--VTESDATGYRVYRSNSGDGPF--TKVATVTTtsYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  592 PGDPQDVKATPLNSTSIHVSWKPPLEKDrngiIRGYHIHaqelRDEGKGFLNEPFKfDVVDTLEFNVTGLQPDTKYSIQV 671
Cdd:COG3401   327 PAAPSGLTATAVGSSSITLSWTASSDAD----VTGYNVY----RSTSGGGTYTKIA-ETVTTTSYTDTGLTPGTTYYYKV 397

                         410       420       430
                  ....*....|....*....|....*....|.
gi 386769894  672 AALTRKGDGDRSAAIVVKTPGGVPVRPTVSL 702
Cdd:COG3401   398 TAVDAAGNESAPSEEVSATTASAASGESLTA 428
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 123-210 2.69e-23

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05738:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 91  Bit Score: 95.85  E-value: 2.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  123 VITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDM--SNPRYS-LKDGFLQIENSREEDQGKYECVAENSMGT 199
Cdd:cd05738     1 IIDMGPQLKVVEKARTATMLCAASGNPDPEISWFKDFLPVDTatSNGRIKqLRSGALQIENSEESDQGKYECVATNSAGT 80

                          90
                  ....*....|.
gi 386769894  200 EHSKATNLYVK 210
Cdd:cd05738    81 RYSAPANLYVR 91
I-set pfam07679
Immunoglobulin I-set domain;
18-111 1.57e-20

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 87.70  E-value: 1.57e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    18 PEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSgtQSRYTVLEQPGGISILRIEPVRAGrDDAPYECVAEN 97
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLR--SSDRFKVTYEGGTYTLTISNVQPD-DSGKYTCVATN 77

                           90
                   ....*....|....
gi 386769894    98 GVGdAVSADATLTI 111
Cdd:pfam07679   78 SAG-EAEASAELTV 90
fn3 pfam00041
Fibronectin type III domain;
794-878 1.76e-14

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 70.52  E-value: 1.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   794 GPPSNITIRFQTPDVLCVTWDPPtrEHRNGIITRYDVQFHKKIDHGLGSERNM--TLRKAVFTNLEENTEYIFRVRAYTK 871
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPP--PDGNGPITGYEVEYRPKNSGEPWNEITVpgTTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*..
gi 386769894   872 QGAGPFS 878
Cdd:pfam00041   79 GGEGPPS 85
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
747-1149 1.44e-11

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 69.65  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  747 SGPQMTKKRFDNLERGVEYEFRVAGSNHIGIGQETVKIFQTPEGTPGGPPSNITIRFQTPDVLCVTWDPPTREHrngiIT 826
Cdd:COG3401   187 VTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD----AT 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  827 RYDVQFHKKIDHGLgsERNMTLRKAVFT--NLEENTEYIFRVRAYTKQG-AGPFSDKLIVETERDMGRAPMSLQAEATSE 903
Cdd:COG3401   263 GYRVYRSNSGDGPF--TKVATVTTTSYTdtGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTPPAAPSGLTATAVGS 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  904 QTAEIWWEPVTSrGKLLGYKIFYTmTAVEDLDDWQTKTVGLTESADLvNLEKFAQYAVAIAARFKNGL-GRLSEKVTVRI 982
Cdd:COG3401   341 SSITLSWTASSD-ADVTGYNVYRS-TSGGGTYTKIAETVTTTSYTDT-GLTPGTTYYYKVTAVDAAGNeSAPSEEVSATT 417

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  983 -------KPEDVPLNLRAHDVSTHSMTLSWSPPIRLTPVNYKISFDAMKVFVDSQGFSQTQIVPKREIILKHYVKTHTIN 1055
Cdd:COG3401   418 asaasgeSLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLV 497

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1056 ELSPFTTYNVNVSAIpSDYSYRPPTKITVTTQMAAPQPMVKPDFYGVVNGEEILVILPQASEEYGPISHYYLVVVPEDKS 1135
Cdd:COG3401   498 GGSGASSVTNSVSVI-GASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITT 576

                         410
                  ....*....|....
gi 386769894 1136 NLHKIPDQFLTDDL 1149
Cdd:COG3401   577 LGGSLLTTTSTNTN 590
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 712-778 3.74e-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 [Multi-domain]  Cd Length: 83  Bit Score: 43.76  E-value: 3.74e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    712 SIELEWERPAQTYGelRGYRLRWGVKDQALK---EEMLSGPQMTKKRFDNLERGVEYEFRVAGSNHIGIG 778
Cdd:smart00060   16 SVTLSWEPPPDDGI--TGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
 
Name Accession Description Interval E-value
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1378-1615 1.81e-177

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 536.21  E-value: 1.81e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1378 EHNKSKNRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRL 1457
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1458 EERTRIKCDQYWPTRGTETYGQIFVTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRR 1537
Cdd:cd14553    81 EERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894 1538 CRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAIIC 1615
Cdd:cd14553   161 VKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAVTC 238
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1664-1901 5.92e-173

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 524.01  E-value: 5.92e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1664 ANLPCNKHKNRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVML 1743
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1744 TKLKEMGREKCFQYWPHERSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDF 1823
Cdd:cd14554    81 TKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894 1824 IGQVHKTKEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAAL 1901
Cdd:cd14554   161 IGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1643-1902 4.12e-109

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 348.11  E-value: 4.12e-109
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   1643 GMEVEFKKLSNVKMDSSKFVTANLPCNKHKNRLVHILPYESSRVYLTPIHGiEGSDYVNASFIDGYRYRSAYIAAQGPVQ 1722
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   1723 DAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHE--RSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTV 1800
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   1801 RQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQFgqDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILR 1880
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTS--TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                           250       260
                    ....*....|....*....|..
gi 386769894   1881 SQRPAMVQTEDQYHFCYRAALE 1902
Cdd:smart00194  238 SQRPGMVQTEEQYIFLYRAILE 259
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1356-1611 6.38e-109

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 347.72  E-value: 6.38e-109
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   1356 KFSQEYESIEPGQQ--FTWDNSNLEHNKSKNRYANVTAYDHSRVQLPAVEGVvGSDYINANYCDGYRKHNAYVATQGPLQ 1433
Cdd:smart00194    1 GLEEEFEKLDRLKPddESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   1434 ETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWP--TRGTETYGQIFVTITETQELATYSIRTFQLCRQGFNDRREI 1511
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPdeEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   1512 KQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQ 1591
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                           250       260
                    ....*....|....*....|
gi 386769894   1592 RNYMVQTEDQYIFIHDAILE 1611
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1380-1611 4.09e-107

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 341.53  E-value: 4.09e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  1380 NKSKNRYANVTAYDHSRVQLPAVEGvvGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEE 1459
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  1460 RTRIKCDQYWPT--RGTETYGQIFVTIT-ETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLR 1536
Cdd:pfam00102   79 KGREKCAQYWPEeeGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769894  1537 RCRALTP-PESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:pfam00102  159 KVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1669-1902 6.91e-99

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 317.65  E-value: 6.91e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  1669 NKHKNRLVHILPYESSRVYLTPIHGieGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKE 1748
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  1749 MGREKCFQYWP--HERSVRYQYYVVDPIAE-YNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIG 1825
Cdd:pfam00102   79 KGREKCAQYWPeeEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894  1826 QVHKtKEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:pfam00102  159 KVRK-SSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PHA02738 PHA02738
hypothetical protein; Provisional
 1340-1623 1.99e-50

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 182.05  E-value: 1.99e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1340 SEFANHIERlkSNDNQKFSQEYESIEPGQ-QFTWDNSnlEHNKSKNRYANVTAYDHSRVQLPAVEGvvGSDYINANYCDG 1418
Cdd:PHA02738   12 AEFLALMEK--SDCEEVITREHQKVISEKvDGTFNAE--KKNRKLNRYLDAVCFDHSRVILPAERN--RGDYINANYVDG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1419 YRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPT--RGTETYGQIFVTITETQELATYsIR 1496
Cdd:PHA02738   86 FEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDveQGSIRFGKFKITTTQVETHPHY-VK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1497 TFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFL---RRC-------------RALTPPesgPVIVHCSAGVGRT 1560
Cdd:PHA02738  165 STLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVlevRQCqkelaqeslqighNRLQPP---PIVVHCNAGLGRT 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769894 1561 GCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAIICGVTEVPAR 1623
Cdd:PHA02738  242 PCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLTVNKVSKK 304
PHA02738 PHA02738
hypothetical protein; Provisional
 1669-1909 1.57e-47

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 173.57  E-value: 1.57e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1669 NKHKNRLVHILPYESSRVYLtPIHGIEGsDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKE 1748
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVIL-PAERNRG-DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1749 MGREKCFQYWP--HERSVRYQYYVVDPIAEYNMPQYKLREFKVTDArDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQ 1826
Cdd:PHA02738  127 NGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDG-TSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLE 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1827 VHKTKEQFGQDG-----------PITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHF 1895
Cdd:PHA02738  206 VRQCQKELAQESlqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFF 285

                         250
                  ....*....|....
gi 386769894 1896 CYRAALEYLGSFDN 1909
Cdd:PHA02738  286 CYRAVKRYVNLTVN 299
IgI_3_RPTP_IIa_LAR_like cd05739
Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F ...
 219-301 4.98e-46

Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F (also known as LAR), type IIa; member of the I-set of IgSF domains; The members here are composed of the third 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. Included in this group is Drosophila LAR (DLAR).


Pssm-ID: 409401  Cd Length: 82  Bit Score: 160.45  E-value: 4.98e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  219 SRPPeTISEVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPIGRNVLQLINIQESANYTCIAASTLGQIDSVSVV 298
Cdd:cd05739     1 SIPP-SNHEVMPGGSVNLTCVAVGAPMPYVKWMKGGEELTKEDEMPVGRNVLELTNIYESANYTCVAISSLGMIEATAQV 79


                  ...
gi 386769894  299 KVQ 301
Cdd:cd05739    80 TVK 82
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1345-1605 4.93e-39

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 147.93  E-value: 4.93e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1345 HIERLKSNDNQKFSQEYESIEPGQQFTWDNSNLEhNKSKNRYANVTAYDHSRVQLPAVegvvgsdYINANYCDGYRKHNA 1424
Cdd:COG5599     8 AIKSEEEKINSRLSTLTNELAPSHNDPQYLQNIN-GSPLNRFRDIQPYKETALRANLG-------YLNANYIQVIGNHRY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1425 YvATQGPLQETFVDFWRMCWELKTATIVMMTRLEE--RTRIKCDQYWPTRGTETYGQIFVTITETQELATYS-IRTFQL- 1500
Cdd:COG5599    80 I-ATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDGEYGKYEVSSELTESIQLRDGIeARTYVLt 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1501 CRQGFNDRREIKQLQFTAWPDHGVPDHPApFLQFLRRCRA----LTPPESGPViVHCSAGVGRTGCYIVIDSMLERMKHE 1576
Cdd:COG5599   159 IKGTGQKKIEIPVLHVKNWPDHGAISAEA-LKNLADLIDKkekiKDPDKLLPV-VHCRAGVGRTGTLIACLALSKSINAL 236

                         250       260       270
                  ....*....|....*....|....*....|..
gi 386769894 1577 KII--DIYGHVTCLRAQRNY-MVQTEDQYIFI 1605
Cdd:COG5599   237 VQItlSVEEIVIDMRTSRNGgMVQTSEQLDVL 268
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1639-1893 2.22e-29

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 119.81  E-value: 2.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1639 ETISGMEVEF-KKLSNVKMDSSKFVTAN----LPCNKHKNRLVHILPYESSRVyltpihGIEGSdYVNASFIDGYRYRSa 1713
Cdd:COG5599     7 IAIKSEEEKInSRLSTLTNELAPSHNDPqylqNINGSPLNRFRDIQPYKETAL------RANLG-YLNANYIQVIGNHR- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1714 YIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMG--REKCFQYWPHERSVRYQYYVVDPIAEYN-MPQYKLREFKVT 1790
Cdd:COG5599    79 YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYFRQDGEYGKYEVSSELTESIQlRDGIEARTYVLT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1791 DARDG-SSRTVRQFQFIDWPEQGVPkSGEGFIDFIGQVHKTKEQFGQD-GPITVHCSAGVGRSGVFItLSIVLERMQYEG 1868
Cdd:COG5599   159 IKGTGqKKIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKEKIKDPDkLLPVVHCRAGVGRTGTLI-ACLALSKSINAL 236

                         250       260
                  ....*....|....*....|....*....
gi 386769894 1869 V---LDVFQTVRILRSQR-PAMVQTEDQY 1893
Cdd:COG5599   237 VqitLSVEEIVIDMRTSRnGGMVQTSEQL 265
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
285-702 2.23e-23

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 107.40  E-value: 2.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  285 AASTLGQIDSVSVVKVQSLPTAPTDVQISEVTATSVRLEWSYKGPEDLQYYVIQYKPKNANQAFSEISGIITMYYVVRAL 364
Cdd:COG3401    11 AGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  365 SPYTEYEFYVIAVNNIGRGPPSAPATC---TTGETKMESAPRNVQVRTLSSSTMVITWEPPETPNGQVTGYKVYYTTNSN 441
Cdd:COG3401    91 ATGLTTLTGSGSVGGATNTGLTSSDEVpspAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  442 QPEASWNSQMVDNSELTTVSELT-------PHAIYTVRVQAYTSMGAGPMSTPVQVKAQQGVPSQPSNFRATDIGETAVT 514
Cdd:COG3401   171 SPDTSATAAVATTSLTVTSTTLVdgggdiePGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVT 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  515 LQWTKptHSSENIVHYELYWNDTYANQAhhKRISNSEA--YTLDGLYPDTLYYIWLAARSQRG-EGATTPPIPVRTKQYV 591
Cdd:COG3401   251 LSWDP--VTESDATGYRVYRSNSGDGPF--TKVATVTTtsYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  592 PGDPQDVKATPLNSTSIHVSWKPPLEKDrngiIRGYHIHaqelRDEGKGFLNEPFKfDVVDTLEFNVTGLQPDTKYSIQV 671
Cdd:COG3401   327 PAAPSGLTATAVGSSSITLSWTASSDAD----VTGYNVY----RSTSGGGTYTKIA-ETVTTTSYTDTGLTPGTTYYYKV 397

                         410       420       430
                  ....*....|....*....|....*....|.
gi 386769894  672 AALTRKGDGDRSAAIVVKTPGGVPVRPTVSL 702
Cdd:COG3401   398 TAVDAAGNESAPSEEVSATTASAASGESLTA 428
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
 123-210 2.69e-23

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


Pssm-ID: 409400 [Multi-domain]  Cd Length: 91  Bit Score: 95.85  E-value: 2.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  123 VITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDM--SNPRYS-LKDGFLQIENSREEDQGKYECVAENSMGT 199
Cdd:cd05738     1 IIDMGPQLKVVEKARTATMLCAASGNPDPEISWFKDFLPVDTatSNGRIKqLRSGALQIENSEESDQGKYECVATNSAGT 80

                          90
                  ....*....|.
gi 386769894  200 EHSKATNLYVK 210
Cdd:cd05738    81 RYSAPANLYVR 91
fn3 pfam00041
Fibronectin type III domain;
400-485 1.09e-20

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 88.24  E-value: 1.09e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   400 SAPRNVQVRTLSSSTMVITWEPPETPNGQVTGYKV-YYTTNSNQPeasWNSQMVDNSELT-TVSELTPHAIYTVRVQAYT 477
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVeYRPKNSGEP---WNEITVPGTTTSvTLTGLKPGTEYEVRVQAVN 77


                   ....*...
gi 386769894   478 SMGAGPMS 485
Cdd:pfam00041   78 GGGEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
18-111 1.57e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 87.70  E-value: 1.57e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    18 PEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSgtQSRYTVLEQPGGISILRIEPVRAGrDDAPYECVAEN 97
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLR--SSDRFKVTYEGGTYTLTISNVQPD-DSGKYTCVATN 77

                           90
                   ....*....|....
gi 386769894    98 GVGdAVSADATLTI 111
Cdd:pfam07679   78 SAG-EAEASAELTV 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 400-491 3.02e-19

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 [Multi-domain]  Cd Length: 93  Bit Score: 84.09  E-value: 3.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  400 SAPRNVQVRTLSSSTMVITWEPPETPNGQVTGYKVYYTTNSNQPEASWNSQMVDNSELtTVSELTPHAIYTVRVQAYTSM 479
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSY-TLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|..
gi 386769894  480 GAGPMSTPVQVK 491
Cdd:cd00063    81 GESPPSESVTVT 92
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 21-111 3.63e-18

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 80.90  E-value: 3.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   21 IRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSgtQSRYTVLEQpggiSILRIEPVRAGrDDAPYECVAENGVG 100
Cdd:cd05725     1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELP--KGRYEILDD----HSLKIRKVTAG-DMGSYTCVAENMVG 73

                          90
                  ....*....|.
gi 386769894  101 dAVSADATLTI 111
Cdd:cd05725    74 -KIEASATLTV 83
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 128-209 2.59e-16

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 75.62  E-value: 2.59e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    128 PGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLK----DGFLQIENSREEDQGKYECVAENSMGTEHSK 203
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSrsgsTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                    ....*.
gi 386769894    204 aTNLYV 209
Cdd:smart00410   81 -TTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 122-195 8.76e-16

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 73.75  E-value: 8.76e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894   122 PVITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTK---VDMSNPRYSLKDGFLQIENSREEDQGKYECVAEN 195
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPissGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 400-482 6.66e-15

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 [Multi-domain]  Cd Length: 83  Bit Score: 71.49  E-value: 6.66e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    400 SAPRNVQVRTLSSSTMVITWEPPETPNGqvTGYKVYYTTNSNQPEASWNSQMVDNSELT-TVSELTPHAIYTVRVQAYTS 478
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVNVTPSSTSyTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 386769894    479 MGAG 482
Cdd:smart00060   80 AGEG 83
fn3 pfam00041
Fibronectin type III domain;
794-878 1.76e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 70.52  E-value: 1.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   794 GPPSNITIRFQTPDVLCVTWDPPtrEHRNGIITRYDVQFHKKIDHGLGSERNM--TLRKAVFTNLEENTEYIFRVRAYTK 871
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPP--PDGNGPITGYEVEYRPKNSGEPWNEITVpgTTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*..
gi 386769894   872 QGAGPFS 878
Cdd:pfam00041   79 GGEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 24-111 1.96e-14

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 70.23  E-value: 1.96e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894     24 PQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTQSRYTVLEQpGGISILRIEPVRAgRDDAPYECVAENGVGDaV 103
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRS-GSTSTLTISNVTP-EDSGTYTCAATNSSGS-A 77


                    ....*...
gi 386769894    104 SADATLTI 111
Cdd:smart00410   78 SSGTTLTV 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 794-885 9.47e-14

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 [Multi-domain]  Cd Length: 93  Bit Score: 68.68  E-value: 9.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  794 GPPSNITIRFQTPDVLCVTWDPPtrEHRNGIITRYDVQFHKKIDHGLG--SERNMTLRKAVFTNLEENTEYIFRVRAYTK 871
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPP--EDDGGPITGYVVEYREKGSGDWKevEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|....
gi 386769894  872 QGAGPFSDKLIVET 885
Cdd:cd00063    80 GGESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 794-875 3.35e-13

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 [Multi-domain]  Cd Length: 83  Bit Score: 66.87  E-value: 3.35e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    794 GPPSNITIRFQTPDVLCVTWDPPTREHRNGIITRYDVQFHKKIDHGLGSERNMTLRKAVFTNLEENTEYIFRVRAYTKQG 873
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 386769894    874 AG 875
Cdd:smart00060   82 EG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
747-1149 1.44e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 69.65  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  747 SGPQMTKKRFDNLERGVEYEFRVAGSNHIGIGQETVKIFQTPEGTPGGPPSNITIRFQTPDVLCVTWDPPTREHrngiIT 826
Cdd:COG3401   187 VTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD----AT 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  827 RYDVQFHKKIDHGLgsERNMTLRKAVFT--NLEENTEYIFRVRAYTKQG-AGPFSDKLIVETERDMGRAPMSLQAEATSE 903
Cdd:COG3401   263 GYRVYRSNSGDGPF--TKVATVTTTSYTdtGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTPPAAPSGLTATAVGS 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  904 QTAEIWWEPVTSrGKLLGYKIFYTmTAVEDLDDWQTKTVGLTESADLvNLEKFAQYAVAIAARFKNGL-GRLSEKVTVRI 982
Cdd:COG3401   341 SSITLSWTASSD-ADVTGYNVYRS-TSGGGTYTKIAETVTTTSYTDT-GLTPGTTYYYKVTAVDAAGNeSAPSEEVSATT 417

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  983 -------KPEDVPLNLRAHDVSTHSMTLSWSPPIRLTPVNYKISFDAMKVFVDSQGFSQTQIVPKREIILKHYVKTHTIN 1055
Cdd:COG3401   418 asaasgeSLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLV 497

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1056 ELSPFTTYNVNVSAIpSDYSYRPPTKITVTTQMAAPQPMVKPDFYGVVNGEEILVILPQASEEYGPISHYYLVVVPEDKS 1135
Cdd:COG3401   498 GGSGASSVTNSVSVI-GASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITT 576

                         410
                  ....*....|....
gi 386769894 1136 NLHKIPDQFLTDDL 1149
Cdd:COG3401   577 LGGSLLTTTSTNTN 590
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 215-285 3.06e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 55.26  E-value: 3.06e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894   215 PPTFSRPPETiSEVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPIGRN----VLQLINIQE--SANYTCIA 285
Cdd:pfam13927    1 KPVITVSPSS-VTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSgsnsTLTISNVTRsdAGTYTCVA 76
fn3 pfam00041
Fibronectin type III domain;
986-1078 4.77e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.03  E-value: 4.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   986 DVPLNLRAHDVSTHSMTLSWSPPIRL--TPVNYKISFDAmkvfVDSQGFSQTQIVPKREIilkhyvkTHTINELSPFTTY 1063
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGngPITGYEVEYRP----KNSGEPWNEITVPGTTT-------SVTLTGLKPGTEY 69

                           90
                   ....*....|....*
gi 386769894  1064 NVNVSAIPSDYSYRP 1078
Cdd:pfam00041   70 EVRVQAVNGGGEGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 892-981 9.82e-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 [Multi-domain]  Cd Length: 93  Bit Score: 51.34  E-value: 9.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  892 APMSLQAEATSEQTAEIWWEPVTS-RGKLLGYKIFYTMTaveDLDDWQT--KTVGLTESADLVNLEKFAQYAVAIAARFK 968
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDdGGPITGYVVEYREK---GSGDWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|...
gi 386769894  969 NGLGRLSEKVTVR 981
Cdd:cd00063    80 GGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 988-1070 2.40e-07

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 [Multi-domain]  Cd Length: 83  Bit Score: 49.92  E-value: 2.40e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    988 PLNLRAHDVSTHSMTLSWSPPIRLTPVNYKISFDAMKVFVDSQGFSQTQIVPKReiilkhyvkTHTINELSPFTTYNVNV 1067
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSST---------SYTLTGLKPGTEYEFRV 74


                    ...
gi 386769894   1068 SAI 1070
Cdd:smart00060   75 RAV 77
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 227-300 3.19e-07

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.81  E-value: 3.19e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    227 EVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENE-----MPIGRNVLQLINIQE--SANYTCIAASTLGQIDSVSVVK 299
Cdd:smart00410    5 TVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGrfsvsRSGSTSTLTISNVTPedSGTYTCAATNSSGSASSGTTLT 84


                    .
gi 386769894    300 V 300
Cdd:smart00410   85 V 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 712-778 3.74e-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 [Multi-domain]  Cd Length: 83  Bit Score: 43.76  E-value: 3.74e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    712 SIELEWERPAQTYGelRGYRLRWGVKDQALK---EEMLSGPQMTKKRFDNLERGVEYEFRVAGSNHIGIG 778
Cdd:smart00060   16 SVTLSWEPPPDDGI--TGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
 
Name Accession Description Interval E-value
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1378-1615 1.81e-177

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 536.21  E-value: 1.81e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1378 EHNKSKNRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRL 1457
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1458 EERTRIKCDQYWPTRGTETYGQIFVTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRR 1537
Cdd:cd14553    81 EERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894 1538 CRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAIIC 1615
Cdd:cd14553   161 VKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAVTC 238
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1664-1901 5.92e-173

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 524.01  E-value: 5.92e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1664 ANLPCNKHKNRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVML 1743
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1744 TKLKEMGREKCFQYWPHERSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDF 1823
Cdd:cd14554    81 TKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894 1824 IGQVHKTKEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAAL 1901
Cdd:cd14554   161 IGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1618-1909 2.08e-172

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 524.68  E-value: 2.08e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1618 TEVPARNLHTHLQKLLITEPGETISGMEVEFKKLSNVKMDSSKFVTANLPCNKHKNRLVHILPYESSRVYLTPIHGIEGS 1697
Cdd:cd14628     1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1698 DYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHERSVRYQYYVVDPIAEY 1777
Cdd:cd14628    81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1778 NMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRSGVFITL 1857
Cdd:cd14628   161 NMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITL 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386769894 1858 SIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALEYLGSFDN 1909
Cdd:cd14628   241 SIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGSFDH 292
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1618-1906 7.43e-171

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 520.45  E-value: 7.43e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1618 TEVPARNLHTHLQKLLITEPGETISGMEVEFKKLSNVKMDSSKFVTANLPCNKHKNRLVHILPYESSRVYLTPIHGIEGS 1697
Cdd:cd14627     2 TEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1698 DYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHERSVRYQYYVVDPIAEY 1777
Cdd:cd14627    82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1778 NMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRSGVFITL 1857
Cdd:cd14627   162 NMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITL 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 386769894 1858 SIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALEYLGS 1906
Cdd:cd14627   242 SIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1618-1907 3.40e-169

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 516.20  E-value: 3.40e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1618 TEVPARNLHTHLQKLLITEPGETISGMEVEFKKLSNVKMDSSKFVTANLPCNKHKNRLVHILPYESSRVYLTPIHGIEGS 1697
Cdd:cd14629     2 TEVPARNLYAHIQKLTQVPPGESVTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1698 DYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHERSVRYQYYVVDPIAEY 1777
Cdd:cd14629    82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1778 NMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRSGVFITL 1857
Cdd:cd14629   162 NMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITL 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 386769894 1858 SIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALEYLGSF 1907
Cdd:cd14629   242 SIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGSF 291
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1340-1615 5.82e-162

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 496.10  E-value: 5.82e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1340 SEFANHIERLKSNDNQKFSQEYESIEPGQQFTWDNSNLEHNKSKNRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGY 1419
Cdd:cd14626     1 SDLADNIERLKANDGLKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1420 RKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTETYGQIFVTITETQELATYSIRTFQ 1499
Cdd:cd14626    81 RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1500 LCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKII 1579
Cdd:cd14626   161 LYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTV 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 386769894 1580 DIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAIIC 1615
Cdd:cd14626   241 DIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATC 276
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1334-1616 6.97e-157

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 482.31  E-value: 6.97e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1334 HPPIPISEFANHIERLKSNDNQKFSQEYESIEPGQQFTWDNSNLEHNKSKNRYANVTAYDHSRVQLPAVEGVVGSDYINA 1413
Cdd:cd14624     1 HPPIPILELADHIERLKANDNLKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1414 NYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTETYGQIFVTITETQELATY 1493
Cdd:cd14624    81 NYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVELATY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1494 SIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERM 1573
Cdd:cd14624   161 CVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 386769894 1574 KHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAIICG 1616
Cdd:cd14624   241 KHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCG 283
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1334-1615 5.90e-153

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 471.50  E-value: 5.90e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1334 HPPIPISEFANHIERLKSNDNQKFSQEYESIEPGQQFTWDNSNLEHNKSKNRYANVTAYDHSRVQLPAVEGVVGSDYINA 1413
Cdd:cd14625     1 HPPIPISELAEHTERLKANDNLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1414 NYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTETYGQIFVTITETQELATY 1493
Cdd:cd14625    81 NYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELATF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1494 SIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERM 1573
Cdd:cd14625   161 CVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 386769894 1574 KHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAIIC 1615
Cdd:cd14625   241 KHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1643-1902 4.12e-109

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 348.11  E-value: 4.12e-109
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   1643 GMEVEFKKLSNVKMDSSKFVTANLPCNKHKNRLVHILPYESSRVYLTPIHGiEGSDYVNASFIDGYRYRSAYIAAQGPVQ 1722
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPG-EGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   1723 DAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHE--RSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTV 1800
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEegEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   1801 RQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQFgqDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILR 1880
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTS--TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                           250       260
                    ....*....|....*....|..
gi 386769894   1881 SQRPAMVQTEDQYHFCYRAALE 1902
Cdd:smart00194  238 SQRPGMVQTEEQYIFLYRAILE 259
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1356-1611 6.38e-109

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 347.72  E-value: 6.38e-109
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   1356 KFSQEYESIEPGQQ--FTWDNSNLEHNKSKNRYANVTAYDHSRVQLPAVEGVvGSDYINANYCDGYRKHNAYVATQGPLQ 1433
Cdd:smart00194    1 GLEEEFEKLDRLKPddESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGE-GSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   1434 ETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWP--TRGTETYGQIFVTITETQELATYSIRTFQLCRQGFNDRREI 1511
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPdeEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   1512 KQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQ 1591
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                           250       260
                    ....*....|....*....|
gi 386769894   1592 RNYMVQTEDQYIFIHDAILE 1611
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1380-1611 4.09e-107

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 341.53  E-value: 4.09e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  1380 NKSKNRYANVTAYDHSRVQLPAVEGvvGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEE 1459
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  1460 RTRIKCDQYWPT--RGTETYGQIFVTIT-ETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLR 1536
Cdd:pfam00102   79 KGREKCAQYWPEeeGESLEYGDFTVTLKkEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769894  1537 RCRALTP-PESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:pfam00102  159 KVRKSSLdGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1410-1607 5.73e-107

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 339.71  E-value: 5.73e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTETYGQIFVTITETQE 1489
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1490 LATYSIRTFQLCRQ------GFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCY 1563
Cdd:cd14549    81 LATYTVRTFSLKNLklkkvkGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTGTY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 386769894 1564 IVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHD 1607
Cdd:cd14549   161 IVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1669-1902 6.91e-99

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 317.65  E-value: 6.91e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  1669 NKHKNRLVHILPYESSRVYLTPIHGieGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKE 1748
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG--PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  1749 MGREKCFQYWP--HERSVRYQYYVVDPIAE-YNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIG 1825
Cdd:pfam00102   79 KGREKCAQYWPeeEGESLEYGDFTVTLKKEkEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894  1826 QVHKtKEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:pfam00102  159 KVRK-SSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1341-1614 1.20e-98

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 318.91  E-value: 1.20e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1341 EFANHIERLKSNDNQKFSQEYESIEPGQQFTWDNSNLEHNKSKNRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYR 1420
Cdd:cd14633     1 DLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1421 KHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTrGTETYGQIFVTITETQELATYSIRTFQL 1500
Cdd:cd14633    81 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPD-DTEIYKDIKVTLIETELLAEYVIRTFAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1501 CRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIID 1580
Cdd:cd14633   160 EKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVD 239

                         250       260       270
                  ....*....|....*....|....*....|....
gi 386769894 1581 IYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAII 1614
Cdd:cd14633   240 IYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1357-1614 3.14e-96

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 311.97  E-value: 3.14e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1357 FSQEYESIE---PGQQFTWDNSNLEHNKSKNRYANVTAYDHSRVQLPAVEGVVG--SDYINANYCDGYRKHNAYVATQGP 1431
Cdd:cd17667     1 FSEDFEEVQrctADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1432 LQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTETYGQIFVTITETQELATYSIRTFQLCR--------- 1502
Cdd:cd17667    81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqkg 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1503 --QGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIID 1580
Cdd:cd17667   161 npKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVN 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 386769894 1581 IYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAII 1614
Cdd:cd17667   241 VLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1410-1607 4.66e-94

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 302.67  E-value: 4.66e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRG--TETYGQIFVTITET 1487
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGgkPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1488 QELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIVID 1567
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGRTGTFIAID 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 386769894 1568 SMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHD 1607
Cdd:cd00047   161 ILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1378-1615 3.40e-92

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 298.86  E-value: 3.40e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1378 EHNKSKNRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRL 1457
Cdd:cd14630     1 DENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1458 EERTRIKCDQYWPTRgTETYGQIFVTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRR 1537
Cdd:cd14630    81 VEVGRVKCVRYWPDD-TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQ 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894 1538 CRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAIIC 1615
Cdd:cd14630   160 VKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEACLC 237
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1334-1620 2.66e-89

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 293.08  E-value: 2.66e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1334 HPPIPISEFANHIERLKSNDNQKFSQEYESIEPGQ-QFTWDNSNLEHNKSKNRYANVTAYDHSRVQLPAVEGVVGSDYIN 1412
Cdd:cd14621     5 YPPLPVDKLEEEINRRMADDNKLFREEFNALPACPiQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYIN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1413 ANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTETYGQIFVTITETQELAT 1492
Cdd:cd14621    85 ASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLVD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1493 YSIRTFqlCRQGFND------RREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIVI 1566
Cdd:cd14621   165 YTVRKF--CIQQVGDvtnkkpQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVI 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386769894 1567 DSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAIICGVTEV 1620
Cdd:cd14621   243 DAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1410-1612 1.49e-88

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 286.81  E-value: 1.49e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTrGTETYGQIFVTITETQE 1489
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPD-DTEVYGDIKVTLVETEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1490 LATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIVIDSM 1569
Cdd:cd14555    80 LAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTGCYIVIDIM 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 386769894 1570 LERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEA 1612
Cdd:cd14555   160 LDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEA 202
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1385-1606 8.38e-88

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 285.40  E-value: 8.38e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1385 RYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIK 1464
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1465 CDQYWPTRGTET-YGQIFVTITETQELATYSIRTFQLCRQGfnDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTP 1543
Cdd:cd14548    81 CDHYWPFDQDPVyYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769894 1544 PESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIH 1606
Cdd:cd14548   159 QEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1410-1615 1.16e-86

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 281.55  E-value: 1.16e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRgTETYGQIFVTITETQE 1489
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD-SDTYGDIKITLLKTET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1490 LATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIVIDSM 1569
Cdd:cd14632    80 LAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTGCYIVLDVM 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 386769894 1570 LERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAIIC 1615
Cdd:cd14632   160 LDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1699-1898 1.21e-86

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 281.48  E-value: 1.21e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHERSVRYQY--YVVDPIAE 1776
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYgdITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1777 YNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRSGVFIT 1856
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARK--PNGPIVVHCSAGVGRTGTFIA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 386769894 1857 LSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYR 1898
Cdd:cd00047   159 IDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1699-1899 3.63e-85

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 277.23  E-value: 3.63e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHERSVRYQYYVVDPIAEYN 1778
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1779 MPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQFGqDGPITVHCSAGVGRSGVFITLS 1858
Cdd:cd14552    81 YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSG-NHPITVHCSAGAGRTGTFCALS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 386769894 1859 IVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRA 1899
Cdd:cd14552   160 TVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKV 200
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1396-1614 2.88e-83

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 272.28  E-value: 2.88e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1396 RVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTrGTE 1475
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD-DTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1476 TYGQIFVTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSA 1555
Cdd:cd14631    80 VYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894 1556 GVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAII 1614
Cdd:cd14631   160 GAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1359-1606 1.56e-82

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 272.70  E-value: 1.56e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1359 QEYESIE---PGQQFTwdNSNLEHNKSKNRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQET 1435
Cdd:cd14543     7 EEYEDIRrepPAGTFL--CSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1436 FVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRG--TETYGQIFVTITETQELATYSIRTFQLCRQGFNDRREIKQ 1513
Cdd:cd14543    85 YSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEgsSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTH 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1514 LQFTAWPDHGVPDHPAPFLQFL--------RRCRALTPPESG-----PVIVHCSAGVGRTGCYIVIDSMLERMKHEKIID 1580
Cdd:cd14543   165 FQFTSWPDFGVPSSAAALLDFLgevrqqqaLAVKAMGDRWKGhppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLN 244

                         250       260
                  ....*....|....*....|....*.
gi 386769894 1581 IYGHVTCLRAQRNYMVQTEDQYIFIH 1606
Cdd:cd14543   245 VMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1667-1902 3.88e-82

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 270.04  E-value: 3.88e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1667 PCNKHKNRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKL 1746
Cdd:cd14553     1 EVNKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1747 KEMGREKCFQYWPHERSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQ 1826
Cdd:cd14553    81 EERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894 1827 VhktKEQFGQD-GPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14553   161 V---KACNPPDaGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1661-1897 3.90e-82

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 271.55  E-value: 3.90e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1661 FVTANLPCNKHKNRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIV 1740
Cdd:cd14543    21 FLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1741 VMLTKLKEMGREKCFQYWPHE--RSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGE 1818
Cdd:cd14543   101 VMTTRVVERGRVKCGQYWPLEegSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFGVPSSAA 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1819 GFIDFIGQVHKTKEQF---------GQDG--PITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMV 1887
Cdd:cd14543   181 ALLDFLGEVRQQQALAvkamgdrwkGHPPgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSI 260

                         250
                  ....*....|
gi 386769894 1888 QTEDQYHFCY 1897
Cdd:cd14543   261 QTPDQYYFCY 270
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1674-1902 5.26e-82

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 269.22  E-value: 5.26e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1674 RLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREK 1753
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1754 CFQYWPHERSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQ 1833
Cdd:cd14623    81 CAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQ 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894 1834 FGqDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14623   161 SG-NHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1386-1611 3.88e-80

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 264.11  E-value: 3.88e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1386 YANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKC 1465
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1466 DQYWPTRGTETYGQIFVTITETQELATYSIRTF----QLCrQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRAL 1541
Cdd:cd14620    81 YQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFciqpQLP-DGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSV 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1542 TPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:cd14620   160 NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1410-1610 2.19e-77

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 255.29  E-value: 2.19e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTETYGQIFVTITETQE 1489
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1490 LATYSIRTFQL--------CRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTG 1561
Cdd:cd17668    81 LAYYTVRNFTLrntkikkgSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 386769894 1562 CYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAIL 1610
Cdd:cd17668   161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1698-1903 4.16e-76

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 251.46  E-value: 4.16e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1698 DYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHERSVRYQYYVVDPIAEY 1777
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1778 NMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQFGqDGPITVHCSAGVGRSGVFITL 1857
Cdd:cd14622    81 LLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTG-NHPIVVHCSAGAGRTGTFIAL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 386769894 1858 SIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALEY 1903
Cdd:cd14622   160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1384-1611 5.53e-74

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 246.27  E-value: 5.53e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1384 NRYANVTAYDHSRVQLpAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRI 1463
Cdd:cd14615     1 NRYNNVLPYDISRVKL-SVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1464 KCDQYWPTRGTETYGQIFVTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQF---LRRCRA 1540
Cdd:cd14615    80 KCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFrhlVREYMK 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386769894 1541 LTPPESgPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:cd14615   160 QNPPNS-PILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1674-1895 2.29e-73

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 244.19  E-value: 2.29e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1674 RLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREK 1753
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1754 CFQYWPH-ERSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDgsSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKE 1832
Cdd:cd14548    81 CDHYWPFdQDPVYYGDITVTMLSESVLPDWTIREFKLERGDE--VRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769894 1833 QfgQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHF 1895
Cdd:cd14548   159 Q--EKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1410-1606 3.62e-72

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 239.73  E-value: 3.62e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPT--RGTETYGQIFVTITET 1487
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1488 QELATYSIRTFQLC--RQGFNDRrEIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIV 1565
Cdd:cd14557    81 KICPDYIIRKLNINnkKEKGSGR-EVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRTGTYIG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 386769894 1566 IDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIH 1606
Cdd:cd14557   160 IDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1673-1902 1.17e-71

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 239.72  E-value: 1.17e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1673 NRLVHILPYESSRVYLTpIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGRE 1752
Cdd:cd14615     1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1753 KCFQYWPHERSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKE 1832
Cdd:cd14615    80 KCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYMK 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1833 QFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14615   160 QNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1375-1610 1.31e-71

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 239.73  E-value: 1.31e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1375 SNLEHNKSKNRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMM 1454
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1455 TRLEERTRIKCDQYWPTRGTETYGQIFVTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQF 1534
Cdd:cd14554    81 TKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894 1535 LRRCRALTPP--ESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAIL 1610
Cdd:cd14554   161 IGQVHKTKEQfgQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1380-1609 1.92e-71

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 240.06  E-value: 1.92e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1380 NKSKNRYANVTAYDHSRVQLPAVE-GVVGSDYINANYC------DGYRKHN-AYVATQGPLQETFVDFWRMCWELKTATI 1451
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDpNVPGSDYINANYIrnenegPTTDENAkTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1452 VMMTRLEERTRIKCDQYWPTRG-TETYGQIFVTITETQELATYSIRTFQLCRQG-FNDRREIKQLQFTAWPDHGVPDHPA 1529
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGmQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDqGDPIREIWHYQYLSWPDHGVPSDPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1530 PFLQFL----RRCRALtpPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKI---IDIYGHVTCLRAQRNYMVQTEDQY 1602
Cdd:cd14544   161 GVLNFLedvnQRQESL--PHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQY 238


                  ....*..
gi 386769894 1603 IFIHDAI 1609
Cdd:cd14544   239 KFIYVAV 245
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1410-1606 4.03e-71

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 237.12  E-value: 4.03e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTETYGQIFVTITETQE 1489
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1490 LATYSIRTFQLCRQ--GFNDR--REIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIV 1565
Cdd:cd14551    81 LVDYTTRKFCIQKVnrGIGEKrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTGTFIV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 386769894 1566 IDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIH 1606
Cdd:cd14551   161 IDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1664-1902 4.62e-71

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 239.94  E-value: 4.62e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1664 ANLPCNKHKNRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVML 1743
Cdd:cd14626    36 SNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMM 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1744 TKLKEMGREKCFQYWPHERSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDF 1823
Cdd:cd14626   116 TRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAF 195

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894 1824 IGQVHKTKEQfgQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14626   196 LRRVKACNPP--DAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1384-1610 7.22e-71

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 237.53  E-value: 7.22e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1384 NRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRI 1463
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1464 KCDQYWPTRGTE-TYGQIFVTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQF--LRRCRA 1540
Cdd:cd14618    81 LCDHYWPSESTPvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFreLVREHV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1541 LTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAIL 1610
Cdd:cd14618   161 QATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1384-1613 3.89e-70

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 235.55  E-value: 3.89e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1384 NRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRI 1463
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1464 KCDQYWPTRGTE-TYGQIFVTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALT 1542
Cdd:cd14619    81 KCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769894 1543 PP--ESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAI 1613
Cdd:cd14619   161 DQtmSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1384-1606 4.91e-69

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 231.90  E-value: 4.91e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1384 NRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYR-KHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERtR 1462
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1463 IKCDQYWPTRGTETYGQIFVTITETQELATYSIRTFQLCRQGfnDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCR--A 1540
Cdd:cd14547    80 EKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEeaR 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769894 1541 LTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIH 1606
Cdd:cd14547   158 QTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1384-1606 7.75e-69

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 231.35  E-value: 7.75e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1384 NRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRI 1463
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1464 KCDQYWPT-RGTETYGQIFVTITETQELATYSIRTFQLCRQG-FNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRAL 1541
Cdd:cd14617    81 KCDHYWPAdQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEqLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894 1542 T--PPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIH 1606
Cdd:cd14617   161 InrTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1373-1610 9.95e-69

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 231.70  E-value: 9.95e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1373 DNSNLEHNKSKNRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIV 1452
Cdd:cd14614     5 FAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1453 MMTRLEERTRIKCDQYWP-TRGTETYGQIFVTITETQELATYSIRTFQLCRQgfNDRREIKQLQFTAWPDHGVPDHPA-- 1529
Cdd:cd14614    85 MLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYA--DEVQDVMHFNYTAWPDHGVPTANAae 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1530 PFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAI 1609
Cdd:cd14614   163 SILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242


                  .
gi 386769894 1610 L 1610
Cdd:cd14614   243 Q 243
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1664-1905 5.41e-68

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 231.14  E-value: 5.41e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1664 ANLPCNKHKNRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVML 1743
Cdd:cd14625    42 SNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMM 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1744 TKLKEMGREKCFQYWPHERSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDF 1823
Cdd:cd14625   122 TKLEEKSRIKCDQYWPSRGTETYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAF 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1824 IGQVHKTKEQfgQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALEY 1903
Cdd:cd14625   202 LRRVKTCNPP--DAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEA 279


                  ..
gi 386769894 1904 LG 1905
Cdd:cd14625   280 VA 281
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1669-1904 1.11e-67

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 228.89  E-value: 1.11e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1669 NKHKNRLVHILPYESSRVYLTPI-HGIEGSDYVNASFI----DGYRYRS---AYIAAQGPVQDAAEDFWRMLWEHNSTIV 1740
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRdPNVPGSDYINANYIrnenEGPTTDEnakTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1741 VMLTKLKEMGREKCFQYWPHERSVR-YQYYVVDPIAEYNMPQYKLREFKVTD-ARDGSSRTVRQFQFIDWPEQGVPKSGE 1818
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQKqYGPYRVQNVSEHDTTDYTLRELQVSKlDQGDPIREIWHYQYLSWPDHGVPSDPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1819 GFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVL---DVFQTVRILRSQRPAMVQTEDQYHF 1895
Cdd:cd14544   161 GVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDcdiDIQKTIQMVRSQRSGMVQTEAQYKF 240


                  ....*....
gi 386769894 1896 CYRAALEYL 1904
Cdd:cd14544   241 IYVAVAQYI 249
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1357-1611 5.18e-67

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 228.85  E-value: 5.18e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1357 FSQEYESIEPGQQFT------------------WDNSNLEHNKSKNRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDG 1418
Cdd:cd14627    12 YIQKLAQVEVGEHVTgmelefkrlanskahtsrFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1419 YRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTETYGQIFVTITETQELATYSIRTF 1498
Cdd:cd14627    92 YRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREF 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1499 QLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPP--ESGPVIVHCSAGVGRTGCYIVIDSMLERMKHE 1576
Cdd:cd14627   172 KVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYE 251

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 386769894 1577 KIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:cd14627   252 GVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALE 286
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1384-1606 5.51e-67

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 225.94  E-value: 5.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1384 NRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRI 1463
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1464 KCDQYWP--TRGTETYGQIFVTITETQELATYSIRTFQLCRQGfnDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRAL 1541
Cdd:cd14616    81 RCHQYWPedNKPVTVFGDIVITKLMEDVQIDWTIRDLKIERHG--DYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRAS 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386769894 1542 TPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIH 1606
Cdd:cd14616   159 RAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1374-1611 6.76e-67

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 228.46  E-value: 6.76e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1374 NSNLEHNKSKNRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVM 1453
Cdd:cd14628    46 SANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1454 MTRLEERTRIKCDQYWPTRGTETYGQIFVTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQ 1533
Cdd:cd14628   126 LTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFID 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1534 FLRRCRALTPP--ESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:cd14628   206 FIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALE 285
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1673-1904 2.37e-66

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 224.38  E-value: 2.37e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1673 NRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGRE 1752
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1753 KCFQYWPHERS-VRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTK 1831
Cdd:cd14619    81 KCEHYWPLDYTpCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769894 1832 EQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALEYL 1904
Cdd:cd14619   161 DQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1677-1902 4.73e-66

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 223.66  E-value: 4.73e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1677 HILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQ 1756
Cdd:cd14620     3 NILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCYQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1757 YWPHERSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDG---SSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQ 1833
Cdd:cd14620    83 YWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDgckAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKSVNPV 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894 1834 FGqdGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14620   163 HA--GPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1334-1611 7.31e-66

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 225.38  E-value: 7.31e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1334 HPPIPISEFANHIERL----KSNDNQKFSQEYESIEPGQQFT--WDNSNLEHNKSKNRYANVTAYDHSRVQLPAVEGVVG 1407
Cdd:cd14629     1 NTEVPARNLYAHIQKLtqvpPGESVTAMELEFKLLANSKAHTsrFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1408 SDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTETYGQIFVTITET 1487
Cdd:cd14629    81 SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1488 QELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPP--ESGPVIVHCSAGVGRTGCYIV 1565
Cdd:cd14629   161 YNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFIT 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 386769894 1566 IDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:cd14629   241 LSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALE 286
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1664-1902 3.65e-65

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 223.07  E-value: 3.65e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1664 ANLPCNKHKNRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVML 1743
Cdd:cd14624    42 SNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMM 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1744 TKLKEMGREKCFQYWPHERSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDF 1823
Cdd:cd14624   122 TKLEERSRVKCDQYWPSRGTETYGLIQVTLLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAF 201

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894 1824 IGQVHKTKEQfgQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14624   202 LRRVKTCNPP--DAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1410-1607 1.23e-63

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 215.96  E-value: 1.23e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCD-GYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPT-RGTETYGQIFVTITET 1487
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSgEYEGEYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1488 QEL--ATYSIRTFQLCRQGfNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRAL--TPPESGPVIVHCSAGVGRTGCY 1563
Cdd:cd18533    81 EENddGGFIVREFELSKED-GKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELndSASLDPPIIVHCSAGVGRTGTF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386769894 1564 IVIDSMLERMKHEKIID---------IYGHVTCLRAQRNYMVQTEDQYIFIHD 1607
Cdd:cd18533   160 IALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1669-1904 1.34e-63

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 217.58  E-value: 1.34e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1669 NKHKNRLVHILPYESSRVYLTPIHGIE-GSDYVNASFI--------DGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTI 1739
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHDGDPNEpVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1740 VVMLTKLKEMGREKCFQYWPHERSVR-YQYYVVDPIAEYNMPQYKLREFKVTDARDGSS-RTVRQFQFIDWPEQGVPKSG 1817
Cdd:cd14605    82 IVMTTKEVERGKSKCVKYWPDEYALKeYGVMRVRNVKESAAHDYILRELKLSKVGQGNTeRTVWQYHFRTWPDHGVPSDP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1818 EGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGV---LDVFQTVRILRSQRPAMVQTEDQYH 1894
Cdd:cd14605   162 GGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQYR 241

                         250
                  ....*....|
gi 386769894 1895 FCYRAALEYL 1904
Cdd:cd14605   242 FIYMAVQHYI 251
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1669-1902 2.10e-63

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 216.43  E-value: 2.10e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1669 NKHKNRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKE 1748
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1749 MGREKCFQYWPHERSVrYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVH 1828
Cdd:cd14630    83 VGRVKCVRYWPDDTEV-YGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQVK 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386769894 1829 KTKEQfgQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14630   162 FLNPP--DAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1664-1902 3.03e-63

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 217.21  E-value: 3.03e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1664 ANLPCNKHKNRLVHILPYESSRVYLTPIHGIEG--SDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVV 1741
Cdd:cd17667    22 SNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1742 MLTKLKEMGREKCFQYWPHERSVRYQYYVV-----DPIAEYNMPQYKLREFKVTDARDG------SSRTVRQFQFIDWPE 1810
Cdd:cd17667   102 MITNLVEKGRRKCDQYWPTENSEEYGNIIVtlkstKIHACYTVRRFSIRNTKVKKGQKGnpkgrqNERTVIQYHYTQWPD 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1811 QGVPKSGEGFIDFIGQvhKTKEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTE 1890
Cdd:cd17667   182 MGVPEYALPVLTFVRR--SSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTE 259

                         250
                  ....*....|..
gi 386769894 1891 DQYHFCYRAALE 1902
Cdd:cd17667   260 EQYIFIHDALLE 271
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1699-1897 4.24e-63

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 214.14  E-value: 4.24e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHERSVRYQYYVVDPIAEYN 1778
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1779 MPQYKLREF-----KVTDARDGSS-RTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPITVHCSAGVGRSG 1852
Cdd:cd14549    81 LATYTVRTFslknlKLKKVKGRSSeRVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANP--PGAGPIVVHCSAGVGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 386769894 1853 VFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCY 1897
Cdd:cd14549   159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1410-1613 5.28e-63

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 213.78  E-value: 5.28e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYC------DGYRkhnaYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTET---YGQI 1480
Cdd:cd14538     1 YINASHIripvggDTYH----YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPlicGGRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1481 FVTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTppESGPVIVHCSAGVGRT 1560
Cdd:cd14538    77 EVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIH--NSGPIVVHCSAGIGRT 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386769894 1561 GCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAI 1613
Cdd:cd14538   155 GVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1699-1897 8.83e-63

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 213.04  E-value: 8.83e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGrEKCFQYWPHERSVRYQYYVVDPIAEYN 1778
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKD-QSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1779 MPQYKLREFKVT-DARDG-SSRTVRQFQFIDWP-EQGVPKSGEGFIDFIGQVHKTKEQFGqDGPITVHCSAGVGRSGVFI 1855
Cdd:cd14556    80 DEDVISRIFRLQnTTRPQeGYRMVQQFQFLGWPrDRDTPPSKRALLKLLSEVEKWQEQSG-EGPIVVHCLNGVGRSGVFC 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 386769894 1856 TLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCY 1897
Cdd:cd14556   159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1365-1613 1.59e-62

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 214.74  E-value: 1.59e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1365 EPGQQFTWDNSNLEHNKSKNRYANVTAYDHSRVQLPAVE-GVVGSDYINANYCDGY-----RKHNAYVATQGPLQETFVD 1438
Cdd:cd14606     3 EVKNLHQRLEGQRPENKSKNRYKNILPFDHSRVILQGRDsNIPGSDYINANYVKNQllgpdENAKTYIASQGCLEATVND 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1439 FWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTET-YGQIFVTITETQELATYSIRTFQLCRQGFNDR-REIKQLQF 1516
Cdd:cd14606    83 FWQMAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQRaYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1517 TAWPDHGVPDHPAPFLQFLRR--CRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKI---IDIYGHVTCLRAQ 1591
Cdd:cd14606   163 LSWPDHGVPSEPGGVLSFLDQinQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQ 242

                         250       260
                  ....*....|....*....|..
gi 386769894 1592 RNYMVQTEDQYIFIHDAILEAI 1613
Cdd:cd14606   243 RSGMVQTEAQYKFIYVAIAQFI 264
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1410-1609 3.01e-62

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 211.36  E-value: 3.01e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTETYGQIFVTITETQE 1489
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1490 LATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPE-SGPVIVHCSAGVGRTGCYIVIDS 1568
Cdd:cd14552    81 YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSgNHPITVHCSAGAGRTGTFCALST 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 386769894 1569 MLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAI 1609
Cdd:cd14552   161 VLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1409-1612 3.10e-62

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 211.80  E-value: 3.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1409 DYINANYCD----GYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWP-TRGTETYGQIFVT 1483
Cdd:cd14541     1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPdLGETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1484 ITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCY 1563
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCSAGIGRTGVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386769894 1564 IVIDSMLERMK-HEKI--IDIyghVTCLRAQRNYMVQTEDQYIFIHDAILEA 1612
Cdd:cd14541   161 ITMETAMCLIEaNEPVypLDI---VRTMRDQRAMLIQTPSQYRFVCEAILRV 209
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1669-1903 3.29e-62

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 215.27  E-value: 3.29e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1669 NKHKNRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKE 1748
Cdd:cd14621    52 NKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1749 MGREKCFQYWPHERSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSS----RTVRQFQFIDWPEQGVPKSGEGFIDFI 1824
Cdd:cd14621   132 RKECKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVGDVTNkkpqRLITQFHFTSWPDFGVPFTPIGMLKFL 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894 1825 GQVHKTKEQFGqdGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALEY 1903
Cdd:cd14621   212 KKVKNCNPQYA--GAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEH 288
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1669-1902 1.37e-60

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 209.51  E-value: 1.37e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1669 NKHKNRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKE 1748
Cdd:cd14633    40 NRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1749 MGREKCFQYWPHERSVrYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVh 1828
Cdd:cd14633   120 VGRVKCCKYWPDDTEI-YKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQV- 197

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386769894 1829 KTKEQfGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14633   198 KSKSP-PNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1673-1898 1.67e-60

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 207.46  E-value: 1.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1673 NRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGRE 1752
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1753 KCFQYWPHER-SVRYQYYVVDPIAEYNMPQYKLREFKV-TDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKT 1830
Cdd:cd14617    81 KCDHYWPADQdSLYYGDLIVQMLSESVLPEWTIREFKIcSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894 1831 KEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYR 1898
Cdd:cd14617   161 INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1385-1611 2.36e-60

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 207.20  E-value: 2.36e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1385 RYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIK 1464
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1465 CDQYWPTRGTETYGQIFVTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRAlTPP 1544
Cdd:cd14623    81 CAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQK-QQQ 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894 1545 ESG--PVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:cd14623   160 QSGnhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1699-1897 2.50e-60

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 206.09  E-value: 2.50e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHERSVrYQYYVVDPIAEYN 1778
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT-YGDIEVELKDTEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1779 MPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFI----GQVHKTKEQFGQDGPITVHCSAGVGRSGVF 1854
Cdd:cd14558    80 SPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIksikQKLPYKNSKHGRSVPIVVHCSDGSSRTGIF 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 386769894 1855 ITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCY 1897
Cdd:cd14558   160 CALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1673-1901 5.11e-60

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 206.33  E-value: 5.11e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1673 NRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGRE 1752
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1753 KCFQYWPHERS-VRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTK 1831
Cdd:cd14618    81 LCDHYWPSESTpVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1832 EQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAAL 1901
Cdd:cd14618   161 QATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1662-1898 5.65e-60

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 206.66  E-value: 5.65e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1662 VTANLPCNKHKNRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVV 1741
Cdd:cd14614     5 FAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1742 MLTKLKEMGREKCFQYWP-HERSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDgsSRTVRQFQFIDWPEQGVP--KSGE 1818
Cdd:cd14614    85 MLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADE--VQDVMHFNYTAWPDHGVPtaNAAE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1819 GFIDFigqVHKTKEQFGQD-GPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCY 1897
Cdd:cd14614   163 SILQF---VQMVRQQAVKSkGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 239


                  .
gi 386769894 1898 R 1898
Cdd:cd14614   240 Q 240
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1699-1897 4.98e-59

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 202.48  E-value: 4.98e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFID-GYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPheRSVRYQYYvvDPIA-- 1775
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWP--SGEYEGEY--GDLTve 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1776 -----EYNMPQYKLREFKVTDArDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGR 1850
Cdd:cd18533    77 lvseeENDDGGFIVREFELSKE-DGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGR 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386769894 1851 SGVFITLSIVLERMQ--------YEGVLD-VFQTVRILRSQRPAMVQTEDQYHFCY 1897
Cdd:cd18533   156 TGTFIALDSLLDELKrglsdsqdLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1673-1898 6.69e-59

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 202.63  E-value: 6.69e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1673 NRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRY-RSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMgR 1751
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYDGeEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1752 EKCFQYWPHERSVRYQYYVVDPIAEYNMPQYKLREFKVTdaRDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTK 1831
Cdd:cd14547    80 EKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLK--YGGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEAR 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894 1832 EQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYR 1898
Cdd:cd14547   158 QTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1380-1610 7.59e-59

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 203.14  E-value: 7.59e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1380 NKSKNRYANVTAYDHSRVQLpAVEGvvgsDYINANYCD---GYRKHnAYVATQGPLQETFVDFWRMCWELKTATIVMMTR 1456
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPL-GDEG----GYINASFIKmpvGDEEF-VYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1457 LEERTRIKCDQYWPT---RGTETYGQIFVTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQ 1533
Cdd:cd14597    77 EVEGGKIKCQRYWPEilgKTTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLT 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894 1534 FLRRCRALTppESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAIL 1610
Cdd:cd14597   157 FISYMRHIH--KSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1699-1904 1.86e-58

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 200.68  E-value: 1.86e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFI----DGYRYRsaYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWP---HERSVRYQYYVV 1771
Cdd:cd14538     1 YINASHIripvGGDTYH--YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdslNKPLICGGRLEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1772 DPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKtkeqFGQDGPITVHCSAGVGRS 1851
Cdd:cd14538    79 SLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRR----IHNSGPIVVHCSAGIGRT 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386769894 1852 GVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALEYL 1904
Cdd:cd14538   155 GVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1667-1906 7.64e-58

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 201.26  E-value: 7.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1667 PCNKHKNRLVHILPYESSRVYLT-PIHGIEGSDYVNASFIDGYRY-----RSAYIAAQGPVQDAAEDFWRMLWEHNSTIV 1740
Cdd:cd14606    16 PENKSKNRYKNILPFDHSRVILQgRDSNIPGSDYINANYVKNQLLgpdenAKTYIASQGCLEATVNDFWQMAWQENSRVI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1741 VMLTKLKEMGREKCFQYWPHERSVR-YQYYVVDPIAEYNMPQYKLREFKVTDARDGSS-RTVRQFQFIDWPEQGVPKSGE 1818
Cdd:cd14606    96 VMTTREVEKGRNKCVPYWPEVGMQRaYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPSEPG 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1819 GFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGV---LDVFQTVRILRSQRPAMVQTEDQYHF 1895
Cdd:cd14606   176 GVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQYKF 255

                         250
                  ....*....|.
gi 386769894 1896 CYRAALEYLGS 1906
Cdd:cd14606   256 IYVAIAQFIET 266
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1644-1902 1.66e-57

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 201.05  E-value: 1.66e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1644 MEVEFKKLSNVKMDSSKFVTANLPCNKHKNRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRS-AYIAAQGPVQ 1722
Cdd:cd14610    19 LEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPRNpAYIATQGPLP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1723 DAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHERSVRYQYYVVDPIAEYNMPQ-YKLREFKVTDARDGSSRTVR 1801
Cdd:cd14610    99 ATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQTNETRTVT 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1802 QFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPITVHCSAGVGRSGVFITLSIVLERMQyEGV--LDVFQTVRIL 1879
Cdd:cd14610   179 QFHFLSWNDQGVPASTRSLLDFRRKVNKCYR--GRSCPIIVHCSDGAGRSGTYILIDMVLNKMA-KGAkeIDIAATLEHL 255

                         250       260
                  ....*....|....*....|...
gi 386769894 1880 RSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14610   256 RDQRPGMVQTKEQFEFALTAVAE 278
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1699-1902 2.11e-57

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 197.83  E-value: 2.11e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHERSVrYQYYVVDPIAEYN 1778
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV-YGDIKVTLVETEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1779 MPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRSGVFITLS 1858
Cdd:cd14555    80 LAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPP--SAGPIVVHCSAGAGRTGCYIVID 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 386769894 1859 IVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14555   158 IMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1685-1902 2.44e-57

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 197.94  E-value: 2.44e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1685 RVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHERSV 1764
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1765 ----RYQYYVVDPIAEYNMPQYKLREFKVTDARDgssrtVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPI 1840
Cdd:cd14631    81 ygdfKVTCVEMEPLAEYVVRTFTLERRGYNEIRE-----VKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPP--SAGPI 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386769894 1841 TVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14631   154 VVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1342-1609 4.75e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 200.16  E-value: 4.75e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1342 FANHIERLKsndnqKFSQEY--ESIEPGqqftwDNSNLEHNKSKNRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGY 1419
Cdd:cd14604    27 FASDFMRLR-----RLSTKYrtEKIYPT-----ATGEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1420 RKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTE--TYGQIFVTITETQELATYSIRT 1497
Cdd:cd14604    97 YGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEpmTFGPFRISCEAEQARTDYFIRT 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1498 FQLCRQgfNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEK 1577
Cdd:cd14604   177 LLLEFQ--NETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGK 254

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 386769894 1578 I---IDIYGHVTCLRAQRNYMVQTEDQYIFIHDAI 1609
Cdd:cd14604   255 IpeeFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1699-1898 1.23e-56

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 195.52  E-value: 1.23e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHERSVRYQYYVVDPIAEYN 1778
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1779 MPQYKLREFKVTDARDGSS----RTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQFgqDGPITVHCSAGVGRSGVF 1854
Cdd:cd14551    81 LVDYTTRKFCIQKVNRGIGekrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPR--AGPIVVHCSAGVGRTGTF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 386769894 1855 ITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYR 1898
Cdd:cd14551   159 IVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1699-1899 1.24e-56

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 195.58  E-value: 1.24e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHERSVRYQYYVVDPIAEYN 1778
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1779 MPQYKLREFKV--TDARDGSS------RTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGR 1850
Cdd:cd17668    81 LAYYTVRNFTLrnTKIKKGSQkgrpsgRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRH--AVGPVVVHCSAGVGR 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 386769894 1851 SGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRA 1899
Cdd:cd17668   159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDA 207
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1380-1613 4.36e-56

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 196.01  E-value: 4.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1380 NKSKNRYANVTAYDHSRVQLPavEGVV---GSDYINANY--------CDGYRKHNAYVATQGPLQETFVDFWRMCWELKT 1448
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLH--DGDPnepVSDYINANIimpefetkCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1449 ATIVMMTRLEERTRIKCDQYWPTR-GTETYGQIFVTITETQELATYSIRTFQLCRQG-FNDRREIKQLQFTAWPDHGVPD 1526
Cdd:cd14605    80 RVIVMTTKEVERGKSKCVKYWPDEyALKEYGVMRVRNVKESAAHDYILRELKLSKVGqGNTERTVWQYHFRTWPDHGVPS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1527 HPAPFLQFLRRC--RALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKI---IDIYGHVTCLRAQRNYMVQTEDQ 1601
Cdd:cd14605   160 DPGGVLDFLEEVhhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQ 239

                         250
                  ....*....|..
gi 386769894 1602 YIFIHDAILEAI 1613
Cdd:cd14605   240 YRFIYMAVQHYI 251
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1669-1902 5.20e-56

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 196.20  E-value: 5.20e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1669 NKHKNRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKE 1748
Cdd:cd14603    30 NVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1749 MGREKCFQYWP-HERSVRYQYYVVDPIAEYNM-PQYKLREFKVTDARDgsSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQ 1826
Cdd:cd14603   110 MGKKKCERYWAqEQEPLQTGPFTITLVKEKRLnEEVILRTLKVTFQKE--SRSVSHFQYMAWPDHGIPDSPDCMLAMIEL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1827 VHktKEQFGQDGPITVHCSAGVGRSGVFITLSIV-----LERMQYEgvLDVFQTVRILRSQRPAMVQTEDQYHFCYRAAL 1901
Cdd:cd14603   188 AR--RLQGSGPEPLCVHCSAGCGRTGVICTVDYVrqlllTQRIPPD--FSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVA 263


                  .
gi 386769894 1902 E 1902
Cdd:cd14603   264 Q 264
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1699-1898 7.07e-56

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 193.12  E-value: 7.07e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPH--ERSVRYQYYVVDPIAE 1776
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1777 YNMPQYKLREFKVTDARD-GSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQFGqdGPITVHCSAGVGRSGVFI 1855
Cdd:cd14557    81 KICPDYIIRKLNINNKKEkGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFS--GPIVVHCSAGVGRTGTYI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 386769894 1856 TLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYR 1898
Cdd:cd14557   159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1409-1609 8.22e-56

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 193.30  E-value: 8.22e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1409 DYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTETYGQIFVTITETQ 1488
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1489 ELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRAlTPPESG--PVIVHCSAGVGRTGCYIVI 1566
Cdd:cd14622    81 LLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQK-QQQQTGnhPIVVHCSAGAGRTGTFIAL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 386769894 1567 DSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAI 1609
Cdd:cd14622   160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1356-1610 1.13e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 195.45  E-value: 1.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1356 KFSQEYESiEPGQQFTWdnSNLEHNKSKNRYANVTAYDHSRVQLPAvegvvGSDYINANYCD----GYRKHNAYVATQGP 1431
Cdd:cd14600    19 QFEQLYRK-KPGLAITC--AKLPQNMDKNRYKDVLPYDATRVVLQG-----NEDYINASYVNmeipSANIVNKYIATQGP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1432 LQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWP-TRGTETYGQIFVTI-TETQELAtYSIRTFQLCRQGFNDRR 1509
Cdd:cd14600    91 LPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPdPPDVMEYGGFRVQChSEDCTIA-YVFREMLLTNTQTGEER 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1510 EIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTpPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLR 1589
Cdd:cd14600   170 TVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKR-VENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMR 248

                         250       260
                  ....*....|....*....|.
gi 386769894 1590 AQRNYMVQTEDQYIFIHDAIL 1610
Cdd:cd14600   249 DQRAMMVQTSSQYKFVCEAIL 269
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1699-1904 1.23e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 193.06  E-value: 1.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFID---GYRYRSaYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWP----HERSVRYQYYVV 1771
Cdd:cd14540     1 YINASHITatvGGKQRF-YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPtlggEHDALTFGEYKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1772 DPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQV-----HKTKEQFGQ--DGPITVHC 1844
Cdd:cd14540    80 STKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEInsvrrHTNQDVAGHnrNPPTLVHC 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1845 SAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALEYL 1904
Cdd:cd14540   160 SAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1382-1606 2.31e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 193.51  E-value: 2.31e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1382 SKNRYANVTAYDHSRVQL--PAVEGVVGSdYINANYCDGYR-KHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLE 1458
Cdd:cd14612    17 SKDRYKTILPNPQSRVCLrrAGSQEEEGS-YINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1459 ERTRiKCDQYWPTRgTETYGQIFVTITETQELATYSIRtfQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRC 1538
Cdd:cd14612    96 EKKE-KCVHYWPEK-EGTYGRFEIRVQDMKECDGYTIR--DLTIQLEEESRSVKHYWFSSWPDHQTPESAGPLLRLVAEV 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1539 --RALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIH 1606
Cdd:cd14612   172 eeSRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1383-1604 2.33e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 192.99  E-value: 2.33e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1383 KNRYANVTAYDHSRVQLPAVEGvvGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTR 1462
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQG--DNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1463 IKCDQYWPTRgtETYGQIF------VTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLR 1536
Cdd:cd14545    79 IKCAQYWPQG--EGNAMIFedtglkVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386769894 1537 RCR--ALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKI--IDIYGHVTCLRAQRNYMVQTEDQYIF 1604
Cdd:cd14545   157 KVResGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1698-1895 2.44e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 192.16  E-value: 2.44e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1698 DYVNASFID----GYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPH-ERSVRYQYYVVD 1772
Cdd:cd14541     1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlGETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1773 PIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPITVHCSAGVGRSG 1852
Cdd:cd14541    81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRV--GMVEPTVVHCSAGIGRTG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 386769894 1853 VFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHF 1895
Cdd:cd14541   159 VLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRF 201
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1380-1611 3.06e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 193.89  E-value: 3.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1380 NKSKNRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEE 1459
Cdd:cd14603    30 NVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACREIE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1460 RTRIKCDQYWP-TRGTETYGQIFVTITETQEL-ATYSIRTFQLCRQgfNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRR 1537
Cdd:cd14603   110 MGKKKCERYWAqEQEPLQTGPFTITLVKEKRLnEEVILRTLKVTFQ--KESRSVSHFQYMAWPDHGIPDSPDCMLAMIEL 187

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894 1538 CRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIID---IYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:cd14603   188 ARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPdfsIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1383-1609 6.74e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 192.77  E-value: 6.74e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1383 KNRYANVTAYDHSRVQLPAVE-GVVGSDYINANYCDGY-RKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEER 1460
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDqDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1461 TRiKCDQYWPTRGTeTYGQIFVTITETQELATYSIRTFQLCRQGfnDRREIKQLQFTAWPDHGVPDHPAPFLQFLRR--- 1537
Cdd:cd14613   108 NE-KCTEYWPEEQV-TYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWYTSWPDQKTPDNAPPLLQLVQEvee 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386769894 1538 CRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAI 1609
Cdd:cd14613   184 ARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1647-1902 8.64e-55

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 193.33  E-value: 8.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1647 EFKKLSNVKMDSSKFVTANLPCNKHKNRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYR-SAYIAAQGPVQDAA 1725
Cdd:cd14609    20 EWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHDPRmPAYIATQGPLSHTI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1726 EDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHERSVRYQYYVVDPIAEYNMPQ-YKLREFKVTDARDGSSRTVRQFQ 1804
Cdd:cd14609   100 ADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQTQETRTLTQFH 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1805 FIDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPITVHCSAGVGRSGVFITLSIVLERMQyEGV--LDVFQTVRILRSQ 1882
Cdd:cd14609   180 FLSWPAEGIPSSTRPLLDFRRKVNKCYR--GRSCPIIVHCSDGAGRTGTYILIDMVLNRMA-KGVkeIDIAATLEHVRDQ 256

                         250       260
                  ....*....|....*....|
gi 386769894 1883 RPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14609   257 RPGMVRTKDQFEFALTAVAE 276
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1664-1901 4.51e-54

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 190.83  E-value: 4.51e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1664 ANLPCNKHKNRLVHILPYESSRVYLTpihgiEGSDYVNASFID----GYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTI 1739
Cdd:cd14600    35 AKLPQNMDKNRYKDVLPYDATRVVLQ-----GNEDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1740 VVMLTKLKEMGREKCFQYWPHERSVR-YQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGE 1818
Cdd:cd14600   110 IVMLTTLTERGRTKCHQYWPDPPDVMeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1819 GFIDFIGQVHKTKEqfgQDGPITVHCSAGVGRSGVFITLSI---VLERMQYEGVLDVfqtVRILRSQRPAMVQTEDQYHF 1895
Cdd:cd14600   190 DFLEFVNYVRSKRV---ENEPVLVHCSAGIGRTGVLVTMETamcLTERNQPVYPLDI---VRKMRDQRAMMVQTSSQYKF 263


                  ....*.
gi 386769894 1896 CYRAAL 1901
Cdd:cd14600   264 VCEAIL 269
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1699-1902 7.26e-54

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 187.57  E-value: 7.26e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPhERSVRYQYYVVDPIAEYN 1778
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1779 MPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRSGVFITLS 1858
Cdd:cd14632    80 LAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPP--DAGPVVVHCSAGAGRTGCYIVLD 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 386769894 1859 IVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14632   158 VMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1673-1895 1.48e-53

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 187.42  E-value: 1.48e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1673 NRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGRE 1752
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1753 KCFQYWPHERS--VRYQYYVVDPIAEYNMPQYKLREFKVtdARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKT 1830
Cdd:cd14616    81 RCHQYWPEDNKpvTVFGDIVITKLMEDVQIDWTIRDLKI--ERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRAS 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386769894 1831 KEqfGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHF 1895
Cdd:cd14616   159 RA--HDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1665-1903 1.62e-53

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 188.12  E-value: 1.62e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1665 NLPCNKHKNRLVHILPYESSRVYL-TPIHGIEGSDYVNASFIDGYRYR-SAYIAAQGPVQDAAEDFWRMLWEHNSTIVVM 1742
Cdd:cd14612    11 DIPGHASKDRYKTILPNPQSRVCLrRAGSQEEEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVM 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1743 LTKLKEmGREKCFQYWPHERSV--RYQYyVVDPIAEYnmPQYKLREFKVTDArdGSSRTVRQFQFIDWPEQGVPKSGEGF 1820
Cdd:cd14612    91 ITKLKE-KKEKCVHYWPEKEGTygRFEI-RVQDMKEC--DGYTIRDLTIQLE--EESRSVKHYWFSSWPDHQTPESAGPL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1821 IDFIGQVHKTKEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAA 1900
Cdd:cd14612   165 LRLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTL 244


                  ...
gi 386769894 1901 LEY 1903
Cdd:cd14612   245 ALY 247
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1672-1902 5.16e-53

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 186.20  E-value: 5.16e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1672 KNRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGR 1751
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1752 EKCFQYW--PHERSVRYQYYVVDPIAEYNMPQYKLREFKVTdaRDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHK 1829
Cdd:cd14602    81 KKCERYWaePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVK--FNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894 1830 TKEQfgQDGPITVHCSAGVGRSGVFITLSIVLeRMQYEGVL----DVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14602   159 YQED--DSVPICIHCSAGCGRTGVICAIDYTW-MLLKDGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1382-1606 8.40e-53

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 185.51  E-value: 8.40e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1382 SKNRYANVTAYDHSRVQL-PAVEGVVGSDYINANYCDGYR-KHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEE 1459
Cdd:cd14611     1 TKNRYKTILPNPHSRVCLkPKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1460 RTRiKCDQYWP-TRGTetYGQIFVTITETQELATYSIRTFQLcRQGfNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRC 1538
Cdd:cd14611    81 KNE-KCVLYWPeKRGI--YGKVEVLVNSVKECDNYTIRNLTL-KQG-SQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDV 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1539 RA--LTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIH 1606
Cdd:cd14611   156 EEdrLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1670-1897 1.16e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 185.29  E-value: 1.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1670 KHKNRLVHILPYESSRVYLTPihgiEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEM 1749
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQ----GDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1750 GREKCFQYWPHERSVRYQY----YVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIG 1825
Cdd:cd14545    77 GQIKCAQYWPQGEGNAMIFedtgLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386769894 1826 QVHKTKEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGV--LDVFQTVRILRSQRPAMVQTEDQYHFCY 1897
Cdd:cd14545   157 KVRESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1347-1613 1.34e-52

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 186.78  E-value: 1.34e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1347 ERLKSNDnqKFSQEYESI-----EPGqqfTWDNSNLEHNKSKNRYANVTAYDHSRVQLPAVEGVVGSDYINAN-YCDGYR 1420
Cdd:cd14609     9 DHLRNRD--RLAKEWQALcayqaEPN---TCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpIIEHDP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1421 KHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTETYGQIFVT-ITETQELATYSIRTFQ 1499
Cdd:cd14609    84 RMPAYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNlVSEHIWCEDFLVRSFY 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1500 LCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERM-KHEKI 1578
Cdd:cd14609   164 LKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKE 243

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 386769894 1579 IDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAI 1613
Cdd:cd14609   244 IDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEV 278
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1410-1606 1.62e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 183.78  E-value: 1.62e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTE--TYGQIFVT-ITE 1486
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEqlQFGPFKISlEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1487 TQELATYSIRTFQLCRQgfNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIVI 1566
Cdd:cd14542    81 KRVGPDFLIRTLKVTFQ--KESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGRTGTICAI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 386769894 1567 DSMLERMKHEKIID---IYGHVTCLRAQRNYMVQTEDQYIFIH 1606
Cdd:cd14542   159 DYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1383-1611 1.66e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 184.66  E-value: 1.66e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1383 KNRYANVTAYDHSRVQLPAVEGVVGSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTR 1462
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1463 IKCDQYWPTRGTET--YGQIFVTITETQELATYSIRTFQLCRQgfNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRA 1540
Cdd:cd14602    81 KKCERYWAEPGEMQleFGPFSVTCEAEKRKSDYIIRTLKVKFN--SETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386769894 1541 LTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKhEKII----DIYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:cd14602   159 YQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1347-1613 1.73e-52

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 186.80  E-value: 1.73e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1347 ERLKSNDnqKFSQEYESI-----EPGQQFTwdnSNLEHNKSKNRYANVTAYDHSRVQLPAVEGVVGSDYINAN-YCDGYR 1420
Cdd:cd14610    11 DHLKNKN--RLEKEWEALcayqaEPNATNV---AQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASpIMDHDP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1421 KHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTETYGQIFVT-ITETQELATYSIRTFQ 1499
Cdd:cd14610    86 RNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNlVSEHIWCEDFLVRSFY 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1500 LCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERM-KHEKI 1578
Cdd:cd14610   166 LKNLQTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKE 245

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 386769894 1579 IDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAI 1613
Cdd:cd14610   246 IDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV 280
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1699-1902 1.84e-52

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 183.80  E-value: 1.84e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRS-AYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHERSVRYQYYVVDPIAEY 1777
Cdd:cd14546     1 YINASTIYDHDPRNpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1778 NM-PQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTkeQFGQDGPITVHCSAGVGRSGVFIT 1856
Cdd:cd14546    81 IWcDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKS--YRGRSCPIVVHCSDGAGRTGTYIL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 386769894 1857 LSIVLERMQyEGV--LDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14546   159 IDMVLNRMA-KGAkeIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1380-1609 2.09e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 185.55  E-value: 2.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1380 NKSKNRYANVTAYDHSRVQLPAVEgvvgSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEE 1459
Cdd:cd14607    24 NRNRNRYRDVSPYDHSRVKLQNTE----NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1460 RTRIKCDQYWPTRGTETYG----QIFVTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFL 1535
Cdd:cd14607   100 KDSVKCAQYWPTDEEEVLSfketGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPASFLNFL 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894 1536 ---RRCRALTpPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEK--IIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAI 1609
Cdd:cd14607   180 fkvRESGSLS-PEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1410-1611 6.65e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 182.66  E-value: 6.65e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYC----DGYRKHnaYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRG----TETYGQIF 1481
Cdd:cd14540     1 YINASHItatvGGKQRF--YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGgehdALTFGEYK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1482 VTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRAL------------TPPesgPV 1549
Cdd:cd14540    79 VSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVrrhtnqdvaghnRNP---PT 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386769894 1550 IVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:cd14540   156 LVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1699-1904 7.39e-52

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 181.87  E-value: 7.39e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFID----GYRYRsaYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHERSV-----RYQYY 1769
Cdd:cd14596     1 YINASYITmpvgEEELF--YIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpmeleNYQLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1770 VVDpiaeYNMPQY-KLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKtkeqFGQDGPITVHCSAGV 1848
Cdd:cd14596    79 LEN----YQALQYfIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRK----VHNTGPIVVHCSAGI 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386769894 1849 GRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALEYL 1904
Cdd:cd14596   151 GRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1375-1611 1.06e-51

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 184.07  E-value: 1.06e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1375 SNLEHNKSKNRYANVTAYDHSRVQLPAVEgvvgSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMM 1454
Cdd:cd14608    20 AKLPKNKNRNRYRDVSPFDHSRIKLHQED----NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVML 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1455 TRLEERTRIKCDQYWPTRgtETYGQIF------VTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHP 1528
Cdd:cd14608    96 NRVMEKGSLKCAQYWPQK--EEKEMIFedtnlkLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESP 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1529 APFLQFLRRCR--ALTPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEK---IIDIYGHVTCLRAQRNYMVQTEDQYI 1603
Cdd:cd14608   174 ASFLNFLFKVResGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDIKKVLLEMRKFRMGLIQTADQLR 253


                  ....*...
gi 386769894 1604 FIHDAILE 1611
Cdd:cd14608   254 FSYLAVIE 261
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1699-1898 1.27e-51

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 181.08  E-value: 1.27e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHERSVRYQY--YVVDPIAE 1776
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFgpFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1777 YNM-PQYKLREFKVTdaRDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTkeQFGQDGPITVHCSAGVGRSGVFI 1855
Cdd:cd14542    81 KRVgPDFLIRTLKVT--FQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVPICVHCSAGCGRTGTIC 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 386769894 1856 TLSIVLERMQYEGV---LDVFQTVRILRSQRPAMVQTEDQYHFCYR 1898
Cdd:cd14542   157 AIDYVWNLLKTGKIpeeFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1669-1904 7.47e-51

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 180.03  E-value: 7.47e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1669 NKHKNRLVHILPYESSRVYLtpihGIEGsDYVNASFID----GYRYrsAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLT 1744
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPL----GDEG-GYINASFIKmpvgDEEF--VYIACQGPLPTTVADFWQMVWEQKSTVIAMMT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1745 KLKEMGREKCFQYWPHERSV------RYQYYVVDPIAEYNmpqYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGE 1818
Cdd:cd14597    76 QEVEGGKIKCQRYWPEILGKttmvdnRLQLTLVRMQQLKN---FVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1819 ---GFIDFIGQVHKTkeqfgqdGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHF 1895
Cdd:cd14597   153 qllTFISYMRHIHKS-------GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIF 225


                  ....*....
gi 386769894 1896 CYRAALEYL 1904
Cdd:cd14597   226 CYQVILYVL 234
PHA02738 PHA02738
hypothetical protein; Provisional
 1340-1623 1.99e-50

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 182.05  E-value: 1.99e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1340 SEFANHIERlkSNDNQKFSQEYESIEPGQ-QFTWDNSnlEHNKSKNRYANVTAYDHSRVQLPAVEGvvGSDYINANYCDG 1418
Cdd:PHA02738   12 AEFLALMEK--SDCEEVITREHQKVISEKvDGTFNAE--KKNRKLNRYLDAVCFDHSRVILPAERN--RGDYINANYVDG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1419 YRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPT--RGTETYGQIFVTITETQELATYsIR 1496
Cdd:PHA02738   86 FEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDveQGSIRFGKFKITTTQVETHPHY-VK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1497 TFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFL---RRC-------------RALTPPesgPVIVHCSAGVGRT 1560
Cdd:PHA02738  165 STLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVlevRQCqkelaqeslqighNRLQPP---PIVVHCNAGLGRT 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769894 1561 GCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAIICGVTEVPAR 1623
Cdd:PHA02738  242 PCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLTVNKVSKK 304
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1410-1613 2.61e-50

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 177.63  E-value: 2.61e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCD---GYRKHnAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTETY--GQIFVTI 1484
Cdd:cd14596     1 YINASYITmpvGEEEL-FYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMelENYQLRL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1485 TETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTppESGPVIVHCSAGVGRTGCYI 1564
Cdd:cd14596    80 ENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVH--NTGPIVVHCSAGIGRAGVLI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 386769894 1565 VIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAI 1613
Cdd:cd14596   158 CVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1410-1613 3.23e-50

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 177.25  E-value: 3.23e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYC-DGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGTETYGQIFVT-ITET 1487
Cdd:cd14546     1 YINASTIyDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHlVSEH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1488 QELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCYIVID 1567
Cdd:cd14546    81 IWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGRTGTYILID 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 386769894 1568 SMLERM-KHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILEAI 1613
Cdd:cd14546   161 MVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1669-1899 9.05e-50

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 179.36  E-value: 9.05e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1669 NKHKNRLVHILPYESSRVYLTPIHGIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKE 1748
Cdd:cd14604    57 NVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFE 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1749 MGREKCFQYWPH--ERSVRYQYYVVDPIAEYNMPQYKLREFKVtdARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQ 1826
Cdd:cd14604   137 MGRKKCERYWPLygEEPMTFGPFRISCEAEQARTDYFIRTLLL--EFQNETRRLYQFHYVNWPDHDVPSSFDSILDMISL 214

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769894 1827 VHKTKEQfgQDGPITVHCSAGVGRSGVFITLSI---VLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRA 1899
Cdd:cd14604   215 MRKYQEH--EDVPICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRA 288
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1409-1611 1.39e-49

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 175.52  E-value: 1.39e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1409 DYINANYCD----GYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWP-TRGTETYGQIFVT 1483
Cdd:cd14601     1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPePSGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1484 ITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCY 1563
Cdd:cd14601    81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVHCSAGIGRTGVL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 386769894 1564 IVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:cd14601   161 ITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1410-1607 2.29e-49

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 174.52  E-value: 2.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRiKCDQYWPTRGTETYGQIFVTITETQE 1489
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQ-SCPQYWPDEGSGTYGPIQVEFVSTTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1490 LATYSIRTFQLCRQGFNDR--REIKQLQFTAWPDHG-VPDHPAPFLQFLRRC-RALTPPESGPVIVHCSAGVGRTGCYIV 1565
Cdd:cd14556    80 DEDVISRIFRLQNTTRPQEgyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVeKWQEQSGEGPIVVHCLNGVGRSGVFCA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 386769894 1566 IDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHD 1607
Cdd:cd14556   160 ISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1410-1607 3.27e-49

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 174.11  E-value: 3.27e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNA-YVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPT-RG-TETYGQIFVTITE 1486
Cdd:cd14539     1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTeRGqALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1487 TQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRA---LTPPESGPVIVHCSAGVGRTGCY 1563
Cdd:cd14539    81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShylQQRSLQTPIVVHCSSGVGRTGAF 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 386769894 1564 -IVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHD 1607
Cdd:cd14539   161 cLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1672-1899 1.57e-48

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 174.28  E-value: 1.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1672 KNRLVHILPYESSRVYLT-PIHGIEGSDYVNASFIDGY-RYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEM 1749
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTsPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1750 GrEKCFQYWPhERSVRYQYYVVDPIAEYNMPQYKLREFkvTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHK 1829
Cdd:cd14613   108 N-EKCTEYWP-EEQVTYEGIEITVKQVIHADDYRLRLI--TLKSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVEE 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386769894 1830 TKEQFGQD-GPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRA 1899
Cdd:cd14613   184 ARQQAEPNcGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHV 254
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1672-1897 2.37e-48

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 172.41  E-value: 2.37e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1672 KNRLVHILPYESSRVYLTPIHGIEG-SDYVNASFIDGYR-YRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEM 1749
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSNDSlSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1750 GrEKCFQYWPHERSVRYQYYV-VDPIAEYNmpQYKLREfkVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVH 1828
Cdd:cd14611    82 N-EKCVLYWPEKRGIYGKVEVlVNSVKECD--NYTIRN--LTLKQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894 1829 KTKEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCY 1897
Cdd:cd14611   157 EDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1698-1902 2.45e-48

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 172.05  E-value: 2.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1698 DYVNASFIDGYRYRSA----YIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHER-SVRYQYYVVD 1772
Cdd:cd14601     1 DYINANYINMEIPSSSiinrYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSgSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1773 PIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEqfGQDGPITVHCSAGVGRSG 1852
Cdd:cd14601    81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRA--GKDEPVVVHCSAGIGRTG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 386769894 1853 VFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14601   159 VLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PHA02738 PHA02738
hypothetical protein; Provisional
 1669-1909 1.57e-47

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 173.57  E-value: 1.57e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1669 NKHKNRLVHILPYESSRVYLtPIHGIEGsDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKE 1748
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVIL-PAERNRG-DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1749 MGREKCFQYWP--HERSVRYQYYVVDPIAEYNMPQYKLREFKVTDArDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQ 1826
Cdd:PHA02738  127 NGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDG-TSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLE 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1827 VHKTKEQFGQDG-----------PITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHF 1895
Cdd:PHA02738  206 VRQCQKELAQESlqighnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFF 285

                         250
                  ....*....|....
gi 386769894 1896 CYRAALEYLGSFDN 1909
Cdd:PHA02738  286 CYRAVKRYVNLTVN 299
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1410-1607 6.14e-47

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 167.57  E-value: 6.14e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGtETYGQIFVTITETQE 1489
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEK-KTYGDIEVELKDTEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1490 LATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTP------PESGPVIVHCSAGVGRTGCY 1563
Cdd:cd14558    80 SPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPyknskhGRSVPIVVHCSDGSSRTGIF 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 386769894 1564 IVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHD 1607
Cdd:cd14558   160 CALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1350-1611 1.12e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 170.57  E-value: 1.12e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1350 KSNDNQKFSQEYESIEPGQQFTWDNSNLEH-NKSKNRYANVTAYDHSRVQLPAVEGvvGSDYINANYCDGYRKHNAYVAT 1428
Cdd:PHA02742   21 ESNLAEILKEEHEHIMQEIVAFSCNESLELkNMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1429 QGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPT--RGTETYGQIFVTITETQELATYSIRTFQLCRQGFN 1506
Cdd:PHA02742   99 QAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPheRGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTG 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1507 DRREIKQLQFTAWPDHGVPDHPAPFLQFLRRCR----ALTPPESG-------PVIVHCSAGVGRTGCYIVIDSMLERMKH 1575
Cdd:PHA02742  179 ASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVReadlKADVDIKGenivkepPILVHCSAGLDRAGAFCAIDICISKYNE 258

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 386769894 1576 EKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:PHA02742  259 RAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLI 294
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1669-1903 2.10e-46

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 169.80  E-value: 2.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1669 NKHKNRLVHILPYESSRVYLTPIHGieGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKE 1748
Cdd:PHA02742   52 NMKKCRYPDAPCFDRNRVILKIEDG--GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1749 MGREKCFQYW-PHERS-VRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFI-- 1824
Cdd:PHA02742  130 DGKEACYPYWmPHERGkATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVla 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1825 -------GQVHKTKEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCY 1897
Cdd:PHA02742  210 vreadlkADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289


                  ....*.
gi 386769894 1898 RAALEY 1903
Cdd:PHA02742  290 FIVLIF 295
IgI_3_RPTP_IIa_LAR_like cd05739
Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F ...
 219-301 4.98e-46

Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F (also known as LAR), type IIa; member of the I-set of IgSF domains; The members here are composed of the third 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. Included in this group is Drosophila LAR (DLAR).


Pssm-ID: 409401  Cd Length: 82  Bit Score: 160.45  E-value: 4.98e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  219 SRPPeTISEVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPIGRNVLQLINIQESANYTCIAASTLGQIDSVSVV 298
Cdd:cd05739     1 SIPP-SNHEVMPGGSVNLTCVAVGAPMPYVKWMKGGEELTKEDEMPVGRNVLELTNIYESANYTCVAISSLGMIEATAQV 79


                  ...
gi 386769894  299 KVQ 301
Cdd:cd05739    80 TVK 82
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1647-1904 9.54e-46

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 167.48  E-value: 9.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1647 EFKKLSNVKMDSSkFVTANLPCNKHKNRLVHILPYESSRVYLTPIHGiEGSDYVNASFID----GYRYRsaYIAAQGPVQ 1722
Cdd:cd14599    17 EYEQIPKKKADGV-FTTATLPENAERNRIREVVPYEENRVELVPTKE-NNTGYINASHIKvtvgGEEWH--YIATQGPLP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1723 DAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPH----ERSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSR 1798
Cdd:cd14599    93 HTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgskHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQER 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1799 TVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQ--------DGPITVHCSAGVGRSGVFITLSIVLERMQYEGVL 1870
Cdd:cd14599   173 TVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSmldstkncNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKV 252

                         250       260       270
                  ....*....|....*....|....*....|....
gi 386769894 1871 DVFQTVRILRSQRPAMVQTEDQYHFCYRAALEYL 1904
Cdd:cd14599   253 EVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFL 286
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1360-1611 1.32e-45

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 167.10  E-value: 1.32e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1360 EYESI---EPGQQFTwdNSNLEHNKSKNRYANVTAYDHSRVQL-PAVEGVVGsdYINANYCD----GYRKHnaYVATQGP 1431
Cdd:cd14599    17 EYEQIpkkKADGVFT--TATLPENAERNRIREVVPYEENRVELvPTKENNTG--YINASHIKvtvgGEEWH--YIATQGP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1432 LQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRGT----ETYGQIFVTITETQELATYSIRTFQLCRQGFND 1507
Cdd:cd14599    91 LPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSkhssATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQ 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1508 RREIKQLQFTAWPDHGVPDHPAPFLQFLRRCRAL----------TPPESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEK 1577
Cdd:cd14599   171 ERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVrrhtnsmldsTKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNE 250

                         250       260       270
                  ....*....|....*....|....*....|....
gi 386769894 1578 IIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:cd14599   251 KVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQ 284
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1699-1904 2.74e-45

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 163.61  E-value: 2.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFID----GYRYrsAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWP----HERSVRYQYYV 1770
Cdd:cd14598     1 YINASHIKvtvgGKEW--DYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsRHNTVTYGRFK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1771 VDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQV-------HKTKEQFGQDGPITVH 1843
Cdd:cd14598    79 ITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIqsvrrhtNSTIDPKSPNPPVLVH 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386769894 1844 CSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALEYL 1904
Cdd:cd14598   159 CSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1699-1897 6.34e-45

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 161.78  E-value: 6.34e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYR-YRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWPHER--SVRYQYYVVDPIA 1775
Cdd:cd14539     1 YINASLIEDLTpYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERgqALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1776 EYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHK-TKEQFGQDGPITVHCSAGVGRSGVF 1854
Cdd:cd14539    81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShYLQQRSLQTPIVVHCSSGVGRTGAF 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 386769894 1855 ITLSIVLERMQYE-GVLDVFQTVRILRSQRPAMVQTEDQYHFCY 1897
Cdd:cd14539   161 CLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1653-1902 8.65e-45

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 164.43  E-value: 8.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1653 NVKMDSSKF--VTANLPCNKHKNRLVHILPYESSRVYLTpihgIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWR 1730
Cdd:cd14608     7 DIRHEASDFpcRVAKLPKNKNRNRYRDVSPFDHSRIKLH----QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1731 MLWEHNSTIVVMLTKLKEMGREKCFQYWPH--ERSVRYQ--YYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFI 1806
Cdd:cd14608    83 MVWEQKSRGVVMLNRVMEKGSLKCAQYWPQkeEKEMIFEdtNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1807 DWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRSGVFI---TLSIVLERMQYEGVLDVFQTVRILRSQR 1883
Cdd:cd14608   163 TWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCladTCLLLMDKRKDPSSVDIKKVLLEMRKFR 242

                         250
                  ....*....|....*....
gi 386769894 1884 PAMVQTEDQYHFCYRAALE 1902
Cdd:cd14608   243 MGLIQTADQLRFSYLAVIE 261
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1667-1899 1.47e-43

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 162.12  E-value: 1.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1667 PCNKHKNRLVHILPYESSRVYLTPiHGI--------------------EGSDYVNASFIDGYRYRSAYIAAQGPVQDAAE 1726
Cdd:PHA02746   49 KENLKKNRFHDIPCWDHSRVVINA-HESlkmfdvgdsdgkkievtsedNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1727 DFWRMLWEHNSTIVVMLTKLKEmGREKCFQYWPHERSV-----RYQYYVVDPIAEYNMPQYKLRefkVTDARDGSSRTVR 1801
Cdd:PHA02746  128 DFFKLISEHESQVIVSLTDIDD-DDEKCFELWTKEEDSelafgRFVAKILDIIEELSFTKTRLM---ITDKISDTSREIH 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1802 QFQFIDWPEQGVPKSGEGFIDFIGQVH-------KTKE-QFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVF 1873
Cdd:PHA02746  204 HFWFPDWPDNGIPTGMAEFLELINKVNeeqaeliKQADnDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLG 283

                         250       260
                  ....*....|....*....|....*.
gi 386769894 1874 QTVRILRSQRPAMVQTEDQYHFCYRA 1899
Cdd:PHA02746  284 EIVLKIRKQRHSSVFLPEQYAFCYKA 309
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1661-1899 1.67e-43

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 159.75  E-value: 1.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1661 FVTANLPCNKHKNRLVHILPYESSRVYLTPIHgiegSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIV 1740
Cdd:cd14607    16 HRVAKYPENRNRNRYRDVSPYDHSRVKLQNTE----NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1741 VMLTKLKEMGREKCFQYWP----HERSVRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKS 1816
Cdd:cd14607    92 VMLNRIVEKDSVKCAQYWPtdeeEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPES 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1817 GEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEG--VLDVFQTVRILRSQRPAMVQTEDQYH 1894
Cdd:cd14607   172 PASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKYRMGLIQTPDQLR 251


                  ....*
gi 386769894 1895 FCYRA 1899
Cdd:cd14607   252 FSYMA 256
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1380-1614 4.20e-43

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 160.96  E-value: 4.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1380 NKSKNRYANVTAYDHSRVQLPAVEGV----VG---------------SDYINANYCDGYRKHNAYVATQGPLQETFVDFW 1440
Cdd:PHA02746   51 NLKKNRFHDIPCWDHSRVVINAHESLkmfdVGdsdgkkievtsednaENYIHANFVDGFKEANKFICAQGPKEDTSEDFF 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1441 RMCWELKTATIVMMTRLEeRTRIKCDQYWPT-RGTE-TYGQIFVTITETQELATYSIRTFQLCRQGFNDRREIKQLQFTA 1518
Cdd:PHA02746  131 KLISEHESQVIVSLTDID-DDDEKCFELWTKeEDSElAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFPD 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1519 WPDHGVPDHPAPFLQFL-----RRCRALTPPES-----GPVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCL 1588
Cdd:PHA02746  210 WPDNGIPTGMAEFLELInkvneEQAELIKQADNdpqtlGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKI 289

                         250       260
                  ....*....|....*....|....*.
gi 386769894 1589 RAQRNYMVQTEDQYIFIHDAILEAII 1614
Cdd:PHA02746  290 RKQRHSSVFLPEQYAFCYKALKYAII 315
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1410-1606 6.01e-43

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 156.47  E-value: 6.01e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYC--DGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTR-IKCDQYWPT--RGTETYGQIFVTI 1484
Cdd:cd17658     1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAeeNESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1485 TEtqelatYSIRTFQLCRQGF--NDRREIKQ------LQFTAWPDHGVPDHPAPFLQFLRRCRALtPPESGPVIVHCSAG 1556
Cdd:cd17658    81 KK------LKHSQHSITLRVLevQYIESEEPplsvlhIQYPEWPDHGVPKDTRSVRELLKRLYGI-PPSAGPIVVHCSAG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386769894 1557 VGRTGCYIVIDSMLERMKHEKI--IDIYGHVTCLRAQRNYMVQTEDQYIFIH 1606
Cdd:cd17658   154 IGRTGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1667-1895 1.47e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 159.01  E-value: 1.47e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1667 PCNKHKNRLVHILPYESSRVYLTPIHGiEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKL 1746
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDSGGG-STSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPT 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1747 KEM-GREKCFQYW-PHER-SVRYQYYVVDPIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGEGFIDF 1823
Cdd:PHA02747  128 KGTnGEEKCYQYWcLNEDgNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIKF 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1824 IGQVHKTKEQFGQD--------GPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHF 1895
Cdd:PHA02747  208 IKIIDINRKKSGKLfnpkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLF 287
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1410-1611 3.03e-41

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 152.05  E-value: 3.03e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCD---GYRKHNaYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCDQYWPTRG----TETYGQIFV 1482
Cdd:cd14598     1 YINASHIKvtvGGKEWD-YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGsrhnTVTYGRFKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1483 TITETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQFL-------RRCRALTPPESG--PVIVHC 1553
Cdd:cd14598    80 TTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLeeiqsvrRHTNSTIDPKSPnpPVLVHC 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894 1554 SAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:cd14598   160 SAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1699-1902 6.06e-41

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 150.56  E-value: 6.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMgrEKCFQYWPHERSVRYQYYVVDPIA--- 1775
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLA--QGCPQYWPEEGMLRYGPIQVECMScsm 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1776 EYNMPQYKLREFKVTDARDGSsRTVRQFQFIDWP-EQGVPKSGEGFIDFIGQVHKTKEQFGQ-DGPITVHCSAGVGRSGV 1853
Cdd:cd14636    79 DCDVISRIFRICNLTRPQEGY-LMVQQFQYLGWAsHREVPGSKRSFLKLILQVEKWQEECDEgEGRTIIHCLNGGGRSGM 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 386769894 1854 FITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14636   158 FCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1371-1606 1.01e-40

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 153.62  E-value: 1.01e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1371 TWDNSNLEHNKSKNRYANVTAYDHSRVQLPAVEGVVgSDYINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTAT 1450
Cdd:PHA02747   42 LIANFEKPENQPKNRYWDIPCWDHNRVILDSGGGST-SDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSI 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1451 IVMMTRLEERT-RIKCDQYW-PTRGTETYGQIFVTIT-ETQELATYSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDH 1527
Cdd:PHA02747  121 IVMLTPTKGTNgEEKCYQYWcLNEDGNIDMEDFRIETlKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSD 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1528 PAPFLQFLR---RCR----ALTPPESG---PVIVHCSAGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQ 1597
Cdd:PHA02747  201 HPDFIKFIKiidINRkksgKLFNPKDAllcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIM 280


                  ....*....
gi 386769894 1598 TEDQYIFIH 1606
Cdd:PHA02747  281 NFDDYLFIQ 289
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1799-1902 1.79e-40

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 145.19  E-value: 1.79e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   1799 TVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYE-GVLDVFQTVR 1877
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 386769894   1878 ILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1799-1902 1.79e-40

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 145.19  E-value: 1.79e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   1799 TVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYE-GVLDVFQTVR 1877
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 386769894   1878 ILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1699-1902 5.39e-40

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 147.75  E-value: 5.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGRE-KCFQYWPHERSVRY---QYYVVDPI 1774
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYgpmEVEFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1775 AEYNMPQYKLREFKVTDARDGSsRTVRQFQFIDW-PEQGVPKSGEGFIDFIGQVHKTKEQFGqDGPITVHCSAGVGRSGV 1853
Cdd:cd14637    81 ADEDIVTRLFRVQNITRLQEGH-LMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESG-EGRTVVHCLNGGGRSGT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 386769894 1854 FITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14637   159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1699-1902 1.46e-39

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 146.76  E-value: 1.46e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMgrEKCFQYWPHERSVRY---QYYVVDPIA 1775
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA--QLCPQYWPENGVHRHgpiQVEFVSADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1776 EYNMPQYKLREFKVTDARDGSsRTVRQFQFIDWPE-QGVPKSGEGFIDFIGQVHKTKEQF-GQDGPITVHCSAGVGRSGV 1853
Cdd:cd14635    79 EEDIISRIFRIYNAARPQDGY-RMVQQFQFLGWPMyRDTPVSKRSFLKLIRQVDKWQEEYnGGEGRTVVHCLNGGGRSGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 386769894 1854 FITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14635   158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1699-1902 1.78e-39

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 146.32  E-value: 1.78e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMgrEKCFQYWPHERSVRYQYYVVDPIAEYN 1778
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAA--QLCMQYWPEKTSCCYGPIQVEFVSADI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1779 MPQYKLREFKVTD-AR--DGSsRTVRQFQFIDWPE-QGVPKSGEGFIDFIGQVHKTKEQF-GQDGPITVHCSAGVGRSGV 1853
Cdd:cd14634    79 DEDIISRIFRICNmARpqDGY-RIVQHLQYIGWPAyRDTPPSKRSILKVVRRLEKWQEQYdGREGRTVVHCLNGGGRSGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 386769894 1854 FITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAALE 1902
Cdd:cd14634   158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1345-1605 4.93e-39

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 147.93  E-value: 4.93e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1345 HIERLKSNDNQKFSQEYESIEPGQQFTWDNSNLEhNKSKNRYANVTAYDHSRVQLPAVegvvgsdYINANYCDGYRKHNA 1424
Cdd:COG5599     8 AIKSEEEKINSRLSTLTNELAPSHNDPQYLQNIN-GSPLNRFRDIQPYKETALRANLG-------YLNANYIQVIGNHRY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1425 YvATQGPLQETFVDFWRMCWELKTATIVMMTRLEE--RTRIKCDQYWPTRGTETYGQIFVTITETQELATYS-IRTFQL- 1500
Cdd:COG5599    80 I-ATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDGEYGKYEVSSELTESIQLRDGIeARTYVLt 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1501 CRQGFNDRREIKQLQFTAWPDHGVPDHPApFLQFLRRCRA----LTPPESGPViVHCSAGVGRTGCYIVIDSMLERMKHE 1576
Cdd:COG5599   159 IKGTGQKKIEIPVLHVKNWPDHGAISAEA-LKNLADLIDKkekiKDPDKLLPV-VHCRAGVGRTGTLIACLALSKSINAL 236

                         250       260       270
                  ....*....|....*....|....*....|..
gi 386769894 1577 KII--DIYGHVTCLRAQRNY-MVQTEDQYIFI 1605
Cdd:COG5599   237 VQItlSVEEIVIDMRTSRNGgMVQTSEQLDVL 268
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1510-1611 1.01e-38

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 140.19  E-value: 1.01e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   1510 EIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTP--PESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKI-IDIYGHVT 1586
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 386769894   1587 CLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1510-1611 1.01e-38

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 140.19  E-value: 1.01e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   1510 EIKQLQFTAWPDHGVPDHPAPFLQFLRRCRALTP--PESGPVIVHCSAGVGRTGCYIVIDSMLERMKHEKI-IDIYGHVT 1586
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNqsESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 386769894   1587 CLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1699-1897 1.15e-38

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 143.62  E-value: 1.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEmgREKCFQYWP-HERSVRYQYYVVDPIAEY 1777
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNEL--NEDEPIYWPtKEKPLECETFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1778 NMP-----QYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSgeGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRSG 1852
Cdd:cd14550    79 HSClsneiRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIH--TVFELINTVQEWAQQ--RDGPIVVHDRYGGVQAA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 386769894 1853 VFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCY 1897
Cdd:cd14550   155 TFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLY 199
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1699-1897 1.08e-37

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 141.06  E-value: 1.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFI--DGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGR-EKCFQYWPHERSVRYQY-YVVDPI 1774
Cdd:cd17658     1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEENESREFgRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1775 AEYNMPQY--KLREFKVTDAR-DGSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKEQFGqdgPITVHCSAGVGRS 1851
Cdd:cd17658    81 KKLKHSQHsiTLRVLEVQYIEsEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRLYGIPPSAG---PIVVHCSAGIGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 386769894 1852 GVFITLSIVLERMqYEG---VLDVFQTVRILRSQRPAMVQTEDQYHFCY 1897
Cdd:cd17658   158 GAYCTIHNTIRRI-LEGdmsAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1699-1901 8.89e-32

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 124.34  E-value: 8.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFqYWPH-ERSVRYQYYVVDPIAE- 1776
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNkDEPINCETFKVTLIAEe 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1777 ----YNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVP--KSGEgFIDFIGQvhktkEQFGQDGPITVHCSAGVGR 1850
Cdd:cd17669    80 hkclSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPisKTFE-LISIIKE-----EAANRDGPMIVHDEHGGVT 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386769894 1851 SGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAAL 1901
Cdd:cd17669   154 AGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1699-1901 1.15e-31

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 124.02  E-value: 1.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1699 YVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKcFQYWP-HERSVRYQYYVV-----D 1772
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDE-FVYWPsREESMNCEAFTVtliskD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1773 PIAEYNMPQYKLREFKVTDARDGSSRTVRQFQFIDWPEQGVPKSGE-GFIDFIGQvhktkEQFGQDGPITVHCSAGVGRS 1851
Cdd:cd17670    80 RLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTfELINVIKE-----EALTRDGPTIVHDEFGAVSA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 386769894 1852 GVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQTEDQYHFCYRAAL 1901
Cdd:cd17670   155 GTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1410-1611 4.03e-31

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 122.44  E-value: 4.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEerTRIKCDQYWPTRGTETYGQI---FVTITE 1486
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMD--AAQLCMQYWPEKTSCCYGPIqveFVSADI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1487 TQELATysiRTFQLC-----RQGFndrREIKQLQFTAWPDH-GVPDHPAPFLQFLRRCRALTPP---ESGPVIVHCSAGV 1557
Cdd:cd14634    79 DEDIIS---RIFRICnmarpQDGY---RIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydgREGRTVVHCLNGG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386769894 1558 GRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:cd14634   153 GRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1639-1893 2.22e-29

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 119.81  E-value: 2.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1639 ETISGMEVEF-KKLSNVKMDSSKFVTAN----LPCNKHKNRLVHILPYESSRVyltpihGIEGSdYVNASFIDGYRYRSa 1713
Cdd:COG5599     7 IAIKSEEEKInSRLSTLTNELAPSHNDPqylqNINGSPLNRFRDIQPYKETAL------RANLG-YLNANYIQVIGNHR- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1714 YIAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMG--REKCFQYWPHERSVRYQYYVVDPIAEYN-MPQYKLREFKVT 1790
Cdd:COG5599    79 YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYFRQDGEYGKYEVSSELTESIQlRDGIEARTYVLT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1791 DARDG-SSRTVRQFQFIDWPEQGVPkSGEGFIDFIGQVHKTKEQFGQD-GPITVHCSAGVGRSGVFItLSIVLERMQYEG 1868
Cdd:COG5599   159 IKGTGqKKIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKEKIKDPDkLLPVVHCRAGVGRTGTLI-ACLALSKSINAL 236

                         250       260
                  ....*....|....*....|....*....
gi 386769894 1869 V---LDVFQTVRILRSQR-PAMVQTEDQY 1893
Cdd:COG5599   237 VqitLSVEEIVIDMRTSRnGGMVQTSEQL 265
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1410-1611 9.83e-29

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 115.51  E-value: 9.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTriKCDQYWPTRGTETYGQIFVTITETQE 1489
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQ--GCPQYWPEEGMLRYGPIQVECMSCSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1490 LATYSIRTFQLC-----RQGFndrREIKQLQFTAWPDH-GVPDHPAPFLQFL---RRCRALTPPESGPVIVHCSAGVGRT 1560
Cdd:cd14636    79 DCDVISRIFRICnltrpQEGY---LMVQQFQYLGWASHrEVPGSKRSFLKLIlqvEKWQEECDEGEGRTIIHCLNGGGRS 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386769894 1561 GCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:cd14636   156 GMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1410-1611 1.34e-28

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 115.01  E-value: 1.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRI-KCDQYWPTRGTETYGQI---FVTIT 1485
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMeveFVSGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1486 ETQELATYSIRTFQLCRQGfNDRREIKQLQFTAW-PDHGVPDHPAPFLQFL-------RRCRaltppeSGPVIVHCSAGV 1557
Cdd:cd14637    81 ADEDIVTRLFRVQNITRLQ-EGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLasvekwqRESG------EGRTVVHCLNGG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386769894 1558 GRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:cd14637   154 GRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1410-1605 1.05e-27

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 112.41  E-value: 1.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTriKCDQYWPTRGTETYGQIF-VTITETQ 1488
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECETFkVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1489 ELAT-----YSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHpaPFLQFLRRCRALTPPESGPVIVHCSAGVGRTGCY 1563
Cdd:cd14550    79 HSCLsneirLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIH--TVFELINTVQEWAQQRDGPIVVHDRYGGVQAATF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 386769894 1564 IVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFI 1605
Cdd:cd14550   157 CALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1664-1904 1.08e-26

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 112.37  E-value: 1.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1664 ANLPCNKHKNRL------VHILPYESSRVYLtpihgIEGSDYVNASFIDGYRYRSAYIAAQGPVQDAAEDFWRMLWEHNS 1737
Cdd:PHA02740   42 ANKACAQAENKAkdenlaLHITRLLHRRIKL-----FNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1738 TIVVMLTKLKEmgrEKCF-QYWP-HERSVR-YQYYVVDPIAEYNMPQYKLREFKVTDaRDGSSRTVRQFQFIDWPEQGVP 1814
Cdd:PHA02740  117 QIIVLISRHAD---KKCFnQFWSlKEGCVItSDKFQIETLEIIIKPHFNLTLLSLTD-KFGQAQKISHFQYTAWPADGFS 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1815 KSGEGFIDFIGQVHKTKEQF------GQDGPITVHCSAGVGRSGVFITLSIVLERMQYEGVLDVFQTVRILRSQRPAMVQ 1888
Cdd:PHA02740  193 HDPDAFIDFFCNIDDLCADLekhkadGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMN 272

                         250
                  ....*....|....*.
gi 386769894 1889 TEDQYHFCYRAALEYL 1904
Cdd:PHA02740  273 CLDDYVFCYHLIAAYL 288
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1410-1611 1.19e-26

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 109.39  E-value: 1.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRikCDQYWPTRGTETYGQI---FVTITE 1486
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWPENGVHRHGPIqveFVSADL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1487 TQELATYSIRTFQLCRQGfNDRREIKQLQFTAWPDHgvPDHPAPFLQFLRRCRALTPPES------GPVIVHCSAGVGRT 1560
Cdd:cd14635    79 EEDIISRIFRIYNAARPQ-DGYRMVQQFQFLGWPMY--RDTPVSKRSFLKLIRQVDKWQEeynggeGRTVVHCLNGGGRS 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386769894 1561 GCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAILE 1611
Cdd:cd14635   156 GTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
285-702 2.23e-23

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 107.40  E-value: 2.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  285 AASTLGQIDSVSVVKVQSLPTAPTDVQISEVTATSVRLEWSYKGPEDLQYYVIQYKPKNANQAFSEISGIITMYYVVRAL 364
Cdd:COG3401    11 AGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  365 SPYTEYEFYVIAVNNIGRGPPSAPATC---TTGETKMESAPRNVQVRTLSSSTMVITWEPPETPNGQVTGYKVYYTTNSN 441
Cdd:COG3401    91 ATGLTTLTGSGSVGGATNTGLTSSDEVpspAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  442 QPEASWNSQMVDNSELTTVSELT-------PHAIYTVRVQAYTSMGAGPMSTPVQVKAQQGVPSQPSNFRATDIGETAVT 514
Cdd:COG3401   171 SPDTSATAAVATTSLTVTSTTLVdgggdiePGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVT 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  515 LQWTKptHSSENIVHYELYWNDTYANQAhhKRISNSEA--YTLDGLYPDTLYYIWLAARSQRG-EGATTPPIPVRTKQYV 591
Cdd:COG3401   251 LSWDP--VTESDATGYRVYRSNSGDGPF--TKVATVTTtsYTDTGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  592 PGDPQDVKATPLNSTSIHVSWKPPLEKDrngiIRGYHIHaqelRDEGKGFLNEPFKfDVVDTLEFNVTGLQPDTKYSIQV 671
Cdd:COG3401   327 PAAPSGLTATAVGSSSITLSWTASSDAD----VTGYNVY----RSTSGGGTYTKIA-ETVTTTSYTDTGLTPGTTYYYKV 397

                         410       420       430
                  ....*....|....*....|....*....|.
gi 386769894  672 AALTRKGDGDRSAAIVVKTPGGVPVRPTVSL 702
Cdd:COG3401   398 TAVDAAGNESAPSEEVSATTASAASGESLTA 428
IgI_2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F; ...
 123-210 2.69e-23

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


Pssm-ID: 409400 [Multi-domain]  Cd Length: 91  Bit Score: 95.85  E-value: 2.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  123 VITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDM--SNPRYS-LKDGFLQIENSREEDQGKYECVAENSMGT 199
Cdd:cd05738     1 IIDMGPQLKVVEKARTATMLCAASGNPDPEISWFKDFLPVDTatSNGRIKqLRSGALQIENSEESDQGKYECVATNSAGT 80

                          90
                  ....*....|.
gi 386769894  200 EHSKATNLYVK 210
Cdd:cd05738    81 RYSAPANLYVR 91
fn3 pfam00041
Fibronectin type III domain;
400-485 1.09e-20

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 88.24  E-value: 1.09e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   400 SAPRNVQVRTLSSSTMVITWEPPETPNGQVTGYKV-YYTTNSNQPeasWNSQMVDNSELT-TVSELTPHAIYTVRVQAYT 477
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVeYRPKNSGEP---WNEITVPGTTTSvTLTGLKPGTEYEVRVQAVN 77


                   ....*...
gi 386769894   478 SMGAGPMS 485
Cdd:pfam00041   78 GGGEGPPS 85
I-set pfam07679
Immunoglobulin I-set domain;
18-111 1.57e-20

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 87.70  E-value: 1.57e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    18 PEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSgtQSRYTVLEQPGGISILRIEPVRAGrDDAPYECVAEN 97
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLR--SSDRFKVTYEGGTYTLTISNVQPD-DSGKYTCVATN 77

                           90
                   ....*....|....
gi 386769894    98 GVGdAVSADATLTI 111
Cdd:pfam07679   78 SAG-EAEASAELTV 90
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1410-1610 3.02e-20

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 90.82  E-value: 3.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRIKCdQYWPTRGTETYGQIFVTITETQE 1489
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINCETFKVTLIAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1490 LATYS------IRTFQLCRQGFNDRREIKQLQFTAWPDhgvPDHP-APFLQFLRRCRALTPPESGPVIVHCSAGVGRTGC 1562
Cdd:cd17669    80 HKCLSneekliIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAANRDGPMIVHDEHGGVTAGT 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 386769894 1563 YIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAIL 1610
Cdd:cd17669   157 FCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1410-1610 2.12e-19

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 88.58  E-value: 2.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1410 YINANYCDGYRKHNAYVATQGPLQETFVDFWRMCWELKTATIVMmtrLEERTRIKCDQ--YWPTRGTETYGQIF-VTITE 1486
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVM---LPDNQGLAEDEfvYWPSREESMNCEAFtVTLIS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1487 TQELATYS-----IRTFQLCRQGFNDRREIKQLQFTAWPDhgvPDHP-APFLQFLRRCRALTPPESGPVIVHCSAGVGRT 1560
Cdd:cd17670    78 KDRLCLSNeeqiiIHDFILEATQDDYVLEVRHFQCPKWPN---PDAPiSSTFELINVIKEEALTRDGPTIVHDEFGAVSA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 386769894 1561 GCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAIL 1610
Cdd:cd17670   155 GTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 400-491 3.02e-19

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 [Multi-domain]  Cd Length: 93  Bit Score: 84.09  E-value: 3.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  400 SAPRNVQVRTLSSSTMVITWEPPETPNGQVTGYKVYYTTNSNQPEASWNSQMVDNSELtTVSELTPHAIYTVRVQAYTSM 479
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGSETSY-TLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|..
gi 386769894  480 GAGPMSTPVQVK 491
Cdd:cd00063    81 GESPPSESVTVT 92
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 21-111 3.63e-18

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 80.90  E-value: 3.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   21 IRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSgtQSRYTVLEQpggiSILRIEPVRAGrDDAPYECVAENGVG 100
Cdd:cd05725     1 VKRPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELP--KGRYEILDD----HSLKIRKVTAG-DMGSYTCVAENMVG 73

                          90
                  ....*....|.
gi 386769894  101 dAVSADATLTI 111
Cdd:cd05725    74 -KIEASATLTV 83
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 123-199 1.35e-17

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 79.46  E-value: 1.35e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894  123 VITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYS-LKDGFLQIENSREEDQGKYECVAENSMGT 199
Cdd:cd20952     1 IILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITtLENGSLQIKGAEKSDTGEYTCVALNLSGE 78
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 592-690 1.47e-17

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 [Multi-domain]  Cd Length: 93  Bit Score: 79.46  E-value: 1.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  592 PGDPQDVKATPLNSTSIHVSWKPPleKDRNGIIRGYHIHAQELRDEGkgflNEPFKFDVVDTLEFNVTGLQPDTKYSIQV 671
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPP--EDDGGPITGYVVEYREKGSGD----WKEVEVTPGSETSYTLTGLKPGTEYEFRV 74

                          90
                  ....*....|....*....
gi 386769894  672 AALTRKGDGDRSAAIVVKT 690
Cdd:cd00063    75 RAVNGGGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 304-393 4.24e-17

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 [Multi-domain]  Cd Length: 93  Bit Score: 78.31  E-value: 4.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  304 PTAPTDVQISEVTATSVRLEWS--YKGPEDLQYYVIQYKPKNANQAFS-EISGIITMYYVVRALSPYTEYEFYVIAVNNI 380
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTppEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 386769894  381 GRGPPSAPATCTT 393
Cdd:cd00063    81 GESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 497-587 4.49e-17

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 [Multi-domain]  Cd Length: 93  Bit Score: 77.92  E-value: 4.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  497 PSQPSNFRATDIGETAVTLQWTKPTHSSENIVHYELYWNDTYANQAHH--KRISNSEAYTLDGLYPDTLYYIWLAARSQR 574
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 386769894  575 GEGATTPPIPVRT 587
Cdd:cd00063    81 GESPPSESVTVTT 93
fn3 pfam00041
Fibronectin type III domain;
595-683 6.08e-17

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 77.46  E-value: 6.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   595 PQDVKATPLNSTSIHVSWKPPleKDRNGIIRGYHIHAQELRDEGkgflnEPFKFDVV-DTLEFNVTGLQPDTKYSIQVAA 673
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPP--PDGNGPITGYEVEYRPKNSGE-----PWNEITVPgTTTSVTLTGLKPGTEYEVRVQA 75

                           90
                   ....*....|
gi 386769894   674 LTRKGDGDRS 683
Cdd:pfam00041   76 VNGGGEGPPS 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
335-878 6.27e-17

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 86.59  E-value: 6.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  335 YVIQYKPKNANQAFSEISGIITMYYVVRALSPYTEYEFYVIAVNNIGRGPPSAPATCTTGETKMESAPRNVQVRTLSSST 414
Cdd:COG3401     1 TGSSYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  415 MVITWEPPETPNGQVTGYKVYYTTNSnqpeasWNSQMVDNSELTTVSELTPHAIYTVRVQAYTSMGAGPmstPVQVKAQQ 494
Cdd:COG3401    81 AVAVAAAPPTATGLTTLTGSGSVGGA------TNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYAL---GAGLYGVD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  495 GVPSQPSNFRATDIGETAVTLQWTKPTHSSENIVHYELYWNdtyanqahhkrisnseAYTLDGLYPDTLYYIWLAARSQR 574
Cdd:COG3401   152 GANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTL----------------VDGGGDIEPGTTYYYRVAATDTG 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  575 GEGATTPPIPVRTKQYVPGDPQDVKATPLNSTSIHVSWKPPLEKDrngiIRGYHIHaqelRDEGKgflNEPFKF-DVVDT 653
Cdd:COG3401   216 GESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD----ATGYRVY----RSNSG---DGPFTKvATVTT 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  654 LEFNVTGLQPDTKYSIQVAALTRKGD-GDRSAAIVVKTPGGVPVRPTvSLKImEREPIVSIELEWErpAQTYGELRGYRL 732
Cdd:COG3401   285 TSYTDTGLTNGTTYYYRVTAVDAAGNeSAPSNVVSVTTDLTPPAAPS-GLTA-TAVGSSSITLSWT--ASSDADVTGYNV 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  733 -RWGVKDQALKE--EMLSGPQMTKKrfdNLERGVEYEFRVAGSNHIGIGQETVKIFQTPEGTPGGPPSNITIRFQTPDVL 809
Cdd:COG3401   361 yRSTSGGGTYTKiaETVTTTSYTDT---GLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTD 437

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894  810 CVTWDPPTREHRNGIITRYDVQFHKKIDHGLGSErnmTLRKAVFTNLEENTEYIFRVRAYTKQGAGPFS 878
Cdd:COG3401   438 VAGATAAASAASNPGVSAAVLADGGDTGNAVPFT---TTSSTVTATTTDTTTANLSVTTGSLVGGSGAS 503
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 18-111 1.14e-16

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 77.21  E-value: 1.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   18 PEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKV----SGTQSRYTVLEQpGGISILRIEPVRAGR-DDAPYE 92
Cdd:cd07693     1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLetdkDDPRSHRIVLPS-GSLFFLRVVHGRKGRsDEGVYV 79

                          90
                  ....*....|....*....
gi 386769894   93 CVAENGVGDAVSADATLTI 111
Cdd:cd07693    80 CVAHNSLGEAVSRNASLEV 98
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1337-1609 1.29e-16

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 82.71  E-value: 1.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1337 IPISEFANHIErlKSNDNQKFSQEYESIEPGQQftwDNSNLEHNKSKNRYAN------VTAYDHSRVQLPAVEGVvgsdy 1410
Cdd:PHA02740    9 INGMDFINFIN--KPDLLSCIIKEYRAIVPEHE---DEANKACAQAENKAKDenlalhITRLLHRRIKLFNDEKV----- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1411 INANYCDGYRKHNAYVATQGpLQETFVD-FWRMCWELKTATIVMMTRLEERtriKC-DQYWPT--RGTETYGQIFVtitE 1486
Cdd:PHA02740   79 LDARFVDGYDFEQKFICIIN-LCEDACDkFLQALSDNKVQIIVLISRHADK---KCfNQFWSLkeGCVITSDKFQI---E 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1487 TQELAT--YSIRTFQLCRQGFNDRREIKQLQFTAWPDHGVPDHPAPFLQF----------LRRCRALTppESGPVIVHCS 1554
Cdd:PHA02740  152 TLEIIIkpHFNLTLLSLTDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFfcniddlcadLEKHKADG--KIAPIIIDCI 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386769894 1555 AGVGRTGCYIVIDSMLERMKHEKIIDIYGHVTCLRAQRNYMVQTEDQYIFIHDAI 1609
Cdd:PHA02740  230 DGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLI 284
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 122-209 1.43e-16

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 76.28  E-value: 1.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQGPGTRVI-EVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLKDGFLQIENSREEDQGKYECVAENSMGTE 200
Cdd:cd20978     1 PKFIQKPEKNVVvKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVEDGTLTIINVQPEDTGYYGCVATNEIGDI 80


                  ....*....
gi 386769894  201 HSKaTNLYV 209
Cdd:cd20978    81 YTE-TLLHV 88
fn3 pfam00041
Fibronectin type III domain;
306-386 1.90e-16

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 75.91  E-value: 1.90e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   306 APTDVQISEVTATSVRLEWS--YKGPEDLQYYVIQYKPKNANQAFSEIS-GIITMYYVVRALSPYTEYEFYVIAVNNIGR 382
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTppPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ....
gi 386769894   383 GPPS 386
Cdd:pfam00041   82 GPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 128-209 2.59e-16

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 75.62  E-value: 2.59e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    128 PGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLK----DGFLQIENSREEDQGKYECVAENSMGTEHSK 203
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSrsgsTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                    ....*.
gi 386769894    204 aTNLYV 209
Cdd:smart00410   81 -TTLTV 85
fn3 pfam00041
Fibronectin type III domain;
498-580 7.88e-16

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 74.37  E-value: 7.88e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   498 SQPSNFRATDIGETAVTLQWTKPTHSSENIVHYEL-YWNDTYANQAHHKRISNSEA-YTLDGLYPDTLYYIWLAARSQRG 575
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVeYRPKNSGEPWNEITVPGTTTsVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 386769894   576 EGATT 580
Cdd:pfam00041   81 EGPPS 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 122-195 8.76e-16

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 73.75  E-value: 8.76e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894   122 PVITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTK---VDMSNPRYSLKDGFLQIENSREEDQGKYECVAEN 195
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPissGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 17-97 2.56e-15

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 72.60  E-value: 2.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    17 PPEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTQSRYTVLEqpGGISILRIEPVRAgRDDAPYECVAE 96
Cdd:pfam13927    1 KPVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLS--GSNSTLTISNVTR-SDAGTYTCVAS 77


                   .
gi 386769894    97 N 97
Cdd:pfam13927   78 N 78
I-set pfam07679
Immunoglobulin I-set domain;
122-205 3.67e-15

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 72.29  E-value: 3.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   122 PVITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDmSNPRYSLK----DGFLQIENSREEDQGKYECVAENSM 197
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLR-SSDRFKVTyeggTYTLTISNVQPDDSGKYTCVATNSA 79


                   ....*...
gi 386769894   198 GTEHSKAT 205
Cdd:pfam07679   80 GEAEASAE 87
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 400-482 6.66e-15

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 [Multi-domain]  Cd Length: 83  Bit Score: 71.49  E-value: 6.66e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    400 SAPRNVQVRTLSSSTMVITWEPPETPNGqvTGYKVYYTTNSNQPEASWNSQMVDNSELT-TVSELTPHAIYTVRVQAYTS 478
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVNVTPSSTSyTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 386769894    479 MGAG 482
Cdd:smart00060   80 AGEG 83
fn3 pfam00041
Fibronectin type III domain;
794-878 1.76e-14

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 70.52  E-value: 1.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   794 GPPSNITIRFQTPDVLCVTWDPPtrEHRNGIITRYDVQFHKKIDHGLGSERNM--TLRKAVFTNLEENTEYIFRVRAYTK 871
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPP--PDGNGPITGYEVEYRPKNSGEPWNEITVpgTTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*..
gi 386769894   872 QGAGPFS 878
Cdd:pfam00041   79 GGEGPPS 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 24-111 1.96e-14

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 70.23  E-value: 1.96e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894     24 PQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTQSRYTVLEQpGGISILRIEPVRAgRDDAPYECVAENGVGDaV 103
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRS-GSTSTLTISNVTP-EDSGTYTCAATNSSGS-A 77


                    ....*...
gi 386769894    104 SADATLTI 111
Cdd:smart00410   78 SSGTTLTV 85
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 126-209 2.02e-14

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 70.12  E-value: 2.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  126 QGPGTRVIEVGHTVLMTCKA-IGNPTPNIYWIKN-QTKVDMSNPRYSLKDGFLQIENSREEDQGKYECVAENSMGTEHSK 203
Cdd:cd05724     2 VEPSDTQVAVGEMAVLECSPpRGHPEPTVSWRKDgQPLNLDNERVRIVDDGNLLIAEARKSDEGTYKCVATNMVGERESR 81


                  ....*.
gi 386769894  204 ATNLYV 209
Cdd:cd05724    82 AARLSV 87
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
382-605 2.07e-14

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 79.22  E-value: 2.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  382 RGPPSAPATCTTGETkmesapRNVQVRTLSSSTMVITWEPPETpngqVTGYKVYYTTNSNqpeaSWNSQMVDNSELTTVS 461
Cdd:COG4733   527 VPPQWPPVNVTTSES------LSVVAQGTAVTTLTVSWDAPAG----AVAYEVEWRRDDG----NWVSVPRTSGTSFEVP 592

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  462 ELTPHaIYTVRVQAYTSMG---AGPMSTPVQVKAQQGVPSQPSNFRATDIGEtAVTLQWTKPTHSseNIVHYELYW--ND 536
Cdd:COG4733   593 GIYAG-DYEVRVRAINALGvssAWAASSETTVTGKTAPPPAPTGLTATGGLG-GITLSWSFPVDA--DTLRTEIRYstTG 668

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894  537 TYANQAHHKRISNSEAYTLDGLYPDTLYYIWLAARSQRGEgATTPPIPVRTKQYVPGDPQDVKATPLNS 605
Cdd:COG4733   669 DWASATVAQALYPGNTYTLAGLKAGQTYYYRARAVDRSGN-VSAWWVSGQASADAAGILDAITGQILET 736
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 20-111 2.63e-14

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 69.83  E-value: 2.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   20 IIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTQSRYTVLEQpggiSILRIEPVRAGrDDAPYECVAENGV 99
Cdd:cd20952     2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDERITTLEN----GSLQIKGAEKS-DTGEYTCVALNLS 76

                          90
                  ....*....|..
gi 386769894  100 GDAvSADATLTI 111
Cdd:cd20952    77 GEA-TWSAVLDV 87
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 592-680 5.80e-14

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 [Multi-domain]  Cd Length: 83  Bit Score: 68.80  E-value: 5.80e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    592 PGDPQDVKATPLNSTSIHVSWKPPLEKDRNGIIRGYHIHAQELRDEGKGFLNEPfkfdvvDTLEFNVTGLQPDTKYSIQV 671
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTP------SSTSYTLTGLKPGTEYEFRV 74


                    ....*....
gi 386769894    672 AALTRKGDG 680
Cdd:smart00060   75 RAVNGAGEG 83
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 124-210 6.81e-14

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


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 68.81  E-value: 6.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  124 ITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLKDGFLQIENSREEDQGKYECVAENSMGTEHSK 203
Cdd:cd20968     2 ITRPPTNVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENNRIAVLESGSLRIHNVQKEDAGQYRCVAKNSLGIAYSK 81


                  ....*..
gi 386769894  204 ATNLYVK 210
Cdd:cd20968    82 PVTIEVE 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 794-885 9.47e-14

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 [Multi-domain]  Cd Length: 93  Bit Score: 68.68  E-value: 9.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  794 GPPSNITIRFQTPDVLCVTWDPPtrEHRNGIITRYDVQFHKKIDHGLG--SERNMTLRKAVFTNLEENTEYIFRVRAYTK 871
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPP--EDDGGPITGYVVEYREKGSGDWKevEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|....
gi 386769894  872 QGAGPFSDKLIVET 885
Cdd:cd00063    80 GGESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 497-577 1.05e-13

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 [Multi-domain]  Cd Length: 83  Bit Score: 68.02  E-value: 1.05e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    497 PSQPSNFRATDIGETAVTLQWTKPTHSSEN--IVHYELYWNDTYANQAHHKRISNSEAYTLDGLYPDTLYYIWLAARSQR 574
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITgyIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 386769894    575 GEG 577
Cdd:smart00060   81 GEG 83
IgI_1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; ...
 122-207 1.58e-13

First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (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. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409435  Cd Length: 96  Bit Score: 68.05  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQGPGTRVIEVG---HTVLMTCKAIGNPTPNIYWIKNQTKVDM-SNPRYSLKDGFLQIENSRE-EDQGKYECVAENS 196
Cdd:cd05848     2 PVFVQEPDDAIFPTDsdeKKVILNCEARGNPVPTYRWLRNGTEIDTeSDYRYSLIDGNLIISNPSEvKDSGRYQCLATNS 81

                          90
                  ....*....|.
gi 386769894  197 MGTEHSKATNL 207
Cdd:cd05848    82 IGSILSREALL 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 794-875 3.35e-13

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 [Multi-domain]  Cd Length: 83  Bit Score: 66.87  E-value: 3.35e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    794 GPPSNITIRFQTPDVLCVTWDPPTREHRNGIITRYDVQFHKKIDHGLGSERNMTLRKAVFTNLEENTEYIFRVRAYTKQG 873
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 386769894    874 AG 875
Cdd:smart00060   82 EG 83
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 139-205 7.15e-13

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 65.43  E-value: 7.15e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  139 VLMTCKAIGNPTPNIYWIKNQTKVDMS---NPRYSLKDGFLQIENSREEDQGKYECVAENSMGTEHSKAT 205
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSsrdSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1384-1602 8.09e-13

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 69.74  E-value: 8.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1384 NRYANVTaydhSRVQLPavegvVGSDyINANYCDGYRKHNAyVATQGPLQETFVDFWRMCWELKTATIVMMTRLEERTRI 1463
Cdd:cd14559     1 NRFTNIQ----TRVSTP-----VGKN-LNANRVQIGNKNVA-IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1464 KCDQYWptRGTETYGQIFVTITETQELA--------TYSIRTfqlcRQGfNDRREIKQLQFTAWPDHG------------ 1523
Cdd:cd14559    70 GLPPYF--RQSGTYGSVTVKSKKTGKDElvdglkadMYNLKI----TDG-NKTITIPVVHVTNWPDHTaisseglkelad 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1524 ----VPDHPAPFLQFLRRCRALTPPESGPVIvHCSAGVGRTGcyiVIDSMLERMKHEKIIDIYGHVTCLRAQRN-YMVQT 1598
Cdd:cd14559   143 lvnkSAEEKRNFYKSKGSSAINDKNKLLPVI-HCRAGVGRTG---QLAAAMELNKSPNNLSVEDIVSDMRTSRNgKMVQK 218


                  ....
gi 386769894 1599 EDQY 1602
Cdd:cd14559   219 DEQL 222
IgC_1_Robo cd07693
First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar ...
 122-209 2.48e-12

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 409490 [Multi-domain]  Cd Length: 99  Bit Score: 64.88  E-value: 2.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKN-----QTKVDMSNPRYSLKDG---FLQIENSR--EEDQGKYEC 191
Cdd:cd07693     1 PRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNgqpleTDKDDPRSHRIVLPSGslfFLRVVHGRkgRSDEGVYVC 80

                          90
                  ....*....|....*...
gi 386769894  192 VAENSMGTEHSKATNLYV 209
Cdd:cd07693    81 VAHNSLGEAVSRNASLEV 98
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 304-383 2.98e-12

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 [Multi-domain]  Cd Length: 83  Bit Score: 64.17  E-value: 2.98e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    304 PTAPTDVQISEVTATSVRLEWSYKGPEDLQYYVIQYKPKNANQAFSEI---SGIITMYYVVRALSPYTEYEFYVIAVNNI 380
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKevnVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    ...
gi 386769894    381 GRG 383
Cdd:smart00060   81 GEG 83
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 23-111 5.80e-12

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 63.30  E-value: 5.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   23 KPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTQSRYTVLEQPGGISILRIEPVragrDDAPYECVAENGVGDA 102
Cdd:cd20970     8 PSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVRENGTTLTIRNIRRS----DMGIYLCIASNGVPGS 83


                  ....*....
gi 386769894  103 VSADATLTI 111
Cdd:cd20970    84 VEKRITLQV 92
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
747-1149 1.44e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 69.65  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  747 SGPQMTKKRFDNLERGVEYEFRVAGSNHIGIGQETVKIFQTPEGTPGGPPSNITIRFQTPDVLCVTWDPPTREHrngiIT 826
Cdd:COG3401   187 VTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD----AT 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  827 RYDVQFHKKIDHGLgsERNMTLRKAVFT--NLEENTEYIFRVRAYTKQG-AGPFSDKLIVETERDMGRAPMSLQAEATSE 903
Cdd:COG3401   263 GYRVYRSNSGDGPF--TKVATVTTTSYTdtGLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTPPAAPSGLTATAVGS 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  904 QTAEIWWEPVTSrGKLLGYKIFYTmTAVEDLDDWQTKTVGLTESADLvNLEKFAQYAVAIAARFKNGL-GRLSEKVTVRI 982
Cdd:COG3401   341 SSITLSWTASSD-ADVTGYNVYRS-TSGGGTYTKIAETVTTTSYTDT-GLTPGTTYYYKVTAVDAAGNeSAPSEEVSATT 417

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  983 -------KPEDVPLNLRAHDVSTHSMTLSWSPPIRLTPVNYKISFDAMKVFVDSQGFSQTQIVPKREIILKHYVKTHTIN 1055
Cdd:COG3401   418 asaasgeSLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLV 497

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1056 ELSPFTTYNVNVSAIpSDYSYRPPTKITVTTQMAAPQPMVKPDFYGVVNGEEILVILPQASEEYGPISHYYLVVVPEDKS 1135
Cdd:COG3401   498 GGSGASSVTNSVSVI-GASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITT 576

                         410
                  ....*....|....
gi 386769894 1136 NLHKIPDQFLTDDL 1149
Cdd:COG3401   577 LGGSLLTTTSTNTN 590
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 18-104 1.96e-11

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 61.64  E-value: 1.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   18 PEIIRKPQNQGVRVGG-VASFYCAARGDPPPSIVWRKNGKKVSGTQSRYTVLEqpggiSILRIEPVRAGrDDAPYECVAE 96
Cdd:cd20978     1 PKFIQKPEKNVVVKGGqDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVED-----GTLTIINVQPE-DTGYYGCVAT 74


                  ....*...
gi 386769894   97 NGVGDAVS 104
Cdd:cd20978    75 NEIGDIYT 82
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1715-1893 3.15e-11

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 65.11  E-value: 3.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1715 IAAQGPVQDAAEDFWRMLWEHNSTIVVMLTKLKEMGREKCFQYWphERSVRY-----------QYYVVDPIA--EYNMpq 1781
Cdd:cd14559    32 IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF--RQSGTYgsvtvkskktgKDELVDGLKadMYNL-- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1782 yklrefKVTDarDGSSRTVRQFQFIDWPEQGvPKSGEGFI---DFIGQVHKTKEQF----------GQDGPITV-HCSAG 1847
Cdd:cd14559   108 ------KITD--GNKTITIPVVHVTNWPDHT-AISSEGLKelaDLVNKSAEEKRNFykskgssainDKNKLLPViHCRAG 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 386769894 1848 VGRSGVFITlsiVLERMQYEGVLDVFQTVRILRSQRPA-MVQTEDQY 1893
Cdd:cd14559   179 VGRTGQLAA---AMELNKSPNNLSVEDIVSDMRTSRNGkMVQKDEQL 222
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
 139-207 3.72e-11

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


Pssm-ID: 409356 [Multi-domain]  Cd Length: 96  Bit Score: 61.49  E-value: 3.72e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386769894  139 VLMTCKAIGNPTPNIYWIKNQTKVDM-SNPRYSLKDGFLQIEN-SREEDQGKYECVAENSMGTEHSKATNL 207
Cdd:cd04967    22 VALNCRARANPVPSYRWLMNGTEIDLeSDYRYSLVDGTLVISNpSKAKDAGHYQCLATNTVGSVLSREATL 92
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 24-111 6.80e-11

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 60.11  E-value: 6.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   24 PQNQGVRVGGVASFYCAA-RGDPPPSIVWRKNGKKVSGTQSRYTVLEqpGGisILRIEPVRAGrDDAPYECVAENGVGDA 102
Cdd:cd05724     4 PSDTQVAVGEMAVLECSPpRGHPEPTVSWRKDGQPLNLDNERVRIVD--DG--NLLIAEARKS-DEGTYKCVATNMVGER 78


                  ....*....
gi 386769894  103 VSADATLTI 111
Cdd:cd05724    79 ESRAARLSV 87
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 127-205 1.06e-10

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 59.72  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  127 GPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKvdMSNPRYS-LKDGFLQIENSREEDQGKYECVAENSMGTEHSKAT 205
Cdd:cd05725     3 RPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGE--LPKGRYEiLDDHSLKIRKVTAGDMGSYTCVAENMVGKIEASAT 80
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 135-198 1.11e-10

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


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 59.87  E-value: 1.11e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894  135 VGHTVLMTCKAIGNPTPNIYWiknqTKVD-MSNPRYSLK--DGFLQIENSREEDQGKYECVAENSMG 198
Cdd:cd04968    15 KGQTVTLECFALGNPVPQIKW----RKVDgSPSSQWEITtsEPVLEIPNVQFEDEGTYECEAENSRG 77
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 35-107 1.11e-10

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 59.27  E-value: 1.11e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769894   35 ASFYCAARGDPPPSIVWRKNGKKVSgtQSRYTVLEQPGGISILRIEPVRAGrDDAPYECVAENGVGDAVSADA 107
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLP--PSSRDSRRSELGNGTLTISNVTLE-DSGTYTCVASNSAGGSASASV 70
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1818-1898 2.38e-10

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 59.67  E-value: 2.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1818 EGFIDFIGQVHKTKEqfgqdgPITVHCSAGVGRSGVFITLSIVLERMqyegvLDVFQTVRILRSQRPA-MVQTEDQYHFC 1896
Cdd:cd14494    43 DRFLEVLDQAEKPGE------PVLVHCKAGVGRTGTLVACYLVLLGG-----MSAEEAVRIVRLIRPGgIPQTIEQLDFL 111


                  ..
gi 386769894 1897 YR 1898
Cdd:cd14494   112 IK 113
IgI_1_Contactin-1 cd05849
First immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily domains; ...
 139-207 2.61e-10

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


Pssm-ID: 409436 [Multi-domain]  Cd Length: 95  Bit Score: 58.81  E-value: 2.61e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  139 VLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLKDGFLQIEN-SREEDQGKYECVAENSMGTEHSKATNL 207
Cdd:cd05849    22 VSVNCRARANPFPIYKWRKNNLDIDLTNDRYSMVGGNLVINNpDKYKDAGRYVCIVSNIYGKVRSREATL 91
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 136-201 2.72e-10

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


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 58.57  E-value: 2.72e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386769894  136 GHTVLMTCKAIGNPTPNIYWIKnqtkvdMSNPRYSLKDGF------LQIENSREEDQGKYECVAENSMGTEH 201
Cdd:cd05731    10 GGVLLLECIAEGLPTPDIRWIK------LGGELPKGRTKFenfnktLKIENVSEADSGEYQCTASNTMGSAR 75
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 21-111 6.20e-10

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 57.63  E-value: 6.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   21 IRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGkkvsGT------QSRYTVLEQPGGISILRIEPvragRDDAPYECV 94
Cdd:cd05763     3 TKTPHDITIRAGSTARLECAATGHPTPQIAWQKDG----GTdfpaarERRMHVMPEDDVFFIVDVKI----EDTGVYSCT 74

                          90
                  ....*....|....*..
gi 386769894   95 AENGVGdAVSADATLTI 111
Cdd:cd05763    75 AQNSAG-SISANATLTV 90
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 122-205 7.60e-10

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


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 57.47  E-value: 7.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQGPGTRVI--EVGHTVLMTCKAIGNPTPNIYWIKNqTKVDMSNPRYS-LKDGFLQIENSREEDQGKYECVAENSMG 198
Cdd:cd04969     1 PDFELNPVKKKIlaAKGGDVIIECKPKASPKPTISWSKG-TELLTNSSRICiLPDGSLKIKNVTKSDEGKYTCFAVNFFG 79


                  ....*..
gi 386769894  199 TEHSKAT 205
Cdd:cd04969    80 KANSTGS 86
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 139-198 1.63e-09

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


Pssm-ID: 143223  Cd Length: 69  Bit Score: 55.65  E-value: 1.63e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  139 VLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLKDGFLQIENSREEDQGKYECVAENSMG 198
Cdd:cd05746     1 VQIPCSAQGDPEPTITWNKDGVQVTESGKFHISPEGYLAIRDVGVADQGRYECVARNTIG 60
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 122-209 1.84e-09

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 56.36  E-value: 1.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVIT--QGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLK-DG-FLQIENSREEDQGKYECVAENSM 197
Cdd:cd20970     1 PVIStpQPSFTVTAREGENATFMCRAEGSPEPEISWTRNGNLIIEFNTRYIVReNGtTLTIRNIRRSDMGIYLCIASNGV 80

                          90
                  ....*....|..
gi 386769894  198 GTEHSKATNLYV 209
Cdd:cd20970    81 PGSVEKRITLQV 92
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 131-198 2.94e-09

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


Pssm-ID: 409442  Cd Length: 92  Bit Score: 55.64  E-value: 2.94e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386769894  131 RVIE--VGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLKDGF-LQIENSREEDQGKYECVAENSMG 198
Cdd:cd05856    12 RVIArpVGSSVRLKCVASGNPRPDITWLKDNKPLTPPEIGENKKKKWtLSLKNLKPEDSGKYTCHVSNRAG 82
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 215-285 3.06e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 55.26  E-value: 3.06e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894   215 PPTFSRPPETiSEVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPIGRN----VLQLINIQE--SANYTCIA 285
Cdd:pfam13927    1 KPVITVSPSS-VTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSgsnsTLTISNVTRsdAGTYTCVA 76
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 136-199 5.52e-09

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, 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: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 54.92  E-value: 5.52e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386769894  136 GHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLKDGFLQIENSREEDQGKYECVAENSMGT 199
Cdd:cd05876    10 GQSLVLECIAEGLPTPTVKWLRPSGPLPPDRVKYQNHNKTLQLLNVGESDDGEYVCLAENSLGS 73
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 18-109 7.27e-09

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 54.73  E-value: 7.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   18 PEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKV--SGTQSRYTVlEQPGGISILRIEPVrAGRDDAPYECVA 95
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIdpSSIPGKYKI-ESEYGVHVLHIRRV-TVEDSAVYSAVA 78

                          90
                  ....*....|....
gi 386769894   96 ENGVGDAvSADATL 109
Cdd:cd20951    79 KNIHGEA-SSSASV 91
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 128-195 1.08e-08

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 54.07  E-value: 1.08e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894  128 PGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLKDGFLQIENSREEDQGKYECVAEN 195
Cdd:cd20957     8 PPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSEDVLVIPSVKREDKGMYQCFVRN 75
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 133-204 1.09e-08

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


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 54.14  E-value: 1.09e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386769894  133 IEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNpRYSLKDGFLQIENSREEDQGKYECVAENSMGTEHSKA 204
Cdd:cd05728    11 ADIGSSLRWECKASGNPRPAYRWLKNGQPLASEN-RIEVEAGDLRITKLSLSDSGMYQCVAENKHGTIYASA 81
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
 136-199 1.15e-08

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


Pssm-ID: 143220  Cd Length: 78  Bit Score: 53.65  E-value: 1.15e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894  136 GHTVLMTCKAIGNPTPNIYWIKNQTKVDmSNPRYSLKD----GFLQIENSREEDQGKYECVAENSMGT 199
Cdd:cd05743     1 GETVEFTCVATGVPTPIINWRLNWGHVP-DSARVSITSeggyGTLTIRDVKESDQGAYTCEAINTRGM 67
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 17-111 1.36e-08

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 53.79  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   17 PPEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTQSRYTVleqPGGISILRIEPVRAgRDDAPYECVAE 96
Cdd:cd20976     1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTC---EAGVGELHIQDVLP-EDHGTYTCLAK 76

                          90
                  ....*....|....*
gi 386769894   97 NGVGdAVSADATLTI 111
Cdd:cd20976    77 NAAG-QVSCSAWVTV 90
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 136-204 1.78e-08

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


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 53.02  E-value: 1.78e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894  136 GHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLKDGFLQIENSREEDQGKYECVAENSMGTEHSKA 204
Cdd:cd05745     2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVA 70
IgI_1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; member of the I-set of (Ig) superfamily domains; ...
 36-109 2.22e-08

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


Pssm-ID: 409356 [Multi-domain]  Cd Length: 96  Bit Score: 53.40  E-value: 2.22e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386769894   36 SFYCAARGDPPPSIVWRKNGKKVS-GTQSRYTVLeqpGGISILRiEPVRAgRDDAPYECVAENGVGDAVSADATL 109
Cdd:cd04967    23 ALNCRARANPVPSYRWLMNGTEIDlESDYRYSLV---DGTLVIS-NPSKA-KDAGHYQCLATNTVGSVLSREATL 92
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 18-102 2.98e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 52.88  E-value: 2.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   18 PEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSgTQSRYTVLEQPGGISILRIEPVRAgRDDAPYECVAEN 97
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVR-PDSAHKMLVRENGRHSLIIEPVTK-RDAGIYTCIARN 78


                  ....*
gi 386769894   98 GVGDA 102
Cdd:cd05744    79 RAGEN 83
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
 136-210 3.81e-08

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


Pssm-ID: 143259  Cd Length: 88  Bit Score: 52.72  E-value: 3.81e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386769894  136 GHTVLMTCKAIGNPTPNIYWIKNQTKVDmSNPRYSLKDGFLQIENSREEDQGKYECVAENSMGTEHSKAtNLYVK 210
Cdd:cd05851    16 GQNVTLECFALGNPVPVIRWRKILEPMP-ATAEISMSGAVLKIFNIQPEDEGTYECEAENIKGKDKHQA-RVYVQ 88
I-set pfam07679
Immunoglobulin I-set domain;
216-300 4.24e-08

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 52.26  E-value: 4.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   216 PTFSRPPETIsEVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPIGRN------VLQLINIQESANYTCIAASTL 289
Cdd:pfam07679    1 PKFTQKPKDV-EVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEggtytlTISNVQPDDSGKYTCVATNSA 79

                           90
                   ....*....|.
gi 386769894   290 GQIDSVSVVKV 300
Cdd:pfam07679   80 GEAEASAELTV 90
IgI_L1-CAM_like cd05733
Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; ...
 122-203 4.29e-08

Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of 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. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lacks a C" strand.


Pssm-ID: 409396 [Multi-domain]  Cd Length: 94  Bit Score: 52.41  E-value: 4.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQGPGTRVI-EVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMS-NPRYSLKD--GFLQIENSR---EEDQGKYECVAE 194
Cdd:cd05733     1 PTITEQSPKDYIvDPRDNITIKCEAKGNPQPTFRWTKDGKFFDPAkDPRVSMRRrsGTLVIDNHNggpEDYQGEYQCYAS 80


                  ....*....
gi 386769894  195 NSMGTEHSK 203
Cdd:cd05733    81 NELGTAISN 89
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
 128-205 4.71e-08

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). 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: 52.21  E-value: 4.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  128 PGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNpRYSLK-----DGFLQIENSREEDQGKYECVAENSMGTEHS 202
Cdd:cd05737     8 PDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQALAFLD-HCNLKveagrTVYFTINGVSSEDSGKYGLVVKNKYGSETS 86


                  ...
gi 386769894  203 KAT 205
Cdd:cd05737    87 DVT 89
fn3 pfam00041
Fibronectin type III domain;
986-1078 4.77e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.03  E-value: 4.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   986 DVPLNLRAHDVSTHSMTLSWSPPIRL--TPVNYKISFDAmkvfVDSQGFSQTQIVPKREIilkhyvkTHTINELSPFTTY 1063
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGngPITGYEVEYRP----KNSGEPWNEITVPGTTT-------SVTLTGLKPGTEY 69

                           90
                   ....*....|....*
gi 386769894  1064 NVNVSAIPSDYSYRP 1078
Cdd:pfam00041   70 EVRVQAVNGGGEGPP 84
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 122-209 4.80e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 52.50  E-value: 4.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKV--DMSNPRYSLKDGF--LQIENSREEDQGKYECVAENSM 197
Cdd:cd05744     1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVrpDSAHKMLVRENGRhsLIIEPVTKRDAGIYTCIARNRA 80

                          90
                  ....*....|..
gi 386769894  198 GtEHSKATNLYV 209
Cdd:cd05744    81 G-ENSFNAELVV 91
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 135-199 4.80e-08

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 52.61  E-value: 4.80e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894  135 VGHTVLMTCKAIGNPTPNIYWIKNQT---KVDMSNPRYSLKDGF-LQIENSREEDQGKYECVAENSMGT 199
Cdd:cd05729    18 AANKVRLECGAGGNPMPNITWLKDGKefkKEHRIGGTKVEEKGWsLIIERAIPRDKGKYTCIVENEYGS 86
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 122-201 5.36e-08

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (IgSF) domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 52.09  E-value: 5.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQ-GPGTRVIEvGHTVLMTCKAIGNPTPNIYWIKNQTKVdMSNPRYSL--KDGFLQIENSREEDQGKYECVAENSMG 198
Cdd:cd05764     1 PLITRhTHELRVLE-GQRATLRCKARGDPEPAIHWISPEGKL-ISNSSRTLvyDNGTLDILITTVKDTGAFTCIASNPAG 78


                  ...
gi 386769894  199 TEH 201
Cdd:cd05764    79 EAT 81
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 128-204 6.59e-08

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 51.87  E-value: 6.59e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894  128 PGTRVIEvGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLKD--GFLQIENSREEDQGKYECVAENSMGTEHSKA 204
Cdd:cd20976     9 KDLEAVE-GQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEAgvGELHIQDVLPEDHGTYTCLAKNAAGQVSCSA 86
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 39-110 6.66e-08

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


Pssm-ID: 143223  Cd Length: 69  Bit Score: 51.03  E-value: 6.66e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386769894   39 CAARGDPPPSIVWRKNGKKVsgTQSRYTVLEQPGGISILRIEPVRAGRddapYECVAENGVGDAvSADATLT 110
Cdd:cd05746     5 CSAQGDPEPTITWNKDGVQV--TESGKFHISPEGYLAIRDVGVADQGR----YECVARNTIGYA-SVSMVLS 69
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 226-300 6.98e-08

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


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 51.83  E-value: 6.98e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894  226 SEVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPI--GRNVLQLINIQESANYTCIAASTLGQIDSVSVVKV 300
Cdd:cd05728     9 TEADIGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVeaGDLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
841-1094 9.55e-08

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 56.93  E-value: 9.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  841 GSERNMTLRKAVFTNLEENTEYIFRVRAYTKQGAGPFSDKLIVETERDMGRAPMSLQAEATSEQTAEIWWEPVTSRGkLL 920
Cdd:COG3401   184 SLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDPVTESD-AT 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  921 GYKIFYTMTavedlDDWQTKTVGLTESADLV--NLEKFAQYAVAIAARFKNGL-GRLSE--KVTVRIKPEDVPLNLRAHD 995
Cdd:COG3401   263 GYRVYRSNS-----GDGPFTKVATVTTTSYTdtGLTNGTTYYYRVTAVDAAGNeSAPSNvvSVTTDLTPPAAPSGLTATA 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  996 VSTHSMTLSWSPPIRLTPVNYKISFDAmkvfvdSQGFSQTQIVPKREIIlkhyvkTHTINELSPFTTYNVNVSAIPSD-Y 1074
Cdd:COG3401   338 VGSSSITLSWTASSDADVTGYNVYRST------SGGGTYTKIAETVTTT------SYTDTGLTPGTTYYYKVTAVDAAgN 405

                         250       260
                  ....*....|....*....|
gi 386769894 1075 SYRPPTKITVTTQMAAPQPM 1094
Cdd:COG3401   406 ESAPSEEVSATTASAASGES 425
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 892-981 9.82e-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 [Multi-domain]  Cd Length: 93  Bit Score: 51.34  E-value: 9.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  892 APMSLQAEATSEQTAEIWWEPVTS-RGKLLGYKIFYTMTaveDLDDWQT--KTVGLTESADLVNLEKFAQYAVAIAARFK 968
Cdd:cd00063     3 PPTNLRVTDVTSTSVTLSWTPPEDdGGPITGYVVEYREK---GSGDWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79

                          90
                  ....*....|...
gi 386769894  969 NGLGRLSEKVTVR 981
Cdd:cd00063    80 GGESPPSESVTVT 92
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 216-300 9.85e-08

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


Pssm-ID: 409442  Cd Length: 92  Bit Score: 51.40  E-value: 9.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  216 PTFSRPPETISEVM---LGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENempIGRN-----VLQLINI--QESANYTCIA 285
Cdd:cd05856     1 PRFTQPAKMRRRVIarpVGSSVRLKCVASGNPRPDITWLKDNKPLTPPE---IGENkkkkwTLSLKNLkpEDSGKYTCHV 77

                          90
                  ....*....|....*
gi 386769894  286 ASTLGQIDSVSVVKV 300
Cdd:cd05856    78 SNRAGEINATYKVDV 92
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 136-202 1.19e-07

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


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 51.41  E-value: 1.19e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894  136 GHTVLMTCKAIGNPTPNIYWIKNQTKVDmSNPRYSLKD---------GFLQIENSREEDQGKYECVAENSMGT-EHS 202
Cdd:cd20956    16 GPSVSLKCVASGNPLPQITWTLDGFPIP-ESPRFRVGDyvtsdgdvvSYVNISSVRVEDGGEYTCTATNDVGSvSHS 91
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
 32-111 1.45e-07

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


Pssm-ID: 409387  Cd Length: 97  Bit Score: 51.32  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   32 GGVASFYCAARGDPPPSIVWRKNGKKVS-GTQSRYTVLEQpGGISILRIEPVRAGR-DDAPYECVAENG-VGDAVSADAT 108
Cdd:cd05722    16 GGPVVLNCSAESDPPPKIEWKKDGVLLNlVSDERRQQLPN-GSLLITSVVHSKHNKpDEGFYQCVAQNEsLGSIVSRTAR 94


                  ...
gi 386769894  109 LTI 111
Cdd:cd05722    95 VTV 97
fn3 pfam00041
Fibronectin type III domain;
712-781 1.47e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.88  E-value: 1.47e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386769894   712 SIELEWERPAQTYGELRGYRLRWGVKD--QALKEEMLSGPQMTKKrFDNLERGVEYEFRVAGSNHIGIGQET 781
Cdd:pfam00041   15 SLTVSWTPPPDGNGPITGYEVEYRPKNsgEPWNEITVPGTTTSVT-LTGLKPGTEYEVRVQAVNGGGEGPPS 85
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 24-108 1.70e-07

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 50.61  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   24 PQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVsGTQSRYTVLEQPggisILRIEPVRAgRDDAPYECVAENgvgDAV 103
Cdd:cd20957     8 PPVQTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPL-GHSSRVQILSED----VLVIPSVKR-EDKGMYQCFVRN---DGD 78


                  ....*
gi 386769894  104 SADAT 108
Cdd:cd20957    79 SAQAT 83
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1529-1607 2.01e-07

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 51.20  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1529 APFLQFLRRcrALTPPEsgPVIVHCSAGVGRTGCYIVIDSMLE-RMKHEKIIDIYghvtclRAQR-NYMVQTEDQYIFIH 1606
Cdd:cd14494    43 DRFLEVLDQ--AEKPGE--PVLVHCKAGVGRTGTLVACYLVLLgGMSAEEAVRIV------RLIRpGGIPQTIEQLDFLI 112


                  .
gi 386769894 1607 D 1607
Cdd:cd14494   113 K 113
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 130-205 2.28e-07

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the 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 (NRG-1, NRG-2, NRG-3, and NRG-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: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while 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 NRG-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: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 50.59  E-value: 2.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  130 TRVIEVGHTVLMTCKAIG-NPTPNIYWIKNQTKVDMSNP-----RYSLKDGFLQIENSREEDQGKYECVAENSMGTEHSK 203
Cdd:cd05750     8 SQTVQEGSKLVLKCEATSeNPSPRYRWFKDGKELNRKRPknikiRNKKKNSELQINKAKLEDSGEYTCVVENILGKDTVT 87


                  ..
gi 386769894  204 AT 205
Cdd:cd05750    88 GN 89
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 122-204 2.31e-07

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 50.27  E-value: 2.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLKDGFLQ---IENSREEDQGKYECVAENSMG 198
Cdd:cd20972     2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHsliIAEAFEEDTGRYSCLATNSVG 81


                  ....*.
gi 386769894  199 TEHSKA 204
Cdd:cd20972    82 SDTTSA 87
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 988-1070 2.40e-07

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 [Multi-domain]  Cd Length: 83  Bit Score: 49.92  E-value: 2.40e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    988 PLNLRAHDVSTHSMTLSWSPPIRLTPVNYKISFDAMKVFVDSQGFSQTQIVPKReiilkhyvkTHTINELSPFTTYNVNV 1067
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPSST---------SYTLTGLKPGTEYEFRV 74


                    ...
gi 386769894   1068 SAI 1070
Cdd:smart00060   75 RAV 77
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 19-111 2.56e-07

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


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 49.91  E-value: 2.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   19 EIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSgTQSRYTVLEQPGGISILRIEpvragrDDAPYECVAENG 98
Cdd:cd05728     1 EWLKVISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLA-SENRIEVEAGDLRITKLSLS------DSGMYQCVAENK 73

                          90
                  ....*....|...
gi 386769894   99 VGdAVSADATLTI 111
Cdd:cd05728    74 HG-TIYASAELAV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 227-300 3.19e-07

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.81  E-value: 3.19e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    227 EVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENE-----MPIGRNVLQLINIQE--SANYTCIAASTLGQIDSVSVVK 299
Cdd:smart00410    5 TVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGrfsvsRSGSTSTLTISNVTPedSGTYTCAATNSSGSASSGTTLT 84


                    .
gi 386769894    300 V 300
Cdd:smart00410   85 V 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 986-1086 3.49e-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 [Multi-domain]  Cd Length: 93  Bit Score: 49.80  E-value: 3.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  986 DVPLNLRAHDVSTHSMTLSWSPP--IRLTPVNYKISFdamkvfvDSQGFSQTQIVPKREIilkhYVKTHTINELSPFTTY 1063
Cdd:cd00063     2 SPPTNLRVTDVTSTSVTLSWTPPedDGGPITGYVVEY-------REKGSGDWKEVEVTPG----SETSYTLTGLKPGTEY 70

                          90       100
                  ....*....|....*....|...
gi 386769894 1064 NVNVSAIPSDYSYRPPTKITVTT 1086
Cdd:cd00063    71 EFRVRAVNGGGESPPSESVTVTT 93
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 122-198 3.61e-07

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


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 49.95  E-value: 3.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNP-RYSL--KDGFLQIENSREEDQGKYECVAENSMG 198
Cdd:cd05736     1 PVIRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSkQLTLiaNGSELHISNVRYEDTGAYTCIAKNEGG 80
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 18-100 3.68e-07

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


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 49.95  E-value: 3.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   18 PEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTQSRYTVLEQPGgiSILRIEPVRAgRDDAPYECVAEN 97
Cdd:cd05736     1 PVIRVYPEFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANG--SELHISNVRY-EDTGAYTCIAKN 77


                  ...
gi 386769894   98 GVG 100
Cdd:cd05736    78 EGG 80
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 231-300 4.44e-07

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 49.53  E-value: 4.44e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894  231 GSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPIGRN-------VLQLINIQESANYTCIAASTLGQIDSVSVVKV 300
Cdd:cd05729    19 ANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVeekgwslIIERAIPRDKGKYTCIVENEYGSINHTYDVDV 95
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
 32-111 5.17e-07

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


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 48.78  E-value: 5.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   32 GGVASFYCAARGDPPPSIVWRKNGKKVSgTQSRYTVLEQpGGISILRIepvrAGRDDAPYECVAENGVGdAVSADATLTI 111
Cdd:cd05745     2 GQTVDFLCEAQGYPQPVIAWTKGGSQLS-VDRRHLVLSS-GTLRISRV----ALHDQGQYECQAVNIVG-SQRTVAQLTV 74
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 228-298 5.69e-07

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 49.03  E-value: 5.69e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894  228 VMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENE----MPIGrnVLQLINIQ--ESANYTCIAASTLGQIdSVSVV 298
Cdd:cd20952    11 VAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKDErittLENG--SLQIKGAEksDTGEYTCVALNLSGEA-TWSAV 84
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 216-300 5.92e-07

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 48.93  E-value: 5.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  216 PTFSRPPETISEVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENE-MPIGRNVLQLINIQ--ESANYTCIAASTLGQI 292
Cdd:cd20978     1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMErATVEDGTLTIINVQpeDTGYYGCVATNEIGDI 80


                  ....*...
gi 386769894  293 DSVSVVKV 300
Cdd:cd20978    81 YTETLLHV 88
IgI_1_Contactin-1 cd05849
First immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily domains; ...
 33-110 6.06e-07

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


Pssm-ID: 409436 [Multi-domain]  Cd Length: 95  Bit Score: 49.18  E-value: 6.06e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894   33 GVASFYCAARGDPPPSIVWRKNGKKVSGTQSRYTVLeqpGGisILRIEPVRAGRDDAPYECVAENGVGDAVSADATLT 110
Cdd:cd05849    20 GKVSVNCRARANPFPIYKWRKNNLDIDLTNDRYSMV---GG--NLVINNPDKYKDAGRYVCIVSNIYGKVRSREATLS 92
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 222-291 6.21e-07

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


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 49.08  E-value: 6.21e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386769894  222 PETISEVMlGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPIGRNVLQLINIQ--ESANYTCIAASTLGQ 291
Cdd:cd04968     8 PADTYALK-GQTVTLECFALGNPVPQIKWRKVDGSPSSQWEITTSEPVLEIPNVQfeDEGTYECEAENSRGK 78
IgI_hNeurofascin_like cd05875
Immunoglobulin (Ig)-like domain of human neurofascin (NF); member of the I-set of Ig ...
 122-207 6.40e-07

Immunoglobulin (Ig)-like domain of human neurofascin (NF); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of human neurofascin (NF). NF 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 a cytoplasmic domain. NF has many alternatively spliced isoforms having different temporal expression patterns during development. NF participates in axon subcellular targeting and synapse formation, however little is known of the functions of the different isoforms. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lacks a C" strand.


Pssm-ID: 409459  Cd Length: 95  Bit Score: 49.20  E-value: 6.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVIT-QGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMS-NPRYSL--KDGFLQIENS---REED-QGKYECVA 193
Cdd:cd05875     1 PTITkQSAKDYIVDPRDNILIECEAKGNPVPTFHWTRNGKFFNVAkDPRVSMrrRSGTLVIDFRgggRPEDyEGEYQCFA 80

                          90
                  ....*....|....
gi 386769894  194 ENSMGTEHSKATNL 207
Cdd:cd05875    81 RNKFGTALSNKIRL 94
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 17-111 6.78e-07

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


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 49.23  E-value: 6.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   17 PPEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGT-----QSRYTVLEQPGGISILRIEPVRAGRddapY 91
Cdd:cd20954     1 PPRWIVEPVDANVAAGQDVMLHCQADGFPTPTVTWKKATGSTPGEykdllYDPNVRILPNGTLVFGHVQKENEGH----Y 76

                          90       100
                  ....*....|....*....|
gi 386769894   92 ECVAENGVGDAVSADATLTI 111
Cdd:cd20954    77 LCEAKNGIGSGLSKVIFLKV 96
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 125-205 7.77e-07

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 48.77  E-value: 7.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  125 TQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNqTKVDMSNPR-----YSLKDGFLQIENSREEDQGKYECVAENSMGT 199
Cdd:cd05763     3 TKTPHDITIRAGSTARLECAATGHPTPQIAWQKD-GGTDFPAARerrmhVMPEDDVFFIVDVKIEDTGVYSCTAQNSAGS 81


                  ....*.
gi 386769894  200 EHSKAT 205
Cdd:cd05763    82 ISANAT 87
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
 139-204 8.56e-07

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the 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. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 48.73  E-value: 8.56e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769894  139 VLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLKDGFLQIENSREEDQGKYECVAENSMGTEHSKA 204
Cdd:cd05723    15 IVFECEVTGKPTPTVKWVKNGDVVIPSDYFKIVKEHNLQVLGLVKSDEGFYQCIAENDVGNAQASA 80
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 712-787 8.57e-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 [Multi-domain]  Cd Length: 93  Bit Score: 48.65  E-value: 8.57e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894  712 SIELEWERPAQTYGELRGYRLRWGVKDQALKEEMLSGP-QMTKKRFDNLERGVEYEFRVAGSNHIGIGQETVKIFQT 787
Cdd:cd00063    16 SVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSESVTVT 92
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1477-1607 9.38e-07

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 50.72  E-value: 9.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1477 YGQIFVTITETQELATYSIRTF-QLCRQgfndrREIKQLQFtAWPDHGVPDHPAPFLQFLRRCR-ALTPPESgpVIVHCS 1554
Cdd:cd14505    43 GVDDVVTLCTDGELEELGVPDLlEQYQQ-----AGITWHHL-PIPDGGVPSDIAQWQELLEELLsALENGKK--VLIHCK 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894 1555 AGVGRTG----CYIVidSMLERMKHEKIIDIyghvtcLRAQRNYMVQTEDQYIFIHD 1607
Cdd:cd14505   115 GGLGRTGliaaCLLL--ELGDTLDPEQAIAA------VRALRPGAIQTPKQENFLHQ 163
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 19-111 1.02e-06

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


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 48.39  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   19 EIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKnGKKVSGTQSRYTVLEQpGGISILRIEPVRAGRddapYECVAENG 98
Cdd:cd20968     1 KITRPPTNVTIIEGLKAVLPCTTMGNPKPSVSWIK-GDDLIKENNRIAVLES-GSLRIHNVQKEDAGQ----YRCVAKNS 74

                          90
                  ....*....|...
gi 386769894   99 VGDAVSADATLTI 111
Cdd:cd20968    75 LGIAYSKPVTIEV 87
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 23-111 1.04e-06

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 48.80  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   23 KPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKV-------SGTQSRYTVlEQPGGISILRIEpvragRDDAPYECVA 95
Cdd:cd05726     5 KPRDQVVALGRTVTFQCETKGNPQPAIFWQKEGSQNllfpyqpPQPSSRFSV-SPTGDLTITNVQ-----RSDVGYYICQ 78

                          90
                  ....*....|....*.
gi 386769894   96 ENGVGDAVSADATLTI 111
Cdd:cd05726    79 ALNVAGSILAKAQLEV 94
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 222-301 1.06e-06

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


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 48.17  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  222 PETISEVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPIGRN-VLQLINIQE--SANYTCIAASTLGQIDSVSVV 298
Cdd:cd05731     1 SESSTMVLRGGVLLLECIAEGLPTPDIRWIKLGGELPKGRTKFENFNkTLKIENVSEadSGEYQCTASNTMGSARHTISV 80


                  ...
gi 386769894  299 KVQ 301
Cdd:cd05731    81 TVE 83
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 32-111 1.12e-06

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 48.34  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   32 GGVASFYCAARGDPPPSIVWRKNGKKVSGTQSRYTVLEQPGGISILRIEPvrAGRDDAPYECVAENGVGDAVSAdATLTI 111
Cdd:cd20973    12 GSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEDGLCSLIISDV--CGDDSGKYTCKAVNSLGEATCS-AELTV 88
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 18-111 1.16e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 48.16  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    18 PEIIRKPQNqgVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTQSrytvleqpggISILRIEPVRAGRddapYECVAEN 97
Cdd:pfam13895    2 PVLTPSPTV--VTEGEPVTLTCSAPGNPPPSYTWYKDGSAISSSPN----------FFTLSVSAEDSGT----YTCVARN 65

                           90
                   ....*....|....
gi 386769894    98 GVGDAVSADATLTI 111
Cdd:pfam13895   66 GRGGKVSNPVELTV 79
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 234-297 1.21e-06

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 47.71  E-value: 1.21e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  234 LNLSCIAVGSPMPHVKWMKGSEDLTPENEMPI----GRNVLQLINIQE--SANYTCIAASTLGQIDSVSV 297
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRrselGNGTLTISNVTLedSGTYTCVASNSAGGSASASV 70
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 124-199 1.24e-06

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and 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. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E and, D strands in one sheet and A', G, F, C, C', and C" strands in the other.


Pssm-ID: 409355 [Multi-domain]  Cd Length: 111  Bit Score: 48.87  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  124 ITQGPGTRVIEVGHTVLMTCKAIG-NPTPNIYW-----------------IKNQTKVDmSNPRYS-----LKDGFLQIEN 180
Cdd:cd00099     1 VTQSPRSLSVQEGESVTLSCEVSSsFSSTYIYWyrqkpgqgpefliylssSKGKTKGG-VPGRFSgsrdgTSSFSLTISN 79

                          90
                  ....*....|....*....
gi 386769894  181 SREEDQGKYECVAENSMGT 199
Cdd:cd00099    80 LQPEDSGTYYCAVSESGGT 98
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 22-111 1.27e-06

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 48.15  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   22 RKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTQS--RYTVLeqPGGISILRIEPVragRDDAPYECVAENGV 99
Cdd:cd20969     7 RKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSngRLTVF--PDGTLEVRYAQV---QDNGTYLCIAANAG 81

                          90
                  ....*....|..
gi 386769894  100 GDAvSADATLTI 111
Cdd:cd20969    82 GND-SMPAHLHV 92
IgI_1_Contactin-2 cd05850
First immunoglobulin (Ig) domain of contactin-2; member of the I-set of Ig superfamily domains; ...
 122-207 1.44e-06

First immunoglobulin (Ig) domain of contactin-2; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (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. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409437 [Multi-domain]  Cd Length: 97  Bit Score: 48.38  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQGPGTRVIEVGHT---VLMTCKAIGNPTPNIYWIKNQTKVDMS-NPRYSLKDGFLQIEN-SREEDQGKYECVAENS 196
Cdd:cd05850     3 PVFEEQPSSTLFPEGSAeekVTLACRARASPPATYRWKMNGTELKMEpDSRYRLVAGNLVISNpVKAKDAGSYQCLASNR 82

                          90
                  ....*....|.
gi 386769894  197 MGTEHSKATNL 207
Cdd:cd05850    83 RGTVVSREASL 93
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 17-103 1.48e-06

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


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 48.33  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   17 PPEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSgTQSRYTVLEQPGG----ISILRIEPVRAgRDDAPYE 92
Cdd:cd20956     1 APVLLETFSEQTLQPGPSVSLKCVASGNPLPQITWTLDGFPIP-ESPRFRVGDYVTSdgdvVSYVNISSVRV-EDGGEYT 78

                          90
                  ....*....|.
gi 386769894   93 CVAENGVGDAV 103
Cdd:cd20956    79 CTATNDVGSVS 89
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 18-105 1.48e-06

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (IgSF) domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 47.86  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   18 PEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTQSRYTVLEQpGGISILriepVRAGRDDAPYECVAEN 97
Cdd:cd05764     1 PLITRHTHELRVLEGQRATLRCKARGDPEPAIHWISPEGKLISNSSRTLVYDN-GTLDIL----ITTVKDTGAFTCIASN 75


                  ....*...
gi 386769894   98 GVGDAVSA 105
Cdd:cd05764    76 PAGEATAR 83
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 215-300 1.53e-06

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 48.02  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  215 PPTFSRPPETIsEVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPIGRNVLQLINIQES-----ANYTCIAASTL 289
Cdd:cd20976     1 APSFSSVPKDL-EAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCEAGVGELHIQDVlpedhGTYTCLAKNAA 79

                          90
                  ....*....|.
gi 386769894  290 GQIDSVSVVKV 300
Cdd:cd20976    80 GQVSCSAWVTV 90
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
 122-204 1.61e-06

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409444  Cd Length: 105  Bit Score: 48.42  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQG-PGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNqtkVDMSNPRYSlKDGF--------------------LQIEN 180
Cdd:cd05858     1 PILQAGlPANTSVVVGTDAEFVCKVYSDAQPHIQWLKH---VEKNGSKYG-PDGLpyvevlktagvnttdkeievLYLRN 76

                          90       100
                  ....*....|....*....|....
gi 386769894  181 SREEDQGKYECVAENSMGTEHSKA 204
Cdd:cd05858    77 VTFEDAGEYTCLAGNSIGISHHSA 100
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1519-1607 1.62e-06

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 49.20  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1519 WPDHGVPDHPA--PFLQFLRRCRAltppESGPVIVHCSAGVGRTG----CYIVIDSMlermkheKIIDIYGHVtclRAQR 1592
Cdd:COG2453    55 IPDFGAPDDEQlqEAVDFIDEALR----EGKKVLVHCRGGIGRTGtvaaAYLVLLGL-------SAEEALARV---RAAR 120

                          90
                  ....*....|....*
gi 386769894 1593 NYMVQTEDQYIFIHD 1607
Cdd:COG2453   121 PGAVETPAQRAFLER 135
IgI_3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily (IgSF) ...
 229-301 1.70e-06

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


Pssm-ID: 143259  Cd Length: 88  Bit Score: 47.71  E-value: 1.70e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386769894  229 MLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPIGRNVLQLINIQ--ESANYTCIAASTLGQIDSVSVVKVQ 301
Cdd:cd05851    14 LKGQNVTLECFALGNPVPVIRWRKILEPMPATAEISMSGAVLKIFNIQpeDEGTYECEAENIKGKDKHQARVYVQ 88
IgI_1_Contactin-2 cd05850
First immunoglobulin (Ig) domain of contactin-2; member of the I-set of Ig superfamily domains; ...
 39-109 1.80e-06

First immunoglobulin (Ig) domain of contactin-2; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (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. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409437 [Multi-domain]  Cd Length: 97  Bit Score: 48.00  E-value: 1.80e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386769894   39 CAARGDPPPSIVWRKNGKKVS-GTQSRYTVLeqPGGISILriEPVRAgRDDAPYECVAENGVGDAVSADATL 109
Cdd:cd05850    27 CRARASPPATYRWKMNGTELKmEPDSRYRLV--AGNLVIS--NPVKA-KDAGSYQCLASNRRGTVVSREASL 93
IgI_3_FGFR cd04974
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
 122-205 2.03e-06

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409363  Cd Length: 102  Bit Score: 48.19  E-value: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQG-PGTRVIEVGHTVLMTCKAIGNPTPNIYWIK----NQTKVDMSNPRY--SLKDGF---------LQIENSREED 185
Cdd:cd04974     1 PILQAGlPANQTVVLGSDVEFHCKVYSDAQPHIQWLKhvevNGSKYGPDGLPYvtVLKVAGvnttgeentLTISNVTFDD 80

                          90       100
                  ....*....|....*....|
gi 386769894  186 QGKYECVAENSMGTEHSKAT 205
Cdd:cd04974    81 AGEYICLAGNSIGLSFHSAW 100
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1518-1607 2.04e-06

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 50.43  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1518 AWPDHGVPdhpaPFLQFLRRCR--ALTPPESGPVIVHCSAGVGRTG----CYIVidsMLERMKHEKIIDIyghvtcLRAQ 1591
Cdd:cd14506    83 GWKDYGVP----SLTTILDIVKvmAFALQEGGKVAVHCHAGLGRTGvliaCYLV---YALRMSADQAIRL------VRSK 149

                          90
                  ....*....|....*.
gi 386769894 1592 RNYMVQTEDQYIFIHD 1607
Cdd:cd14506   150 RPNSIQTRGQVLCVRE 165
IgI_1_Neogenin_like cd05722
First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of ...
 136-209 2.14e-06

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


Pssm-ID: 409387  Cd Length: 97  Bit Score: 47.86  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  136 GHTVLMTCKAIGNPTPNIYWIKNQTKV--DMSNPRYSLKDGFLQIEN---SREE--DQGKYECVAEN-SMGTEHSKATNL 207
Cdd:cd05722    16 GGPVVLNCSAESDPPPKIEWKKDGVLLnlVSDERRQQLPNGSLLITSvvhSKHNkpDEGFYQCVAQNeSLGSIVSRTARV 95


                  ..
gi 386769894  208 YV 209
Cdd:cd05722    96 TV 97
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 133-209 2.31e-06

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 47.77  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  133 IEVGHTVLMTCKAIGNPTPNIYWIKNQTKV--DMSNPRYSL-KDGFLQIENSREEDQGKYECVAENSmGTEHSKATNLYV 209
Cdd:cd20969    14 VDEGHTVQFVCRADGDPPPAILWLSPRKHLvsAKSNGRLTVfPDGTLEVRYAQVQDNGTYLCIAANA-GGNDSMPAHLHV 92
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 18-100 2.52e-06

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 47.40  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   18 PEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSgTQSRYTVLEQPGGISILRIEPVRAgRDDAPYECVAEN 97
Cdd:cd20990     1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIR-PDSAHKMLVRENGVHSLIIEPVTS-RDAGIYTCIATN 78


                  ...
gi 386769894   98 GVG 100
Cdd:cd20990    79 RAG 81
IgI_NrCAM cd05874
Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); ...
 11-104 2.69e-06

Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-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: 409458  Cd Length: 95  Bit Score: 47.67  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   11 SISHVNPPEIIRKPQNQGVrvggvasFYCAARGDPPPSIVWRKNGKKVSGTQSRYTVLEQPGGISILRI-EPVRAGRDDA 89
Cdd:cd05874     2 TITHQSPKDYIVDPRENIV-------IQCEAKGKPPPSFSWTRNGTHFDIDKDPKVTMKPNTGTLVINImNGEKAEAYEG 74

                          90
                  ....*....|....*
gi 386769894   90 PYECVAENGVGDAVS 104
Cdd:cd05874    75 VYQCTARNERGAAVS 89
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
 136-205 3.35e-06

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


Pssm-ID: 409438  Cd Length: 89  Bit Score: 46.92  E-value: 3.35e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386769894  136 GHTVLMTCKAIGNPTPNIYWIKNqTKVDMSNPRYSL-KDGFLQIENSREEDQGKYECVAENSMGTEHSKAT 205
Cdd:cd05852    17 GGRVIIECKPKAAPKPKFSWSKG-TELLVNNSRISIwDDGSLEILNITKLDEGSYTCFAENNRGKANSTGV 86
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 21-109 4.63e-06

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


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 46.67  E-value: 4.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   21 IRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVS--GTQSRYTVLEQpggisILRIEPVRAgRDDAPYECVAENG 98
Cdd:cd04978     3 IIEPPSLVLSPGETGELICEAEGNPQPTITWRLNGVPIEpaPEDMRRTVDGR-----TLIFSNLQP-NDTAVYQCNASNV 76

                          90
                  ....*....|.
gi 386769894   99 VGDAVsADATL 109
Cdd:cd04978    77 HGYLL-ANAFL 86
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 135-198 5.06e-06

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


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 46.85  E-value: 5.06e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769894  135 VGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLKD--GFLQIENSREEDQGKYECVAENSMG 198
Cdd:cd05730    17 LGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSFNEdgSEMTILDVDKLDEAEYTCIAENKAG 82
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here ...
 222-301 6.04e-06

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, 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: 409460 [Multi-domain]  Cd Length: 83  Bit Score: 46.06  E-value: 6.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  222 PETISEVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPIGRN-VLQLINIQES--ANYTCIAASTLGQIDSVSVV 298
Cdd:cd05876     1 SSSSLVALRGQSLVLECIAEGLPTPTVKWLRPSGPLPPDRVKYQNHNkTLQLLNVGESddGEYVCLAENSLGSARHAYYV 80


                  ...
gi 386769894  299 KVQ 301
Cdd:cd05876    81 TVE 83
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 17-111 7.27e-06

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


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 46.08  E-value: 7.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   17 PPEI-IRKPQ-NQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTQSRYTVLEQPGGISILRIEPvragRDDAPYECV 94
Cdd:cd05730     1 PPTIrARQSEvNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEKYSFNEDGSEMTILDVDK----LDEAEYTCI 76

                          90
                  ....*....|....*..
gi 386769894   95 AENGVGDavsADATLTI 111
Cdd:cd05730    77 AENKAGE---QEAEIHL 90
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
 17-110 7.48e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 46.19  E-value: 7.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   17 PPEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTQsRYTVLEQPGGiSILRIEPVRAGrDDAPYECVAE 96
Cdd:cd05747     3 PATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQ-RHQITSTEYK-STFEISKVQMS-DEGNYTVVVE 79

                          90
                  ....*....|....
gi 386769894   97 NGVGDAvSADATLT 110
Cdd:cd05747    80 NSEGKQ-EAQFTLT 92
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 21-102 7.70e-06

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 46.17  E-value: 7.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   21 IRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGT---QSRYTVLEQpgGISILRIEpvraGRDDAPYECVAEN 97
Cdd:cd20949     3 TENAYVTTVKEGQSATILCEVKGEPQPNVTWHFNGQPISASvadMSKYRILAD--GLLINKVT----QDDTGEYTCRAYQ 76


                  ....*
gi 386769894   98 GVGDA 102
Cdd:cd20949    77 VNSIA 81
COG3979 COG3979
Chitodextrinase [Carbohydrate transport and metabolism];
497-615 7.70e-06

Chitodextrinase [Carbohydrate transport and metabolism];


Pssm-ID: 443178 [Multi-domain]  Cd Length: 369  Bit Score: 50.54  E-value: 7.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  497 PSQPSNFRATDIGETAVTLQWtkpTHSSEN--IVHYELYWNDTYANQAHhkrisNSEAYTLDGLYPDTLYYIWLAAR--- 571
Cdd:COG3979     3 PTAPTGLTASNVTSSSVSLSW---DASTDNvgVTGYDVYRGGDQVATVT-----GLTAWTVTGLTPGTEYTFTVGACdaa 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 386769894  572 ---SQRGEGATTPPIPVRTKQYVPGDPQDVKATPLNSTSIHVSWKPP 615
Cdd:COG3979    75 gnvSAASGTSTAMFGGSSTTLGSAEGVADTSGNLAASGAFFGVTTPP 121
IgI_1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; ...
 39-109 8.56e-06

First immunoglobulin (Ig) domain of contactin-5; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (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. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409435  Cd Length: 96  Bit Score: 46.09  E-value: 8.56e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769894   39 CAARGDPPPSIVWRKNGKKVSgTQS--RYTVLEqpggiSILRIEPVRAGRDDAPYECVAENGVGDAVSADATL 109
Cdd:cd05848    26 CEARGNPVPTYRWLRNGTEID-TESdyRYSLID-----GNLIISNPSEVKDSGRYQCLATNSIGSILSREALL 92
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
 123-200 1.07e-05

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of 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: 45.67  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  123 VITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNpRYSL-----KDGFLQIENSREEDQGKYECVAENSM 197
Cdd:cd05891     3 VIGGLPDVVTIMEGKTLNLTCTVFGNPDPEVIWFKNDQDIELSE-HYSVkleqgKYASLTIKGVTSEDSGKYSINVKNKY 81


                  ...
gi 386769894  198 GTE 200
Cdd:cd05891    82 GGE 84
fn3 pfam00041
Fibronectin type III domain;
892-975 1.42e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.10  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   892 APMSLQAEATSEQTAEIWWEPVTS-RGKLLGYKIFYTMtaVEDLDDWQTKTVGLTE-SADLVNLEKFAQYAVAIAARFKN 969
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDgNGPITGYEVEYRP--KNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....*.
gi 386769894   970 GLGRLS 975
Cdd:pfam00041   80 GEGPPS 85
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 122-198 1.57e-05

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


Pssm-ID: 409473  Cd Length: 92  Bit Score: 45.14  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQGP-GTRVIEvGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSL-KDGF----LQIENSREEDQGKYECVAEN 195
Cdd:cd05892     1 PMFIQKPqNKKVLE-GDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLyQDNCgricLLIQNANKKDAGWYTVSAVN 79


                  ...
gi 386769894  196 SMG 198
Cdd:cd05892    80 EAG 82
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
 17-111 1.69e-05

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


Pssm-ID: 409397 [Multi-domain]  Cd Length: 97  Bit Score: 45.18  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   17 PPEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNgkKVSGTQSRYTVLEQPGGISILR-----IEPVRAgRDDAPY 91
Cdd:cd05734     1 PPRFVVQPNDQDGIYGKAVVLNCSADGYPPPTIVWKHS--KGSGVPQFQHIVPLNGRIQLLSngsllIKHVLE-EDSGYY 77

                          90       100
                  ....*....|....*....|
gi 386769894   92 ECVAENGVGDAVSADATLTI 111
Cdd:cd05734    78 LCKVSNDVGADISKSMYLTV 97
COG3979 COG3979
Chitodextrinase [Carbohydrate transport and metabolism];
304-539 1.92e-05

Chitodextrinase [Carbohydrate transport and metabolism];


Pssm-ID: 443178 [Multi-domain]  Cd Length: 369  Bit Score: 49.00  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  304 PTAPTDVQISEVTATSVRLEWSYkGPEDlqYYVIQYKPKNANQAFSEISGIITmyYVVRALSPYTEYEFYVIAV---NNI 380
Cdd:COG3979     3 PTAPTGLTASNVTSSSVSLSWDA-STDN--VGVTGYDVYRGGDQVATVTGLTA--WTVTGLTPGTEYTFTVGACdaaGNV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  381 GRGPPSAPATCTTGETKMESAPRNVQVRTLSSSTmvitweppeTPNGQVTGYKVYYTTNSNQPEASWNSQMVDNSELTTV 460
Cdd:COG3979    78 SAASGTSTAMFGGSSTTLGSAEGVADTSGNLAAS---------GAFFGVTTPPTPSSTLVVDGTTTVNAAATANGGTGGS 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894  461 SELTPHAIYTVRVQAYTSMGAGPMSTPVQVKAQQGVPSQPSNfratDIGETAVTLQWTKPTHSSENIVHYELYWNDTYA 539
Cdd:COG3979   149 GGTTTIITTGVEGGGGSKTAQSLNAITAAGTAALNGGVVGGA----DEVLTCSAVKDDGSGGAGAGNTYWALNTLGVSD 223
IgI_NrCAM cd05874
Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); ...
 122-202 1.99e-05

Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-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: 409458  Cd Length: 95  Bit Score: 44.97  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVIT-QGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDM-SNPRYSLK--DGFLQIENSREED----QGKYECVA 193
Cdd:cd05874     1 PTIThQSPKDYIVDPRENIVIQCEAKGKPPPSFSWTRNGTHFDIdKDPKVTMKpnTGTLVINIMNGEKaeayEGVYQCTA 80


                  ....*....
gi 386769894  194 ENSMGTEHS 202
Cdd:cd05874    81 RNERGAAVS 89
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 17-106 2.04e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 44.88  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   17 PPEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTQSryTVLEQPGGISILRIepVRAGRDDA-PYECVA 95
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPD--IQIHQEGDLHSLII--AEAFEEDTgRYSCLA 76

                          90
                  ....*....|..
gi 386769894   96 ENGVG-DAVSAD 106
Cdd:cd20972    77 TNSVGsDTTSAE 88
IgI_5_Dscam cd20958
Fifth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 136-211 2.21e-05

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


Pssm-ID: 409550 [Multi-domain]  Cd Length: 89  Bit Score: 44.48  E-value: 2.21e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894  136 GHTVLMTCKAIGNPTPNIYWIKNQTKVDmSNPRYSL-KDGFLQIEN-SREEDQGKYECVAENSMGteHSKATNLYVKV 211
Cdd:cd20958    15 GQTLRLHCPVAGYPISSITWEKDGRRLP-LNHRQRVfPNGTLVIENvQRSSDEGEYTCTARNQQG--QSASRSVFVKV 89
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1802-1900 2.25e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 46.12  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1802 QFQFIDWPEQGVPkSGEGFIDFIGQVHktkEQFGQDGPITVHCSAGVGRSGVFITLSIVLERMQYEgvldvfQTVRILRS 1881
Cdd:COG2453    49 EYLHLPIPDFGAP-DDEQLQEAVDFID---EALREGKKVLVHCRGGIGRTGTVAAAYLVLLGLSAE------EALARVRA 118

                          90
                  ....*....|....*....
gi 386769894 1882 QRPAMVQTEDQYHFCYRAA 1900
Cdd:COG2453   119 ARPGAVETPAQRAFLERFA 137
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 892-972 2.58e-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 [Multi-domain]  Cd Length: 83  Bit Score: 44.14  E-value: 2.58e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    892 APMSLQAEATSEQTAEIWWEPVTSRGkLLGYKIFYTMTAVEDLDDWQTKTVGLTE-SADLVNLEKFAQYAVAIAARFKNG 970
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDG-ITGYIVGYRVEYREEGSEWKEVNVTPSStSYTLTGLKPGTEYEFRVRAVNGAG 81


                    ..
gi 386769894    971 LG 972
Cdd:smart00060   82 EG 83
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
 219-290 2.82e-05

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


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 44.54  E-value: 2.82e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386769894  219 SRPPETIsEVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPI-GRNVLQLINIQ--ESANYTCIAASTLG 290
Cdd:cd20968     3 TRPPTNV-TIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENNRIAVlESGSLRIHNVQkeDAGQYRCVAKNSLG 76
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 128-204 2.99e-05

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391 [Multi-domain]  Cd Length: 98  Bit Score: 44.56  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  128 PGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDM-------SNPRYSL-KDGFLQIENSREEDQGKYECVAENSMGT 199
Cdd:cd05726     6 PRDQVVALGRTVTFQCETKGNPQPAIFWQKEGSQNLLfpyqppqPSSRFSVsPTGDLTITNVQRSDVGYYICQALNVAGS 85


                  ....*
gi 386769894  200 EHSKA 204
Cdd:cd05726    86 ILAKA 90
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 136-198 3.66e-05

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 44.32  E-value: 3.66e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894  136 GHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLK---DGF--LQIENSREEDQGKYECVAENSMG 198
Cdd:cd05893    15 GMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQrdlDGTcsLHTTASTLDDDGNYTIMAANPQG 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 712-778 3.74e-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 [Multi-domain]  Cd Length: 83  Bit Score: 43.76  E-value: 3.74e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894    712 SIELEWERPAQTYGelRGYRLRWGVKDQALK---EEMLSGPQMTKKRFDNLERGVEYEFRVAGSNHIGIG 778
Cdd:smart00060   16 SVTLSWEPPPDDGI--TGYIVGYRVEYREEGsewKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGAGEG 83
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
 136-209 3.76e-05

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


Pssm-ID: 409397 [Multi-domain]  Cd Length: 97  Bit Score: 44.41  E-value: 3.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  136 GHTVLMTCKAIGNPTPNIYW-------IKNQTKVDMSNPRYS-LKDGFLQIENSREEDQGKYECVAENSMGTEHSKATNL 207
Cdd:cd05734    16 GKAVVLNCSADGYPPPTIVWkhskgsgVPQFQHIVPLNGRIQlLSNGSLLIKHVLEEDSGYYLCKVSNDVGADISKSMYL 95


                  ..
gi 386769894  208 YV 209
Cdd:cd05734    96 TV 97
IgI_3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) ...
 17-100 4.44e-05

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


Pssm-ID: 409357 [Multi-domain]  Cd Length: 88  Bit Score: 43.69  E-value: 4.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   17 PPEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRkngkKVSGTQSRYTVLEQPGGisILRIEPVRAgRDDAPYECVAE 96
Cdd:cd04968     1 PSIKVRFPADTYALKGQTVTLECFALGNPVPQIKWR----KVDGSPSSQWEITTSEP--VLEIPNVQF-EDEGTYECEAE 73


                  ....
gi 386769894   97 NGVG 100
Cdd:cd04968    74 NSRG 77
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 28-104 4.57e-05

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


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 43.60  E-value: 4.57e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894   28 GVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTqSRYTVLEQpGGISILRIEPVRAGRddapYECVAENGVGDAVS 104
Cdd:cd04969    13 LAAKGGDVIIECKPKASPKPTISWSKGTELLTNS-SRICILPD-GSLKIKNVTKSDEGK----YTCFAVNFFGKANS 83
IgI_1_NCAM-2 cd05866
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; member of the ...
 133-205 5.04e-05

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-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. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409452  Cd Length: 93  Bit Score: 43.89  E-value: 5.04e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894  133 IEVGHTVLMTCKAIGNPTpNIYWIKNQTKVDMSNPRYSL-KDGF---LQIENSREEDQGKYECVAENSMGtEHSKAT 205
Cdd:cd05866    12 LSVGESKFFTCTAIGEPE-SIDWYNPQGEKIVSSQRVVVqKEGVrsrLTIYNANIEDAGIYRCQATDAKG-QTQEAT 86
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 49-238 5.31e-05

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 47.32  E-value: 5.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   49 IVWRKNGKkvsgtqSRYTVLEQPGGISILRIEPVRAgrDDAPYECVAENGV-GDAVSADATL-TIYEGDKTPAGFPvitq 126
Cdd:PHA02785   63 ILWEKRGA------DNDRIIPIDNGSNMLILNPTQS--DSGIYICITKNETyCDMMSLNLTIvSVSESNIDLISYP---- 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  127 gpgtRVIEVGHTVLMTCKAIG-----NPTPNIYWIKNQTkvdMSNPRYSLKD-GFLQIENSREEDQGKYECVAENSMGTE 200
Cdd:PHA02785  131 ----QIVNERSTGEMVCPNINafiasNVNADIIWSGHRR---LRNKRLKQRTpGIITIEDVRKNDAGYYTCVLKYIYGDK 203

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 386769894  201 HSKAT---NLYVKVRRVPPTFSRPPETISEvmLGSNLNLSC 238
Cdd:PHA02785  204 TYNVTrivKLEVRDRIIPPTMQLPEGVVTS--IGSNLTIAC 242
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
 29-100 5.67e-05

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


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 43.69  E-value: 5.67e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386769894   29 VRVGGVASFYCAARGDPPPSIVWRKNGK--KVSGTQSRYTVLEQPGGISILRIEPvragRDDAPYECVAENGVG 100
Cdd:cd05857    16 VPAANTVKFRCPAAGNPTPTMRWLKNGKefKQEHRIGGYKVRNQHWSLIMESVVP----SDKGNYTCVVENEYG 85
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 132-209 6.72e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 43.15  E-value: 6.72e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894   132 VIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDmSNPRYSLKdgflqieNSREEDQGKYECVAENSMGTEHSKATNLYV 209
Cdd:pfam13895   10 VVTEGEPVTLTCSAPGNPPPSYTWYKDGSAIS-SSPNFFTL-------SVSAEDSGTYTCVARNGRGGKVSNPVELTV 79
IgI_3_FGFR2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member ...
 24-100 7.16e-05

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409444  Cd Length: 105  Bit Score: 43.80  E-value: 7.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   24 PQNQGVRVGGVASFYCAARGDPPPSIVW----RKNGKKVSGTQSRY-TVLEQPG------GISILRIEPVrAGRDDAPYE 92
Cdd:cd05858     8 PANTSVVVGTDAEFVCKVYSDAQPHIQWlkhvEKNGSKYGPDGLPYvEVLKTAGvnttdkEIEVLYLRNV-TFEDAGEYT 86


                  ....*...
gi 386769894   93 CVAENGVG 100
Cdd:cd05858    87 CLAGNSIG 94
IgC1_hNephrin_like cd05773
Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig ...
 18-100 7.28e-05

Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin-like domain in human nephrin and similar proteins. Nephrin is an integral component of the slit diaphragm and is a central component of the glomerular ultrafilter. Nephrin plays a structural role and has a role in signaling. Nephrin is a transmembrane protein having a short intracellular portion, an extracellular portion comprised of eight Ig-like domains, and one fibronectin type III-like domain. The extracellular portions of nephrin from neighboring foot processes of separate podocyte cells may interact with each other, and in association with other components of the slit diaphragm form a porous molecular sieve within the slit pore. The intracellular portion of nephrin is associated with linker proteins, which connect nephrin to the actin cytoskeleton. The intracellular portion is tyrosine phosphorylated, and mediates signaling from the slit diaphragm into the podocytes.


Pssm-ID: 143250  Cd Length: 109  Bit Score: 43.77  E-value: 7.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   18 PEIIRKPQNQGVRVGG----VASFYCAARGDPPPSIVWRKNGKKVSGTQSRYT-VLEQPGGI--SILRIEPVRAGRDDAP 90
Cdd:cd05773     5 PDLQKGPQLRKVASRGdgssDANLVCQAQGVPRVQFRWAKNGVPLDLGNPRYEeTTEHTGTVhtSILTIINVSAALDYAL 84

                          90
                  ....*....|
gi 386769894   91 YECVAENGVG 100
Cdd:cd05773    85 FTCTAHNSLG 94
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 132-199 7.50e-05

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 43.09  E-value: 7.50e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386769894  132 VIEV--GHTVLMTCKAIGNPTPNIYWIKN-----QTKVDMSnpRYSLKDGFLQIENSREEDQGKYECVAENSMGT 199
Cdd:cd20949     8 VTTVkeGQSATILCEVKGEPQPNVTWHFNgqpisASVADMS--KYRILADGLLINKVTQDDTGEYTCRAYQVNSI 80
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 136-211 7.60e-05

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


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 43.46  E-value: 7.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  136 GHTVLMTCKAIGNPTPNIYWIK------NQTKVDMSNPRYSLKD-GFLQIENSREEDQGKYECVAENSMGTEHSKAtnLY 208
Cdd:cd20954    16 GQDVMLHCQADGFPTPTVTWKKatgstpGEYKDLLYDPNVRILPnGTLVFGHVQKENEGHYLCEAKNGIGSGLSKV--IF 93


                  ...
gi 386769894  209 VKV 211
Cdd:cd20954    94 LKV 96
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 18-111 1.03e-04

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


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 42.92  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   18 PEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNgkkvsgTQSRYTVLEQP------------GGISILRIEPvrag 85
Cdd:cd05765     1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEKQ------VPGKENLIMRPnhvrgnvvvtniGQLVIYNAQP---- 70

                          90       100
                  ....*....|....*....|....*.
gi 386769894   86 RDDAPYECVAENGVGdAVSADATLTI 111
Cdd:cd05765    71 QDAGLYTCTARNSGG-LLRANFPLSV 95
Ig_DSCAM cd05735
Immunoglobulin (Ig) domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here ...
 116-198 1.09e-04

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


Pssm-ID: 409398  Cd Length: 101  Bit Score: 43.25  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  116 KTPAgfpVITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMS-NPRY--SLKDG------FLQIENSREEDQ 186
Cdd:cd05735     1 KIPA---MITSYPNTTLATKGQKKEMSCTAHGEKPIIVRWEKEDTIINPSeMSRYlvTTKEVgdevisTLQILPTVREDS 77

                          90
                  ....*....|..
gi 386769894  187 GKYECVAENSMG 198
Cdd:cd05735    78 GFFSCHAINSYG 89
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
 125-198 1.10e-04

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


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 42.57  E-value: 1.10e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769894  125 TQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMS--NPRYSLKDGFLQIENSREEDQGKYECVAENSMG 198
Cdd:cd05867     3 TRRPQSHLYGPGETARLDCQVEGIPTPNITWSINGAPIEGTdpDPRRHVSSGALILTDVQPSDTAVYQCEARNRHG 78
IgI_Perlecan_like cd05754
Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of ...
 21-109 1.11e-04

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409412  Cd Length: 85  Bit Score: 42.54  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   21 IRKPQNQGVRVGGVASFYCAARG-DPPPSIVWRKNGKKVSGTQSRYtvleqpGGisILRIEPVRAgRDDAPYECVAENgV 99
Cdd:cd05754     5 VEEPRSQEVRPGADVSFICRAKSkSPAYTLVWTRVNGTLPSRAMDF------NG--ILTIRNVQL-SDAGTYVCTGSN-M 74

                          90
                  ....*....|
gi 386769894  100 GDAVSADATL 109
Cdd:cd05754    75 LDTDEATATL 84
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 18-109 1.12e-04

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


Pssm-ID: 409473  Cd Length: 92  Bit Score: 42.83  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   18 PEIIRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTQSRYTVLEQPGGISILRIEPVRAgRDDAPYECVAEN 97
Cdd:cd05892     1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLQYNTDRISLYQDNCGRICLLIQNANK-KDAGWYTVSAVN 79

                          90
                  ....*....|..
gi 386769894   98 GVGdAVSADATL 109
Cdd:cd05892    80 EAG-VVSCNARL 90
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 230-301 1.13e-04

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


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 42.63  E-value: 1.13e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894  230 LGSNLNLSCIAVGSPMPHVKWMKGSEDLTPE--NEMPIGRNVLQLI----NIQESANYTCIAASTLGQIDSVSVVKVQ 301
Cdd:cd05736    14 PGVEASLRCHAEGIPLPRVQWLKNGMDINPKlsKQLTLIANGSELHisnvRYEDTGAYTCIAKNEGGVDEDISSLFVE 91
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 128-212 1.15e-04

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


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 42.82  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  128 PGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLKD--GFLQIENSREEDQGKYECVAENSMGTehsKAT 205
Cdd:cd04978     6 PPSLVLSPGETGELICEAEGNPQPTITWRLNGVPIEPAPEDMRRTVdgRTLIFSNLQPNDTAVYQCNASNVHGY---LLA 82


                  ....*..
gi 386769894  206 NLYVKVR 212
Cdd:cd04978    83 NAFLHVL 89
IgI_1_NCAM-1_like cd04977
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar ...
 133-205 1.40e-04

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1. NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-nonNCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409366  Cd Length: 95  Bit Score: 42.62  E-value: 1.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894  133 IEVGHTVLMTCKAIGNPTpNIYWIK-NQTKVDMSNPRYSL--KDGF---LQIENSREEDQGKYECVAENSMGTEhSKAT 205
Cdd:cd04977    12 ISVGESKFFLCKVSGDAK-NINWVSpNGEKVLTKHGNLKVvnHGSVlssLTIYNANINDAGIYKCVATNGKGTE-SEAT 88
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
 37-111 1.77e-04

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the 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. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 41.80  E-value: 1.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386769894   37 FYCAARGDPPPSIVWRKNGKKVsgTQSRYTVLEQPGGISILRIepVRAgrDDAPYECVAENGVGDAVSAdATLTI 111
Cdd:cd05723    17 FECEVTGKPTPTVKWVKNGDVV--IPSDYFKIVKEHNLQVLGL--VKS--DEGFYQCIAENDVGNAQAS-AQLII 84
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1838-1910 2.13e-04

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 44.65  E-value: 2.13e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386769894 1838 GPITVHCSAGVGRSGVFITLSIV-LERMQYEgvldvfQTVRILRSQRPAMVQTedqyhfcyRAALEYLGSFDNY 1910
Cdd:cd14506   110 GKVAVHCHAGLGRTGVLIACYLVyALRMSAD------QAIRLVRSKRPNSIQT--------RGQVLCVREFAQF 169
IgI_2_Axl_Tyro3_like cd05749
Second immunoglobulin (Ig)-like domain of Axl/Tyro3 family receptor tyrosine kinases (RTKs); ...
 218-292 2.24e-04

Second immunoglobulin (Ig)-like domain of Axl/Tyro3 family receptor tyrosine kinases (RTKs); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in the Axl/Tyro3 family of receptor tyrosine kinases (RTKs). This family includes Axl (also known as Ark, Ufo, and Tyro7), Tyro3 (also known as Sky, Rse, Brt, Dtk, and Tif), and Mer (also known as Nyk, c-Eyk, and Tyro12). Axl/Tyro3 family receptors have an extracellular portion with two Ig-like domains followed by two fibronectin-types III (FNIII) domains, a membrane-spanning single helix, and a cytoplasmic tyrosine kinase domain. Axl, Tyro3, and Mer are widely expressed in adult tissues, though they show higher expression in the brain, lymphatic and vascular systems, and testis. Axl, Tyro3, and Mer bind the vitamin K dependent protein Gas6 with high affinity, and in doing so activate their tyrosine kinase activity. Axl/Gas6 signaling may play a part in cell adhesion processes, prevention of apoptosis, and cell proliferation.


Pssm-ID: 409407  Cd Length: 82  Bit Score: 41.68  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  218 FSRPPETISeVMLGSNLNLSCIAVGSPMP-HVKWMKGSedlTPENEMP-IGRNVLQLINIQESANYTC-------IAAST 288
Cdd:cd05749     2 FTVEPEDLA-VTANTPFNLTCQAVGPPEPvEILWWQGG---SPLGGPPaPSPSVLNVPGLNETTKFSCeahnakgLTSSR 77


                  ....
gi 386769894  289 LGQI 292
Cdd:cd05749    78 TATV 81
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1524-1605 2.42e-04

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 43.03  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1524 VPDHPAP-------FLQFLRRCRALtppeSGPVIVHCSAGVGRTG----CYIVidsmleRMKHEKIIDIyghVTCLRAQR 1592
Cdd:cd14504    57 IEDYTPPtleqideFLDIVEEANAK----NEAVLVHCLAGKGRTGtmlaCYLV------KTGKISAVDA---INEIRRIR 123

                          90
                  ....*....|...
gi 386769894 1593 NYMVQTEDQYIFI 1605
Cdd:cd14504   124 PGSIETSEQEKFV 136
IgI_2_Palladin_C cd20990
Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 122-198 2.44e-04

Second C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409582  Cd Length: 91  Bit Score: 42.01  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKV--DMSNPRYSLKDGF--LQIENSREEDQGKYECVAENSM 197
Cdd:cd20990     1 PHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIrpDSAHKMLVRENGVhsLIIEPVTSRDAGIYTCIATNRA 80


                  .
gi 386769894  198 G 198
Cdd:cd20990    81 G 81
IgI_2_Dscam cd20953
Second immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 133-200 2.51e-04

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


Pssm-ID: 409545  Cd Length: 95  Bit Score: 41.76  E-value: 2.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769894  133 IEVGHTVLMTCKAIGNPTPNIYWIK-----NQTKVDMSNPRYSLKDGFLQIENSREEDQGKYECVAENSMGTE 200
Cdd:cd20953    15 VSSASSIALLCPAQGYPAPSFRWYKfiegtTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGE 87
IgI_1_NCAM-1_like cd04977
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar ...
 29-113 2.80e-04

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1. NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-nonNCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409366  Cd Length: 95  Bit Score: 41.85  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   29 VRVGGVASFYCAARGDPPpSIVW-RKNGKKVSGTQSRYTVLEQPGGISILRIepVRAGRDDAP-YECVAENGVGDAVSAD 106
Cdd:cd04977    12 ISVGESKFFLCKVSGDAK-NINWvSPNGEKVLTKHGNLKVVNHGSVLSSLTI--YNANINDAGiYKCVATNGKGTESEAT 88


                  ....*..
gi 386769894  107 ATLTIYE 113
Cdd:cd04977    89 VKLDIIQ 95
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 220-300 2.85e-04

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 41.23  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  220 RPPETISeVMLGSNLNLSCIAVGSPMPHVKWMKgsedltPENEMPIGR------NVLQLINIQES--ANYTCIAASTLGQ 291
Cdd:cd05725     2 KRPQNQV-VLVDDSAEFQCEVGGDPVPTVRWRK------EDGELPKGRyeilddHSLKIRKVTAGdmGSYTCVAENMVGK 74


                  ....*....
gi 386769894  292 IDSVSVVKV 300
Cdd:cd05725    75 IEASATLTV 83
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
 136-199 3.16e-04

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


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 41.76  E-value: 3.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386769894  136 GHTVLMTCKAIGNPTPNIYWIKNQTKVD----MSNPRYSLKDGFLQIENSREEDQGKYECVAENSMGT 199
Cdd:cd05857    19 ANTVKFRCPAAGNPTPTMRWLKNGKEFKqehrIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGS 86
IgI_5_KIRREL3-like cd05758
Fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, and similar ...
 18-109 3.46e-04

Fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth 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 (also known as Neph1), Kirrel2 (also known as Neph3), and Drosophila RST (also known as 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: 319310  Cd Length: 98  Bit Score: 41.75  E-value: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   18 PEIIRKPQNQGVRVGGVASFYCAARGDPPP-SIVWR-KNGKKVSGTQSRYTVLEQP---GGISILRIEPVRAGRDDAPYE 92
Cdd:cd05758     2 PPIITAEATQPAILGEKARLECLVFSSPPPdRIVWSwDEGFLESGSSGRFSVETFPtepGVISVLHISGTQRSDFQTSFN 81

                          90
                  ....*....|....*..
gi 386769894   93 CVAENGVGDAvSADATL 109
Cdd:cd05758    82 CSAWNRFGEG-TAIVSL 97
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 1524-1570 3.68e-04

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 43.07  E-value: 3.68e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 386769894  1524 VPDHPAP----FLQFLRRCRALtpPESGPVIVHCSAGVGRTGCYIVIDSML 1570
Cdd:pfam14566  108 ITDEKAPleedFDALISIVKDA--PEDTALVFNCQMGRGRTTTAMVIADLV 156
IgI_hNeurofascin_like cd05875
Immunoglobulin (Ig)-like domain of human neurofascin (NF); member of the I-set of Ig ...
 39-104 4.16e-04

Immunoglobulin (Ig)-like domain of human neurofascin (NF); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of human neurofascin (NF). NF 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 a cytoplasmic domain. NF has many alternatively spliced isoforms having different temporal expression patterns during development. NF participates in axon subcellular targeting and synapse formation, however little is known of the functions of the different isoforms. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lacks a C" strand.


Pssm-ID: 409459  Cd Length: 95  Bit Score: 41.11  E-value: 4.16e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   39 CAARGDPPPSIVWRKNGKKVS-GTQSRYTVLEQPGgisILRIEPVRAGRDD---APYECVAENGVGDAVS 104
Cdd:cd05875    23 CEAKGNPVPTFHWTRNGKFFNvAKDPRVSMRRRSG---TLVIDFRGGGRPEdyeGEYQCFARNKFGTALS 89
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
 123-216 4.29e-04

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


Pssm-ID: 409359  Cd Length: 102  Bit Score: 41.38  E-value: 4.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  123 VITQGPGTRVIEVGHTVLMTCKAIGNPTPNI--YWIKNQTKVDMSNP-----RYSLKD--GFLQIENSREEDQGKYECVA 193
Cdd:cd04970     4 RITLAPSNADITVGENATLQCHASHDPTLDLtfTWSFNGVPIDLEKIeghyrRRYGKDsnGDLEIVNAQLKHAGRYTCTA 83

                          90       100
                  ....*....|....*....|...
gi 386769894  194 ENSMGTEHSKATnLYVkvrRVPP 216
Cdd:cd04970    84 QTVVDSDSASAT-LVV---RGPP 102
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 18-100 4.31e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 41.05  E-value: 4.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   18 PEIIRKPQnQGVRVGGVASFYCAARGDPPPSIVWRKNGK--KVSGTQSRYTVLEQPGGISILRIEPvragRDDAPYECVA 95
Cdd:cd05729     6 TEKMEERE-HALPAANKVRLECGAGGNPMPNITWLKDGKefKKEHRIGGTKVEEKGWSLIIERAIP----RDKGKYTCIV 80


                  ....*
gi 386769894   96 ENGVG 100
Cdd:cd05729    81 ENEYG 85
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 32-102 4.88e-04

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


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 40.86  E-value: 4.88e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386769894   32 GGVASFYCAARGDPPPSIVWRK-NGKKVSGTqsryTVLEQPGgiSILRIEPVRAgRDDAPYECVAENGVGDA 102
Cdd:cd05731    10 GGVLLLECIAEGLPTPDIRWIKlGGELPKGR----TKFENFN--KTLKIENVSE-ADSGEYQCTASNTMGSA 74
IgI_3_hemolin-like cd20977
Third immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 122-209 4.93e-04

Third immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The third Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules, including vascular (VCAM), intercellular (ICAM), neural (NCAM) and mucosal addressin (MADCAM) cell adhesion molecules, as well as junction adhesion molecules (JAM).


Pssm-ID: 409569  Cd Length: 93  Bit Score: 40.84  E-value: 4.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLKDGF-----LQIENSREEDQGKYECVAENS 196
Cdd:cd20977     1 PVPQYVSKDMMAKAGDVTMIYCMYGSNPTAHPNYFKNGKDVNGNPEDRITRHNRtsgkrLLFKTTLPEDEGVYTCEVDNG 80

                          90
                  ....*....|...
gi 386769894  197 MGTEHSKATNLYV 209
Cdd:cd20977    81 VGKPQKHSLKLTV 93
IgI_3_WFIKKN-like cd05765
Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz ...
 122-198 5.08e-04

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


Pssm-ID: 409422 [Multi-domain]  Cd Length: 95  Bit Score: 41.00  E-value: 5.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIK---NQTKVDMSnPRYSLKD------GFLQIENSREEDQGKYECV 192
Cdd:cd05765     1 PALVNSPTHQTVKVGETASFHCDVTGRPQPEITWEKqvpGKENLIMR-PNHVRGNvvvtniGQLVIYNAQPQDAGLYTCT 79


                  ....*.
gi 386769894  193 AENSMG 198
Cdd:cd05765    80 ARNSGG 85
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 126-209 5.16e-04

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


Pssm-ID: 462230  Cd Length: 109  Bit Score: 41.29  E-value: 5.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   126 QGPGTRVIEVGHTVLMTCKAIGNPTPN---IYWIKNQTK----------VDMSNP-----RYSLK------DGFLQIENS 181
Cdd:pfam07686    1 QTPREVTVALGGSVTLPCTYSSSMSEAstsVYWYRQPPGkgptfliayySNGSEEgvkkgRFSGRgdpsngDGSLTIQNL 80

                           90       100
                   ....*....|....*....|....*....
gi 386769894   182 REEDQGKYEC-VAENSMGTEHSKaTNLYV 209
Cdd:pfam07686   81 TLSDSGTYTCaVIPSGEGVFGKG-TRLTV 108
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
 223-291 5.29e-04

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 40.97  E-value: 5.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  223 ETISEvmlGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPIGRNV---------LQLINIQ--ESANYTCIAASTLGQ 291
Cdd:cd05732    11 QTAVE---LEQITLTCEAEGDPIPEITWRRATRGISFEEGDLDGRIVvrgharvssLTLKDVQltDAGRYDCEASNRIGG 87
Ig4_NrCAM cd05868
Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The ...
 128-198 5.51e-04

Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); The members here are composed of the 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: 409454  Cd Length: 89  Bit Score: 40.73  E-value: 5.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769894  128 PGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLK-DGFLQI-ENSREEDQGKYECVAENSMG 198
Cdd:cd05868     6 PTNLVLSPGEDGTLICRANGNPKPSISWLTNGVPIEIAPTDPSRKvDGDTIIfSKVQERSSAVYQCNASNEYG 78
IgI_NCAM-1 cd05869
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members ...
 122-200 5.60e-04

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


Pssm-ID: 143277 [Multi-domain]  Cd Length: 97  Bit Score: 41.12  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWiKNQTKVDMSNP---------RYSLKDGFLQIENSREEDQGKYECV 192
Cdd:cd05869     3 PKITYVENQTAMELEEQITLTCEASGDPIPSITW-RTSTRNISSEEktldghivvRSHARVSSLTLKYIQYTDAGEYLCT 81


                  ....*...
gi 386769894  193 AENSMGTE 200
Cdd:cd05869    82 ASNTIGQD 89
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 215-296 5.64e-04

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 40.64  E-value: 5.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  215 PPTFSRPPETiSEVMLGSNLNLSCIAVGSPMPHVKWMKGSEDL--TPENEMPIGRNVLQLInIQE-----SANYTCIAAS 287
Cdd:cd20972     1 PPQFIQKLRS-QEVAEGSKVRLECRVTGNPTPVVRWFCEGKELqnSPDIQIHQEGDLHSLI-IAEafeedTGRYSCLATN 78


                  ....*....
gi 386769894  288 TLGQiDSVS 296
Cdd:cd20972    79 SVGS-DTTS 86
Ig6_Contactin cd04970
Sixth immunoglobulin (Ig) domain of contactin; The members here are composed of the sixth ...
 16-111 5.92e-04

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


Pssm-ID: 409359  Cd Length: 102  Bit Score: 41.00  E-value: 5.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   16 NPPEIIRKPQNQGVRVGGVASFYCAARGDPPPSIV--WRKNG-----KKVSGTQSRYTVLEQPGGISILRIEPVRAGRdd 88
Cdd:cd04970     1 DATRITLAPSNADITVGENATLQCHASHDPTLDLTftWSFNGvpidlEKIEGHYRRRYGKDSNGDLEIVNAQLKHAGR-- 78

                          90       100
                  ....*....|....*....|...
gi 386769894   89 apYECVAENGVgDAVSADATLTI 111
Cdd:cd04970    79 --YTCTAQTVV-DSDSASATLVV 98
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 215-292 6.49e-04

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


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 40.62  E-value: 6.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  215 PPTFSrppETISEVML--GSNLNLSCIAVGSPMPHVKW----MKGSEDL--------TPENEmpigrnVLQLINI----- 275
Cdd:cd20956     1 APVLL---ETFSEQTLqpGPSVSLKCVASGNPLPQITWtldgFPIPESPrfrvgdyvTSDGD------VVSYVNIssvrv 71

                          90
                  ....*....|....*..
gi 386769894  276 QESANYTCIAASTLGQI 292
Cdd:cd20956    72 EDGGEYTCTATNDVGSV 88
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1820-1895 7.48e-04

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 41.88  E-value: 7.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769894 1820 FIDFIGQVHKTKEqfgqdgPITVHCSAGVGRSGVFITLSIVLERMQYEGvldvfQTVRILRSQRPAMVQTEDQYHF 1895
Cdd:cd14504    71 FLDIVEEANAKNE------AVLVHCLAGKGRTGTMLACYLVKTGKISAV-----DAINEIRRIRPGSIETSEQEKF 135
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 146-211 8.28e-04

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


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 39.88  E-value: 8.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  146 IGNPTPNIYWIKNQTKVDMSnPRYSL----KDGFLQIENSREEDQGKYECVAENSMGTehsKATNLYVKV 211
Cdd:cd05748    17 KGRPTPTVTWSKDGQPLKET-GRVQIettaSSTSLVIKNAKRSDSGKYTLTLKNSAGE---KSATINVKV 82
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 1806-1898 8.49e-04

protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), also known as protein-tyrosine phosphatase of regenerating liver 3 (PRL-3), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It exerts its oncogenic functions through activation of PI3K/Akt, which is a key regulator of the rapamycin-sensitive mTOR complex 1. PRL-3 is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350511 [Multi-domain]  Cd Length: 154  Bit Score: 41.93  E-value: 8.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1806 IDWP-EQGVPKSGEGFIDFIGQVhktKEQFGQDGP--ITVHCSAGVGRSGVFITLSIVLERMQYEgvlDVFQTVRilRSQ 1882
Cdd:cd18535    62 VDWPfDDGAPPPGKVVEDWLSLL---KTKFCEDPGccVAVHCVAGLGRAPVLVALALIESGMKYE---DAIQFIR--QKR 133

                          90
                  ....*....|....*.
gi 386769894 1883 RPAMVQTEDQYHFCYR 1898
Cdd:cd18535   134 RGAINSKQLTYLEKYR 149
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 1520-1575 8.61e-04

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 42.05  E-value: 8.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1520 PDHGVPDhPAPFLQFLRRCRAltppESGPVIVHCSAGVGRTG----CYIvidsmlerMKH 1575
Cdd:cd14499    88 PDGSTPS-DDIVKKFLDICEN----EKGAIAVHCKAGLGRTGtliaCYL--------MKH 134
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 21-111 8.81e-04

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the 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 (NRG-1, NRG-2, NRG-3, and NRG-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: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while 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 NRG-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: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 40.19  E-value: 8.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   21 IRKPQNQGVRVGGVASFYC-AARGDPPPSIVWRKNGKKVSGTQSRYTVLEQPGGISILRIEPVRAgRDDAPYECVAENGV 99
Cdd:cd05750     3 LKEMKSQTVQEGSKLVLKCeATSENPSPRYRWFKDGKELNRKRPKNIKIRNKKKNSELQINKAKL-EDSGEYTCVVENIL 81

                          90
                  ....*....|..
gi 386769894  100 GDAvSADATLTI 111
Cdd:cd05750    82 GKD-TVTGNVTV 92
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 122-205 9.01e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 40.10  E-value: 9.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQGPGTRVIEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSN--PRYSL--KDGF--LQIENSREEDQGKYECVAEN 195
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSipGKYKIesEYGVhvLHIRRVTVEDSAVYSAVAKN 80

                          90
                  ....*....|
gi 386769894  196 SMGTEHSKAT 205
Cdd:cd20951    81 IHGEASSSAS 90
IgI_3_FGFR cd04974
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of ...
 24-110 9.19e-04

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor (FGFR). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409363  Cd Length: 102  Bit Score: 40.48  E-value: 9.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   24 PQNQGVRVGGVASFYCAARGDPPPSIVWRK----NGKKVSGTQSRY-TVLEQPGG-----ISILRIEPVRAgrDDAP-YE 92
Cdd:cd04974     8 PANQTVVLGSDVEFHCKVYSDAQPHIQWLKhvevNGSKYGPDGLPYvTVLKVAGVnttgeENTLTISNVTF--DDAGeYI 85

                          90
                  ....*....|....*....
gi 386769894   93 CVAENGVGdaVSAD-ATLT 110
Cdd:cd04974    86 CLAGNSIG--LSFHsAWLT 102
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 215-301 9.37e-04

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 40.10  E-value: 9.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  215 PPTFSRP-PETISEvmlGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPI-------GRNVLQLINI--QESANYTCI 284
Cdd:cd20951     1 PEFIIRLqSHTVWE---KSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKykieseyGVHVLHIRRVtvEDSAVYSAV 77

                          90
                  ....*....|....*..
gi 386769894  285 AASTLGQIDSVSVVKVQ 301
Cdd:cd20951    78 AKNIHGEASSSASVVVE 94
DSP_bac cd14527
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
 1827-1902 1.11e-03

unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily is composed of uncharacterized bacterial and plant dual-specificity protein phosphatases. DUSPs function as a protein-serine/threonine phosphatases (EC 3.1.3.16) and a protein-tyrosine-phosphatases (EC 3.1.3.48).


Pssm-ID: 350376 [Multi-domain]  Cd Length: 136  Bit Score: 41.11  E-value: 1.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386769894 1827 VHKTKEQFGQDGPITVHCSAGVGRSgVFITLSIVLErmqYEGVLDVFQTVRILRSQRPAMVQTEDQyhfcyRAALE 1902
Cdd:cd14527    66 VAWIEELRAQGGPVLVHCALGYGRS-ATVVAAWLLA---YGRAKSVAEAEALIRAARPQVVLNPAQ-----RKALE 132
IgI_Perlecan_like cd05754
Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of ...
 123-205 1.20e-03

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409412  Cd Length: 85  Bit Score: 39.85  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  123 VITQGPGTRVIEVGHTVLMTCKAIG-NPTPNIYWIKNQTKVDmSNPRYSlkDGFLQIENSREEDQGKYECVAENSMGTEH 201
Cdd:cd05754     3 VTVEEPRSQEVRPGADVSFICRAKSkSPAYTLVWTRVNGTLP-SRAMDF--NGILTIRNVQLSDAGTYVCTGSNMLDTDE 79


                  ....
gi 386769894  202 SKAT 205
Cdd:cd05754    80 ATAT 83
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
 18-100 1.22e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 39.82  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   18 PEIIrKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVS---GTQSRYTVLEQPGGISILRIEPVR---AGRddapY 91
Cdd:cd05732     3 PKIT-YLENQTAVELEQITLTCEAEGDPIPEITWRRATRGISfeeGDLDGRIVVRGHARVSSLTLKDVQltdAGR----Y 77


                  ....*....
gi 386769894   92 ECVAENGVG 100
Cdd:cd05732    78 DCEASNRIG 86
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
 215-300 1.30e-03

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


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 39.92  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  215 PPTF-SRPPETISEVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPE----------NEMPIgRNVLQLiniqESANYTC 283
Cdd:cd05730     1 PPTIrARQSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGeekysfnedgSEMTI-LDVDKL----DEAEYTC 75

                          90
                  ....*....|....*..
gi 386769894  284 IAASTLGQIDSVSVVKV 300
Cdd:cd05730    76 IAENKAGEQEAEIHLKV 92
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 225-297 1.33e-03

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the 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 (NRG-1, NRG-2, NRG-3, and NRG-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: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while 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 NRG-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: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 39.80  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  225 ISEVMLGSNLNLSCIAVG-SPMPHVKWMKGSEDLT---PEN----------EMPIGRnvlqlINIQESANYTCIAASTLG 290
Cdd:cd05750     8 SQTVQEGSKLVLKCEATSeNPSPRYRWFKDGKELNrkrPKNikirnkkknsELQINK-----AKLEDSGEYTCVVENILG 82


                  ....*..
gi 386769894  291 QiDSVSV 297
Cdd:cd05750    83 K-DTVTG 88
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 136-205 1.46e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 39.48  E-value: 1.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386769894  136 GHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSLKDG----FLQIENSREEDQGKYECVAENSMGTEHSKAT 205
Cdd:cd20973    12 GSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDEdglcSLIISDVCGDDSGKYTCKAVNSLGEATCSAE 85
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 1806-1880 1.47e-03

protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), also known as protein-tyrosine phosphatase of regenerating liver 1 (PRL-1), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It may play a role in the development and maintenance of differentiating epithelial tissues. PRL-1 promotes cell growth and migration by activating both the ERK1/2 and RhoA pathways. It is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350513 [Multi-domain]  Cd Length: 167  Bit Score: 41.60  E-value: 1.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894 1806 IDWP-EQGVPKSGEGFIDFIGQVH-KTKEQFGqdGPITVHCSAGVGRSGVFITLSIVLERMQYEgvlDVFQTVRILR 1880
Cdd:cd18537    66 LDWPfDDGAPPSNQIVDDWLNLLKvKFREEPG--CCIAVHCVAGLGRAPVLVALALIECGMKYE---DAVQFIRQKR 137
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
 21-97 1.73e-03

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


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 39.49  E-value: 1.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894   21 IRKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTQSRYTVLEQPGGISILRIEPvragRDDAPYECVAEN 97
Cdd:cd05867     3 TRRPQSHLYGPGETARLDCQVEGIPTPNITWSINGAPIEGTDPDPRRHVSSGALILTDVQP----SDTAVYQCEARN 75
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 227-300 1.81e-03

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 39.09  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  227 EVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPIGRN-------VLQLINIQESANYTCIAASTLGQIDSVSVVK 299
Cdd:cd20973     8 EVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIDQDedglcslIISDVCGDDSGKYTCKAVNSLGEATCSAELT 87


                  .
gi 386769894  300 V 300
Cdd:cd20973    88 V 88
IgI_L1-CAM_like cd05733
Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; ...
 39-109 1.97e-03

Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of 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. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lacks a C" strand.


Pssm-ID: 409396 [Multi-domain]  Cd Length: 94  Bit Score: 39.31  E-value: 1.97e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386769894   39 CAARGDPPPSIVWRKNGKKVS-GTQSRYTVLEQPGGISIlRIEPVRAGRDDAPYECVAENGVGDAVSADATL 109
Cdd:cd05733    23 CEAKGNPQPTFRWTKDGKFFDpAKDPRVSMRRRSGTLVI-DNHNGGPEDYQGEYQCYASNELGTAISNEIRL 93
IgC1_hNephrin_like cd05773
Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig ...
 141-200 2.17e-03

Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin-like domain in human nephrin and similar proteins. Nephrin is an integral component of the slit diaphragm and is a central component of the glomerular ultrafilter. Nephrin plays a structural role and has a role in signaling. Nephrin is a transmembrane protein having a short intracellular portion, an extracellular portion comprised of eight Ig-like domains, and one fibronectin type III-like domain. The extracellular portions of nephrin from neighboring foot processes of separate podocyte cells may interact with each other, and in association with other components of the slit diaphragm form a porous molecular sieve within the slit pore. The intracellular portion of nephrin is associated with linker proteins, which connect nephrin to the actin cytoskeleton. The intracellular portion is tyrosine phosphorylated, and mediates signaling from the slit diaphragm into the podocytes.


Pssm-ID: 143250  Cd Length: 109  Bit Score: 39.53  E-value: 2.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894  141 MTCKAIGNPTPNIYWIKNQTKVDMSNPRY--------SLKDGFLQIEN-SREEDQGKYECVAENSMGTE 200
Cdd:cd05773    28 LVCQAQGVPRVQFRWAKNGVPLDLGNPRYeettehtgTVHTSILTIINvSAALDYALFTCTAHNSLGED 96
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 216-300 2.39e-03

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


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 38.98  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  216 PTFSRPP-ETISEVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPIGRN-VLQLINIQES--ANYTCIAASTLGQ 291
Cdd:cd04969     1 PDFELNPvKKKILAAKGGDVIIECKPKASPKPTISWSKGTELLTNSSRICILPDgSLKIKNVTKSdeGKYTCFAVNFFGK 80


                  ....*....
gi 386769894  292 IDSVSVVKV 300
Cdd:cd04969    81 ANSTGSLSV 89
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here ...
 122-199 2.49e-03

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


Pssm-ID: 409417  Cd Length: 95  Bit Score: 39.14  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQGPGTRV-IEVGHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYSL--KDGFLQIENSREEDQGKYECVAENSMG 198
Cdd:cd05760     1 PVVLKHPASAAeIQPSSRVTLRCHIDGHPRPTYQWFRDGTPLSDGQGNYSVssKERTLTLRSAGPDDSGLYYCCAHNAFG 80


                  .
gi 386769894  199 T 199
Cdd:cd05760    81 S 81
IgI_3_RPTP_IIa_LAR_like cd05739
Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F ...
 22-111 2.72e-03

Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F (also known as LAR), type IIa; member of the I-set of IgSF domains; The members here are composed of the third 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. Included in this group is Drosophila LAR (DLAR).


Pssm-ID: 409401  Cd Length: 82  Bit Score: 38.73  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   22 RKPQNQGVRVGGVASFYCAARGDPPPSIVWRKNGKKVSGTQsrytvlEQPGGISILRIEPVragRDDAPYECVAENGVGd 101
Cdd:cd05739     2 IPPSNHEVMPGGSVNLTCVAVGAPMPYVKWMKGGEELTKED------EMPVGRNVLELTNI---YESANYTCVAISSLG- 71

                          90
                  ....*....|
gi 386769894  102 AVSADATLTI 111
Cdd:cd05739    72 MIEATAQVTV 81
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 24-100 2.91e-03

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


Pssm-ID: 395002  Cd Length: 86  Bit Score: 38.72  E-value: 2.91e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894    24 PQNQGVRVGGVASFYCAAR-GDPPPSIVWRKNGKkvSGTQSRYTVlEQPGGISILRIEPVRAGRDDAP-YECVAENGVG 100
Cdd:pfam00047    3 PPTVTVLEGDSATLTCSAStGSPGPDVTWSKEGG--TLIESLKVK-HDNGRTTQSSLLISNVTKEDAGtYTCVVNNPGG 78
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
 122-209 2.97e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 39.04  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQGPGTRVIEVGHtVLMTCKAIGNPTPNIYWiknQTKVD-MSNPRYSLkDG-----------FLQIENSREEDQGKY 189
Cdd:cd05732     3 PKITYLENQTAVELEQ-ITLTCEAEGDPIPEITW---RRATRgISFEEGDL-DGrivvrgharvsSLTLKDVQLTDAGRY 77

                          90       100
                  ....*....|....*....|
gi 386769894  190 ECVAENSMGtEHSKATNLYV 209
Cdd:cd05732    78 DCEASNRIG-GDQQSMYLEV 96
IgI_1_Dscam cd20955
First immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 122-199 3.06e-03

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


Pssm-ID: 409547  Cd Length: 99  Bit Score: 38.93  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  122 PVITQGPGTRVIEVGHT-VLMTCKAIGNPTPNIYWIKNQTKV--DMSNPRYSLKDGFLQIENSREEDQGK------YECV 192
Cdd:cd20955     2 PVFLKEPTNRIDFSNSTgAEIECKASGNPMPEIIWIRSDGTAvgDVPGLRQISSDGKLVFPPFRAEDYRQevhaqvYACL 81


                  ....*..
gi 386769894  193 AENSMGT 199
Cdd:cd20955    82 ARNQFGS 88
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
 136-204 3.50e-03

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the human APEG-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409567  Cd Length: 91  Bit Score: 38.61  E-value: 3.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386769894  136 GHTVLMTCKAIGNPTPNIYWIKNQTKVDMSNPRYS--LKDGF--LQIENSREEDQGKYECVAENSMGTEHSKA 204
Cdd:cd20975    15 GQDVIMSIRVQGEPKPVVSWLRNRQPVRPDQRRFAeeAEGGLcrLRILAAERGDAGFYTCKAVNEYGARQCEA 87
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 1821-1887 3.61e-03

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 39.55  E-value: 3.61e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386769894  1821 IDFIGQVHKtkeqfgQDGPITVHCSAGVGRSGVFITLSIvlerMQYEGvLDVFQTVRILRSQRPAMV 1887
Cdd:pfam00782   59 VEFIDDARQ------KGGKVLVHCQAGISRSATLIIAYL----MKTRN-LSLNEAYSFVKERRPGIS 114
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1779-1895 3.80e-03

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 39.94  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894 1779 MPQYKLREFKVTDARDGSSR---TVRQFQFIDwpeQGVPKSGEGF---IDFIgqvhktKEQFGQDGPITVHCSAGVGRSG 1852
Cdd:cd14505    51 CTDGELEELGVPDLLEQYQQagiTWHHLPIPD---GGVPSDIAQWqelLEEL------LSALENGKKVLIHCKGGLGRTG 121

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 386769894 1853 VfITLSIVLERMQYEGVLDVFQTVRILrsqRPAMVQTEDQYHF 1895
Cdd:cd14505   122 L-IAACLLLELGDTLDPEQAIAAVRAL---RPGAIQTPKQENF 160
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
1795-1887 4.18e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 39.57  E-value: 4.18e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   1795 GSSRTVRQFQFIDWPEQGVPKSGEGFIDFIGQVHKTKeqfgqdGPITVHCSAGVGRSGVFITLSIvlerMQYEGvLDVFQ 1874
Cdd:smart00195   42 GSDFTYLGVPIDDNTETKISPYFPEAVEFIEDAESKG------GKVLVHCQAGVSRSATLIIAYL----MKTRN-MSLND 110

                            90
                    ....*....|...
gi 386769894   1875 TVRILRSQRPAMV 1887
Cdd:smart00195  111 AYDFVKDRRPIIS 123
IgI_NCAM-1 cd05869
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members ...
 223-291 4.51e-03

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


Pssm-ID: 143277 [Multi-domain]  Cd Length: 97  Bit Score: 38.42  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894  223 ETISEVMLGSNLNLSCIAVGSPMPHVKWMKGSEDLTPENEMPIGRNV---------LQLINIQ--ESANYTCIAASTLGQ 291
Cdd:cd05869     9 ENQTAMELEEQITLTCEASGDPIPSITWRTSTRNISSEEKTLDGHIVvrsharvssLTLKYIQytDAGEYLCTASNTIGQ 88
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 32-100 4.88e-03

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 38.15  E-value: 4.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386769894   32 GGVASFYCAARGDPPPSIVWRKNGKKVSGTQSRYTVLEQPGGISILRIEpVRAGRDDAPYECVAENGVG 100
Cdd:cd05893    15 GMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRDLDGTCSLHTT-ASTLDDDGNYTIMAANPQG 82
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
 32-111 5.21e-03

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


Pssm-ID: 143220  Cd Length: 78  Bit Score: 37.47  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386769894   32 GGVASFYCAARGDPPPSIVWRKNGKKVSgtQSRYTVLEQPGGISILRIEPVRAgRDDAPYECVAENGVGDA-VSADATLT 110
Cdd:cd05743     1 GETVEFTCVATGVPTPIINWRLNWGHVP--DSARVSITSEGGYGTLTIRDVKE-SDQGAYTCEAINTRGMVfGIPDGILT 77


                  .
gi 386769894  111 I 111
Cdd:cd05743    78 V 78
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
1525-1561 7.09e-03

Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 40.33  E-value: 7.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 386769894 1525 PDHPAPFLQFLRrcrALTPPESGPVIVHCSAGVGRTG 1561
Cdd:COG2365   115 PDAADAYRAAFR---ALADAENGPVLFHCTAGKDRTG 148
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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