|
Name |
Accession |
Description |
Interval |
E-value |
| PTPc |
smart00194 |
Protein tyrosine phosphatase, catalytic domain; |
1216-1474 |
4.27e-116 |
|
Protein tyrosine phosphatase, catalytic domain;
Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 365.44 E-value: 4.27e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1216 GFAEEYQGLANVG-TNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLdRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLP 1294
Cdd:smart00194 1 GLEEEFEKLDRLKpDDESCTVAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1295 NTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTI 1373
Cdd:smart00194 80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLtYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1374 TQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRM 1453
Cdd:smart00194 160 THYHYTNWPDHGVPESPESILDLIRAVRKS-QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238
|
250 260
....*....|....*....|.
gi 1822521627 1454 SRTCMVQTENQYIFLHQCILD 1474
Cdd:smart00194 239 QRPGMVQTEEQYIFLYRAILE 259
|
|
| R3-PTPc |
cd14548 |
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ... |
1246-1470 |
2.45e-111 |
|
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: 350.89 E-value: 2.45e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1246 RYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVK 1325
Cdd:cd14548 1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1326 CERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLN 1405
Cdd:cd14548 81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822521627 1406 KNrAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1470
Cdd:cd14548 159 QE-KGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
|
|
| Y_phosphatase |
pfam00102 |
Protein-tyrosine phosphatase; |
1241-1474 |
9.97e-110 |
|
Protein-tyrosine phosphatase;
Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 346.92 E-value: 9.97e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1241 NKVKNRYTNIFPYDVARVKLdrQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1320
Cdd:pfam00102 1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1321 QNRVKCERYWPMDMS-SCLYGDIVVNIVSEET-SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQR 1398
Cdd:pfam00102 79 KGREKCAQYWPEEEGeSLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521627 1399 MMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:pfam00102 159 KVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
|
|
| R-PTPc-J |
cd14615 |
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ... |
1245-1474 |
3.31e-108 |
|
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: 342.57 E-value: 3.31e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1245 NRYTNIFPYDVARVKLDrQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1324
Cdd:cd14615 1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1325 KCERYWPMDMSSClYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYL 1404
Cdd:cd14615 80 KCEEYWPSKQKKD-YGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521627 1405 NKNRAGLPV-VHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:cd14615 159 KQNPPNSPIlVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
|
|
| R-PTPc-H |
cd14619 |
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ... |
1245-1474 |
4.08e-105 |
|
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: 334.16 E-value: 4.08e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1245 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1324
Cdd:cd14619 1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1325 KCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYL 1404
Cdd:cd14619 81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521627 1405 NKNRA-GLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:cd14619 161 DQTMSgGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
|
|
| PTPc |
cd00047 |
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ... |
1271-1470 |
2.62e-97 |
|
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: 310.76 E-value: 2.62e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSE 1349
Cdd:cd00047 1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLeYGDITVTLVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1350 ETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRaGLPVVHCSAGVGRTGTLIAL 1429
Cdd:cd00047 81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPN-GPIVVHCSAGVGRTGTFIAI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1822521627 1430 DYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1470
Cdd:cd00047 160 DILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
|
|
| R-PTPc-B |
cd14617 |
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ... |
1245-1470 |
1.71e-95 |
|
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: 306.85 E-value: 1.71e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1245 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1324
Cdd:cd14617 1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1325 KCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVkktgCPE-----PRTITQFHFTSWPDHGVPKTTDKLLQFQRM 1399
Cdd:cd14617 81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKI----CSEeqldaPRLVRHFHYTVWPDHGVPETTQSLIQFVRT 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822521627 1400 MRDYLNK-NRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1470
Cdd:cd14617 157 VRDYINRtPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
|
|
| R-PTPc-O |
cd14614 |
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ... |
1232-1473 |
5.19e-92 |
|
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: 297.96 E-value: 5.19e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1232 SKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKV 1311
Cdd:cd14614 3 PHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1312 IVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVP--KT 1389
Cdd:cd14614 83 IVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYAD--EVQDVMHFNYTAWPDHGVPtaNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1390 TDKLLQFQRMMRDYLNKnRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1469
Cdd:cd14614 161 AESILQFVQMVRQQAVK-SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 239
|
....
gi 1822521627 1470 QCIL 1473
Cdd:cd14614 240 QCVQ 243
|
|
| R-PTPc-LAR-1 |
cd14553 |
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ... |
1241-1474 |
2.64e-91 |
|
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: 295.46 E-value: 2.64e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1241 NKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1320
Cdd:cd14553 3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1321 QNRVKCERYWPMDMSScLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMM 1400
Cdd:cd14553 83 RSRVKCDQYWPTRGTE-TYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822521627 1401 RdYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:cd14553 162 K-ACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
|
|
| R-PTPc-V |
cd14618 |
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ... |
1245-1473 |
2.48e-86 |
|
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: 281.06 E-value: 2.48e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1245 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1324
Cdd:cd14618 1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1325 KCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYL 1404
Cdd:cd14618 81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1405 NKNRAGLPV-VHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1473
Cdd:cd14618 161 QATKGKGPTlVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
|
|
| R5-PTPc-1 |
cd14549 |
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ... |
1271-1469 |
1.61e-81 |
|
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: 266.52 E-value: 1.61e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSClYGDIVVNIVSEE 1350
Cdd:cd14549 1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTET-YGNIQVTLLSTE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1351 TSPEWTTRKFNVK------KTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRmMRDYLNKNRAGLPVVHCSAGVGRTG 1424
Cdd:cd14549 80 VLATYTVRTFSLKnlklkkVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVR-KSSAANPPGAGPIVVHCSAGVGRTG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1822521627 1425 TLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1469
Cdd:cd14549 159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
|
|
| R-PTPc-Q |
cd14616 |
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ... |
1245-1470 |
4.24e-80 |
|
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: 263.31 E-value: 4.24e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1245 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1324
Cdd:cd14616 1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1325 KCERYWPMDMSS-CLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdy 1403
Cdd:cd14616 81 RCHQYWPEDNKPvTVFGDIVITKLMEDVQIDWTIRDLKIERHG--DYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR-- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1404 lnKNRAGLP---VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1470
Cdd:cd14616 157 --ASRAHDNtpmIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
|
|
| PTPc-N9 |
cd14543 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ... |
1216-1469 |
1.65e-79 |
|
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: 263.46 E-value: 1.65e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1216 GFAEEYQGLAN---VGTNQSKEAfqvPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGP 1292
Cdd:cd14543 4 GIYEEYEDIRReppAGTFLCSLA---PANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1293 LPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPR 1371
Cdd:cd14543 81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLrYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1372 TITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLN----------KNRAGLP--VVHCSAGVGRTGTLIALDYLLQRIEKE 1439
Cdd:cd14543 161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQAlavkamgdrwKGHPPGPpiVVHCSAGIGRTGTFCTLDICLSQLEDV 240
|
250 260 270
....*....|....*....|....*....|
gi 1822521627 1440 AVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1469
Cdd:cd14543 241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
|
|
| R-PTPc-T-1 |
cd14630 |
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ... |
1240-1474 |
4.69e-76 |
|
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: 252.25 E-value: 4.69e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1240 DNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCV 1319
Cdd:cd14630 2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1320 EQNRVKCERYWPMDMSscLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRM 1399
Cdd:cd14630 82 EVGRVKCVRYWPDDTE--VYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822521627 1400 MRdYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:cd14630 160 VK-FLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
|
|
| R-PTPc-F-1 |
cd14626 |
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ... |
1200-1474 |
6.92e-75 |
|
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: 250.34 E-value: 6.92e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1200 SEYKSYYQRKHADTDIGFAEEYQGLaNVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPG 1279
Cdd:cd14626 1 SDLADNIERLKANDGLKFSQEYESI-DPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1280 YHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSClYGDIVVNIVSEETSPEWTTRK 1359
Cdd:cd14626 80 YRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTET-YGMIQVTLLDTVELATYSVRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1360 FNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKE 1439
Cdd:cd14626 159 FALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKA-CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHE 237
|
250 260 270
....*....|....*....|....*....|....*
gi 1822521627 1440 AVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:cd14626 238 KTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
|
|
| PTPc-KIM |
cd14547 |
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ... |
1245-1470 |
6.50e-74 |
|
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: 245.38 E-value: 6.50e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1245 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGY-HLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEqNR 1323
Cdd:cd14547 1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1324 VKCERYWPMDMSScLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQR-MMRD 1402
Cdd:cd14547 80 EKCAQYWPEEENE-TYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQeVEEA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521627 1403 YLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1470
Cdd:cd14547 157 RQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
|
|
| R-PTPc-M-1 |
cd14633 |
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ... |
1216-1474 |
1.08e-73 |
|
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: 246.88 E-value: 1.08e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1216 GFAEEYQGLANvGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPN 1295
Cdd:cd14633 16 GFKEEYESFFE-GQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1296 TVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSscLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQ 1375
Cdd:cd14633 95 TIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1376 FHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNrAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSR 1455
Cdd:cd14633 173 FHFTGWPDHGVPYHATGLLGFVRQVKSKSPPN-AGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRR 251
|
250
....*....|....*....
gi 1822521627 1456 TCMVQTENQYIFLHQCILD 1474
Cdd:cd14633 252 VNMVQTEEQYVFIHDAILE 270
|
|
| R-PTPc-A-1 |
cd14621 |
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ... |
1194-1474 |
5.35e-73 |
|
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: 245.70 E-value: 5.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1194 FKPIPVSEYKSYYQRKHADTDIGFAEEYQGLANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYIN 1273
Cdd:cd14621 5 YPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYIN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1274 ASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEETSP 1353
Cdd:cd14621 85 ASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP-DQGCWTYGNIRVSVEDVTVLV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1354 EWTTRKFNVKK----TGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTLIAL 1429
Cdd:cd14621 164 DYTVRKFCIQQvgdvTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKN-CNPQYAGAIVVHCSAGVGRTGTFIVI 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1822521627 1430 DYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:cd14621 243 DAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287
|
|
| R-PTPc-S-1 |
cd14625 |
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ... |
1196-1477 |
2.13e-72 |
|
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: 243.46 E-value: 2.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1196 PIPVSEYKSYYQRKHADTDIGFAEEYQGLaNVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINAS 1275
Cdd:cd14625 3 PIPISELAEHTERLKANDNLKLSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1276 YMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEETSPEW 1355
Cdd:cd14625 82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP-SRGTETYGMIQVTLLDTIELATF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1356 TTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQR 1435
Cdd:cd14625 161 CVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKT-CNPPDAGPIVVHCSAGVGRTGCFIVIDAMLER 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1822521627 1436 IEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDVTG 1477
Cdd:cd14625 240 IKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVA 281
|
|
| R-PTPc-G-1 |
cd17667 |
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ... |
1217-1474 |
3.78e-72 |
|
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: 242.63 E-value: 3.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1217 FAEEYQGL--ANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQP--NSSSSDYINASYMPGYHLDKAFIAAQGP 1292
Cdd:cd17667 1 FSEDFEEVqrCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPgkDSKHSDYINANYVDGYNKAKAYIATQGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1293 LPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEETSPEWTTRKFNVKKT------- 1365
Cdd:cd17667 81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE-EYGNIIVTLKSTKIHACYTVRRFSIRNTkvkkgqk 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1366 ----GCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRmmrdylNKNRAGLP-----VVHCSAGVGRTGTLIALDYLLQRI 1436
Cdd:cd17667 160 gnpkGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVR------RSSAARTPemgpvLVHCSAGVGRTGTYIVIDSMLQQI 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 1822521627 1437 EKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:cd17667 234 KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
|
|
| R-PTP-LAR-2 |
cd14554 |
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ... |
1238-1473 |
3.45e-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: 238.19 E-value: 3.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1238 VPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTN 1317
Cdd:cd14554 3 LPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1318 CVEQNRVKCERYWPMDmSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQF- 1396
Cdd:cd14554 83 LREMGREKCHQYWPAE-RSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFi 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521627 1397 QRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1473
Cdd:cd14554 162 GQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
|
|
| R-PTPc-C-1 |
cd14557 |
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ... |
1271-1470 |
4.18e-71 |
|
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: 236.65 E-value: 4.18e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWP-MDMSSCLYGDIVVNIVSE 1349
Cdd:cd14557 1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsMEEGSRAFGDVVVKINEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1350 ETSPEWTTRKFNV--KKTGCPEpRTITQFHFTSWPDHGVPKTTDKLLQFQRMMrDYLNKNRAGLPVVHCSAGVGRTGTLI 1427
Cdd:cd14557 81 KICPDYIIRKLNInnKKEKGSG-REVTHIQFTSWPDHGVPEDPHLLLKLRRRV-NAFNNFFSGPIVVHCSAGVGRTGTYI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1822521627 1428 ALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1470
Cdd:cd14557 159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
|
|
| R-PTPc-D-1 |
cd14624 |
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ... |
1196-1474 |
5.60e-71 |
|
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: 239.63 E-value: 5.60e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1196 PIPVSEYKSYYQRKHADTDIGFAEEYQGLaNVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINAS 1275
Cdd:cd14624 3 PIPILELADHIERLKANDNLKFSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1276 YMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEETSPEW 1355
Cdd:cd14624 82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWP-SRGTETYGLIQVTLLDTVELATY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1356 TTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQR 1435
Cdd:cd14624 161 CVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKT-CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLER 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 1822521627 1436 IEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:cd14624 240 IKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
|
|
| R-PTPc-typeIIb-1 |
cd14555 |
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ... |
1271-1474 |
7.10e-71 |
|
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: 235.97 E-value: 7.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDmsSCLYGDIVVNIVSEE 1350
Cdd:cd14555 1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD--TEVYGDIKVTLVETE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1351 TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdYLNKNRAGLPVVHCSAGVGRTGTLIALD 1430
Cdd:cd14555 79 PLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVK-ASNPPSAGPIVVHCSAGAGRTGCYIVID 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1822521627 1431 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:cd14555 158 IMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
|
|
| PTPc-N11_6 |
cd14544 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ... |
1241-1472 |
9.03e-69 |
|
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: 231.97 E-value: 9.03e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1241 NKVKNRYTNIFPYDVARVKL-DRQPNSSSSDYINASYM-----PGYHLD--KAFIAAQGPLPNTVVDFWRMVWEQKTKVI 1312
Cdd:cd14544 1 NKGKNRYKNILPFDHTRVILkDRDPNVPGSDYINANYIrneneGPTTDEnaKTYIATQGCLENTVSDFWSMVWQENSRVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1313 VMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEP-RTITQFHFTSWPDHGVPKTTD 1391
Cdd:cd14544 81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPiREIWHYQYLSWPDHGVPSDPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1392 KLLQF-QRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAV---VDVYGIVHNMRMSRTCMVQTENQYIF 1467
Cdd:cd14544 161 GVLNFlEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKF 240
|
....*
gi 1822521627 1468 LHQCI 1472
Cdd:cd14544 241 IYVAV 245
|
|
| R-PTPc-E-1 |
cd14620 |
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ... |
1247-1474 |
1.18e-68 |
|
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: 230.60 E-value: 1.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1247 YTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKC 1326
Cdd:cd14620 1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1327 ERYWPmDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKT---GCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDy 1403
Cdd:cd14620 81 YQYWP-DQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521627 1404 LNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:cd14620 159 VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
|
|
| PTP_fungal |
cd18533 |
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ... |
1271-1470 |
2.40e-66 |
|
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: 223.28 E-value: 2.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYM-PGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSE 1349
Cdd:cd18533 1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1350 ET--SPEWTTRKFNVKKTGCPePRTITQFHFTSWPDHGVPKTTDKLLQfqrMMR--DYLNKN-RAGLP-VVHCSAGVGRT 1423
Cdd:cd18533 81 EEndDGGFIVREFELSKEDGK-VKKVYHIQYKSWPDFGVPDSPEDLLT---LIKlkRELNDSaSLDPPiIVHCSAGVGRT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521627 1424 GTLIALDYLLQRIEK--------EAVVD-VYGIVHNMRMSRTCMVQTENQYIFLHQ 1470
Cdd:cd18533 157 GTFIALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
|
|
| R-PTPc-K-1 |
cd14631 |
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ... |
1257-1474 |
3.00e-66 |
|
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: 223.36 E-value: 3.00e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1257 RVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSs 1336
Cdd:cd14631 1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1337 cLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdYLNKNRAGLPVVHC 1416
Cdd:cd14631 80 -VYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK-LSNPPSAGPIVVHC 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521627 1417 SAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:cd14631 158 SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
|
|
| PTPc-N18 |
cd14603 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ... |
1232-1472 |
4.74e-66 |
|
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: 224.70 E-value: 4.74e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1232 SKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKV 1311
Cdd:cd14603 21 STVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1312 IVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEE-TSPEWTTRKFNVkkTGCPEPRTITQFHFTSWPDHGVPKTT 1390
Cdd:cd14603 101 ILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKrLNEEVILRTLKV--TFQKESRSVSHFQYMAWPDHGIPDSP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1391 DKLLQFQRMMRDYLNKNRAGLpVVHCSAGVGRTGTLIALDY-----LLQRIEKEavVDVYGIVHNMRMSRTCMVQTENQY 1465
Cdd:cd14603 179 DCMLAMIELARRLQGSGPEPL-CVHCSAGCGRTGVICTVDYvrqllLTQRIPPD--FSIFDVVLEMRKQRPAAVQTEEQY 255
|
....*..
gi 1822521627 1466 IFLHQCI 1472
Cdd:cd14603 256 EFLYHTV 262
|
|
| PTPc-N13 |
cd14597 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ... |
1240-1475 |
7.94e-66 |
|
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: 222.78 E-value: 7.94e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1240 DNKVKNRYTNIFPYDVARVKLdrqpnSSSSDYINASY--MPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTN 1317
Cdd:cd14597 2 ENRKKNRYKNILPYDTTRVPL-----GDEGGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1318 CVEQNRVKCERYWPMDMSSCLYGD--IVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQ 1395
Cdd:cd14597 77 EVEGGKIKCQRYWPEILGKTTMVDnrLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1396 FQRMMRdylNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1475
Cdd:cd14597 157 FISYMR---HIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILYV 233
|
|
| R-PTPc-A-E-1 |
cd14551 |
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ... |
1271-1470 |
8.09e-66 |
|
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: 221.32 E-value: 8.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEE 1350
Cdd:cd14551 1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGCWTYGNLRVRVEDTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1351 TSPEWTTRKFNVKK----TGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTL 1426
Cdd:cd14551 80 VLVDYTTRKFCIQKvnrgIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKS-ANPPRAGPIVVHCSAGVGRTGTF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1822521627 1427 IALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1470
Cdd:cd14551 159 IVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
|
|
| PTPc-N22_18_12 |
cd14542 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ... |
1271-1470 |
9.08e-66 |
|
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: 221.14 E-value: 9.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSE 1349
Cdd:cd14542 1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLqFGPFKISLEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1350 E-TSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlnKNRAGLPV-VHCSAGVGRTGTLI 1427
Cdd:cd14542 81 KrVGPDFLIRTLKVTFQK--ESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVPIcVHCSAGCGRTGTIC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1822521627 1428 ALDY---LLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1470
Cdd:cd14542 157 AIDYvwnLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
|
|
| PTPc-N20_13 |
cd14538 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ... |
1271-1475 |
4.21e-65 |
|
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: 219.55 E-value: 4.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYM------PGYHldkaFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWP--MDMSSCLYGDI 1342
Cdd:cd14538 1 YINASHIripvggDTYH----YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdsLNKPLICGGRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1343 VVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlnkNRAGLPVVHCSAGVGR 1422
Cdd:cd14538 77 EVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRI---HNSGPIVVHCSAGIGR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1822521627 1423 TGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1475
Cdd:cd14538 154 TGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
|
|
| R-PTPc-U-1 |
cd14632 |
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ... |
1271-1474 |
7.35e-65 |
|
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: 218.77 E-value: 7.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDmsSCLYGDIVVNIVSEE 1350
Cdd:cd14632 1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD--SDTYGDIKITLLKTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1351 TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNrAGLPVVHCSAGVGRTGTLIALD 1430
Cdd:cd14632 79 TLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPD-AGPVVVHCSAGAGRTGCYIVLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1822521627 1431 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:cd14632 158 VMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
|
|
| R-PTP-S-2 |
cd14627 |
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ... |
1197-1477 |
3.38e-62 |
|
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: 214.60 E-value: 3.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1197 IPVSEYKSYYQR----KHADTDIGFAEEYQGLANVGTNQSKE-AFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDY 1271
Cdd:cd14627 4 VPARNLYSYIQKlaqvEVGEHVTGMELEFKRLANSKAHTSRFiSANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1272 INASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEET 1351
Cdd:cd14627 84 INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1352 SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPV-VHCSAGVGRTGTLIALD 1430
Cdd:cd14627 163 MPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPIsVHCSAGVGRTGVFITLS 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1822521627 1431 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDVTG 1477
Cdd:cd14627 243 IVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLG 289
|
|
| PTPc-N1_2 |
cd14545 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ... |
1244-1467 |
4.85e-62 |
|
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: 211.87 E-value: 4.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1244 KNRYTNIFPYDVARVKLdrqpNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNR 1323
Cdd:cd14545 3 RYRDRDPYDHDRSRVKL----KQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1324 VKCERYWPMDMSS---CLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMM 1400
Cdd:cd14545 79 IKCAQYWPQGEGNamiFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521627 1401 RDY--LNKNrAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAV--VDVYGIVHNMRMSRTCMVQTENQYIF 1467
Cdd:cd14545 159 RESgsLSSD-VGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
|
|
| PTPc-N3_4 |
cd14541 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ... |
1270-1475 |
4.99e-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: 211.03 E-value: 4.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1270 DYINASY----MPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVN 1345
Cdd:cd14541 1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1346 IVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdylnKNRAGL--P-VVHCSAGVGR 1422
Cdd:cd14541 81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVR----QNRVGMvePtVVHCSAGIGR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1822521627 1423 TGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1475
Cdd:cd14541 157 TGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
|
|
| PTPc-N12 |
cd14604 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ... |
1199-1472 |
9.15e-62 |
|
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: 213.64 E-value: 9.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1199 VSEYKSYYQRKHADTDiGFAEEYQGLANVGTNQSKEAF------QVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYI 1272
Cdd:cd14604 10 IERVQAMKSTDHNGED-NFASDFMRLRRLSTKYRTEKIyptatgEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1273 NASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSEET 1351
Cdd:cd14604 89 NANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMtFGPFRISCEAEQA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1352 SPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlnKNRAGLPV-VHCSAGVGRTGTLIALD 1430
Cdd:cd14604 169 RTDYFIRTLLLEFQN--ETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKY--QEHEDVPIcIHCSAGCGRTGAICAID 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1822521627 1431 Y---LLQ--RIEKEavVDVYGIVHNMRMSRTCMVQTENQYIFLHQCI 1472
Cdd:cd14604 245 YtwnLLKagKIPEE--FNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289
|
|
| R-PTPc-Z-1 |
cd17668 |
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ... |
1271-1473 |
1.20e-61 |
|
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: 209.83 E-value: 1.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEE 1350
Cdd:cd17668 1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE-EYGNFLVTQKSVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1351 TSPEWTTRKFNVKKT--------GCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRmMRDYLNKNRAGLPVVHCSAGVGR 1422
Cdd:cd17668 80 VLAYYTVRNFTLRNTkikkgsqkGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVR-KASYAKRHAVGPVVVHCSAGVGR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1822521627 1423 TGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1473
Cdd:cd17668 159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
|
|
| R-PTP-D-2 |
cd14628 |
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ... |
1197-1477 |
4.48e-61 |
|
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: 211.51 E-value: 4.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1197 IPVSEYKSYYQR----KHADTDIGFAEEYQGLANVGTNQSKE-AFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDY 1271
Cdd:cd14628 3 VPARNLYAYIQKltqiETGENVTGMELEFKRLASSKAHTSRFiSANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1272 INASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEET 1351
Cdd:cd14628 83 INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1352 SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPV-VHCSAGVGRTGTLIALD 1430
Cdd:cd14628 162 MPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPIsVHCSAGVGRTGVFITLS 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1822521627 1431 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDVTG 1477
Cdd:cd14628 242 IVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLG 288
|
|
| R-PTP-F-2 |
cd14629 |
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ... |
1220-1477 |
8.32e-61 |
|
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: 210.74 E-value: 8.32e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1220 EYQGLANVGTNQSKE-AFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVV 1298
Cdd:cd14629 31 EFKLLANSKAHTSRFiSANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1299 DFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHF 1378
Cdd:cd14629 111 DFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQF 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1379 TSWPDHGVPKTTDKLLQF-QRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTC 1457
Cdd:cd14629 190 TDWPEQGVPKTGEGFIDFiGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPA 269
|
250 260
....*....|....*....|
gi 1822521627 1458 MVQTENQYIFLHQCILDVTG 1477
Cdd:cd14629 270 MVQTEDQYQLCYRAALEYLG 289
|
|
| R-PTP-N |
cd14609 |
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ... |
1206-1467 |
4.74e-60 |
|
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: 207.97 E-value: 4.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1206 YQRKHADTDIGFAEEYQGL-ANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINAS-------YM 1277
Cdd:cd14609 6 YMEDHLRNRDRLAKEWQALcAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpiiehdpRM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1278 PgyhldkAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEET-SPEWT 1356
Cdd:cd14609 86 P------AYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWP-DEGSSLYHIYEVNLVSEHIwCEDFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1357 TRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLnKNRAGLPVVHCSAGVGRTGTLIALDYLLQRI 1436
Cdd:cd14609 159 VRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCY-RGRSCPIIVHCSDGAGRTGTYILIDMVLNRM 237
|
250 260 270
....*....|....*....|....*....|..
gi 1822521627 1437 EKEAV-VDVYGIVHNMRMSRTCMVQTENQYIF 1467
Cdd:cd14609 238 AKGVKeIDIAATLEHVRDQRPGMVRTKDQFEF 269
|
|
| PTPc-N11 |
cd14605 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ... |
1240-1472 |
9.46e-60 |
|
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: 206.02 E-value: 9.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1240 DNKVKNRYTNIFPYDVARVKL-DRQPNSSSSDYINASY-MPGYHLD-------KAFIAAQGPLPNTVVDFWRMVWEQKTK 1310
Cdd:cd14605 1 ENKNKNRYKNILPFDHTRVVLhDGDPNEPVSDYINANIiMPEFETKcnnskpkKSYIATQGCLQNTVNDFWRMVFQENSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1311 VIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPE-PRTITQFHFTSWPDHGVPKT 1389
Cdd:cd14605 81 VIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNtERTVWQYHFRTWPDHGVPSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1390 TDKLLQF-QRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAV---VDVYGIVHNMRMSRTCMVQTENQY 1465
Cdd:cd14605 161 PGGVLDFlEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQY 240
|
....*..
gi 1822521627 1466 IFLHQCI 1472
Cdd:cd14605 241 RFIYMAV 247
|
|
| R-PTP-C-2 |
cd14558 |
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ... |
1271-1469 |
1.73e-59 |
|
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: 203.39 E-value: 1.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSclYGDIVVNIVSEE 1350
Cdd:cd14558 1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT--YGDIEVELKDTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1351 TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLP-----VVHCSAGVGRTGT 1425
Cdd:cd14558 79 KSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKHGrsvpiVVHCSDGSSRTGI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1822521627 1426 LIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1469
Cdd:cd14558 159 FCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
|
|
| PTPc-N3 |
cd14600 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ... |
1237-1475 |
2.54e-59 |
|
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: 205.47 E-value: 2.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1237 QVPDNKVKNRYTNIFPYDVARVKLDrqpnsSSSDYINASYM----PGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVI 1312
Cdd:cd14600 36 KLPQNMDKNRYKDVLPYDATRVVLQ-----GNEDYINASYVnmeiPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1313 VMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDK 1392
Cdd:cd14600 111 VMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1393 LLQFQRMMRdylNKNRAGLPV-VHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQC 1471
Cdd:cd14600 191 FLEFVNYVR---SKRVENEPVlVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEA 267
|
....
gi 1822521627 1472 ILDV 1475
Cdd:cd14600 268 ILRV 271
|
|
| PTPc-N22 |
cd14602 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ... |
1244-1475 |
2.17e-58 |
|
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: 201.22 E-value: 2.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1244 KNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNR 1323
Cdd:cd14602 1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1324 VKCERYWP-MDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRD 1402
Cdd:cd14602 81 KKCERYWAePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS--ETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521627 1403 YlnKNRAGLPV-VHCSAGVGRTGTLIALDYLLqRIEKEAVV----DVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1475
Cdd:cd14602 159 Y--QEDDSVPIcIHCSAGCGRTGVICAIDYTW-MLLKDGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233
|
|
| PTPc-N6 |
cd14606 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ... |
1229-1473 |
1.42e-57 |
|
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: 200.49 E-value: 1.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1229 TNQSKEAfQVPDNKVKNRYTNIFPYDVARVKLD-RQPNSSSSDYINASYMPGYHL-----DKAFIAAQGPLPNTVVDFWR 1302
Cdd:cd14606 7 LHQRLEG-QRPENKSKNRYKNILPFDHSRVILQgRDSNIPGSDYINANYVKNQLLgpdenAKTYIASQGCLEATVNDFWQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1303 MVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPE-PRTITQFHFTSW 1381
Cdd:cd14606 86 MAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGElIREIWHYQYLSW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1382 PDHGVPKTTDKLLQFQrmmrDYLNKNRAGLP-----VVHCSAGVGRTGTLIALDYLLQRIEKEAV---VDVYGIVHNMRM 1453
Cdd:cd14606 166 PDHGVPSEPGGVLSFL----DQINQRQESLPhagpiIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRA 241
|
250 260
....*....|....*....|
gi 1822521627 1454 SRTCMVQTENQYIFLHQCIL 1473
Cdd:cd14606 242 QRSGMVQTEAQYKFIYVAIA 261
|
|
| PTPc-N7 |
cd14612 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ... |
1232-1469 |
2.80e-56 |
|
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: 195.82 E-value: 2.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1232 SKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSS-SSDYINASYMPGYH-LDKAFIAAQGPLPNTVVDFWRMVWEQKT 1309
Cdd:cd14612 6 SPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQEeEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEEC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1310 KVIVMLTNCVEQNRvKCERYWPMDMSSclYG--DIVVNIVSEetSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVP 1387
Cdd:cd14612 86 PIIVMITKLKEKKE-KCVHYWPEKEGT--YGrfEIRVQDMKE--CDGYTIRDLTIQLEE--ESRSVKHYWFSSWPDHQTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1388 KTTDKLLQFQRMMRDYLNKNRA-GLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYI 1466
Cdd:cd14612 159 ESAGPLLRLVAEVEESRQTAASpGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQ 238
|
...
gi 1822521627 1467 FLH 1469
Cdd:cd14612 239 FLH 241
|
|
| R-PTPc-A-E-2 |
cd14552 |
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ... |
1271-1472 |
8.25e-56 |
|
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: 192.87 E-value: 8.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDmSSCLYGDIVVNIVSEE 1350
Cdd:cd14552 1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPED-GSVSSGDITVELKDQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1351 TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALD 1430
Cdd:cd14552 80 DYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1822521627 1431 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCI 1472
Cdd:cd14552 160 TVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
|
|
| R-PTP-N2 |
cd14610 |
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ... |
1237-1467 |
1.13e-55 |
|
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: 195.66 E-value: 1.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1237 QVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINAS-YMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVML 1315
Cdd:cd14610 40 QREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVML 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1316 TNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEET-SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLL 1394
Cdd:cd14610 120 TPLAENGVKQCYHYWP-DEGSNLYHIYEVNLVSEHIwCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLL 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822521627 1395 QFQRMMrDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAV-VDVYGIVHNMRMSRTCMVQTENQYIF 1467
Cdd:cd14610 199 DFRRKV-NKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQFEF 271
|
|
| PTPc-N2 |
cd14607 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ... |
1230-1472 |
1.19e-54 |
|
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: 191.72 E-value: 1.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1230 NQSKE-AFQV---PDNKVKNRYTNIFPYDVARVKLDRQPNssssDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVW 1305
Cdd:cd14607 9 NESHDyPHRVakyPENRNRNRYRDVSPYDHSRVKLQNTEN----DYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1306 EQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLY---GDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWP 1382
Cdd:cd14607 85 QQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSfkeTGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1383 DHGVPKTTDKLLQFQRMMRDYLNKN-RAGLPVVHCSAGVGRTGTLIALDYLLQRIEKE--AVVDVYGIVHNMRMSRTCMV 1459
Cdd:cd14607 165 DFGVPESPASFLNFLFKVRESGSLSpEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKdpDSVDIKQVLLDMRKYRMGLI 244
|
250
....*....|...
gi 1822521627 1460 QTENQYIFLHQCI 1472
Cdd:cd14607 245 QTPDQLRFSYMAV 257
|
|
| PTPc-N20 |
cd14596 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ... |
1271-1475 |
1.87e-54 |
|
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: 189.19 E-value: 1.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASY--MPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIV 1347
Cdd:cd14596 1 YINASYitMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMeLENYQLRLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1348 SEETSPEWTTRKFNV--KKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKnraGLPVVHCSAGVGRTGT 1425
Cdd:cd14596 81 NYQALQYFIIRIIKLveKETG--ENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT---GPIVVHCSAGIGRAGV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1426 LIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1475
Cdd:cd14596 156 LICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
|
|
| R-PTPc-R |
cd14611 |
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ... |
1244-1470 |
1.28e-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: 187.43 E-value: 1.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1244 KNRYTNIFPYDVARVKLD-RQPNSSSSDYINASYMPGYH-LDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQ 1321
Cdd:cd14611 2 KNRYKTILPNPHSRVCLKpKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1322 NRvKCERYWPMDMSscLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQ-RMM 1400
Cdd:cd14611 82 NE-KCVLYWPEKRG--IYGKVEVLVNSVKECDNYTIRNLTLKQGS--QSRSVKHYWYTSWPDHKTPDSAQPLLQLMlDVE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1401 RDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1470
Cdd:cd14611 157 EDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
|
|
| R-PTPc-A-2 |
cd14623 |
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ... |
1246-1472 |
1.29e-53 |
|
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: 187.56 E-value: 1.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1246 RYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVK 1325
Cdd:cd14623 1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1326 CERYWPMDmSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLN 1405
Cdd:cd14623 81 CAQYWPSD-GSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521627 1406 KNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCI 1472
Cdd:cd14623 160 QSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
|
|
| PTPc-N1 |
cd14608 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ... |
1217-1483 |
1.31e-53 |
|
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: 189.47 E-value: 1.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1217 FAEEYQGLANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNssssDYINASYMPGYHLDKAFIAAQGPLPNT 1296
Cdd:cd14608 1 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDN----DYINASLIKMEEAQRSYILTQGPLPNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1297 VVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLY---GDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTI 1373
Cdd:cd14608 77 CGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIfedTNLKLTLISEDIKSYYTVRQLELENLTTQETREI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1374 TQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKN-RAGLPVVHCSAGVGRTGTLIALDYLLQRIEKE---AVVDVYGIVH 1449
Cdd:cd14608 157 LHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSpEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDIKKVLL 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 1822521627 1450 NMRMSRTCMVQTENQYIFLHQCILD----VTGDKSIDE 1483
Cdd:cd14608 237 EMRKFRMGLIQTADQLRFSYLAVIEgakfIMGDSSVQD 274
|
|
| R-PTPc-E-2 |
cd14622 |
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ... |
1270-1474 |
6.24e-53 |
|
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: 184.44 E-value: 6.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1270 DYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDmSSCLYGDIVVNIVSE 1349
Cdd:cd14622 1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSE-GSVTHGEITIEIKND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1350 ETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIAL 1429
Cdd:cd14622 80 TLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGTFIAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1822521627 1430 DYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:cd14622 160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204
|
|
| PTPc-N4 |
cd14601 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ... |
1270-1475 |
8.86e-53 |
|
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: 184.38 E-value: 8.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1270 DYINASYM----PGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVN 1345
Cdd:cd14601 1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1346 IVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdylnKNRAGLP---VVHCSAGVGR 1422
Cdd:cd14601 81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVR----NKRAGKDepvVVHCSAGIGR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1822521627 1423 TGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1475
Cdd:cd14601 157 TGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKV 209
|
|
| R-PTP-N-N2 |
cd14546 |
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ... |
1271-1472 |
1.17e-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: 1.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMpgYHLD---KAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSClYGDIVVNIV 1347
Cdd:cd14546 1 YINASTI--YDHDprnPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEV-YHIYEVHLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1348 SEET-SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMmrdyLNKNRAGLP---VVHCSAGVGRT 1423
Cdd:cd14546 78 SEHIwCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRK----VNKSYRGRScpiVVHCSDGAGRT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1424 GTLIALDYLLQRIEKEAV-VDVYGIVHNMRMSRTCMVQTENQYIFLHQCI 1472
Cdd:cd14546 154 GTYILIDMVLNRMAKGAKeIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203
|
|
| PTPc-N21_14 |
cd14540 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ... |
1271-1475 |
4.63e-51 |
|
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: 179.57 E-value: 4.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKA--FIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSC---LYGDIVVN 1345
Cdd:cd14540 1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdalTFGEYKVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1346 IVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQF--------QRMMRDYLNKNRAGLPVVHCS 1417
Cdd:cd14540 81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsvrRHTNQDVAGHNRNPPTLVHCS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521627 1418 AGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1475
Cdd:cd14540 161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
|
|
| PTP-N23 |
cd14539 |
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ... |
1271-1470 |
1.53e-50 |
|
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: 177.58 E-value: 1.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGY-HLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVS 1348
Cdd:cd14539 1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALvYGAITVSLQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1349 EETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRA-GLP-VVHCSAGVGRTGTL 1426
Cdd:cd14539 81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSlQTPiVVHCSSGVGRTGAF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1822521627 1427 IALDYLLQRIEKE-AVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1470
Cdd:cd14539 161 CLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
|
|
| PTPc-N5 |
cd14613 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ... |
1233-1469 |
5.53e-50 |
|
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: 178.13 E-value: 5.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1233 KEAFQVPDNKV------------KNRYTNIFPYDVARVKL-DRQPNSSSSDYINASYMPGY-HLDKAFIAAQGPLPNTVV 1298
Cdd:cd14613 5 AEFFEIPMNFVdpkeydipglvrKNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1299 DFWRMVWEQKTKVIVMLTNCVEQNRvKCERYWPMDmsSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHF 1378
Cdd:cd14613 85 DFWRMVWQERSPIIVMITNIEEMNE-KCTEYWPEE--QVTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1379 TSWPDHGVPKTTDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRT 1456
Cdd:cd14613 160 TSWPDQKTPDNAPPLLQLVQEVEEARQQAEPncGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRG 239
|
250
....*....|...
gi 1822521627 1457 CMVQTENQYIFLH 1469
Cdd:cd14613 240 GMIQTCEQYQFVH 252
|
|
| R-PTPc-typeIIb-2 |
cd14556 |
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ... |
1271-1470 |
1.12e-44 |
|
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: 160.65 E-value: 1.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLtNCVEQNRVKCERYWPMDMSSClYGDIVVNIVSEE 1350
Cdd:cd14556 1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGT-YGPIQVEFVSTT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1351 TSPEWTTRKFNVKKTGCPEP--RTITQFHFTSWPDHG-VPKTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLI 1427
Cdd:cd14556 79 IDEDVISRIFRLQNTTRPQEgyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRSGVFC 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1822521627 1428 ALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1470
Cdd:cd14556 159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
|
|
| COG5599 |
COG5599 |
Protein tyrosine phosphatase [Signal transduction mechanisms]; |
1229-1468 |
3.60e-43 |
|
Protein tyrosine phosphatase [Signal transduction mechanisms];
Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 159.49 E-value: 3.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1229 TNQSKEAFQVPDNKVKNRYTNIFPYDVARVkldrqpnSSSSDYINASY--MPGYHLdkaFIAAQGPLPNTVVDFWRMVWE 1306
Cdd:COG5599 30 SHNDPQYLQNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYiqVIGNHR---YIATQYPLEEQLEDFFQMLFD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1307 QKTKVIVMLTNCVE--QNRVKCERYWPMDMSsclYGDIVVNIVSEET---SPEWTTRKFNVKKTGC-PEPRTITQFHFTS 1380
Cdd:COG5599 100 NNTPVLVVLASDDEisKPKVKMPVYFRQDGE---YGKYEVSSELTESiqlRDGIEARTYVLTIKGTgQKKIEIPVLHVKN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1381 WPDHGVPkTTDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTLIALDYLLQRI--EKEAVVDVYGIVHNMRMSRT 1456
Cdd:COG5599 177 WPDHGAI-SAEALKNLADLIDKKEKIKDPdkLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRN 255
|
250
....*....|...
gi 1822521627 1457 C-MVQTENQYIFL 1468
Cdd:COG5599 256 GgMVQTSEQLDVL 268
|
|
| PTPc_plant_PTP1 |
cd17658 |
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ... |
1271-1467 |
1.90e-42 |
|
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: 154.54 E-value: 1.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYM--PGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNR-VKCERYWPM-DMSSCLYGDIVVNI 1346
Cdd:cd17658 1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAeENESREFGRISVTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1347 VSEETSPE-WTTRKFNVKKTGCPE-PRTITQFHFTSWPDHGVPKTTDKLLQFQRmmRDYLNKNRAGLPVVHCSAGVGRTG 1424
Cdd:cd17658 81 KKLKHSQHsITLRVLEVQYIESEEpPLSVLHIQYPEWPDHGVPKDTRSVRELLK--RLYGIPPSAGPIVVHCSAGIGRTG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1822521627 1425 TLIALDYLLQRIEKEAV--VDVYGIVHNMRMSRTCMVQTENQYIF 1467
Cdd:cd17658 159 AYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIF 203
|
|
| PTPc-N14 |
cd14599 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ... |
1238-1473 |
2.53e-42 |
|
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: 157.08 E-value: 2.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1238 VPDNKVKNRYTNIFPYDVARVKLdrQPN-SSSSDYINASYMP------GYHldkaFIAAQGPLPNTVVDFWRMVWEQKTK 1310
Cdd:cd14599 35 LPENAERNRIREVVPYEENRVEL--VPTkENNTGYINASHIKvtvggeEWH----YIATQGPLPHTCHDFWQMVWEQGVN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1311 VIVMLTNCVEQNRVKCERYWP---MDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVP 1387
Cdd:cd14599 109 VIAMVTAEEEGGRSKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1388 KTTDKLLQFQ---RMMRDYLN------KNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCM 1458
Cdd:cd14599 189 EEVQGFLSYLeeiQSVRRHTNsmldstKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFM 268
|
250
....*....|....*
gi 1822521627 1459 VQTENQYIFLHQCIL 1473
Cdd:cd14599 269 IQTIAQYKFVYQVLI 283
|
|
| PHA02738 |
PHA02738 |
hypothetical protein; Provisional |
1241-1497 |
6.93e-42 |
|
hypothetical protein; Provisional
Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 157.01 E-value: 6.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1241 NKVKNRYTNIFPYDVARVKLDRQPNSSssDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1320
Cdd:PHA02738 49 NRKLNRYLDAVCFDHSRVILPAERNRG--DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1321 QNRVKCERYWP-MDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKtGCPEPRTITQFHFTSWPDHGVPKTTDKLLQF--- 1396
Cdd:PHA02738 127 NGREKCFPYWSdVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFvle 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1397 ----QRMM---RDYLNKNRAGLP--VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIF 1467
Cdd:PHA02738 206 vrqcQKELaqeSLQIGHNRLQPPpiVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFF 285
|
250 260 270
....*....|....*....|....*....|...
gi 1822521627 1468 LHQCI---LDVTGDKSIDEPIYENQADLIYENV 1497
Cdd:PHA02738 286 CYRAVkryVNLTVNKVSKKLIPNVQTVSFNKNL 318
|
|
| PHA02747 |
PHA02747 |
protein tyrosine phosphatase; Provisional |
1220-1504 |
4.91e-41 |
|
protein tyrosine phosphatase; Provisional
Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 154.39 E-value: 4.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1220 EYQGLANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQpNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVD 1299
Cdd:PHA02747 30 EHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSG-GGSTSDYIHANWIDGFEDDKKFIATQGPFAETCAD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1300 FWRMVWEQKTKVIVMLTNCVEQN-RVKCERYW-PMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFH 1377
Cdd:PHA02747 109 FWKAVWQEHCSIIVMLTPTKGTNgEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1378 FTSWPDHGVPKTTDKLLQF--------QRMMRDYLNKNRAGLP-VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIV 1448
Cdd:PHA02747 189 CSEWFEDETPSDHPDFIKFikiidinrKKSGKLFNPKDALLCPiVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTA 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521627 1449 HNMRMSRTCMVQTENQYIFLhqcildvtgdksidEPIYENQADLIYENVDAIKVAN 1504
Cdd:PHA02747 269 EKIREQRHAGIMNFDDYLFI--------------QPGYEVLHYFLSKIKAIDKIKF 310
|
|
| PTPc_motif |
smart00404 |
Protein tyrosine phosphatase, catalytic domain motif; |
1372-1474 |
3.46e-40 |
|
Protein tyrosine phosphatase, catalytic domain motif;
Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 144.04 E-value: 3.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1372 TITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLP-VVHCSAGVGRTGTLIALDYLLQRIEKEA-VVDVYGIVH 1449
Cdd:smart00404 1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPvVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80
|
90 100
....*....|....*....|....*
gi 1822521627 1450 NMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:smart00404 81 ELRSQRPGMVQTEEQYLFLYRALLE 105
|
|
| PTPc_DSPc |
smart00012 |
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ... |
1372-1474 |
3.46e-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: 144.04 E-value: 3.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1372 TITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLP-VVHCSAGVGRTGTLIALDYLLQRIEKEA-VVDVYGIVH 1449
Cdd:smart00012 1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPvVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80
|
90 100
....*....|....*....|....*
gi 1822521627 1450 NMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:smart00012 81 ELRSQRPGMVQTEEQYLFLYRALLE 105
|
|
| PHA02742 |
PHA02742 |
protein tyrosine phosphatase; Provisional |
1241-1473 |
8.78e-38 |
|
protein tyrosine phosphatase; Provisional
Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 144.37 E-value: 8.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1241 NKVKNRYTNIFPYDVARVKLDRQpnSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1320
Cdd:PHA02742 52 NMKKCRYPDAPCFDRNRVILKIE--DGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1321 QNRVKCERYW-PMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRM 1399
Cdd:PHA02742 130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1400 MR--------DYLNKNRAGLP--VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1469
Cdd:PHA02742 210 VReadlkadvDIKGENIVKEPpiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289
|
....
gi 1822521627 1470 QCIL 1473
Cdd:PHA02742 290 FIVL 293
|
|
| R-PTPc-T-2 |
cd14634 |
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ... |
1271-1474 |
2.06e-36 |
|
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: 137.07 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTncvEQNRVK-CERYWPmDMSSCLYGDIVVNIVSE 1349
Cdd:cd14634 1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDAAQlCMQYWP-EKTSCCYGPIQVEFVSA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1350 ETSPEWTTRKFNVKKTGCPEP--RTITQFHFTSWPDH-GVPKTTDKLLQFQRMMRDYLNK--NRAGLPVVHCSAGVGRTG 1424
Cdd:cd14634 77 DIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydGREGRTVVHCLNGGGRSG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1425 TLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:cd14634 157 TFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
|
|
| PTPc-N21 |
cd14598 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ... |
1271-1473 |
7.95e-35 |
|
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: 133.18 E-value: 7.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMP----GYHLDkaFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMS---SCLYGDIV 1343
Cdd:cd14598 1 YINASHIKvtvgGKEWD--YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSrhnTVTYGRFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1344 VNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQF-------QRMMRDYLNKNRAGLPV-VH 1415
Cdd:cd14598 79 ITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsvRRHTNSTIDPKSPNPPVlVH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521627 1416 CSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1473
Cdd:cd14598 159 CSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLI 216
|
|
| PHA02746 |
PHA02746 |
protein tyrosine phosphatase; Provisional |
1239-1472 |
3.49e-34 |
|
protein tyrosine phosphatase; Provisional
Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 134.77 E-value: 3.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1239 PDNKVKNRYTNIFPYDVARVKL------------DRQPN-------SSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVD 1299
Cdd:PHA02746 49 KENLKKNRFHDIPCWDHSRVVInaheslkmfdvgDSDGKkievtseDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1300 FWRMVWEQKTKVIVMLTNcVEQNRVKCERYWPMDMSSCL-YGDIVVNI--VSEETSpeWTTRKFNVKKTGCPEPRTITQF 1376
Cdd:PHA02746 129 FFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSELaFGRFVAKIldIIEELS--FTKTRLMITDKISDTSREIHHF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1377 HFTSWPDHGVPKTTDKLLQF--------QRMMRDYLNKNRAGLP-VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGI 1447
Cdd:PHA02746 206 WFPDWPDNGIPTGMAEFLELinkvneeqAELIKQADNDPQTLGPiVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285
|
250 260
....*....|....*....|....*
gi 1822521627 1448 VHNMRMSRTCMVQTENQYIFLHQCI 1472
Cdd:PHA02746 286 VLKIRKQRHSSVFLPEQYAFCYKAL 310
|
|
| R-PTPc-U-2 |
cd14637 |
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ... |
1271-1474 |
2.66e-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: 113.85 E-value: 2.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV-KCERYWPmDMSSCLYGDIVVNIVSE 1349
Cdd:cd14637 1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP-EPGLQQYGPMEVEFVSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1350 ETSPEWTTRKFNVKKTG--CPEPRTITQFHFTSW-PDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTL 1426
Cdd:cd14637 80 SADEDIVTRLFRVQNITrlQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1822521627 1427 IALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:cd14637 160 CASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
|
|
| R-PTPc-M-2 |
cd14635 |
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ... |
1271-1474 |
7.25e-28 |
|
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: 112.47 E-value: 7.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLtNCVEQNRVkCERYWPmDMSSCLYGDIVVNIVSEE 1350
Cdd:cd14635 1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVML-NDVDPAQL-CPQYWP-ENGVHRHGPIQVEFVSAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1351 TSPEWTTRKFNVKKTGCPEP--RTITQFHFTSWPDH-GVPKTTDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGT 1425
Cdd:cd14635 78 LEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGgeGRTVVHCLNGGGRSGT 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1822521627 1426 LIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:cd14635 158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
|
|
| R5-PTP-2 |
cd14550 |
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ... |
1271-1470 |
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: 112.03 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCveQNRVKCERYWPMDMSSCLYGDIVVNIVSEE 1350
Cdd:cd14550 1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN--ELNEDEPIYWPTKEKPLECETFKVTLSGED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1351 TSPEW-----TTRKFNVKKTGCPEPRTITQFHFTSWPDHGVP-KTTDKLLQ-FQRmmrdyLNKNRAGLPVVHCSAGVGRT 1423
Cdd:cd14550 79 HSCLSneirlIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPiHTVFELINtVQE-----WAQQRDGPIVVHDRYGGVQA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1822521627 1424 GTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1470
Cdd:cd14550 154 ATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
|
|
| R-PTPc-K-2 |
cd14636 |
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ... |
1271-1474 |
2.76e-26 |
|
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: 108.19 E-value: 2.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTncvEQNRVK-CERYWPmDMSSCLYGDIVVNIVSE 1349
Cdd:cd14636 1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN---EVDLAQgCPQYWP-EEGMLRYGPIQVECMSC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1350 ETSPEWTTRKFNVKKTGCPEP--RTITQFHFTSWPDH-GVPKTTDKLLQFQRMMRDYLNK--NRAGLPVVHCSAGVGRTG 1424
Cdd:cd14636 77 SMDCDVISRIFRICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEEcdEGEGRTIIHCLNGGGRSG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1425 TLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1474
Cdd:cd14636 157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
|
|
| R-PTP-Z-2 |
cd17669 |
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ... |
1271-1473 |
9.08e-24 |
|
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: 100.84 E-value: 9.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNcvEQNRVKCE-RYWPMDMSSCLYGDIVVNIVSE 1349
Cdd:cd17669 1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPD--GQNMAEDEfVYWPNKDEPINCETFKVTLIAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1350 E-----TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPktTDKLLQFQRMMRDYlNKNRAGLPVVHCSAGVGRTG 1424
Cdd:cd17669 79 EhkclsNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSP--ISKTFELISIIKEE-AANRDGPMIVHDEHGGVTAG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1822521627 1425 TLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1473
Cdd:cd17669 156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
|
|
| R-PTP-G-2 |
cd17670 |
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ... |
1271-1473 |
1.34e-23 |
|
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: 100.14 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1271 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNcvEQNRVKCER-YWPMDMSSCLYGDIVVNIVSE 1349
Cdd:cd17670 1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEFvYWPSREESMNCEAFTVTLISK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1350 E-----TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTD----KLLQFQRMMRDylnknraGLPVVHCSAGV 1420
Cdd:cd17670 79 DrlclsNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTfeliNVIKEEALTRD-------GPTIVHDEFGA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1822521627 1421 GRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1473
Cdd:cd17670 152 VSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
|
|
| PTP_YopH-like |
cd14559 |
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ... |
1245-1465 |
9.59e-20 |
|
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: 89.77 E-value: 9.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1245 NRYTNIfpydVARVKLDRQPNssssdyINASYMP--GYHLdkaFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQN 1322
Cdd:cd14559 1 NRFTNI----QTRVSTPVGKN------LNANRVQigNKNV---AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1323 RVKCERYWPMdmsSCLYGDIVVNivSEETSPEWTTRKFNVK----KTGCPEPR-TITQFHFTSWPDHG------------ 1385
Cdd:cd14559 68 RKGLPPYFRQ---SGTYGSVTVK--SKKTGKDELVDGLKADmynlKITDGNKTiTIPVVHVTNWPDHTaisseglkelad 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1386 -VPKTTDKLLQF--QRMMRDYLNKNRaGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDvygIVHNMRMSRTC-MVQT 1461
Cdd:cd14559 143 lVNKSAEEKRNFykSKGSSAINDKNK-LLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVED---IVSDMRTSRNGkMVQK 218
|
....
gi 1822521627 1462 ENQY 1465
Cdd:cd14559 219 DEQL 222
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
200-744 |
1.08e-15 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 82.36 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 200 SVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTESLRIKWT-RPTDTRASDYTYRVTVTNVTGGVSWTESTSKDKTTFTA 278
Cdd:COG3401 30 GGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGgRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 279 TGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSS 358
Cdd:COG3401 110 GLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 359 TTVTSRGETTFKATGLQpgdqYLLSVQSVTPEDTWSTPVEVT-NTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYT 437
Cdd:COG3401 190 TTLVDGGGDIEPGTTYY----YRVAATDTGGESAPSNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 438 YKVTVTnvaGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEV----TSTTNPSPVTGLSVVNGTTQS 513
Cdd:COG3401 266 VYRSNS---GDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSS 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 514 LTIEWTSPNDTTASNyiYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVT---PEDTLSTPEQVTNTTN 590
Cdd:COG3401 343 ITLSWTASSDADVTG--YNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDaagNESAPSEEVSATTASA 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 591 PSPVTGLSVVNGTTQSLGIEWT-------SPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSV 663
Cdd:COG3401 421 ASGESLTASVDAVPLTDVAGATaaasaasNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGS 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 664 QSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGT--------TQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTS 735
Cdd:COG3401 501 GASSVTNSVSVIGASAAAAVGGAPDGTPNVTGAspvtvgasTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGS 580
|
....*....
gi 1822521627 736 KDETTFTAT 744
Cdd:COG3401 581 LLTTTSTNT 589
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
572-1031 |
2.67e-15 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 81.20 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 572 SVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTAT 651
Cdd:COG3401 30 GGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 652 GLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWT 731
Cdd:COG3401 110 GLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 732 QSTSKDETtftatRLQPGDQYLLSVQSVTPEDTLSTPAQV---TSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNY 808
Cdd:COG3401 190 TTLVDGGG-----DIEPGTTYYYRVAATDTGGESAPSNEVsvtTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 809 T-YRVTvtnvTGGVSWSKSTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVKSTT----DPSPVTGLSVVNSTT 883
Cdd:COG3401 265 RvYRSN----SGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTtdltPPAAPSGLTATAVGS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 884 QSLRIEWTTPNNIRASNYtyNVTVTNVTDGASSTTITSKGETTFTVTGLQPGDQYRLSVRSVT---PEDTWSTPAQVTST 960
Cdd:COG3401 341 SSITLSWTASSDADVTGY--NVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDaagNESAPSEEVSATTA 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521627 961 SNPSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAIDTGPGVTTFTVTNLVPGVEY 1031
Cdd:COG3401 419 SAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANL 489
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
479-1033 |
1.66e-14 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 78.51 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 479 SVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTAT 558
Cdd:COG3401 30 GGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 559 GLQPGDQYQ-LSVQSVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRS 637
Cdd:COG3401 110 GLTSSDEVPsPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 638 TTVTSKGETAFTATGLQpgdqYQLSVQSVTPEGTLSTPVEVT-STTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYt 716
Cdd:COG3401 190 TTLVDGGGDIEPGTTYY----YRVAATDTGGESAPSNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGY- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 717 yNVTVTNVTGGvSWTQSTSKDETTFTATRLQPGDQYLLSVQSVTPEDTLSTPAQV----TSTTNPSPVTGLSVVNGTTQS 792
Cdd:COG3401 265 -RVYRSNSGDG-PFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSS 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 793 LTIEWTRPTDTRASNYT-YRVTvtnvTGGVSWSK-STSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVKSTTDP 870
Cdd:COG3401 343 ITLSWTASSDADVTGYNvYRST----SGGGTYTKiAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 871 SPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSKGETTFTVTGLQPGDQYRLSVRSVTPEDT 950
Cdd:COG3401 419 SAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVG 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 951 WSTPAQVTSTSNPSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAIDTGPGVTTFTVTNLVPGVE 1030
Cdd:COG3401 499 GSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLG 578
|
...
gi 1822521627 1031 YEL 1033
Cdd:COG3401 579 GSL 581
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
59-651 |
3.99e-13 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 74.27 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 59 TRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTPEDTLSTPVEVTSTTNPSPVIGLSVVNGT 138
Cdd:COG3401 12 GIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 139 TQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTATGLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTN 218
Cdd:COG3401 92 TGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 219 PSPVTGLSVVNGTTESLRI--KWTRPTDTRASDYTYRVTVTNVTGGVSWTESTSKdkttftatglqpgdqyqlsvqsvtp 296
Cdd:COG3401 172 PDTSATAAVATTSLTVTSTtlVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSV------------------------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 297 edtvsspleVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNytYIVTVTNVTGGvSSTTVTSRGETTFKATGLQP 376
Cdd:COG3401 227 ---------TTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATG--YRVYRSNSGDG-PFTKVATVTTTSYTDTGLTN 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 377 GDQYLLSVQSVTPEDTWSTPVEV----TNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNytYKVTVTNVAGGVSST 452
Cdd:COG3401 295 GTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTG--YNVYRSTSGGGTYTK 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 453 TITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLS-------VVNGTTQSLTIEWTSPNDTT 525
Cdd:COG3401 373 IAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESltasvdaVPLTDVAGATAAASAASNPG 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 526 ASNYIYNVTVTNVTGGVSWTESTSKGETT---------FTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTG 596
Cdd:COG3401 453 VSAAVLADGGDTGNAVPFTTTSSTVTATTtdtttanlsVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTG 532
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521627 597 LSVVNGT--TQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTAT 651
Cdd:COG3401 533 ASPVTVGasTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNT 589
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
34-558 |
1.31e-12 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 72.34 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 34 SPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTPEDT 113
Cdd:COG3401 82 VAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTAS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 114 LSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGgvswtkstnkdkttftatglqpgdq 193
Cdd:COG3401 162 SVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGG------------------------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 194 yqlsvrsvtpEDTLSTPVEVT-NTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYT-YRVTvtnvTGGVSWTESTSK 271
Cdd:COG3401 217 ----------ESAPSNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYRvYRSN----SGDGPFTKVATV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 272 DKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEV----TNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNytYIV 347
Cdd:COG3401 283 TTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTG--YNV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 348 TVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVT---PEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIE 424
Cdd:COG3401 361 YRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAG 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 425 WT-------PPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTN 497
Cdd:COG3401 441 ATaaasaasNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAV 520
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1822521627 498 PSPVTGLSVVNGT--------TQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTAT 558
Cdd:COG3401 521 GGAPDGTPNVTGAspvtvgasTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNT 589
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
604-1081 |
9.03e-11 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 66.56 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 604 TQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTN 683
Cdd:COG3401 1 TGSSYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 684 PSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYLLSVQSVTPED 763
Cdd:COG3401 81 AVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 764 TLSTPAQVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSKSTSKgettftatglqpgd 843
Cdd:COG3401 161 SSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSV-------------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 844 qyqlsvqsvtpedtlstpveVKSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNytYNVTVTNVTDGaSSTTITSKG 923
Cdd:COG3401 227 --------------------TTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATG--YRVYRSNSGDG-PFTKVATVT 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 924 ETTFTVTGLQPGDQYRLSVRSVTPEDTWSTPAQV----TSTSNPSPVSGLTVVNRTTVSIEVTWAAPTDARApeYTYRIT 999
Cdd:COG3401 284 TTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADV--TGYNVY 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1000 LANVTRRGRGAIDTGPGVTTFTVTNLVPGVEYELRLQSVTPAGTRSSPETVRNATIPAAISDFRCSGSTGYMVEAKWSQP 1079
Cdd:COG3401 362 RSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGA 441
|
..
gi 1822521627 1080 NG 1081
Cdd:COG3401 442 TA 443
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
27-368 |
5.89e-10 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 63.87 E-value: 5.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 27 SQNVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTvTNVAGGVSSITTTgkNETTFTATGLQPGDQYLLSVR 106
Cdd:COG3401 227 TTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYRVYRS-NSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 107 SVTPEDTLSTPVEV----TSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNytYIVTVTNVTGGVSWTKSTNKDKTT 182
Cdd:COG3401 304 AVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTG--YNVYRSTSGGGTYTKIAETVTTTS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 183 FTATGLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTEslrikWTRPTDTRASDYTYRVTVTNVTGG 262
Cdd:COG3401 382 YTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDA-----VPLTDVAGATAAASAASNPGVSAA 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 263 VSWTESTSKDKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTiewtrPTDTRATN 342
Cdd:COG3401 457 VLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGA-----PDGTPNVT 531
|
330 340
....*....|....*....|....*.
gi 1822521627 343 YTYIVTVTNVTGGVSSTTVTSRGETT 368
Cdd:COG3401 532 GASPVTVGASTGDVLITDLVSLTTSA 557
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
29-906 |
1.04e-09 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 63.63 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 29 NVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSV 108
Cdd:COG3210 820 TITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 109 TPEDTLSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTATGL 188
Cdd:COG3210 900 GTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGT 979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 189 QPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVT-GLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWTE 267
Cdd:COG3210 980 SANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAiVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISGGNAA 1059
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 268 STSKDKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIV 347
Cdd:COG3210 1060 ALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEA 1139
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 348 TVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTP 427
Cdd:COG3210 1140 AGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTT 1219
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 428 PTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVV 507
Cdd:COG3210 1220 TTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGATATGSTVDIGSTSATSAGGS 1299
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 508 NGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTN 587
Cdd:COG3210 1300 LDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNGATDSAAGAGSGGAAGSLAATAG 1379
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 588 TTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSVT 667
Cdd:COG3210 1380 AGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNTTGTSVAGAGGGNADASAIN 1459
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 668 PEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSKDETTFTATRLQ 747
Cdd:COG3210 1460 TGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAEVAKASLEGGEGTYGGSSVAEA 1539
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 748 PGDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSKST 827
Cdd:COG3210 1540 GTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNTATLTLSLAEGTNAEYGGTTNVTSGT 1619
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1822521627 828 SKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVT 906
Cdd:COG3210 1620 AGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVDLTDATLAGLGGATTAAAGNVATGDTAP 1698
|
|
| COG4733 |
COG4733 |
Phage-related protein, tail protein J [Mobilome: prophages, transposons]; |
275-784 |
2.08e-09 |
|
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 62.27 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 275 TFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSpvtgLSVVNGTT--QSLTIEWTRPTDtrATNYTYIVTVtnv 352
Cdd:COG4733 503 TYTITAVQHAPEKYAAIDAGAFDDVPPQWPPVNVTTSES----LSVVAQGTavTTLTVSWDAPAG--AVAYEVEWRR--- 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 353 tGGVSSTTVTSRGETTFKATGLQPGDqYLLSVQSVTPEDT---WSTPVEVT---NTTNPSPVTGLTVVNGTTHsLRIEWT 426
Cdd:COG4733 574 -DDGNWVSVPRTSGTSFEVPGIYAGD-YEVRVRAINALGVssaWAASSETTvtgKTAPPPAPTGLTATGGLGG-ITLSWS 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 427 PPTDTRATnyTYKVTVTNVAGGVSSTTITNKGET-AFTATGLQPGDQYQLSVQSVtpeDTL--STPVEVTSTTNPSPVTG 503
Cdd:COG4733 651 FPVDADTL--RTEIRYSTTGDWASATVAQALYPGnTYTLAGLKAGQTYYYRARAV---DRSgnVSAWWVSGQASADAAGI 725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 504 LSVVNGttQSLTIEWTSPNDTTASNyiynvtvtnvtggvswteSTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPE 583
Cdd:COG4733 726 LDAITG--QILETELGQELDAIIQN------------------ATVAEVVAATVTDVTAQIDTAVLFAGVATAAAIGAEA 785
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 584 QVTNTTNpSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSV 663
Cdd:COG4733 786 RVAATVA-ESATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAASTTRVAAAVVLAGVVVYGDAIIESGNTGDIVATG 864
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 664 QSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEwtrptdTRASNYTYNVTVTNVTGGVSWTQSTSKdETTFTA 743
Cdd:COG4733 865 DIASAAAGAVATTVSGTTAADVSAVADSTAASLTAIVIAA------TTIIDAIGDGTTREPAGDIGASGGAQG-FAVTIV 937
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1822521627 744 TRLQPGDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLS 784
Cdd:COG4733 938 GSFDGAGAVATVDAGQSVVDGVGTAVEAANGTETAAGGGSQ 978
|
|
| PHA02740 |
PHA02740 |
protein tyrosine phosphatase; Provisional |
1219-1472 |
2.22e-09 |
|
protein tyrosine phosphatase; Provisional
Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 60.37 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1219 EEYQGLANVGTNQSKEAFQVPDNKVK--NRYTNIFPYDVARVKLdrqpnSSSSDYINASYMPGYHLDKAFIAAQGPLPNT 1296
Cdd:PHA02740 29 KEYRAIVPEHEDEANKACAQAENKAKdeNLALHITRLLHRRIKL-----FNDEKVLDARFVDGYDFEQKFICIINLCEDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1297 VVDFWRMVWEQKTKVIVMLTNCVEQNRVkcERYWPMDmSSCLygdIVVNIVSEETSPEWTTRKFNVK------KTGcpEP 1370
Cdd:PHA02740 104 CDKFLQALSDNKVQIIVLISRHADKKCF--NQFWSLK-EGCV---ITSDKFQIETLEIIIKPHFNLTllsltdKFG--QA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1371 RTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDY---LNKNRA----GLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVD 1443
Cdd:PHA02740 176 QKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLcadLEKHKAdgkiAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLS 255
|
250 260
....*....|....*....|....*....
gi 1822521627 1444 VYGIVHNMRMSRTCMVQTENQYIFLHQCI 1472
Cdd:PHA02740 256 IANALKKVRQKKYGCMNCLDDYVFCYHLI 284
|
|
| COG4733 |
COG4733 |
Phage-related protein, tail protein J [Mobilome: prophages, transposons]; |
636-1024 |
2.36e-09 |
|
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 62.27 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 636 RSTTVTSKGETAFTATGLQpgdqYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTT--QSLTIEWTRPTDtrAS 713
Cdd:COG4733 492 RVVSIEENEDGTYTITAVQ----HAPEKYAAIDAGAFDDVPPQWPPVNVTTSESLSVVAQGTavTTLTVSWDAPAG--AV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 714 NYTYNVTVtnvtGGVSWTQSTSKDETTFTATRLQPGDqYLLSVQSVTPEDTLSTPAQVTSTT------NPSPVTGLSVVN 787
Cdd:COG4733 566 AYEVEWRR----DDGNWVSVPRTSGTSFEVPGIYAGD-YEVRVRAINALGVSSAWAASSETTvtgktaPPPAPTGLTATG 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 788 GTTQsLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSKSTSKGeTTFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVKST 867
Cdd:COG4733 641 GLGG-ITLSWSFPVDADTLRTEIRYSTTGDWASATVAQALYPG-NTYTLAGLKAGQTYYYRARAVDRSGNVSAWWVSGQA 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 868 TDPspvtglsvVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSKGETTFTVTGLQPGDQYRLSVRSVTP 947
Cdd:COG4733 719 SAD--------AAGILDAITGQILETELGQELDAIIQNATVAEVVAATVTDVTAQIDTAVLFAGVATAAAIGAEARVAAT 790
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521627 948 EDTWSTPAQVTSTSNPSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRG-RGAIDTGPGVTTFTVTN 1024
Cdd:COG4733 791 VAESATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAASTTRVAAAVVLAGVVVYGDAiIESGNTGDIVATGDIAS 868
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
498-574 |
5.02e-09 |
|
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: 54.54 E-value: 5.02e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521627 498 PSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTE-STSKGETTFTATGLQPGDQYQLSVQSVT 574
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
220-295 |
6.03e-09 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 54.34 E-value: 6.03e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521627 220 SPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWTEST-SKDKTTFTATGLQPGDQYQLSVQSVT 295
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
219-295 |
1.84e-08 |
|
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: 53.00 E-value: 1.84e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521627 219 PSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWTE-STSKDKTTFTATGLQPGDQYQLSVQSVT 295
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
30-501 |
1.93e-08 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 58.86 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 30 VTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVT 109
Cdd:COG3401 149 GVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 110 PEDTLSTPVEVTSTTNPSPVIGLSvvngttqslwieWTSPTDTRATNytYIVTVTNVTGGvSWTKSTNKDKTTFTATGLQ 189
Cdd:COG3401 229 PTTPPSAPTGLTATADTPGSVTLS------------WDPVTESDATG--YRVYRSNSGDG-PFTKVATVTTTSYTDTGLT 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 190 PGDQYQLSVRSVTPEDTLSTPVEV----TNTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASdyTYRVTVTNVTGGVSW 265
Cdd:COG3401 294 NGTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVT--GYNVYRSTSGGGTYT 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 266 TESTSKDKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTqsltiEWTRPTDTRATNYTY 345
Cdd:COG3401 372 KIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVD-----AVPLTDVAGATAAAS 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 346 IVTVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEW 425
Cdd:COG3401 447 AASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDG 526
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521627 426 TPPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPV 501
Cdd:COG3401 527 TPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGVHGGTLLV 602
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
777-853 |
2.22e-08 |
|
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: 52.62 E-value: 2.22e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521627 777 PSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSK-STSKGETTFTATGLQPGDQYQLSVQSVT 853
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
964-1042 |
5.07e-08 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 51.65 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 964 SPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGA-IDTGPGVTTFTVTNLVPGVEYELRLQSVTPAG 1042
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
405-481 |
5.40e-08 |
|
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: 51.46 E-value: 5.40e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521627 405 PSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKG-ETAFTATGLQPGDQYQLSVQSVT 481
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPsSTSYTLTGLKPGTEYEFRVRAVN 78
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
126-202 |
6.07e-08 |
|
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: 51.46 E-value: 6.07e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521627 126 PSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTK-STNKDKTTFTATGLQPGDQYQLSVRSVT 202
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
963-1051 |
6.92e-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: 51.73 E-value: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 963 PSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAIDTGPG-VTTFTVTNLVPGVEYELRLQSVTPA 1041
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGsETSYTLTGLKPGTEYEFRVRAVNGG 80
|
90
....*....|..
gi 1822521627 1042 GT--RSSPETVR 1051
Cdd:cd00063 81 GEspPSESVTVT 92
|
|
| RhsA |
COG3209 |
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ... |
135-904 |
7.46e-08 |
|
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only];
Pssm-ID: 442442 [Multi-domain] Cd Length: 1103 Bit Score: 57.46 E-value: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 135 VNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTATGLQPGDQYQLSVRSVTPEDTLSTPVEVT 214
Cdd:COG3209 1 ETSLGLVGGTTGASSTLLAATNAGGGTAVTNAGSTVLLAKGGLSTAAAAGGAATLTARSASTTDVVGTLTGAGGTSAGGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 215 NTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWTESTSKDKTTFTATGlqpGDQYQLSVQSV 294
Cdd:COG3209 81 TALGDASAAGGGYVGGAAAGGGATLTGLAAATASAGRLVSTGAGAGGTVTAATGGTLGATAGSATT---GSTDGGRGGVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 295 TPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSSTTVTSRGETTFKATGL 374
Cdd:COG3209 158 VTGLAGGGASAYGLTLGGAAAGPATGVGTGAVTLATGLAGSALLALGSGAILGGLAGAYSGSATTATGTALGTPASVAAT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 375 QPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTI 454
Cdd:COG3209 238 VTGSATGAAGAGAAVATAATTLGGTTGAGTGASGAGLDASTGTGGAGGSNAAATAGGLGGAGLGSGGAGGGGTAGGTTTA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 455 TNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVT 534
Cdd:COG3209 318 AGTTGTAAVSGAADAGTTTTTGTGTGGTTTTVGGGGSLTLGGYGAAGGLTTSVGAGGGGSTSGSTTTVGGGGTATGSGGG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 535 VTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTTQSLGIEWTSP 614
Cdd:COG3209 398 SSTTGVGAGTTTTSTTGGDGGPATAAGALTAGGTATGTGTGGGGTTAGTDATTTTGGAGASGTLTTTGGAATGATTGGGT 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 615 TDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVN 694
Cdd:COG3209 478 EAGTGGGTLTSGSAGATTLGTDTTLDDTLGGTTTTTAGARGLVVTTGTTLTLGTTTTATLSATDATGTGDTTTTGTVGTG 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 695 GTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYLLSVQSVTPEDTLSTPAQVTST 774
Cdd:COG3209 558 TSTGTGGTGTVTTTGDGTGGASTTTGTTGGTATTTTVTTTTTTSTAGTTTTTTSGYTRAGLTLTLGTGTASGLERATAST 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 775 TNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSKSTSKGETTFTATGLQPGDQYQLSVQSVTP 854
Cdd:COG3209 638 GSTTGGTTGTGVTTTGTTTTRATGTTGTGTGVTAGLTTLATGGTTVGGGTGTTSTATTGATTGGTETGTTVTTLAGGTTT 717
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1822521627 855 EDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSlrieWTTPNNIRASNYTYN 904
Cdd:COG3209 718 RLGTTTTGGGGGTTTDGTGTGGTTGTLTTTS----TTTTTTAGALTYTYD 763
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
963-1042 |
7.75e-08 |
|
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: 51.08 E-value: 7.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 963 PSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGA-IDTGPGVTTFTVTNLVPGVEYELRLQSVTPA 1041
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKeVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80
|
.
gi 1822521627 1042 G 1042
Cdd:smart00060 81 G 81
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
871-946 |
9.11e-08 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 50.88 E-value: 9.11e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521627 871 SPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTIT-SKGETTFTVTGLQPGDQYRLSVRSVT 946
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77
|
|
| CDC14 |
COG2453 |
Protein-tyrosine phosphatase [Signal transduction mechanisms]; |
1369-1470 |
9.97e-08 |
|
Protein-tyrosine phosphatase [Signal transduction mechanisms];
Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 52.67 E-value: 9.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1369 EPRTITQFHFTsWPDHGVPKTTdkllQFQRMMRDYLNKNRAGLPV-VHCSAGVGRTGTLIALdYLLQR-IE-KEAVVDVy 1445
Cdd:COG2453 44 EEAGLEYLHLP-IPDFGAPDDE----QLQEAVDFIDEALREGKKVlVHCRGGIGRTGTVAAA-YLVLLgLSaEEALARV- 116
|
90 100
....*....|....*....|....*
gi 1822521627 1446 givhnmRMSRTCMVQTENQYIFLHQ 1470
Cdd:COG2453 117 ------RAARPGAVETPAQRAFLER 135
|
|
| PTP_DSP_cys |
cd14494 |
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ... |
1393-1470 |
1.03e-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: 51.58 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1393 LLQFQRMMRDYLNKNRAGLPV-VHCSAGVGRTGTLIALDYLLQRIEkeavvDVYGIVHNMRMSRT-CMVQTENQYIFLHQ 1470
Cdd:cd14494 39 LAMVDRFLEVLDQAEKPGEPVlVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRPgGIPQTIEQLDFLIK 113
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
33-124 |
1.05e-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: 50.96 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 33 PSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNV-AGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTpE 111
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKgSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79
|
90
....*....|...
gi 1822521627 112 DTLSTPVEVTSTT 124
Cdd:cd00063 80 GGESPPSESVTVT 92
|
|
| CDKN3-like |
cd14505 |
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ... |
1373-1470 |
1.11e-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: 53.04 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1373 ITQFHFtSWPDHGVPkttDKLLQFQRMMRDYLNKNRAGLPVV-HCSAGVGRTGTLIA--LDYLLQRIEKEAVVDvygIVh 1449
Cdd:cd14505 73 ITWHHL-PIPDGGVP---SDIAQWQELLEELLSALENGKKVLiHCKGGLGRTGLIAAclLLELGDTLDPEQAIA---AV- 144
|
90 100
....*....|....*....|.
gi 1822521627 1450 nmRMSRTCMVQTENQYIFLHQ 1470
Cdd:cd14505 145 --RALRPGAIQTPKQENFLHQ 163
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
870-946 |
1.33e-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: 50.69 E-value: 1.33e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521627 870 PSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSKG-ETTFTVTGLQPGDQYRLSVRSVT 946
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPsSTSYTLTGLKPGTEYEFRVRAVN 78
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
778-853 |
1.72e-07 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 50.11 E-value: 1.72e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521627 778 SPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSW-SKSTSKGETTFTATGLQPGDQYQLSVQSVT 853
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
406-481 |
1.74e-07 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 50.11 E-value: 1.74e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521627 406 SPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKG-ETAFTATGLQPGDQYQLSVQSVT 481
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGtTTSVTLTGLKPGTEYEVRVQAVN 77
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
684-760 |
1.81e-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: 50.31 E-value: 1.81e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521627 684 PSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQ-STSKDETTFTATRLQPGDQYLLSVQSVT 760
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
405-496 |
1.89e-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: 50.57 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 405 PSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSST-TITNKGETAFTATGLQPGDQYQLSVQSVTpE 483
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79
|
90
....*....|...
gi 1822521627 484 DTLSTPVEVTSTT 496
Cdd:cd00063 80 GGESPPSESVTVT 92
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
870-959 |
2.37e-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: 50.19 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 870 PSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASST-TITSKGETTFTVTGLQPGDQYRLSVRSVTpE 948
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79
|
90
....*....|.
gi 1822521627 949 DTWSTPAQVTS 959
Cdd:cd00063 80 GGESPPSESVT 90
|
|
| PTP_PTEN-like |
cd14497 |
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ... |
1369-1453 |
2.55e-07 |
|
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.
Pssm-ID: 350347 [Multi-domain] Cd Length: 160 Bit Score: 51.81 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1369 EPRTITQFHFT----SWPDHGVPkTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIA--LDYLLQRI-EKEAV 1441
Cdd:cd14497 52 EYDDDSKFEGRvlhyGFPDHHPP-PLGLLLEIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICayLLYYGQYStADEAL 130
|
90
....*....|..
gi 1822521627 1442 VDVYgivhNMRM 1453
Cdd:cd14497 131 EYFA----KKRF 138
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
312-403 |
2.71e-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: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 312 PSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSST-TVTSRGETTFKATGLQPGDQYLLSVQSVTpE 390
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79
|
90
....*....|...
gi 1822521627 391 DTWSTPVEVTNTT 403
Cdd:cd00063 80 GGESPPSESVTVT 92
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
219-310 |
4.12e-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: 49.42 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 219 PSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWT-ESTSKDKTTFTATGLQPGDQYQLSVQSVTpE 297
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79
|
90
....*....|...
gi 1822521627 298 DTVSSPLEVTNTT 310
Cdd:cd00063 80 GGESPPSESVTVT 92
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
33-109 |
4.37e-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: 49.15 E-value: 4.37e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521627 33 PSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSIT-TTGKNETTFTATGLQPGDQYLLSVRSVT 109
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
591-679 |
6.92e-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: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 591 PSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRST-TVTSKGETAFTATGLQPGDQYQLSVQSVTP- 668
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVNGg 80
|
90
....*....|..
gi 1822521627 669 -EGTLSTPVEVT 679
Cdd:cd00063 81 gESPPSESVTVT 92
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
499-574 |
7.09e-07 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 48.57 E-value: 7.09e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521627 499 SPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTEST-SKGETTFTATGLQPGDQYQLSVQSVT 574
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
312-388 |
8.50e-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: 48.38 E-value: 8.50e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521627 312 PSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSSTTV-TSRGETTFKATGLQPGDQYLLSVQSVT 388
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVnVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
591-670 |
8.58e-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: 48.38 E-value: 8.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 591 PSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKG-ETAFTATGLQPGDQYQLSVQSVTPE 669
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPsSTSYTLTGLKPGTEYEFRVRAVNGA 80
|
.
gi 1822521627 670 G 670
Cdd:smart00060 81 G 81
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
777-868 |
1.14e-06 |
|
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: 48.26 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 777 PSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGvSWSK--STSKGETTFTATGLQPGDQYQLSVQSVTp 854
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSG-DWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVN- 78
|
90
....*....|....
gi 1822521627 855 EDTLSTPVEVKSTT 868
Cdd:cd00063 79 GGGESPPSESVTVT 92
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
685-760 |
2.00e-06 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 47.02 E-value: 2.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521627 685 SPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSW-TQSTSKDETTFTATRLQPGDQYLLSVQSVT 760
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
34-109 |
2.02e-06 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 47.02 E-value: 2.02e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521627 34 SPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSIT-TTGKNETTFTATGLQPGDQYLLSVRSVT 109
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEiTVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
126-217 |
4.05e-06 |
|
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: 46.72 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 126 PSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGvSWTK--STNKDKTTFTATGLQPGDQYQLSVRSVTp 203
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSG-DWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVN- 78
|
90
....*....|....
gi 1822521627 204 EDTLSTPVEVTNTT 217
Cdd:cd00063 79 GGGESPPSESVTVT 92
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
313-388 |
4.08e-06 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 46.25 E-value: 4.08e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521627 313 SPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSSTTVT-SRGETTFKATGLQPGDQYLLSVQSVT 388
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
321-1061 |
4.80e-06 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 51.69 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 321 VNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVT 400
Cdd:COG3210 814 VTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANA 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 401 NTTNPSPVTGLTVVNGTTHSLriewTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSV 480
Cdd:COG3210 894 GTLTNLGTTTNAASGNGAVLA----TVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGAS 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 481 TPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATGL 560
Cdd:COG3210 970 SAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVN 1049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 561 QPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTV 640
Cdd:COG3210 1050 ASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGA 1129
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 641 TSKGETAFTATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVT 720
Cdd:COG3210 1130 TGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTT 1209
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 721 VTNVTGGVSWTQSTSKDETTFTATRLQPGDQyllSVQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNGTTQSLTIEWTRP 800
Cdd:COG3210 1210 TIGTTNVTTTTTLTASDTGNTTATGGSSAGQ---TGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGATATGSTV 1286
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 801 TDTRASNYTYRVTVTNVTGGVSWSKSTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVKSTTDPSPVTGLSVVN 880
Cdd:COG3210 1287 DIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNGATDSAAGAG 1366
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 881 STTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSKGETTFTVTGLQPGDQYRLSVRSVTPEDTWSTPAQVTST 960
Cdd:COG3210 1367 SGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNTTGTSVA 1446
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 961 SNPSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAIDTGPGVTTFTVTNLVPGVEYELRLQSVTP 1040
Cdd:COG3210 1447 GAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAEVAKASLEG 1526
|
730 740
....*....|....*....|.
gi 1822521627 1041 AGTRSSPETVRNATIPAAISD 1061
Cdd:COG3210 1527 GEGTYGGSSVAEAGTGGGILG 1547
|
|
| RhsA |
COG3209 |
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ... |
27-718 |
5.66e-06 |
|
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only];
Pssm-ID: 442442 [Multi-domain] Cd Length: 1103 Bit Score: 51.30 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 27 SQNVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVR 106
Cdd:COG3209 77 AGGVTALGDASAAGGGYVGGAAAGGGATLTGLAAATASAGRLVSTGAGAGGTVTAATGGTLGATAGSATTGSTDGGRGGV 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 107 SVTPEDTLSTPVEVTSTTNPSPVIGLSVVNGTTqSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTAT 186
Cdd:COG3209 157 AVTGLAGGGASAYGLTLGGAAAGPATGVGTGAV-TLATGLAGSALLALGSGAILGGLAGAYSGSATTATGTALGTPASVA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 187 GLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWT 266
Cdd:COG3209 236 ATVTGSATGAAGAGAAVATAATTLGGTTGAGTGASGAGLDASTGTGGAGGSNAAATAGGLGGAGLGSGGAGGGGTAGGTT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 267 ESTSKDKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYI 346
Cdd:COG3209 316 TAAGTTGTAAVSGAADAGTTTTTGTGTGGTTTTVGGGGSLTLGGYGAAGGLTTSVGAGGGGSTSGSTTTVGGGGTATGSG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 347 VTVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWT 426
Cdd:COG3209 396 GGSSTTGVGAGTTTTSTTGGDGGPATAAGALTAGGTATGTGTGGGGTTAGTDATTTTGGAGASGTLTTTGGAATGATTGG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 427 PPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSV 506
Cdd:COG3209 476 GTEAGTGGGTLTSGSAGATTLGTDTTLDDTLGGTTTTTAGARGLVVTTGTTLTLGTTTTATLSATDATGTGDTTTTGTVG 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 507 VNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVT 586
Cdd:COG3209 556 TGTSTGTGGTGTVTTTGDGTGGASTTTGTTGGTATTTTVTTTTTTSTAGTTTTTTSGYTRAGLTLTLGTGTASGLERATA 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 587 NTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSV 666
Cdd:COG3209 636 STGSTTGGTTGTGVTTTGTTTTRATGTTGTGTGVTAGLTTLATGGTTVGGGTGTTSTATTGATTGGTETGTTVTTLAGGT 715
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1822521627 667 TPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSltieWTRPTDTRASNYTYN 718
Cdd:COG3209 716 TTRLGTTTTGGGGGTTTDGTGTGGTTGTLTTTS----TTTTTTAGALTYTYD 763
|
|
| PRK15375 |
PRK15375 |
type III secretion system effector GTPase-activating protein SptP; |
1294-1428 |
6.53e-06 |
|
type III secretion system effector GTPase-activating protein SptP;
Pssm-ID: 185273 [Multi-domain] Cd Length: 535 Bit Score: 50.57 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1294 PNTVVDFWRMVWEQKTKVIVMLTNcveQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEW-TTRKFNVKKTGCPEPRT 1372
Cdd:PRK15375 346 PDALEAHMKMLLEKECSCLVVLTS---EDQMQAKQLPPYFRGSYTFGEVHTNSQKVSSASQGeAIDQYNMQLSCGEKRYT 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521627 1373 ITQFHFTSWPDHGVPKTTDKLLQFQRMMRdylNKNRAG----------LPVVHCSAGVGRTGTLIA 1428
Cdd:PRK15375 423 IPVLHVKNWPDHQPLPSTDQLEYLADRVK---NSNQNGapgrsssdkhLPMIHCLGGVGRTGTMAA 485
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
592-667 |
7.41e-06 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 45.48 E-value: 7.41e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521627 592 SPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVT-SKGETAFTATGLQPGDQYQLSVQSVT 667
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
498-574 |
8.01e-06 |
|
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: 45.95 E-value: 8.01e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521627 498 PSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWT-ESTSKGETTFTATGLQPGDQYQLSVQSVT 574
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
|
|
| PTP_PTPDC1 |
cd14506 |
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ... |
1376-1469 |
8.61e-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: 48.50 E-value: 8.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1376 FHFTSWPDHGVPkTTDKLLQFQRMMRDYLNKnrAGLPVVHCSAGVGRTGTLIA--LDYLLQRIEKEAVVDVygivhnmRM 1453
Cdd:cd14506 79 FYNFGWKDYGVP-SLTTILDIVKVMAFALQE--GGKVAVHCHAGLGRTGVLIAcyLVYALRMSADQAIRLV-------RS 148
|
90
....*....|....*.
gi 1822521627 1454 SRTCMVQTENQYIFLH 1469
Cdd:cd14506 149 KRPNSIQTRGQVLCVR 164
|
|
| PTP_VSP_TPTE |
cd14510 |
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ... |
1382-1469 |
9.45e-06 |
|
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.
Pssm-ID: 350360 [Multi-domain] Cd Length: 177 Bit Score: 47.74 E-value: 9.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1382 PDHGVPkTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIA---LDYLLQRIEKEAvVDVYGivhNMRMSRTCM 1458
Cdd:cd14510 82 DDHNVP-TLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCawlIYSGQFESAKEA-LEYFG---ERRTDKSVS 156
|
90
....*....|....*.
gi 1822521627 1459 -----VQTENQYIFLH 1469
Cdd:cd14510 157 skfqgVETPSQSRYVG 172
|
|
| COG4733 |
COG4733 |
Phage-related protein, tail protein J [Mobilome: prophages, transposons]; |
71-671 |
1.02e-05 |
|
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 50.33 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 71 TNVAGGVSSITttGKNETTFTATGLQPGDQYLlsvRSVTPEDTlstPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPT 150
Cdd:COG4733 412 RRIGGRVSSVD--GRVVTLDRPVTMEAGDRYL---RVRLPDGT---SVARTVQSVAGRTLTVSTAYSETPEAGAVWAFGP 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 151 DTRATNYTYIVTVTNVTGGvswtkstnkdktTFTATGLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSpvtgLSVVNG 230
Cdd:COG4733 484 DELETQLFRVVSIEENEDG------------TYTITAVQHAPEKYAAIDAGAFDDVPPQWPPVNVTTSES----LSVVAQ 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 231 TTE--SLRIKWTRPTDT------------------------------RASDYTYRVTVTNVTGGVS-WTESTSkdkttFT 277
Cdd:COG4733 548 GTAvtTLTVSWDAPAGAvayevewrrddgnwvsvprtsgtsfevpgiYAGDYEVRVRAINALGVSSaWAASSE-----TT 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 278 ATGLqpgdqyqlsvqsvtpedtvssplevtnTTNPSPVTGLSVVNGTTQsLTIEWTRPTDTRATnYTYIVTVTNVTGGVS 357
Cdd:COG4733 623 VTGK---------------------------TAPPPAPTGLTATGGLGG-ITLSWSFPVDADTL-RTEIRYSTTGDWASA 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 358 STTVTSRGETTFKATGLQPGDQYLLSVQSVtpeDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYT 437
Cdd:COG4733 674 TVAQALYPGNTYTLAGLKAGQTYYYRARAV---DRSGNVSAWWVSGQASADAAGILDAITGQILETELGQELDAIIQNAT 750
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 438 YKVTVTNVAGGVSSTTITNKGETAFTATglqpgdqyqlSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIE 517
Cdd:COG4733 751 VAEVVAATVTDVTAQIDTAVLFAGVATA----------AAIGAEARVAATVAESATAAAATGTAADAAGDASGGVTAGTS 820
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 518 WTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFtatglQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGL 597
Cdd:COG4733 821 GTTGAGDTAASTTRVAAAVVLAGVVVYGDAIIESGNTG-----DIVATGDIASAAAGAVATTVSGTTAADVSAVADSTAA 895
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521627 598 SVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTG--GGRSTTVTSKGETAFTATGLQPGDQYQLSVQSVTPEGT 671
Cdd:COG4733 896 SLTAIVIAATTIIDAIGDGTTREPAGDIGASGGAQGfaVTIVGSFDGAGAVATVDAGQSVVDGVGTAVEAANGTET 971
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
684-775 |
1.10e-05 |
|
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: 45.57 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 684 PSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGvSWTQ--STSKDETTFTATRLQPGDQYLLSVQSVTp 761
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSG-DWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVN- 78
|
90
....*....|....
gi 1822521627 762 EDTLSTPAQVTSTT 775
Cdd:cd00063 79 GGGESPPSESVTVT 92
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
216-931 |
1.38e-05 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 50.15 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 216 TTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWTESTSKDKTTFTATGLQPGDQYQLSVQSVT 295
Cdd:COG3210 1 GSGGLAGTTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 296 PEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSSTTVTSRGETTFKATGLQ 375
Cdd:COG3210 81 IGAAAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 376 PGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTP-PTDTRATNYTYKVTVTNVAGGVSSTTI 454
Cdd:COG3210 161 NTNTNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAgGGTAGGVASANSTLTGGVVAAGTGAGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 455 TNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVT 534
Cdd:COG3210 241 ISTGGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 535 VTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTTQSLGIEWTSP 614
Cdd:COG3210 321 TTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 615 TDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVN 694
Cdd:COG3210 401 GSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 695 GTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYLLSVQSVTPEDTLSTPAQVTST 774
Cdd:COG3210 481 SATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 775 TNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSKSTSKGETTFTATGLQPGDQYQLSVQSVTP 854
Cdd:COG3210 561 SNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVG 640
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521627 855 EDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSKGETTFTVTG 931
Cdd:COG3210 641 AALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTG 717
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
127-202 |
2.80e-05 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 43.94 E-value: 2.80e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521627 127 SPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSW-TKSTNKDKTTFTATGLQPGDQYQLSVRSVT 202
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
27-1024 |
2.84e-05 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 48.99 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 27 SQNVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVR 106
Cdd:COG3210 278 TGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGT 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 107 SVTPEDTLSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTAT 186
Cdd:COG3210 358 GAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITG 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 187 GLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWT 266
Cdd:COG3210 438 NGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGI 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 267 ESTSKDKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYI 346
Cdd:COG3210 518 TAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSG 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 347 VTVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWT 426
Cdd:COG3210 598 GTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGT 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 427 PPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGlQPGDQYQLSVQSVTpedTLSTPVEVTSTTNpspvTGLSV 506
Cdd:COG3210 678 VTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTG-QIGALANANGDTVT---FGNLGTGATLTLN----AGVTI 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 507 VNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATG-LQPGDQYQLSVQSVTPEDTLSTPEQV 585
Cdd:COG3210 750 TSGNAGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNAGAEISIDITADGtITAAGTTAINVTGSGGTITINTATTG 829
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 586 TNTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQS 665
Cdd:COG3210 830 LTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGN 909
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 666 VTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSKDETTFTATR 745
Cdd:COG3210 910 GAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGG 989
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 746 LQPGDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNGTTQSLTIE-WTRPTDTRASNYTYRVTVTNVTGGVSWS 824
Cdd:COG3210 990 VIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAgGQNGVGVNASGISGGNAAALTASGTAGT 1069
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 825 KSTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYN 904
Cdd:COG3210 1070 TGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLV 1149
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 905 VTVTNVTDGASSTTITSKGETTFTVTGLQPGDQYRLSVRSVTPEDTWSTPAQVTSTSNPSPVSGLTVVNRTTVSIEVTWA 984
Cdd:COG3210 1150 AVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGN 1229
|
970 980 990 1000
....*....|....*....|....*....|....*....|
gi 1822521627 985 APTDARAPEYTYRITLANVTRRGRGAIDTGPGVTTFTVTN 1024
Cdd:COG3210 1230 TTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGA 1269
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
443-930 |
3.81e-05 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 48.62 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 443 TNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPN 522
Cdd:COG4625 1 GGGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 523 DTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGLSVVNG 602
Cdd:COG4625 81 GGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 603 TTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGeTAFTATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTT 682
Cdd:COG4625 161 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGG-GGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 683 NPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYLLSVQSVTPE 762
Cdd:COG4625 240 GGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 763 DTLSTPAQVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSKSTSKGETTFTATGLQPG 842
Cdd:COG4625 320 GGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 843 DQYQLSVQSVTPEDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSK 922
Cdd:COG4625 400 GGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLT 479
|
....*...
gi 1822521627 923 GETTFTVT 930
Cdd:COG4625 480 GNNTYTGT 487
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
440-931 |
9.93e-05 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 47.08 E-value: 9.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 440 VTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWT 519
Cdd:COG4625 7 GGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 520 SPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGLSV 599
Cdd:COG4625 87 GGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 600 VNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSVTPEGTLSTPVEVT 679
Cdd:COG4625 167 GGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 680 STTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYLLSVQSV 759
Cdd:COG4625 247 GAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 760 TPEDTLSTPAQVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSKSTSKGETTFTATGL 839
Cdd:COG4625 327 GGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGGAG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 840 QPGDQYQLSVQSVTPEDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASS--- 916
Cdd:COG4625 407 GTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNTytg 486
|
490
....*....|....*.
gi 1822521627 917 -TTITSKGETTFTVTG 931
Cdd:COG4625 487 tTTVNGGGNYTQSAGS 502
|
|
| COG4733 |
COG4733 |
Phage-related protein, tail protein J [Mobilome: prophages, transposons]; |
917-1132 |
1.07e-04 |
|
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 46.86 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 917 TTITSKGETTFTVTGLQPGDQYRLSVRSVTPEDTWSTPAQVTSTSNPSpvsgLTVVNRTTV--SIEVTWAAPTDARAPEY 994
Cdd:COG4733 494 VSIEENEDGTYTITAVQHAPEKYAAIDAGAFDDVPPQWPPVNVTTSES----LSVVAQGTAvtTLTVSWDAPAGAVAYEV 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 995 TYRITLANVTRRGRgaidtgPGVTTFTVTNLVPGvEYELRLQSVTPAGTRSSPETVRNATI------PAAISDFRCSGST 1068
Cdd:COG4733 570 EWRRDDGNWVSVPR------TSGTSFEVPGIYAG-DYEVRVRAINALGVSSAWAASSETTVtgktapPPAPTGLTATGGL 642
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1069 GyMVEAKWSQPNG----QFSMFKALTYDGEQLISNLSLGKeERSLTVDNLQPGRTYTLRV--VTESGNTS 1132
Cdd:COG4733 643 G-GITLSWSFPVDadtlRTEIRYSTTGDWASATVAQALYP-GNTYTLAGLKAGQTYYYRAraVDRSGNVS 710
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
29-280 |
1.14e-04 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 46.53 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 29 NVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYtyNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSV 108
Cdd:COG3401 323 DLTPPAAPSGLTATAVGSSSITLSWTASSDADVTGY--NVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAV 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 109 T---PEDTLSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPT----DTRATNYTYIVTVTNVTGGVSWTKSTNKDKT 181
Cdd:COG3401 401 DaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAAsaasNPGVSAAVLADGGDTGNAVPFTTTSSTVTAT 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 182 T---------FTATGLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTY 252
Cdd:COG3401 481 TtdtttanlsVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSS 560
|
250 260
....*....|....*....|....*...
gi 1822521627 253 RVTVTNVTGGVSWTESTSKDKTTFTATG 280
Cdd:COG3401 561 VSGAGLGSGNLYLITTLGGSLLTTTSTN 588
|
|
| DUSP23 |
cd14504 |
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ... |
1375-1428 |
1.43e-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: 43.42 E-value: 1.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1822521627 1375 QFHFTSWPDHGVPkTTDKLLQFQRMMRDYLNKNRAGLpvVHCSAGVGRTGTLIA 1428
Cdd:cd14504 51 RYHHIPIEDYTPP-TLEQIDEFLDIVEEANAKNEAVL--VHCLAGKGRTGTMLA 101
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
131-651 |
1.64e-04 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 46.31 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 131 GLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTATGLQPGDQYQLSVRSVTPEDTLSTP 210
Cdd:COG4625 2 GGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 211 VEVTNTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWTESTSKDKTTFTATGLQPGDQYQLS 290
Cdd:COG4625 82 GGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 291 VQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSSTTVTSRGETTFK 370
Cdd:COG4625 162 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 371 ATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIeWTPPTDTRATNYTYKVTVTNVAGGVS 450
Cdd:COG4625 242 GGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGG-GGGGGGGGGGGGGGGGGGGGGGGGGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 451 STTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYI 530
Cdd:COG4625 321 GGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 531 YNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTtqslgie 610
Cdd:COG4625 401 GGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGA------- 473
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1822521627 611 wtsPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTAT 651
Cdd:COG4625 474 ---GTLTLTGNNTYTGTTTVNGGGNYTQSAGSTLAVEVDAA 511
|
|
| MJ0795 |
COG1361 |
S-layer protein MJ0795, predicted component of type IV pili-like system [General function ... |
188-540 |
2.99e-04 |
|
S-layer protein MJ0795, predicted component of type IV pili-like system [General function prediction only];
Pssm-ID: 440972 [Multi-domain] Cd Length: 409 Bit Score: 45.07 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 188 LQPGDQYQLSV----------RSVTPEDTLSTPVEVTNTTNPspvTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVT 257
Cdd:COG1361 36 VAPGEEVTLTVtitndgtltaRNVTVELEGDYPFEVKSGEQS---VGGSLPPGQSVTVTFTVTVPEDAEPGTYPIPVTVS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 258 NVTGGVSWTESTSKDKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTtnpspvtglsvVNGTTQSLTIEWTRPTD 337
Cdd:COG1361 113 YSYGYTDRTETETYTVTVKVEGEPRFEVVSVTSPDSLTPGDTGTLTLTIKNT-----------GTGTAKNVTVTLTSPSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 338 TRATNYTYIVTVTNVTGGVSSTtVTSRGETTFKATGLQPGDQ----YLLSVQSVTPEDTWSTPVEVT------NTTNPSP 407
Cdd:COG1361 182 DLTDLEPGPRPATNVVVVLSSP-VSPVGSNSVALGTLEPGESatftFKVDVSEDAEPGPYPLPLTVTyrdedgDTYSDTV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 408 VTGLTVVNGTthSLRIEWTPPTDTRATNYTYKVTVTNV-AGGVSSTTITNKGETAFTATG-------LQPGDqyqlsvqs 479
Cdd:COG1361 261 TIGVYVAPKA--DFEVENVESTITAGETVTITITVTNTgNETAKNVVARLSADDPLSSLDdeafigdLAPGE-------- 330
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521627 480 vtpEDTLSTPVEVTSTTNPSPVTGlsvvngttqSLTIEWTSPNDTTASNYIYNVTVTNVTG 540
Cdd:COG1361 331 ---SATVTFTVSASSDATPGTYPI---------TVTIRYDDDDGNTQLSDTITVPVEVTEP 379
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
492-931 |
3.19e-04 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 45.32 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 492 VTSTTNPSPVTGLSVVNGTTQSLTIEwTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQ 571
Cdd:COG3468 3 SGGGGGATGLGGGGTGGGGGLGGTGG-GNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 572 SVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTAT 651
Cdd:COG3468 82 GGTGGNSTGGGGGNSGTGGTGGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 652 GLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWT 731
Cdd:COG3468 162 GSGGGGSGGGGGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 732 QSTSKDETTFTATRlqpgdQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYr 811
Cdd:COG3468 242 GGSAGGTGGGGLTG-----GGAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGG- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 812 VTVTNVTGGVSWSKSTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSlriewt 891
Cdd:COG3468 316 GGGGSNAGGGSGGGGGGGGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSD------ 389
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1822521627 892 tpNNIRASNYTYNVTVTNVTDGASSTTITSKGETTFTVTG 931
Cdd:COG3468 390 --GVGTGLTTGGTGNNGGGGVGGGGGGGLTLTGGTLTVNG 427
|
|
| CDC14_C |
cd14499 |
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ... |
1414-1435 |
3.34e-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: 43.21 E-value: 3.34e-04
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
392-598 |
7.94e-04 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 43.97 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 392 TWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGD 471
Cdd:COG3469 1 SSSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 472 QYQLSV-------QSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSW 544
Cdd:COG3469 81 TATAAAaaatstsATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETAT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1822521627 545 TESTSKGETTFTATGLQPGDQYQlSVQSVTPEDTLSTPEQVTNTTNPSPVTGLS 598
Cdd:COG3469 161 GGTTTTSTTTTTTSASTTPSATT-TATATTASGATTPSATTTATTTGPPTPGLP 213
|
|
| PTP_PTEN |
cd14509 |
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ... |
1382-1452 |
1.65e-03 |
|
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.
Pssm-ID: 350359 [Multi-domain] Cd Length: 158 Bit Score: 40.65 E-value: 1.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521627 1382 PDHGVPkTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALdYLLQRIE----KEAvVDVYGI--VHNMR 1452
Cdd:cd14509 68 DDHNPP-PLELIKPFCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICC-YLLYLGKfpsaKEA-LDFYGAkrTKNKK 141
|
|
| DSP_DUSP16 |
cd14646 |
dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual ... |
1367-1437 |
1.65e-03 |
|
dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual specificity protein phosphatase 16 (DUSP16), also called mitogen-activated protein kinase (MAPK) phosphatase 7 (MKP-7), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class III subfamily and is a JNK/p38-selective cytoplasmic MKP. DUSP16/MKP-7 plays an essential role in perinatal survival and selectively controls the differentiation and cytokine production of myeloid cells. It is acetylated by Mycobacterium tuberculosis Eis protein, which leads to the inhibition of JNK-dependent autophagy, phagosome maturation, and ROS generation, and thus, initiating suppression of host immune responses. DUSP16/MKP-7 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.
Pssm-ID: 350494 [Multi-domain] Cd Length: 145 Bit Score: 40.39 E-value: 1.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822521627 1367 CPEPRTITQFHFTSWPDHGvpKTTDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTlIALDYLLQRIE 1437
Cdd:cd14646 39 CPKPDFIPESHFLRVPVND--SFCEKILPWLDKSVDFIEKAKAsnGRVLVHCLAGISRSAT-IAIAYIMKRMD 108
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
270-748 |
2.00e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 42.98 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 270 SKDKTTFTATGLQPGDQYQLSVQSVTPEDtvssplevTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTR---------- 339
Cdd:pfam05109 312 SQDMPTNTTDITYVGDNATYSVPMVTSED--------ANSPNVTVTAFWAWPNNTETDFKCKWTLTSGTPsgcenisgaf 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 340 ATNYTYIVTVTNVtGGVSSTTVTSRGETTFKATGLQpgdqyllSVQSVTPEDTWSTP-VEVTNTTNPSPVTGLTvvnGTT 418
Cdd:pfam05109 384 ASNRTFDITVSGL-GTAPKTLIITRTATNATTTTHK-------VIFSKAPESTTTSPtLNTTGFAAPNTTTGLP---SST 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 419 HsLRIEWTPPTDTRATNYTYKVTVTNVAGGVS-STTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTtn 497
Cdd:pfam05109 453 H-VPTNLTAPASTGPTVSTADVTSPTPAGTTSgASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTT-- 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 498 PSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGET-TFTATGLQPGDQY-QLSVQSVTP 575
Cdd:pfam05109 530 PTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTpTPNATSPTVGETSpQANTTNHTL 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 576 EDTLSTPEQVT---NTTNPSPVTGLSVVNGTTQSLGIEWTSPTDT-------RASNYTYIVTVTNVTGGGRSTTVTSKGE 645
Cdd:pfam05109 610 GGTSSTPVVTSppkNATSAVTTGQHNITSSSTSSMSLRPSSISETlspstsdNSTSHMPLLTSAHPTGGENITQVTPAST 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 646 TAFTATGLQPGDQYQLSVQSVTP--EGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYT------- 716
Cdd:pfam05109 690 STHHVSTSSPAPRPGTTSQASGPgnSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTggkhttg 769
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1822521627 717 ----YNVTVTNVTGGVSWTQSTSKDETTF----TATRLQP 748
Cdd:pfam05109 770 hgarTSTEPTTDYGGDSTTPRTRYNATTYlppsTSSKLRP 809
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
424-647 |
2.03e-03 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 42.43 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 424 EWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTG 503
Cdd:COG3469 4 VSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 504 LSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTftatglqpgdqyqlSVQSVTPEDTLSTPE 583
Cdd:COG3469 84 AAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTT--------------TSGASATSSAGSTTT 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822521627 584 QVTNTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYtyivTVTNVTGGGRSTTVTSKGETA 647
Cdd:COG3469 150 TTTVSGTETATGGTTTTSTTTTTTSASTTPSATTTATAT----TASGATTPSATTTATTTGPPT 209
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
1058-1134 |
2.31e-03 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 38.55 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1058 AISDFRCSGSTGYMVEAKWSQP---NGQFSMFKaLTY---DGEQLISNLSLGKEERSLTVDNLQPGRTYTLRVVTESGNT 1131
Cdd:pfam00041 2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYE-VEYrpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
|
...
gi 1822521627 1132 SSQ 1134
Cdd:pfam00041 81 EGP 83
|
|
| DSPc |
smart00195 |
Dual specificity phosphatase, catalytic domain; |
1389-1470 |
2.52e-03 |
|
Dual specificity phosphatase, catalytic domain;
Pssm-ID: 214551 [Multi-domain] Cd Length: 138 Bit Score: 39.96 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1389 TTDKLLQFQRMMRDYLN--KNRAGLPVVHCSAGVGRTGTLIALdYLLQRiEKEAVVDVYGIVhnmRMSRTCMVQTENqyi 1466
Cdd:smart00195 56 TETKISPYFPEAVEFIEdaESKGGKVLVHCQAGVSRSATLIIA-YLMKT-RNMSLNDAYDFV---KDRRPIISPNFG--- 127
|
....
gi 1822521627 1467 FLHQ 1470
Cdd:smart00195 128 FLRQ 131
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
299-518 |
2.67e-03 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 42.05 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 299 TVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSSTTVTSRGETTfkATGLQPGD 378
Cdd:COG3469 1 SSSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTA--ATSSTTST 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 379 QYLLSV---QSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTIT 455
Cdd:COG3469 79 TATATAaaaAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTET 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822521627 456 NKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEW 518
Cdd:COG3469 159 ATGGTTTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTPGLPKHVLVGYW 221
|
|
| DSPc |
pfam00782 |
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ... |
1389-1470 |
3.55e-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: 39.17 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1389 TTDKLLQFQRMMRDYLN--KNRAGLPVVHCSAGVGRTGTLIALdYLLQRiEKEAVVDVYGIVhnmRMSRTCMVQTENqyi 1466
Cdd:pfam00782 47 HETNISKYLEEAVEFIDdaRQKGGKVLVHCQAGISRSATLIIA-YLMKT-RNLSLNEAYSFV---KERRPGISPNFG--- 118
|
....
gi 1822521627 1467 FLHQ 1470
Cdd:pfam00782 119 FKRQ 122
|
|
| TpbA-like |
cd14529 |
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ... |
1370-1454 |
3.94e-03 |
|
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.
Pssm-ID: 350378 [Multi-domain] Cd Length: 158 Bit Score: 39.66 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1370 PRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDylnKNRAGlPVV-HCSAGVGRTGTLIALdYLlqriekeavvDVYG-- 1446
Cdd:cd14529 53 AAKIDGVKYVNLPLSATRPTESDVQSFLLIMDL---KLAPG-PVLiHCKHGKDRTGLVSAL-YR----------IVYGgs 117
|
90
....*....|.
gi 1822521627 1447 ---IVHNMRMS 1454
Cdd:cd14529 118 keeANEDYRLS 128
|
|
| DSP_MKP |
cd14512 |
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ... |
1365-1435 |
4.96e-03 |
|
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs, which are involved in gene regulation, cell proliferation, programmed cell death and stress responses, as an important feedback control mechanism that limits MAPK cascades. MKPs, also referred to as typical DUSPs, function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III).
Pssm-ID: 350362 [Multi-domain] Cd Length: 136 Bit Score: 39.00 E-value: 4.96e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822521627 1365 TGCPEPRTITQFHFTSWP--DHgvpkTTDKLLQFQRMMRDYLN--KNRAGLPVVHCSAGVGRTGTlIALDYLLQR 1435
Cdd:cd14512 35 NTCPNPDFIGLFHYKRIPvnDS----FCQNISPWFDEAIEFIEeaKASNGGVLVHCLAGISRSAT-IAIAYLMKR 104
|
|
| DUF4959 |
pfam16323 |
Domain of unknown function (DUF4959); This family consists of uncharacterized proteins around ... |
213-307 |
5.78e-03 |
|
Domain of unknown function (DUF4959); This family consists of uncharacterized proteins around 400 residues in length and is mainly found in various Bacteroides, Pedobacter and Parabacteroides species. Several proteins are annotated as Galactose-binding like proteins, but the specific function of this protein is unknown.
Pssm-ID: 465093 [Multi-domain] Cd Length: 106 Bit Score: 38.00 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 213 VTNTTNPSPVTGLSVVNGTTESLrIKWTRPTDtraSDYTYRVTVTNVTGGVSWTESTSKDKTTFTATGLQPGDQYQLSVQ 292
Cdd:pfam16323 13 GTDGTAPGPVTNVKVKNIPGGAT-ISYTLPDD---PDLLYVKAVYTIRNGKEREVKASYYTDSLTVEGFGDTGEYEVKLY 88
|
90
....*....|....*
gi 1822521627 293 SVTPEDTVSSPLEVT 307
Cdd:pfam16323 89 AVSRSENESEPVEVK 103
|
|
| DSP_DUSP11 |
cd17665 |
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ... |
1382-1427 |
5.91e-03 |
|
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar proteins; dual specificity protein phosphatase 11 (DUSP11), also known as RNA/RNP complex-1-interacting phosphatase or phosphatase that interacts with RNA/RNP complex 1 (PIR1), has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity. It has activity for short RNAs but is less active toward mononucleotide triphosphates, suggesting that its primary function in vivo is to dephosphorylate RNA 5'-ends. It may play a role in nuclear mRNA metabolism. Also included in this subfamily is baculovirus RNA 5'-triphosphatase for Autographa californica nuclear polyhedrosis virus.
Pssm-ID: 350503 Cd Length: 169 Bit Score: 39.18 E-value: 5.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1822521627 1382 PDHGVPKTtDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTLI 1427
Cdd:cd17665 85 PGHQVPDD-KTIQSFKDAVKDFLEKNKDndKLIGVHCTHGLNRTGYLI 131
|
|
| DSP_MKP_classIII |
cd14568 |
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ... |
1361-1452 |
6.79e-03 |
|
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class III MKPs consist of DUSP8, DUSP10/MKP-5 and DUSP16/MKP-7, and are JNK/p38-selective phosphatases, which are found in both the cell nucleus and cytoplasm. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.
Pssm-ID: 350416 [Multi-domain] Cd Length: 140 Bit Score: 38.55 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 1361 NVKKTgCPEPRTITQFHFTSWPDHGVPKttDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTlIALDYLLQRIeK 1438
Cdd:cd14568 32 NVSNT-CPKPDFIPDSHFLRIPVNDSYC--EKLLPWLDKAVEFIEKARAsnKRVLVHCLAGISRSAT-IAIAYIMKHM-R 106
|
90
....*....|....
gi 1822521627 1439 EAVVDVYGIVHNMR 1452
Cdd:cd14568 107 MSLDDAYRFVKEKR 120
|
|
| MJ0795 |
COG1361 |
S-layer protein MJ0795, predicted component of type IV pili-like system [General function ... |
467-819 |
7.87e-03 |
|
S-layer protein MJ0795, predicted component of type IV pili-like system [General function prediction only];
Pssm-ID: 440972 [Multi-domain] Cd Length: 409 Bit Score: 40.45 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 467 LQPGDQYQLSVQ----------SVTPEDTLSTPVEVTSTTNPspvTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVT 536
Cdd:COG1361 36 VAPGEEVTLTVTitndgtltarNVTVELEGDYPFEVKSGEQS---VGGSLPPGQSVTVTFTVTVPEDAEPGTYPIPVTVS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 537 nvtggVSWTESTSKGETTFTATgLQPGDQYQLSVQSVTPEDTLstpeqVTNTTNPSPVTGLSVVNGTTQSLGIEWTSPTD 616
Cdd:COG1361 113 -----YSYGYTDRTETETYTVT-VKVEGEPRFEVVSVTSPDSL-----TPGDTGTLTLTIKNTGTGTAKNVTVTLTSPSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 617 TRASNYTYIVTVTNVTgGGRSTTVTSKGETAFTATGLQPGDQ----YQLSVQSVTPEGTLSTPVEVT------STTNPSP 686
Cdd:COG1361 182 DLTDLEPGPRPATNVV-VVLSSPVSPVGSNSVALGTLEPGESatftFKVDVSEDAEPGPYPLPLTVTyrdedgDTYSDTV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521627 687 VTGLSVVNgtTQSLTIEWTRPTDTRASNYTYNVTVTN--------VTGGVSWTQSTSKDETTFTATRLQPGDqyllsvqs 758
Cdd:COG1361 261 TIGVYVAP--KADFEVENVESTITAGETVTITITVTNtgnetaknVVARLSADDPLSSLDDEAFIGDLAPGE-------- 330
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521627 759 vtpEDTLSTPAQVTSTTNPSPVTGlsvvngttqSLTIEWTRPTDTRASNYTYRVTVTNVTG 819
Cdd:COG1361 331 ---SATVTFTVSASSDATPGTYPI---------TVTIRYDDDDGNTQLSDTITVPVEVTEP 379
|
|
| |
