|
Name |
Accession |
Description |
Interval |
E-value |
| PTPc |
smart00194 |
Protein tyrosine phosphatase, catalytic domain; |
1123-1381 |
2.24e-116 |
|
Protein tyrosine phosphatase, catalytic domain;
Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 365.06 E-value: 2.24e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1123 GFAEEYQGLANVG-TNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLdRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLP 1201
Cdd:smart00194 1 GLEEEFEKLDRLKpDDESCTVAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1202 NTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTI 1280
Cdd:smart00194 80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLtYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1281 TQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRM 1360
Cdd:smart00194 160 THYHYTNWPDHGVPESPESILDLIRAVRKS-QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238
|
250 260
....*....|....*....|.
gi 1822521639 1361 SRTCMVQTENQYIFLHQCILD 1381
Cdd:smart00194 239 QRPGMVQTEEQYIFLYRAILE 259
|
|
| R3-PTPc |
cd14548 |
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ... |
1153-1377 |
8.07e-112 |
|
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: 351.27 E-value: 8.07e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1153 RYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVK 1232
Cdd:cd14548 1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1233 CERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLN 1312
Cdd:cd14548 81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822521639 1313 KNrAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14548 159 QE-KGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
|
|
| Y_phosphatase |
pfam00102 |
Protein-tyrosine phosphatase; |
1148-1381 |
6.57e-110 |
|
Protein-tyrosine phosphatase;
Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 346.54 E-value: 6.57e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1148 NKVKNRYTNIFPYDVARVKLdrQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1227
Cdd:pfam00102 1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1228 QNRVKCERYWPMDMS-SCLYGDIVVNIVSEET-SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQR 1305
Cdd:pfam00102 79 KGREKCAQYWPEEEGeSLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521639 1306 MMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:pfam00102 159 KVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
|
|
| R-PTPc-J |
cd14615 |
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ... |
1152-1381 |
1.36e-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: 1.36e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1152 NRYTNIFPYDVARVKLDrQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1231
Cdd:cd14615 1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1232 KCERYWPMDMSSClYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYL 1311
Cdd:cd14615 80 KCEEYWPSKQKKD-YGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521639 1312 NKNRAGLPV-VHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14615 159 KQNPPNSPIlVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
|
|
| R-PTPc-H |
cd14619 |
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ... |
1152-1381 |
1.49e-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: 334.55 E-value: 1.49e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1152 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1231
Cdd:cd14619 1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1232 KCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYL 1311
Cdd:cd14619 81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521639 1312 NKNRA-GLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14619 161 DQTMSgGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
|
|
| PTPc |
cd00047 |
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ... |
1178-1377 |
2.12e-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: 310.37 E-value: 2.12e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSE 1256
Cdd:cd00047 1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLeYGDITVTLVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1257 ETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRaGLPVVHCSAGVGRTGTLIAL 1336
Cdd:cd00047 81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPN-GPIVVHCSAGVGRTGTFIAI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1822521639 1337 DYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd00047 160 DILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
|
|
| R-PTPc-B |
cd14617 |
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ... |
1152-1377 |
8.90e-96 |
|
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: 307.23 E-value: 8.90e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1152 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1231
Cdd:cd14617 1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1232 KCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVkktgCPE-----PRTITQFHFTSWPDHGVPKTTDKLLQFQRM 1306
Cdd:cd14617 81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKI----CSEeqldaPRLVRHFHYTVWPDHGVPETTQSLIQFVRT 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822521639 1307 MRDYLNK-NRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14617 157 VRDYINRtPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
|
|
| R-PTPc-O |
cd14614 |
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ... |
1139-1380 |
4.38e-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: 297.57 E-value: 4.38e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1139 SKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKV 1218
Cdd:cd14614 3 PHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1219 IVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVP--KT 1296
Cdd:cd14614 83 IVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYAD--EVQDVMHFNYTAWPDHGVPtaNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1297 TDKLLQFQRMMRDYLNKnRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1376
Cdd:cd14614 161 AESILQFVQMVRQQAVK-SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 239
|
....
gi 1822521639 1377 QCIL 1380
Cdd:cd14614 240 QCVQ 243
|
|
| R-PTPc-LAR-1 |
cd14553 |
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ... |
1148-1381 |
1.41e-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: 295.85 E-value: 1.41e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1148 NKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1227
Cdd:cd14553 3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1228 QNRVKCERYWPMDMSScLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMM 1307
Cdd:cd14553 83 RSRVKCDQYWPTRGTE-TYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822521639 1308 RdYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14553 162 K-ACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
|
|
| R-PTPc-V |
cd14618 |
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ... |
1152-1380 |
1.80e-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: 281.45 E-value: 1.80e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1152 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1231
Cdd:cd14618 1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1232 KCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYL 1311
Cdd:cd14618 81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1312 NKNRAGLPV-VHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1380
Cdd:cd14618 161 QATKGKGPTlVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
|
|
| R5-PTPc-1 |
cd14549 |
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ... |
1178-1376 |
1.00e-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: 266.91 E-value: 1.00e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSClYGDIVVNIVSEE 1257
Cdd:cd14549 1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTET-YGNIQVTLLSTE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1258 TSPEWTTRKFNVK------KTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRmMRDYLNKNRAGLPVVHCSAGVGRTG 1331
Cdd:cd14549 80 VLATYTVRTFSLKnlklkkVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVR-KSSAANPPGAGPIVVHCSAGVGRTG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1822521639 1332 TLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1376
Cdd:cd14549 159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
|
|
| R-PTPc-Q |
cd14616 |
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ... |
1152-1377 |
3.47e-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: 3.47e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1152 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1231
Cdd:cd14616 1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1232 KCERYWPMDMSS-CLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdy 1310
Cdd:cd14616 81 RCHQYWPEDNKPvTVFGDIVITKLMEDVQIDWTIRDLKIERHG--DYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR-- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1311 lnKNRAGLP---VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14616 157 --ASRAHDNtpmIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
|
|
| PTPc-N9 |
cd14543 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ... |
1123-1376 |
1.10e-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: 263.84 E-value: 1.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1123 GFAEEYQGLAN---VGTNQSKEAfqvPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGP 1199
Cdd:cd14543 4 GIYEEYEDIRReppAGTFLCSLA---PANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1200 LPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPR 1278
Cdd:cd14543 81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLrYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1279 TITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLN----------KNRAGLP--VVHCSAGVGRTGTLIALDYLLQRIEKE 1346
Cdd:cd14543 161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQAlavkamgdrwKGHPPGPpiVVHCSAGIGRTGTFCTLDICLSQLEDV 240
|
250 260 270
....*....|....*....|....*....|
gi 1822521639 1347 AVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1376
Cdd:cd14543 241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
|
|
| R-PTPc-T-1 |
cd14630 |
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ... |
1147-1381 |
4.07e-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: 4.07e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1147 DNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCV 1226
Cdd:cd14630 2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1227 EQNRVKCERYWPMDMSscLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRM 1306
Cdd:cd14630 82 EVGRVKCVRYWPDDTE--VYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822521639 1307 MRdYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14630 160 VK-FLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
|
|
| R-PTPc-F-1 |
cd14626 |
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ... |
1107-1381 |
4.38e-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: 250.72 E-value: 4.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1107 SEYKSYYQRKHADTDIGFAEEYQGLaNVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPG 1186
Cdd:cd14626 1 SDLADNIERLKANDGLKFSQEYESI-DPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1187 YHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSClYGDIVVNIVSEETSPEWTTRK 1266
Cdd:cd14626 80 YRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTET-YGMIQVTLLDTVELATYSVRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1267 FNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKE 1346
Cdd:cd14626 159 FALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKA-CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHE 237
|
250 260 270
....*....|....*....|....*....|....*
gi 1822521639 1347 AVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14626 238 KTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
|
|
| PTPc-KIM |
cd14547 |
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ... |
1152-1377 |
6.20e-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: 6.20e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1152 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGY-HLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEqNR 1230
Cdd:cd14547 1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1231 VKCERYWPMDMSScLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQR-MMRD 1309
Cdd:cd14547 80 EKCAQYWPEEENE-TYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQeVEEA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 1310 YLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14547 157 RQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
|
|
| R-PTPc-M-1 |
cd14633 |
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ... |
1123-1381 |
1.02e-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: 1.02e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1123 GFAEEYQGLANvGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPN 1202
Cdd:cd14633 16 GFKEEYESFFE-GQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1203 TVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSscLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQ 1282
Cdd:cd14633 95 TIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1283 FHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNrAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSR 1362
Cdd:cd14633 173 FHFTGWPDHGVPYHATGLLGFVRQVKSKSPPN-AGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRR 251
|
250
....*....|....*....
gi 1822521639 1363 TCMVQTENQYIFLHQCILD 1381
Cdd:cd14633 252 VNMVQTEEQYVFIHDAILE 270
|
|
| R-PTPc-A-1 |
cd14621 |
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ... |
1101-1381 |
5.19e-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: 5.19e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1101 FKPIPVSEYKSYYQRKHADTDIGFAEEYQGLANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYIN 1180
Cdd:cd14621 5 YPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYIN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1181 ASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEETSP 1260
Cdd:cd14621 85 ASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP-DQGCWTYGNIRVSVEDVTVLV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1261 EWTTRKFNVKK----TGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTLIAL 1336
Cdd:cd14621 164 DYTVRKFCIQQvgdvTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKN-CNPQYAGAIVVHCSAGVGRTGTFIVI 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1822521639 1337 DYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14621 243 DAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287
|
|
| R-PTPc-S-1 |
cd14625 |
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ... |
1103-1384 |
1.68e-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: 243.85 E-value: 1.68e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1103 PIPVSEYKSYYQRKHADTDIGFAEEYQGLaNVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINAS 1182
Cdd:cd14625 3 PIPISELAEHTERLKANDNLKLSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1183 YMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEETSPEW 1262
Cdd:cd14625 82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP-SRGTETYGMIQVTLLDTIELATF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1263 TTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQR 1342
Cdd:cd14625 161 CVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKT-CNPPDAGPIVVHCSAGVGRTGCFIVIDAMLER 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1822521639 1343 IEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDVTG 1384
Cdd:cd14625 240 IKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVA 281
|
|
| R-PTPc-G-1 |
cd17667 |
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ... |
1124-1381 |
2.87e-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: 2.87e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1124 FAEEYQGL--ANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQP--NSSSSDYINASYMPGYHLDKAFIAAQGP 1199
Cdd:cd17667 1 FSEDFEEVqrCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPgkDSKHSDYINANYVDGYNKAKAYIATQGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1200 LPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEETSPEWTTRKFNVKKT------- 1272
Cdd:cd17667 81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE-EYGNIIVTLKSTKIHACYTVRRFSIRNTkvkkgqk 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1273 ----GCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRmmrdylNKNRAGLP-----VVHCSAGVGRTGTLIALDYLLQRI 1343
Cdd:cd17667 160 gnpkGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVR------RSSAARTPemgpvLVHCSAGVGRTGTYIVIDSMLQQI 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 1822521639 1344 EKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
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 ... |
1145-1380 |
2.94e-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: 2.94e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1145 VPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTN 1224
Cdd:cd14554 3 LPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1225 CVEQNRVKCERYWPMDmSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQF- 1303
Cdd:cd14554 83 LREMGREKCHQYWPAE-RSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFi 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521639 1304 QRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1380
Cdd:cd14554 162 GQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
|
|
| R-PTPc-C-1 |
cd14557 |
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ... |
1178-1377 |
3.79e-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: 3.79e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWP-MDMSSCLYGDIVVNIVSE 1256
Cdd:cd14557 1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsMEEGSRAFGDVVVKINEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1257 ETSPEWTTRKFNV--KKTGCPEpRTITQFHFTSWPDHGVPKTTDKLLQFQRMMrDYLNKNRAGLPVVHCSAGVGRTGTLI 1334
Cdd:cd14557 81 KICPDYIIRKLNInnKKEKGSG-REVTHIQFTSWPDHGVPEDPHLLLKLRRRV-NAFNNFFSGPIVVHCSAGVGRTGTYI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1822521639 1335 ALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14557 159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
|
|
| R-PTPc-D-1 |
cd14624 |
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ... |
1103-1381 |
4.49e-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: 4.49e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1103 PIPVSEYKSYYQRKHADTDIGFAEEYQGLaNVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINAS 1182
Cdd:cd14624 3 PIPILELADHIERLKANDNLKFSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1183 YMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEETSPEW 1262
Cdd:cd14624 82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWP-SRGTETYGLIQVTLLDTVELATY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1263 TTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQR 1342
Cdd:cd14624 161 CVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKT-CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLER 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 1822521639 1343 IEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14624 240 IKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
|
|
| R-PTPc-typeIIb-1 |
cd14555 |
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ... |
1178-1381 |
6.21e-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: 6.21e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDmsSCLYGDIVVNIVSEE 1257
Cdd:cd14555 1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD--TEVYGDIKVTLVETE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1258 TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdYLNKNRAGLPVVHCSAGVGRTGTLIALD 1337
Cdd:cd14555 79 PLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVK-ASNPPSAGPIVVHCSAGAGRTGCYIVID 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1822521639 1338 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14555 158 IMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
|
|
| PTPc-N11_6 |
cd14544 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ... |
1148-1379 |
7.47e-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: 7.47e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1148 NKVKNRYTNIFPYDVARVKL-DRQPNSSSSDYINASYM-----PGYHLD--KAFIAAQGPLPNTVVDFWRMVWEQKTKVI 1219
Cdd:cd14544 1 NKGKNRYKNILPFDHTRVILkDRDPNVPGSDYINANYIrneneGPTTDEnaKTYIATQGCLENTVSDFWSMVWQENSRVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1220 VMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEP-RTITQFHFTSWPDHGVPKTTD 1298
Cdd:cd14544 81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPiREIWHYQYLSWPDHGVPSDPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1299 KLLQF-QRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAV---VDVYGIVHNMRMSRTCMVQTENQYIF 1374
Cdd:cd14544 161 GVLNFlEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKF 240
|
....*
gi 1822521639 1375 LHQCI 1379
Cdd:cd14544 241 IYVAV 245
|
|
| R-PTPc-E-1 |
cd14620 |
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ... |
1154-1381 |
1.08e-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: 1.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1154 YTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKC 1233
Cdd:cd14620 1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1234 ERYWPmDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKT---GCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDy 1310
Cdd:cd14620 81 YQYWP-DQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521639 1311 LNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14620 159 VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
|
|
| PTP_fungal |
cd18533 |
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ... |
1178-1377 |
2.38e-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: 2.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYM-PGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSE 1256
Cdd:cd18533 1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1257 ET--SPEWTTRKFNVKKTGCPePRTITQFHFTSWPDHGVPKTTDKLLQfqrMMR--DYLNKN-RAGLP-VVHCSAGVGRT 1330
Cdd:cd18533 81 EEndDGGFIVREFELSKEDGK-VKKVYHIQYKSWPDFGVPDSPEDLLT---LIKlkRELNDSaSLDPPiIVHCSAGVGRT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521639 1331 GTLIALDYLLQRIEKEAVVD---------VYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd18533 157 GTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
|
|
| R-PTPc-K-1 |
cd14631 |
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ... |
1164-1381 |
2.81e-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: 2.81e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1164 RVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSs 1243
Cdd:cd14631 1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1244 cLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdYLNKNRAGLPVVHC 1323
Cdd:cd14631 80 -VYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK-LSNPPSAGPIVVHC 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 1324 SAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14631 158 SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
|
|
| PTPc-N18 |
cd14603 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ... |
1139-1379 |
4.42e-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: 4.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1139 SKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKV 1218
Cdd:cd14603 21 STVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1219 IVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEE-TSPEWTTRKFNVkkTGCPEPRTITQFHFTSWPDHGVPKTT 1297
Cdd:cd14603 101 ILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKrLNEEVILRTLKV--TFQKESRSVSHFQYMAWPDHGIPDSP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1298 DKLLQFQRMMRDYLNKNRAGLpVVHCSAGVGRTGTLIALDY-----LLQRIEKEavVDVYGIVHNMRMSRTCMVQTENQY 1372
Cdd:cd14603 179 DCMLAMIELARRLQGSGPEPL-CVHCSAGCGRTGVICTVDYvrqllLTQRIPPD--FSIFDVVLEMRKQRPAAVQTEEQY 255
|
....*..
gi 1822521639 1373 IFLHQCI 1379
Cdd:cd14603 256 EFLYHTV 262
|
|
| R-PTPc-A-E-1 |
cd14551 |
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ... |
1178-1377 |
6.56e-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: 221.71 E-value: 6.56e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEE 1257
Cdd:cd14551 1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGCWTYGNLRVRVEDTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1258 TSPEWTTRKFNVKK----TGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTL 1333
Cdd:cd14551 80 VLVDYTTRKFCIQKvnrgIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKS-ANPPRAGPIVVHCSAGVGRTGTF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1822521639 1334 IALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14551 159 IVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
|
|
| PTPc-N13 |
cd14597 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ... |
1147-1382 |
7.22e-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: 7.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1147 DNKVKNRYTNIFPYDVARVKLdrqpnSSSSDYINASY--MPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTN 1224
Cdd:cd14597 2 ENRKKNRYKNILPYDTTRVPL-----GDEGGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1225 CVEQNRVKCERYWPMDMSSCLYGD--IVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQ 1302
Cdd:cd14597 77 EVEGGKIKCQRYWPEILGKTTMVDnrLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1303 FQRMMRdylNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1382
Cdd:cd14597 157 FISYMR---HIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILYV 233
|
|
| PTPc-N22_18_12 |
cd14542 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ... |
1178-1377 |
8.43e-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: 8.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSE 1256
Cdd:cd14542 1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLqFGPFKISLEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1257 E-TSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlnKNRAGLPV-VHCSAGVGRTGTLI 1334
Cdd:cd14542 81 KrVGPDFLIRTLKVTFQK--ESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVPIcVHCSAGCGRTGTIC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1822521639 1335 ALDY---LLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14542 157 AIDYvwnLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
|
|
| PTPc-N20_13 |
cd14538 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ... |
1178-1382 |
4.02e-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: 4.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYM------PGYHldkaFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWP--MDMSSCLYGDI 1249
Cdd:cd14538 1 YINASHIripvggDTYH----YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdsLNKPLICGGRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1250 VVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlnkNRAGLPVVHCSAGVGR 1329
Cdd:cd14538 77 EVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRI---HNSGPIVVHCSAGIGR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1822521639 1330 TGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1382
Cdd:cd14538 154 TGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
|
|
| R-PTPc-U-1 |
cd14632 |
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ... |
1178-1381 |
6.83e-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: 6.83e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDmsSCLYGDIVVNIVSEE 1257
Cdd:cd14632 1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD--SDTYGDIKITLLKTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1258 TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNrAGLPVVHCSAGVGRTGTLIALD 1337
Cdd:cd14632 79 TLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPD-AGPVVVHCSAGAGRTGCYIVLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1822521639 1338 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14632 158 VMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
|
|
| R-PTP-S-2 |
cd14627 |
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ... |
1104-1384 |
2.79e-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: 2.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1104 IPVSEYKSYYQR----KHADTDIGFAEEYQGLANVGTNQSKE-AFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDY 1178
Cdd:cd14627 4 VPARNLYSYIQKlaqvEVGEHVTGMELEFKRLANSKAHTSRFiSANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1179 INASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEET 1258
Cdd:cd14627 84 INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1259 SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPV-VHCSAGVGRTGTLIALD 1337
Cdd:cd14627 163 MPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPIsVHCSAGVGRTGVFITLS 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1822521639 1338 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDVTG 1384
Cdd:cd14627 243 IVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLG 289
|
|
| PTPc-N1_2 |
cd14545 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ... |
1151-1374 |
4.51e-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: 4.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1151 KNRYTNIFPYDVARVKLdrqpNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNR 1230
Cdd:cd14545 3 RYRDRDPYDHDRSRVKL----KQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1231 VKCERYWPMDMSS---CLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMM 1307
Cdd:cd14545 79 IKCAQYWPQGEGNamiFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521639 1308 RDY--LNKNrAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAV--VDVYGIVHNMRMSRTCMVQTENQYIF 1374
Cdd:cd14545 159 RESgsLSSD-VGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
|
|
| PTPc-N3_4 |
cd14541 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ... |
1177-1382 |
4.64e-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: 4.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1177 DYINASY----MPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVN 1252
Cdd:cd14541 1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1253 IVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdylnKNRAGL--P-VVHCSAGVGR 1329
Cdd:cd14541 81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVR----QNRVGMvePtVVHCSAGIGR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1822521639 1330 TGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1382
Cdd:cd14541 157 TGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
|
|
| PTPc-N12 |
cd14604 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ... |
1106-1379 |
8.48e-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: 8.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1106 VSEYKSYYQRKHADTDiGFAEEYQGLANVGTNQSKEAF------QVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYI 1179
Cdd:cd14604 10 IERVQAMKSTDHNGED-NFASDFMRLRRLSTKYRTEKIyptatgEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1180 NASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSEET 1258
Cdd:cd14604 89 NANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMtFGPFRISCEAEQA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1259 SPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlnKNRAGLPV-VHCSAGVGRTGTLIALD 1337
Cdd:cd14604 169 RTDYFIRTLLLEFQN--ETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKY--QEHEDVPIcIHCSAGCGRTGAICAID 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1822521639 1338 Y---LLQ--RIEKEavVDVYGIVHNMRMSRTCMVQTENQYIFLHQCI 1379
Cdd:cd14604 245 YtwnLLKagKIPEE--FNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289
|
|
| R-PTPc-Z-1 |
cd17668 |
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ... |
1178-1380 |
9.09e-62 |
|
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: 9.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEE 1257
Cdd:cd17668 1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE-EYGNFLVTQKSVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1258 TSPEWTTRKFNVKKT--------GCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRmMRDYLNKNRAGLPVVHCSAGVGR 1329
Cdd:cd17668 80 VLAYYTVRNFTLRNTkikkgsqkGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVR-KASYAKRHAVGPVVVHCSAGVGR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1822521639 1330 TGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1380
Cdd:cd17668 159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
|
|
| R-PTP-D-2 |
cd14628 |
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ... |
1104-1384 |
3.96e-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: 3.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1104 IPVSEYKSYYQR----KHADTDIGFAEEYQGLANVGTNQSKE-AFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDY 1178
Cdd:cd14628 3 VPARNLYAYIQKltqiETGENVTGMELEFKRLASSKAHTSRFiSANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1179 INASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEET 1258
Cdd:cd14628 83 INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1259 SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPV-VHCSAGVGRTGTLIALD 1337
Cdd:cd14628 162 MPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPIsVHCSAGVGRTGVFITLS 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1822521639 1338 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDVTG 1384
Cdd:cd14628 242 IVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLG 288
|
|
| R-PTP-F-2 |
cd14629 |
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ... |
1127-1384 |
6.67e-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: 6.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1127 EYQGLANVGTNQSKE-AFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVV 1205
Cdd:cd14629 31 EFKLLANSKAHTSRFiSANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1206 DFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHF 1285
Cdd:cd14629 111 DFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQF 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1286 TSWPDHGVPKTTDKLLQF-QRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTC 1364
Cdd:cd14629 190 TDWPEQGVPKTGEGFIDFiGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPA 269
|
250 260
....*....|....*....|
gi 1822521639 1365 MVQTENQYIFLHQCILDVTG 1384
Cdd:cd14629 270 MVQTEDQYQLCYRAALEYLG 289
|
|
| R-PTP-N |
cd14609 |
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ... |
1113-1374 |
4.40e-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: 4.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1113 YQRKHADTDIGFAEEYQGL-ANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINAS-------YM 1184
Cdd:cd14609 6 YMEDHLRNRDRLAKEWQALcAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpiiehdpRM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1185 PgyhldkAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEET-SPEWT 1263
Cdd:cd14609 86 P------AYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWP-DEGSSLYHIYEVNLVSEHIwCEDFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1264 TRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLnKNRAGLPVVHCSAGVGRTGTLIALDYLLQRI 1343
Cdd:cd14609 159 VRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCY-RGRSCPIIVHCSDGAGRTGTYILIDMVLNRM 237
|
250 260 270
....*....|....*....|....*....|..
gi 1822521639 1344 EKEAV-VDVYGIVHNMRMSRTCMVQTENQYIF 1374
Cdd:cd14609 238 AKGVKeIDIAATLEHVRDQRPGMVRTKDQFEF 269
|
|
| PTPc-N11 |
cd14605 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ... |
1147-1379 |
8.79e-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: 8.79e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1147 DNKVKNRYTNIFPYDVARVKL-DRQPNSSSSDYINASY-MPGYHLD-------KAFIAAQGPLPNTVVDFWRMVWEQKTK 1217
Cdd:cd14605 1 ENKNKNRYKNILPFDHTRVVLhDGDPNEPVSDYINANIiMPEFETKcnnskpkKSYIATQGCLQNTVNDFWRMVFQENSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1218 VIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPE-PRTITQFHFTSWPDHGVPKT 1296
Cdd:cd14605 81 VIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNtERTVWQYHFRTWPDHGVPSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1297 TDKLLQF-QRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAV---VDVYGIVHNMRMSRTCMVQTENQY 1372
Cdd:cd14605 161 PGGVLDFlEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQY 240
|
....*..
gi 1822521639 1373 IFLHQCI 1379
Cdd:cd14605 241 RFIYMAV 247
|
|
| R-PTP-C-2 |
cd14558 |
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ... |
1178-1376 |
1.81e-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: 203.01 E-value: 1.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSclYGDIVVNIVSEE 1257
Cdd:cd14558 1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT--YGDIEVELKDTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1258 TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLP-----VVHCSAGVGRTGT 1332
Cdd:cd14558 79 KSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKHGrsvpiVVHCSDGSSRTGI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1822521639 1333 LIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1376
Cdd:cd14558 159 FCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
|
|
| PTPc-N3 |
cd14600 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ... |
1144-1382 |
1.98e-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: 205.85 E-value: 1.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1144 QVPDNKVKNRYTNIFPYDVARVKLDrqpnsSSSDYINASYM----PGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVI 1219
Cdd:cd14600 36 KLPQNMDKNRYKDVLPYDATRVVLQ-----GNEDYINASYVnmeiPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1220 VMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDK 1299
Cdd:cd14600 111 VMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1300 LLQFQRMMRdylNKNRAGLPV-VHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQC 1378
Cdd:cd14600 191 FLEFVNYVR---SKRVENEPVlVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEA 267
|
....
gi 1822521639 1379 ILDV 1382
Cdd:cd14600 268 ILRV 271
|
|
| PTPc-N22 |
cd14602 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ... |
1151-1382 |
2.41e-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: 2.41e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1151 KNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNR 1230
Cdd:cd14602 1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1231 VKCERYWP-MDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRD 1309
Cdd:cd14602 81 KKCERYWAePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS--ETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 1310 YlnKNRAGLPV-VHCSAGVGRTGTLIALDYLLqRIEKEAVV----DVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1382
Cdd:cd14602 159 Y--QEDDSVPIcIHCSAGCGRTGVICAIDYTW-MLLKDGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233
|
|
| PTPc-N6 |
cd14606 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ... |
1136-1380 |
1.33e-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: 200.11 E-value: 1.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1136 TNQSKEAfQVPDNKVKNRYTNIFPYDVARVKLD-RQPNSSSSDYINASYMPGYHL-----DKAFIAAQGPLPNTVVDFWR 1209
Cdd:cd14606 7 LHQRLEG-QRPENKSKNRYKNILPFDHSRVILQgRDSNIPGSDYINANYVKNQLLgpdenAKTYIASQGCLEATVNDFWQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1210 MVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPE-PRTITQFHFTSW 1288
Cdd:cd14606 86 MAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGElIREIWHYQYLSW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1289 PDHGVPKTTDKLLQFQrmmrDYLNKNRAGLP-----VVHCSAGVGRTGTLIALDYLLQRIEKEAV---VDVYGIVHNMRM 1360
Cdd:cd14606 166 PDHGVPSEPGGVLSFL----DQINQRQESLPhagpiIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRA 241
|
250 260
....*....|....*....|
gi 1822521639 1361 SRTCMVQTENQYIFLHQCIL 1380
Cdd:cd14606 242 QRSGMVQTEAQYKFIYVAIA 261
|
|
| PTPc-N7 |
cd14612 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ... |
1139-1376 |
2.58e-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: 2.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1139 SKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSS-SSDYINASYMPGYH-LDKAFIAAQGPLPNTVVDFWRMVWEQKT 1216
Cdd:cd14612 6 SPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQEeEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEEC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1217 KVIVMLTNCVEQNRvKCERYWPMDMSSclYG--DIVVNIVSEetSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVP 1294
Cdd:cd14612 86 PIIVMITKLKEKKE-KCVHYWPEKEGT--YGrfEIRVQDMKE--CDGYTIRDLTIQLEE--ESRSVKHYWFSSWPDHQTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1295 KTTDKLLQFQRMMRDYLNKNRA-GLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYI 1373
Cdd:cd14612 159 ESAGPLLRLVAEVEESRQTAASpGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQ 238
|
...
gi 1822521639 1374 FLH 1376
Cdd:cd14612 239 FLH 241
|
|
| R-PTPc-A-E-2 |
cd14552 |
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ... |
1178-1379 |
6.92e-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: 6.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDmSSCLYGDIVVNIVSEE 1257
Cdd:cd14552 1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPED-GSVSSGDITVELKDQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1258 TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALD 1337
Cdd:cd14552 80 DYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1822521639 1338 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCI 1379
Cdd:cd14552 160 TVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
|
|
| R-PTP-N2 |
cd14610 |
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ... |
1144-1374 |
1.05e-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: 1.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1144 QVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINAS-YMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVML 1222
Cdd:cd14610 40 QREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVML 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1223 TNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEET-SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLL 1301
Cdd:cd14610 120 TPLAENGVKQCYHYWP-DEGSNLYHIYEVNLVSEHIwCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLL 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822521639 1302 QFQRMMrDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAV-VDVYGIVHNMRMSRTCMVQTENQYIF 1374
Cdd:cd14610 199 DFRRKV-NKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQFEF 271
|
|
| PTPc-N2 |
cd14607 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ... |
1137-1379 |
1.17e-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: 191.33 E-value: 1.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1137 NQSKE-AFQV---PDNKVKNRYTNIFPYDVARVKLDRQPNssssDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVW 1212
Cdd:cd14607 9 NESHDyPHRVakyPENRNRNRYRDVSPYDHSRVKLQNTEN----DYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1213 EQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLY---GDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWP 1289
Cdd:cd14607 85 QQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSfkeTGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1290 DHGVPKTTDKLLQFQRMMRDYLNKN-RAGLPVVHCSAGVGRTGTLIALDYLLQRIEKE--AVVDVYGIVHNMRMSRTCMV 1366
Cdd:cd14607 165 DFGVPESPASFLNFLFKVRESGSLSpEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKdpDSVDIKQVLLDMRKYRMGLI 244
|
250
....*....|...
gi 1822521639 1367 QTENQYIFLHQCI 1379
Cdd:cd14607 245 QTPDQLRFSYMAV 257
|
|
| PTPc-N20 |
cd14596 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ... |
1178-1382 |
1.96e-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: 188.80 E-value: 1.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASY--MPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIV 1254
Cdd:cd14596 1 YINASYitMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMeLENYQLRLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1255 SEETSPEWTTRKFNV--KKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKnraGLPVVHCSAGVGRTGT 1332
Cdd:cd14596 81 NYQALQYFIIRIIKLveKETG--ENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT---GPIVVHCSAGIGRAGV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1333 LIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1382
Cdd:cd14596 156 LICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
|
|
| R-PTPc-R |
cd14611 |
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ... |
1151-1377 |
1.03e-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: 1.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1151 KNRYTNIFPYDVARVKLD-RQPNSSSSDYINASYMPGYH-LDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQ 1228
Cdd:cd14611 2 KNRYKTILPNPHSRVCLKpKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1229 NRvKCERYWPMDMSscLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQ-RMM 1307
Cdd:cd14611 82 NE-KCVLYWPEKRG--IYGKVEVLVNSVKECDNYTIRNLTLKQGS--QSRSVKHYWYTSWPDHKTPDSAQPLLQLMlDVE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1308 RDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14611 157 EDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
|
|
| R-PTPc-A-2 |
cd14623 |
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ... |
1153-1379 |
1.19e-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: 1.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1153 RYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVK 1232
Cdd:cd14623 1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1233 CERYWPMDmSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLN 1312
Cdd:cd14623 81 CAQYWPSD-GSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521639 1313 KNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCI 1379
Cdd:cd14623 160 QSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
|
|
| PTPc-N1 |
cd14608 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ... |
1124-1390 |
1.22e-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: 1.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1124 FAEEYQGLANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNssssDYINASYMPGYHLDKAFIAAQGPLPNT 1203
Cdd:cd14608 1 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDN----DYINASLIKMEEAQRSYILTQGPLPNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1204 VVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLY---GDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTI 1280
Cdd:cd14608 77 CGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIfedTNLKLTLISEDIKSYYTVRQLELENLTTQETREI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1281 TQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKN-RAGLPVVHCSAGVGRTGTLIALDYLLQRIEKE---AVVDVYGIVH 1356
Cdd:cd14608 157 LHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSpEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDIKKVLL 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 1822521639 1357 NMRMSRTCMVQTENQYIFLHQCILD----VTGDKSIDE 1390
Cdd:cd14608 237 EMRKFRMGLIQTADQLRFSYLAVIEgakfIMGDSSVQD 274
|
|
| R-PTPc-E-2 |
cd14622 |
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ... |
1177-1381 |
5.82e-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: 5.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1177 DYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDmSSCLYGDIVVNIVSE 1256
Cdd:cd14622 1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSE-GSVTHGEITIEIKND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1257 ETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIAL 1336
Cdd:cd14622 80 TLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGTFIAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1822521639 1337 DYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14622 160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204
|
|
| PTPc-N4 |
cd14601 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ... |
1177-1382 |
8.26e-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: 8.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1177 DYINASYM----PGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVN 1252
Cdd:cd14601 1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1253 IVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdylnKNRAGLP---VVHCSAGVGR 1329
Cdd:cd14601 81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVR----NKRAGKDepvVVHCSAGIGR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1822521639 1330 TGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1382
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 ... |
1178-1379 |
1.04e-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: 1.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMpgYHLD---KAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSClYGDIVVNIV 1254
Cdd:cd14546 1 YINASTI--YDHDprnPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEV-YHIYEVHLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1255 SEET-SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMmrdyLNKNRAGLP---VVHCSAGVGRT 1330
Cdd:cd14546 78 SEHIwCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRK----VNKSYRGRScpiVVHCSDGAGRT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1331 GTLIALDYLLQRIEKEAV-VDVYGIVHNMRMSRTCMVQTENQYIFLHQCI 1379
Cdd:cd14546 154 GTYILIDMVLNRMAKGAKeIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203
|
|
| PTPc-N21_14 |
cd14540 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ... |
1178-1382 |
3.63e-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: 179.96 E-value: 3.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKA--FIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL---YGDIVVN 1252
Cdd:cd14540 1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHDaltFGEYKVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1253 IVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQF--------QRMMRDYLNKNRAGLPVVHCS 1324
Cdd:cd14540 81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsvrRHTNQDVAGHNRNPPTLVHCS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 1325 AGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1382
Cdd:cd14540 161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
|
|
| PTP-N23 |
cd14539 |
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ... |
1178-1377 |
1.43e-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: 1.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGY-HLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVS 1255
Cdd:cd14539 1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALvYGAITVSLQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1256 EETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRA-GLP-VVHCSAGVGRTGTL 1333
Cdd:cd14539 81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSlQTPiVVHCSSGVGRTGAF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1822521639 1334 IALDYLLQRIEKE-AVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14539 161 CLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
|
|
| PTPc-N5 |
cd14613 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ... |
1140-1376 |
4.80e-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: 4.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1140 KEAFQVPDNKV------------KNRYTNIFPYDVARVKL-DRQPNSSSSDYINASYMPGY-HLDKAFIAAQGPLPNTVV 1205
Cdd:cd14613 5 AEFFEIPMNFVdpkeydipglvrKNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1206 DFWRMVWEQKTKVIVMLTNCVEQNRvKCERYWPMDmsSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHF 1285
Cdd:cd14613 85 DFWRMVWQERSPIIVMITNIEEMNE-KCTEYWPEE--QVTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1286 TSWPDHGVPKTTDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRT 1363
Cdd:cd14613 160 TSWPDQKTPDNAPPLLQLVQEVEEARQQAEPncGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRG 239
|
250
....*....|...
gi 1822521639 1364 CMVQTENQYIFLH 1376
Cdd:cd14613 240 GMIQTCEQYQFVH 252
|
|
| R-PTPc-typeIIb-2 |
cd14556 |
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ... |
1178-1377 |
9.66e-45 |
|
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: 9.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLtNCVEQNRVKCERYWPMDMSSClYGDIVVNIVSEE 1257
Cdd:cd14556 1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGT-YGPIQVEFVSTT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1258 TSPEWTTRKFNVKKTGCPEP--RTITQFHFTSWPDHG-VPKTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLI 1334
Cdd:cd14556 79 IDEDVISRIFRLQNTTRPQEgyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRSGVFC 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1822521639 1335 ALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14556 159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
|
|
| COG5599 |
COG5599 |
Protein tyrosine phosphatase [Signal transduction mechanisms]; |
1136-1375 |
4.55e-43 |
|
Protein tyrosine phosphatase [Signal transduction mechanisms];
Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 159.10 E-value: 4.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1136 TNQSKEAFQVPDNKVKNRYTNIFPYDVARVkldrqpnSSSSDYINASY--MPGYHLdkaFIAAQGPLPNTVVDFWRMVWE 1213
Cdd:COG5599 30 SHNDPQYLQNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYiqVIGNHR---YIATQYPLEEQLEDFFQMLFD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1214 QKTKVIVMLTNCVE--QNRVKCERYWPMDMSsclYGDIVVNIVSEET---SPEWTTRKFNVKKTGC-PEPRTITQFHFTS 1287
Cdd:COG5599 100 NNTPVLVVLASDDEisKPKVKMPVYFRQDGE---YGKYEVSSELTESiqlRDGIEARTYVLTIKGTgQKKIEIPVLHVKN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1288 WPDHGVPkTTDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTLIALDYLLQRI--EKEAVVDVYGIVHNMRMSRT 1363
Cdd:COG5599 177 WPDHGAI-SAEALKNLADLIDKKEKIKDPdkLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRN 255
|
250
....*....|...
gi 1822521639 1364 C-MVQTENQYIFL 1375
Cdd:COG5599 256 GgMVQTSEQLDVL 268
|
|
| PTPc_plant_PTP1 |
cd17658 |
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ... |
1178-1374 |
1.69e-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: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYM--PGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNR-VKCERYWPM-DMSSCLYGDIVVNI 1253
Cdd:cd17658 1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAeENESREFGRISVTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1254 VSEETSPE-WTTRKFNVKKTGCPE-PRTITQFHFTSWPDHGVPKTTDKLLQFQRmmRDYLNKNRAGLPVVHCSAGVGRTG 1331
Cdd:cd17658 81 KKLKHSQHsITLRVLEVQYIESEEpPLSVLHIQYPEWPDHGVPKDTRSVRELLK--RLYGIPPSAGPIVVHCSAGIGRTG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1822521639 1332 TLIALDYLLQRIEKEAV--VDVYGIVHNMRMSRTCMVQTENQYIF 1374
Cdd:cd17658 159 AYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIF 203
|
|
| PTPc-N14 |
cd14599 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ... |
1145-1380 |
1.73e-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: 157.47 E-value: 1.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1145 VPDNKVKNRYTNIFPYDVARVKLdrQPN-SSSSDYINASYMP------GYHldkaFIAAQGPLPNTVVDFWRMVWEQKTK 1217
Cdd:cd14599 35 LPENAERNRIREVVPYEENRVEL--VPTkENNTGYINASHIKvtvggeEWH----YIATQGPLPHTCHDFWQMVWEQGVN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1218 VIVMLTNCVEQNRVKCERYWP---MDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVP 1294
Cdd:cd14599 109 VIAMVTAEEEGGRSKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1295 KTTDKLLQFQ---RMMRDYLN------KNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCM 1365
Cdd:cd14599 189 EEVQGFLSYLeeiQSVRRHTNsmldstKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFM 268
|
250
....*....|....*
gi 1822521639 1366 VQTENQYIFLHQCIL 1380
Cdd:cd14599 269 IQTIAQYKFVYQVLI 283
|
|
| PHA02738 |
PHA02738 |
hypothetical protein; Provisional |
1148-1404 |
7.48e-42 |
|
hypothetical protein; Provisional
Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 156.62 E-value: 7.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1148 NKVKNRYTNIFPYDVARVKLDRQPNSSssDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1227
Cdd:PHA02738 49 NRKLNRYLDAVCFDHSRVILPAERNRG--DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1228 QNRVKCERYWP-MDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKtGCPEPRTITQFHFTSWPDHGVPKTTDKLLQF--- 1303
Cdd:PHA02738 127 NGREKCFPYWSdVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFvle 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1304 ----QRMM---RDYLNKNRAGLP--VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIF 1374
Cdd:PHA02738 206 vrqcQKELaqeSLQIGHNRLQPPpiVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFF 285
|
250 260 270
....*....|....*....|....*....|...
gi 1822521639 1375 LHQCI---LDVTGDKSIDEPIYENQADLIYENV 1404
Cdd:PHA02738 286 CYRAVkryVNLTVNKVSKKLIPNVQTVSFNKNL 318
|
|
| PHA02747 |
PHA02747 |
protein tyrosine phosphatase; Provisional |
1127-1411 |
4.55e-41 |
|
protein tyrosine phosphatase; Provisional
Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 154.39 E-value: 4.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1127 EYQGLANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQpNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVD 1206
Cdd:PHA02747 30 EHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSG-GGSTSDYIHANWIDGFEDDKKFIATQGPFAETCAD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1207 FWRMVWEQKTKVIVMLTNCVEQN-RVKCERYW-PMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFH 1284
Cdd:PHA02747 109 FWKAVWQEHCSIIVMLTPTKGTNgEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1285 FTSWPDHGVPKTTDKLLQF--------QRMMRDYLNKNRAGLP-VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIV 1355
Cdd:PHA02747 189 CSEWFEDETPSDHPDFIKFikiidinrKKSGKLFNPKDALLCPiVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTA 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521639 1356 HNMRMSRTCMVQTENQYIFLhqcildvtgdksidEPIYENQADLIYENVDAIKVAN 1411
Cdd:PHA02747 269 EKIREQRHAGIMNFDDYLFI--------------QPGYEVLHYFLSKIKAIDKIKF 310
|
|
| PTPc_motif |
smart00404 |
Protein tyrosine phosphatase, catalytic domain motif; |
1279-1381 |
3.24e-40 |
|
Protein tyrosine phosphatase, catalytic domain motif;
Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 144.04 E-value: 3.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1279 TITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLP-VVHCSAGVGRTGTLIALDYLLQRIEKEA-VVDVYGIVH 1356
Cdd:smart00404 1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPvVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80
|
90 100
....*....|....*....|....*
gi 1822521639 1357 NMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:smart00404 81 ELRSQRPGMVQTEEQYLFLYRALLE 105
|
|
| PTPc_DSPc |
smart00012 |
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ... |
1279-1381 |
3.24e-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: 3.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1279 TITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLP-VVHCSAGVGRTGTLIALDYLLQRIEKEA-VVDVYGIVH 1356
Cdd:smart00012 1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPvVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80
|
90 100
....*....|....*....|....*
gi 1822521639 1357 NMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:smart00012 81 ELRSQRPGMVQTEEQYLFLYRALLE 105
|
|
| PHA02742 |
PHA02742 |
protein tyrosine phosphatase; Provisional |
1148-1380 |
8.38e-38 |
|
protein tyrosine phosphatase; Provisional
Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 144.37 E-value: 8.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1148 NKVKNRYTNIFPYDVARVKLDRQpnSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1227
Cdd:PHA02742 52 NMKKCRYPDAPCFDRNRVILKIE--DGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1228 QNRVKCERYW-PMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRM 1306
Cdd:PHA02742 130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1307 MR--------DYLNKNRAGLP--VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1376
Cdd:PHA02742 210 VReadlkadvDIKGENIVKEPpiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289
|
....
gi 1822521639 1377 QCIL 1380
Cdd:PHA02742 290 FIVL 293
|
|
| R-PTPc-T-2 |
cd14634 |
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ... |
1178-1381 |
1.92e-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: 1.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTncvEQNRVK-CERYWPmDMSSCLYGDIVVNIVSE 1256
Cdd:cd14634 1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDAAQlCMQYWP-EKTSCCYGPIQVEFVSA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1257 ETSPEWTTRKFNVKKTGCPEP--RTITQFHFTSWPDH-GVPKTTDKLLQFQRMMRDYLNK--NRAGLPVVHCSAGVGRTG 1331
Cdd:cd14634 77 DIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydGREGRTVVHCLNGGGRSG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1332 TLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14634 157 TFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
|
|
| PTPc-N21 |
cd14598 |
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ... |
1178-1380 |
5.24e-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: 133.56 E-value: 5.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMP----GYHLDkaFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMS---SCLYGDIV 1250
Cdd:cd14598 1 YINASHIKvtvgGKEWD--YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSrhnTVTYGRFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1251 VNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQF-------QRMMRDYLNKNRAGLPV-VH 1322
Cdd:cd14598 79 ITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsvRRHTNSTIDPKSPNPPVlVH 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 1323 CSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1380
Cdd:cd14598 159 CSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLI 216
|
|
| PHA02746 |
PHA02746 |
protein tyrosine phosphatase; Provisional |
1146-1379 |
3.14e-34 |
|
protein tyrosine phosphatase; Provisional
Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 134.77 E-value: 3.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1146 PDNKVKNRYTNIFPYDVARVKL------------DRQPN-------SSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVD 1206
Cdd:PHA02746 49 KENLKKNRFHDIPCWDHSRVVInaheslkmfdvgDSDGKkievtseDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1207 FWRMVWEQKTKVIVMLTNcVEQNRVKCERYWPMDMSSCL-YGDIVVNI--VSEETSpeWTTRKFNVKKTGCPEPRTITQF 1283
Cdd:PHA02746 129 FFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSELaFGRFVAKIldIIEELS--FTKTRLMITDKISDTSREIHHF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1284 HFTSWPDHGVPKTTDKLLQF--------QRMMRDYLNKNRAGLP-VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGI 1354
Cdd:PHA02746 206 WFPDWPDNGIPTGMAEFLELinkvneeqAELIKQADNDPQTLGPiVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285
|
250 260
....*....|....*....|....*
gi 1822521639 1355 VHNMRMSRTCMVQTENQYIFLHQCI 1379
Cdd:PHA02746 286 VLKIRKQRHSSVFLPEQYAFCYKAL 310
|
|
| R-PTPc-U-2 |
cd14637 |
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ... |
1178-1381 |
2.50e-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: 2.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV-KCERYWPmDMSSCLYGDIVVNIVSE 1256
Cdd:cd14637 1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP-EPGLQQYGPMEVEFVSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1257 ETSPEWTTRKFNVKKTG--CPEPRTITQFHFTSW-PDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTL 1333
Cdd:cd14637 80 SADEDIVTRLFRVQNITrlQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1822521639 1334 IALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14637 160 CASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
|
|
| R-PTPc-M-2 |
cd14635 |
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ... |
1178-1381 |
6.76e-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: 6.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLtNCVEQNRVkCERYWPmDMSSCLYGDIVVNIVSEE 1257
Cdd:cd14635 1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVML-NDVDPAQL-CPQYWP-ENGVHRHGPIQVEFVSAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1258 TSPEWTTRKFNVKKTGCPEP--RTITQFHFTSWPDH-GVPKTTDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGT 1332
Cdd:cd14635 78 LEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGgeGRTVVHCLNGGGRSGT 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1822521639 1333 LIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14635 158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
|
|
| R5-PTP-2 |
cd14550 |
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ... |
1178-1377 |
1.06e-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: 111.64 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCveQNRVKCERYWPMDMSSCLYGDIVVNIVSEE 1257
Cdd:cd14550 1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN--ELNEDEPIYWPTKEKPLECETFKVTLSGED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1258 TSPEW-----TTRKFNVKKTGCPEPRTITQFHFTSWPDHGVP-KTTDKLLQ-FQRmmrdyLNKNRAGLPVVHCSAGVGRT 1330
Cdd:cd14550 79 HSCLSneirlIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPiHTVFELINtVQE-----WAQQRDGPIVVHDRYGGVQA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1822521639 1331 GTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14550 154 ATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
|
|
| R-PTPc-K-2 |
cd14636 |
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ... |
1178-1381 |
2.58e-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: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTncvEQNRVK-CERYWPmDMSSCLYGDIVVNIVSE 1256
Cdd:cd14636 1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN---EVDLAQgCPQYWP-EEGMLRYGPIQVECMSC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1257 ETSPEWTTRKFNVKKTGCPEP--RTITQFHFTSWPDH-GVPKTTDKLLQFQRMMRDYLNK--NRAGLPVVHCSAGVGRTG 1331
Cdd:cd14636 77 SMDCDVISRIFRICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEEcdEGEGRTIIHCLNGGGRSG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1332 TLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14636 157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
|
|
| R-PTP-Z-2 |
cd17669 |
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ... |
1178-1380 |
8.46e-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: 8.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNcvEQNRVKCE-RYWPMDMSSCLYGDIVVNIVSE 1256
Cdd:cd17669 1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPD--GQNMAEDEfVYWPNKDEPINCETFKVTLIAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1257 E-----TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPktTDKLLQFQRMMRDYlNKNRAGLPVVHCSAGVGRTG 1331
Cdd:cd17669 79 EhkclsNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSP--ISKTFELISIIKEE-AANRDGPMIVHDEHGGVTAG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1822521639 1332 TLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1380
Cdd:cd17669 156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
|
|
| R-PTP-G-2 |
cd17670 |
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ... |
1178-1380 |
1.25e-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: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNcvEQNRVKCER-YWPMDMSSCLYGDIVVNIVSE 1256
Cdd:cd17670 1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEFvYWPSREESMNCEAFTVTLISK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1257 E-----TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTD----KLLQFQRMMRDylnknraGLPVVHCSAGV 1327
Cdd:cd17670 79 DrlclsNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTfeliNVIKEEALTRD-------GPTIVHDEFGA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1822521639 1328 GRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1380
Cdd:cd17670 152 VSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
|
|
| PTP_YopH-like |
cd14559 |
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ... |
1152-1372 |
1.10e-19 |
|
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: 89.38 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1152 NRYTNIfpydVARVKLDRQPNssssdyINASYMP--GYHLdkaFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQN 1229
Cdd:cd14559 1 NRFTNI----QTRVSTPVGKN------LNANRVQigNKNV---AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1230 RVKCERYWPMdmsSCLYGDIVVNivSEETSPEWTTRKFNVK----KTGCPEPR-TITQFHFTSWPDHG------------ 1292
Cdd:cd14559 68 RKGLPPYFRQ---SGTYGSVTVK--SKKTGKDELVDGLKADmynlKITDGNKTiTIPVVHVTNWPDHTaisseglkelad 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1293 -VPKTTDKLLQF--QRMMRDYLNKNRaGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDvygIVHNMRMSRTC-MVQT 1368
Cdd:cd14559 143 lVNKSAEEKRNFykSKGSSAINDKNK-LLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVED---IVSDMRTSRNGkMVQK 218
|
....
gi 1822521639 1369 ENQY 1372
Cdd:cd14559 219 DEQL 222
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
386-940 |
6.35e-16 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 83.13 E-value: 6.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 386 SVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTAT 465
Cdd:COG3401 30 GGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 466 GLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWT 545
Cdd:COG3401 110 GLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 546 QSTSKDETtftatRLQPGDQYLLSVQSVTPEDTLSTPAQV---TSTTNPSPVTGLSVVNGTTESLTIEWTSPNDTRASNY 622
Cdd:COG3401 190 TTLVDGGG-----DIEPGTTYYYRVAATDTGGESAPSNEVsvtTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 623 iyNVTVTNVTGGvSWTQSTSKDETTFTATRLQPGDQYQLSVQSVTPEDTLSTPVEV----TSTTNPSPVTGLSVVNGTTQ 698
Cdd:COG3401 265 --RVYRSNSGDG-PFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 699 SLTIEWTRPTDTRASNYT-YRVTvtnvTGGVSWSK-STSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVKSTTD 776
Cdd:COG3401 342 SITLSWTASSDADVTGYNvYRST----SGGGTYTKiAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATT 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 777 PSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSKGETTFTVTGLQPGDQYRLSVRSVTPED 856
Cdd:COG3401 418 ASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLV 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 857 TWSTPAQVTSTSNPSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAIDTGPGVTTFTVTNLVPGV 936
Cdd:COG3401 498 GGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTL 577
|
....
gi 1822521639 937 EYEL 940
Cdd:COG3401 578 GGSL 581
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
36-558 |
7.35e-16 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 82.74 E-value: 7.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 36 VTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTPEDTLS 115
Cdd:COG3401 52 PGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 116 TPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTftatgLQPGDQYQ 195
Cdd:COG3401 132 AGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGD-----IEPGTTYY 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 196 LSVRSVTP--EDTLSTPVEVT-NTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTnvaGGVSSTTITNKG 272
Cdd:COG3401 207 YRVAATDTggESAPSNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYRVYRSNS---GDGPFTKVATVT 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 273 ETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEV----TSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNyiYNVT 348
Cdd:COG3401 284 TTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTG--YNVY 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 349 VTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVT---PEDTLSTPEQVTNTTNPSPVTGLSVVNGTTQSLGIEW 425
Cdd:COG3401 362 RSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGA 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 426 T-------SPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNP 498
Cdd:COG3401 442 TaaasaasNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVG 521
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 499 SPVTGLSVVNGT--------TQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSKDETTFTAT 558
Cdd:COG3401 522 GAPDGTPNVTGAspvtvgasTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNT 589
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
460-938 |
3.13e-15 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 80.82 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 460 TAFTATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTR-ASNYTYNVTVTNV 538
Cdd:COG3401 4 SYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTgGRAGTTSGVAAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 539 TGGVSWTQSTSKDETTFTATRLQPGDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNGTTESLTIEWTSPNDTR 618
Cdd:COG3401 84 VAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 619 ASNYIYNVTVTNVTGGVSWTQSTSKDETTF-TATRLQPGDQYQLSVQSVTP--EDTLSTPVEVT-STTNPSPVTGLSVVN 694
Cdd:COG3401 164 AGAGVVVSPDTSATAAVATTSLTVTSTTLVdGGGDIEPGTTYYYRVAATDTggESAPSNEVSVTtPTTPPSAPTGLTATA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 695 GTTQSLTIEWTRPTDTRASNYT-YRVTvtnvTGGVSWSKSTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVKS 773
Cdd:COG3401 244 DTPGSVTLSWDPVTESDATGYRvYRSN----SGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 774 TT----DPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYtyNVTVTNVTDGASSTTITSKGETTFTVTGLQPGDQYRLSV 849
Cdd:COG3401 320 VTtdltPPAAPSGLTATAVGSSSITLSWTASSDADVTGY--NVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 850 RSVT---PEDTWSTPAQVTSTSNPSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAIDTGPGVTT 926
Cdd:COG3401 398 TAVDaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTV 477
|
490
....*....|..
gi 1822521639 927 FTVTNLVPGVEY 938
Cdd:COG3401 478 TATTTDTTTANL 489
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
59-687 |
1.19e-14 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 78.89 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 59 TRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTPEDTLSTPVEVTSTTNPSPVIGLSVVNGT 138
Cdd:COG3401 12 GIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 139 TQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTATGLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTN 218
Cdd:COG3401 92 TGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 219 PSPVTGLTVVNGTTHSLRIEWTPPTDTRA--TNYTYKVTVTNVAGgvssttitnkgetaftatglqpgdqyqlsvqsvtp 296
Cdd:COG3401 172 PDTSATAAVATTSLTVTSTTLVDGGGDIEpgTTYYYRVAATDTGG----------------------------------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 297 EDTLSTPVEVT-STTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNyiYNVTVTNVTGGvSWTESTSKGETTFTATGLQ 375
Cdd:COG3401 217 ESAPSNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATG--YRVYRSNSGDG-PFTKVATVTTTSYTDTGLT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 376 PGDQYQLSVQSVTPEDTLSTPEQV----TNTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNytYIVTVTNVTGGGRS 451
Cdd:COG3401 294 NGTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTG--YNVYRSTSGGGTYT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 452 TTVTSKGETAFTATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTqsltiEWTRPTDTRASNYTY 531
Cdd:COG3401 372 KIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVD-----AVPLTDVAGATAAAS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 532 NVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNGTTESLTIEW 611
Cdd:COG3401 447 AASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDG 526
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521639 612 TSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPV 687
Cdd:COG3401 527 TPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGVHGGTLLV 602
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
247-833 |
2.97e-12 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 71.19 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 247 ATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQ 326
Cdd:COG3401 16 SAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 327 SLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPS 406
Cdd:COG3401 96 TLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 407 PVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGggrsttvtskgetaftatglqpgdqyqlsvqsvtpEGTL 486
Cdd:COG3401 176 ATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGG-----------------------------------ESAP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 487 STPVEVT-STTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNytYNVTVTNVTGGvSWTQSTSKDETTFTATRLQPGDQ 565
Cdd:COG3401 221 SNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATG--YRVYRSNSGDG-PFTKVATVTTTSYTDTGLTNGTT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 566 YLLSVQSVTPEDTLSTPAQV----TSTTNPSPVTGLSVVNGTTESLTIEWTSPNDTRASNyiYNVTVTNVTGGVSWTQST 641
Cdd:COG3401 298 YYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTG--YNVYRSTSGGGTYTKIAE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 642 SKDETTFTATRLQPGDQYQLSVQSVT---PEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTR-------PTDTR 711
Cdd:COG3401 376 TVTTTSYTDTGLTPGTTYYYKVTAVDaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAaasaasnPGVSA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 712 ASNYTYRVTVTNVTGGVSWSKSTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVKSTTDPSPVTGLSVVNSTTQ 791
Cdd:COG3401 456 AVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASP 535
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1822521639 792 SLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSKGETT 833
Cdd:COG3401 536 VTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTL 577
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
27-372 |
1.93e-11 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 68.49 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 27 SQNVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTvTNVAGGVSSITTTgkNETTFTATGLQPGDQYLLSVR 106
Cdd:COG3401 227 TTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYRVYRS-NSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 107 SVTPEDTLSTPVEV----TSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNytYIVTVTNVTGGVSWTKSTNKDKTT 182
Cdd:COG3401 304 AVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTG--YNVYRSTSGGGTYTKIAETVTTTS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 183 FTATGLQPGDQYQLSVRSVT---PEDTLSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWT-------PPTDTRATNYTY 252
Cdd:COG3401 382 YTDTGLTPGTTYYYKVTAVDaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATaaasaasNPGVSAAVLADG 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 253 KVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGT-------- 324
Cdd:COG3401 462 GDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGAspvtvgas 541
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1822521639 325 TQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTAT 372
Cdd:COG3401 542 TGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNT 589
|
|
| COG4733 |
COG4733 |
Phage-related protein, tail protein J [Mobilome: prophages, transposons]; |
77-598 |
2.02e-10 |
|
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 65.74 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 77 VSSITTTGKNETTFTATGLQPG-----DQYLLSVRSVTPedtlsTPVEVTSTTNpspvigLSVVNGTT--QSLWIEWTSP 149
Cdd:COG4733 493 VVSIEENEDGTYTITAVQHAPEkyaaiDAGAFDDVPPQW-----PPVNVTTSES------LSVVAQGTavTTLTVSWDAP 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 150 TDtrATNYTYIVTVtnvtGGVSWTKSTNKDKTTFTATGLQPGDqYQLSVRSVTPEDTLS---TPVEVT---NTTNPSPVT 223
Cdd:COG4733 562 AG--AVAYEVEWRR----DDGNWVSVPRTSGTSFEVPGIYAGD-YEVRVRAINALGVSSawaASSETTvtgKTAPPPAPT 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 224 GLTVVNGTTHsLRIEWTPPTDTRATnyTYKVTVTNVAGGVSSTTITNKGET-AFTATGLQPGDQYQLSVQSVtpeDTL-- 300
Cdd:COG4733 635 GLTATGGLGG-ITLSWSFPVDADTL--RTEIRYSTTGDWASATVAQALYPGnTYTLAGLKAGQTYYYRARAV---DRSgn 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 301 STPVEVTSTTNPSPVTGLSVVNGttQSLTIEWTSPNDTTASNyiynvtvtnvtggvswteSTSKGETTFTATGLQPGDQY 380
Cdd:COG4733 709 VSAWWVSGQASADAAGILDAITG--QILETELGQELDAIIQN------------------ATVAEVVAATVTDVTAQIDT 768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 381 QLSVQSVTPEDTLSTPEQVTNTTNpSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGET 460
Cdd:COG4733 769 AVLFAGVATAAAIGAEARVAATVA-ESATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAASTTRVAAAVVLAGVVVY 847
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 461 AFTATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEwtrptdTRASNYTYNVTVTNVTG 540
Cdd:COG4733 848 GDAIIESGNTGDIVATGDIASAAAGAVATTVSGTTAADVSAVADSTAASLTAIVIAA------TTIIDAIGDGTTREPAG 921
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 541 GVSWTQSTSKdETTFTATRLQPGDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLS 598
Cdd:COG4733 922 DIGASGGAQG-FAVTIVGSFDGAGAVATVDAGQSVVDGVGTAVEAANGTETAAGGGSQ 978
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
29-886 |
8.62e-10 |
|
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: 8.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 29 NVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSV 108
Cdd:COG3210 820 TITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 109 TPEDTLSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTATGL 188
Cdd:COG3210 900 GTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGT 979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 189 QPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLTVVNGTThslrieWTPPTDTRATNYTYKVTVTNVAGGVSSTTI 268
Cdd:COG3210 980 SANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVT------GTTGTASATGTGTAATAGGQNGVGVNASGI 1053
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 269 TNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVT 348
Cdd:COG3210 1054 SGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTS 1133
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 349 VTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTTQSLGIEWTSP 428
Cdd:COG3210 1134 TASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGT 1213
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 429 TDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVN 508
Cdd:COG3210 1214 TNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGATATGSTVDIGSTSA 1293
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 509 GTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYLLSVQSVTPEDTLSTPAQVTST 588
Cdd:COG3210 1294 TSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNGATDSAAGAGSGGAAGS 1373
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 589 TNPSPVTGLSVVNGTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYQLSVQSVTP 668
Cdd:COG3210 1374 LAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNTTGTSVAGAGGGNA 1453
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 669 EDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSKSTSKGETTFTATGLQP 748
Cdd:COG3210 1454 DASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAEVAKASLEGGEGTYGG 1533
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 749 GDQYQLSVQSVTPEDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITS 828
Cdd:COG3210 1534 SSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNTATLTLSLAEGTNAEYGGTT 1613
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 829 KGETTFTVTGLQPGDQYRLSVRSVTPEDTWSTPAQVTSTSNPSPVSGLTVVNRTTVSI 886
Cdd:COG3210 1614 NVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVD 1671
|
|
| PHA02740 |
PHA02740 |
protein tyrosine phosphatase; Provisional |
1126-1379 |
2.06e-09 |
|
protein tyrosine phosphatase; Provisional
Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 60.37 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1126 EEYQGLANVGTNQSKEAFQVPDNKVK--NRYTNIFPYDVARVKLdrqpnSSSSDYINASYMPGYHLDKAFIAAQGPLPNT 1203
Cdd:PHA02740 29 KEYRAIVPEHEDEANKACAQAENKAKdeNLALHITRLLHRRIKL-----FNDEKVLDARFVDGYDFEQKFICIINLCEDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1204 VVDFWRMVWEQKTKVIVMLTNCVEQNRVkcERYWPMDmSSCLygdIVVNIVSEETSPEWTTRKFNVK------KTGcpEP 1277
Cdd:PHA02740 104 CDKFLQALSDNKVQIIVLISRHADKKCF--NQFWSLK-EGCV---ITSDKFQIETLEIIIKPHFNLTllsltdKFG--QA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1278 RTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDY---LNKNRA----GLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVD 1350
Cdd:PHA02740 176 QKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLcadLEKHKAdgkiAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLS 255
|
250 260
....*....|....*....|....*....
gi 1822521639 1351 VYGIVHNMRMSRTCMVQTENQYIFLHQCI 1379
Cdd:PHA02740 256 IANALKKVRQKKYGCMNCLDDYVFCYHLI 284
|
|
| COG4733 |
COG4733 |
Phage-related protein, tail protein J [Mobilome: prophages, transposons]; |
450-937 |
2.42e-09 |
|
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 62.27 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 450 RSTTVTSKGETAFTATGLQpgdqYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTT--QSLTIEWTRPTDtrAS 527
Cdd:COG4733 492 RVVSIEENEDGTYTITAVQ----HAPEKYAAIDAGAFDDVPPQWPPVNVTTSESLSVVAQGTavTTLTVSWDAPAG--AV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 528 NYTYNVTVtnvtGGVSWTQSTSKDETTFTATRLQPGDqYLLSVQSVTPEDTLSTPAQVTSTT------NPSPVTGLSVVN 601
Cdd:COG4733 566 AYEVEWRR----DDGNWVSVPRTSGTSFEVPGIYAGD-YEVRVRAINALGVSSAWAASSETTvtgktaPPPAPTGLTATG 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 602 GtTESLTIEWTSPNDTRASNYI--YNVTVTNVTGGVSWTQSTSkdeTTFTATRLQPGDQYQLSVQSVtpeDTL--STPVE 677
Cdd:COG4733 641 G-LGGITLSWSFPVDADTLRTEirYSTTGDWASATVAQALYPG---NTYTLAGLKAGQTYYYRARAV---DRSgnVSAWW 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 678 VTSTTNPSPVTGLSVVNGttQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSKSTSKGETTFTATglqpgdqyqlSVQ 757
Cdd:COG4733 714 VSGQASADAAGILDAITG--QILETELGQELDAIIQNATVAEVVAATVTDVTAQIDTAVLFAGVATA----------AAI 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 758 SVTPEDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVtdGASSTTITSKGETTFTVT 837
Cdd:COG4733 782 GAEARVAATVAESATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAASTTRVAAAVVL--AGVVVYGDAIIESGNTGD 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 838 GLQPGDQYRLSVRSVTPEDTWSTPAQVTSTSNPSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGA 917
Cdd:COG4733 860 IVATGDIASAAAGAVATTVSGTTAADVSAVADSTAASLTAIVIAATTIIDAIGDGTTREPAGDIGASGGAQGFAVTIVGS 939
|
490 500
....*....|....*....|
gi 1822521639 918 IDTGPGVTTFTVTNLVPGVE 937
Cdd:COG4733 940 FDGAGAVATVDAGQSVVDGV 959
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
312-388 |
3.76e-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: 54.93 E-value: 3.76e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 312 PSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTE-STSKGETTFTATGLQPGDQYQLSVQSVT 388
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
591-667 |
1.51e-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: 1.51e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 591 PSPVTGLSVVNGTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQ-STSKDETTFTATRLQPGDQYQLSVQSVT 667
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
684-760 |
1.69e-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: 1.69e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 684 PSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSK-STSKGETTFTATGLQPGDQYQLSVQSVT 760
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
871-949 |
3.65e-08 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.03 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 871 SPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGA-IDTGPGVTTFTVTNLVPGVEYELRLQSVTPAG 949
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
219-295 |
4.12e-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: 51.85 E-value: 4.12e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 219 PSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKG-ETAFTATGLQPGDQYQLSVQSVT 295
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPsSTSYTLTGLKPGTEYEFRVRAVN 78
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
870-958 |
4.34e-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: 52.11 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 870 PSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAIDTGPG-VTTFTVTNLVPGVEYELRLQSVTPA 948
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGsETSYTLTGLKPGTEYEFRVRAVNGG 80
|
90
....*....|..
gi 1822521639 949 GT--RSSPETVR 958
Cdd:cd00063 81 GEspPSESVTVT 92
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
126-202 |
4.63e-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: 51.85 E-value: 4.63e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 126 PSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTK-STNKDKTTFTATGLQPGDQYQLSVRSVT 202
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
870-949 |
5.63e-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: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 870 PSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGA-IDTGPGVTTFTVTNLVPGVEYELRLQSVTPA 948
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKeVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80
|
.
gi 1822521639 949 G 949
Cdd:smart00060 81 G 81
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
778-853 |
6.75e-08 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 51.26 E-value: 6.75e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521639 778 SPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTIT-SKGETTFTVTGLQPGDQYRLSVRSVT 853
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77
|
|
| RhsA |
COG3209 |
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ... |
59-811 |
6.92e-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: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 59 TRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTPEDTLSTPVEVTSTTNPSPVIGLSVVNGT 138
Cdd:COG3209 15 STLLAATNAGGGTAVTNAGSTVLLAKGGLSTAAAAGGAATLTARSASTTDVVGTLTGAGGTSAGGVTALGDASAAGGGYV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 139 TQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTATGLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTN 218
Cdd:COG3209 95 GGAAAGGGATLTGLAAATASAGRLVSTGAGAGGTVTAATGGTLGATAGSATTGSTDGGRGGVAVTGLAGGGASAYGLTLG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 219 PSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPED 298
Cdd:COG3209 175 GAAAGPATGVGTGAVTLATGLAGSALLALGSGAILGGLAGAYSGSATTATGTALGTPASVAATVTGSATGAAGAGAAVAT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 299 TLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGD 378
Cdd:COG3209 255 AATTLGGTTGAGTGASGAGLDASTGTGGAGGSNAAATAGGLGGAGLGSGGAGGGGTAGGTTTAAGTTGTAAVSGAADAGT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 379 QYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKG 458
Cdd:COG3209 335 TTTTGTGTGGTTTTVGGGGSLTLGGYGAAGGLTTSVGAGGGGSTSGSTTTVGGGGTATGSGGGSSTTGVGAGTTTTSTTG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 459 ETAFTATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNV 538
Cdd:COG3209 415 GDGGPATAAGALTAGGTATGTGTGGGGTTAGTDATTTTGGAGASGTLTTTGGAATGATTGGGTEAGTGGGTLTSGSAGAT 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 539 TGGVSWTQSTSKDETTFTATRLQPGDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNGTTESLTIEWTSPNDTR 618
Cdd:COG3209 495 TLGTDTTLDDTLGGTTTTTAGARGLVVTTGTTLTLGTTTTATLSATDATGTGDTTTTGTVGTGTSTGTGGTGTVTTTGDG 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 619 ASNYIYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQ 698
Cdd:COG3209 575 TGGASTTTGTTGGTATTTTVTTTTTTSTAGTTTTTTSGYTRAGLTLTLGTGTASGLERATASTGSTTGGTTGTGVTTTGT 654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 699 SLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSKSTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVKSTTDPS 778
Cdd:COG3209 655 TTTRATGTTGTGTGVTAGLTTLATGGTTVGGGTGTTSTATTGATTGGTETGTTVTTLAGGTTTRLGTTTTGGGGGTTTDG 734
|
730 740 750
....*....|....*....|....*....|...
gi 1822521639 779 PVTGLSVVNSTTQSlrieWTTPNNIRASNYTYN 811
Cdd:COG3209 735 TGTGGTTGTLTTTS----TTTTTTAGALTYTYD 763
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
33-124 |
7.57e-08 |
|
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.
Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 51.34 E-value: 7.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 33 PSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNV-AGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTpE 111
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKgSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79
|
90
....*....|...
gi 1822521639 112 DTLSTPVEVTSTT 124
Cdd:cd00063 80 GGESPPSESVTVT 92
|
|
| CDC14 |
COG2453 |
Protein-tyrosine phosphatase [Signal transduction mechanisms]; |
1276-1377 |
9.32e-08 |
|
Protein-tyrosine phosphatase [Signal transduction mechanisms];
Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 52.67 E-value: 9.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1276 EPRTITQFHFTsWPDHGVPKTTdkllQFQRMMRDYLNKNRAGLPV-VHCSAGVGRTGTLIALdYLLQR-IE-KEAVVDVy 1352
Cdd:COG2453 44 EEAGLEYLHLP-IPDFGAPDDE----QLQEAVDFIDEALREGKKVlVHCRGGIGRTGTVAAA-YLVLLgLSaEEALARV- 116
|
90 100
....*....|....*....|....*
gi 1822521639 1353 givhnmRMSRTCMVQTENQYIFLHQ 1377
Cdd:COG2453 117 ------RAARPGAVETPAQRAFLER 135
|
|
| PTP_DSP_cys |
cd14494 |
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ... |
1300-1377 |
9.61e-08 |
|
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: 9.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1300 LLQFQRMMRDYLNKNRAGLPV-VHCSAGVGRTGTLIALDYLLQRIEkeavvDVYGIVHNMRMSRT-CMVQTENQYIFLHQ 1377
Cdd:cd14494 39 LAMVDRFLEVLDQAEKPGEPVlVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRPgGIPQTIEQLDFLIK 113
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
777-853 |
9.92e-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: 50.69 E-value: 9.92e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 777 PSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSKG-ETTFTVTGLQPGDQYRLSVRSVT 853
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPsSTSYTLTGLKPGTEYEFRVRAVN 78
|
|
| CDKN3-like |
cd14505 |
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ... |
1280-1377 |
1.04e-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: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1280 ITQFHFtSWPDHGVPkttDKLLQFQRMMRDYLNKNRAGLPVV-HCSAGVGRTGTLIA--LDYLLQRIEKEAVVDvygIVh 1356
Cdd:cd14505 73 ITWHHL-PIPDGGVP---SDIAQWQELLEELLSALENGKKVLiHCKGGLGRTGLIAAclLLELGDTLDPEQAIA---AV- 144
|
90 100
....*....|....*....|.
gi 1822521639 1357 nmRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14505 145 --RALRPGAIQTPKQENFLHQ 163
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
220-295 |
1.26e-07 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 50.49 E-value: 1.26e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521639 220 SPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKG-ETAFTATGLQPGDQYQLSVQSVT 295
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGtTTSVTLTGLKPGTEYEVRVQAVN 77
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
685-760 |
1.27e-07 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 50.49 E-value: 1.27e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521639 685 SPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSW-SKSTSKGETTFTATGLQPGDQYQLSVQSVT 760
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
219-310 |
1.33e-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: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 219 PSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSST-TITNKGETAFTATGLQPGDQYQLSVQSVTpE 297
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79
|
90
....*....|...
gi 1822521639 298 DTLSTPVEVTSTT 310
Cdd:cd00063 80 GGESPPSESVTVT 92
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
498-574 |
1.40e-07 |
|
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.
Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 50.31 E-value: 1.40e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 498 PSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQ-STSKDETTFTATRLQPGDQYLLSVQSVT 574
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
|
|
| myxo_dep_M36 |
NF038112 |
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
253-824 |
1.70e-07 |
|
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.
Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 56.20 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 253 KVTVTNV-AGGVSSTTITNKGETAftatGLQPGDQYQLSVQSVTP--EDTLSTPVEVTSTTnPSPVTGLSVVNGTTQSLT 329
Cdd:NF038112 892 RVTVRNVgAGPLSAFTATVSSSTA----GVTFPNGGTVSFPALARgaTATVTVPVSLTGAG-TVARAGFTVAFRDEPQLP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 330 iewtsPNDTTAS-----NY--IYNVTVTNV--TGGVSWTESTSK--GETTFTATGLQPGDQYQLSVQSVTPED-TLSTPE 397
Cdd:NF038112 967 -----PGDKTATfdvrvNYdeVPASSTTETveSGLSPWTVSTDEllASGDWSVVEEPDGNRYFHGPNPSVAADiRLTSPW 1041
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 398 -QVTNTTN----------------PSPVTGLSVVNGTTQSLGIEWTSPTDTRASNyTYIVTV----TNVTGGGRSTTVTS 456
Cdd:NF038112 1042 lQVSATGDfvfsfkhrhsfesdygGAPPYYDGAVIELSEDGGQTWVDIGDLDADP-GYTGTLyeggGNPLEGRPAFVGTS 1120
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 457 KGETAFTATGLQPGDQYQ--------------------LSVQSVTPEGTLSTP----VEVTSTTNPSPVT--GLSVVNGT 510
Cdd:NF038112 1121 AGFPAFISATLNLGTAFAgktvrfrfrigsdvavgaygWDLDDLKFTGITNTPftslVAEPGVCNRRPVAnaGPDQTVLE 1200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 511 TQSLTIEWTRPTDTRASNYTYNvtvtnvtggvsWTQsTSKDETTFT-ATRLQPG--------DQYLLSVQSVTPEDTLST 581
Cdd:NF038112 1201 RTTVTLNGSGSFDPDGDPLTYA-----------WTQ-VSGPAVTLTgADTATPSftapevtaDTVLTFQLVVSDGTKTSA 1268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 582 PAQVTSTTN-----PSPVTGL--SVVNGTTESLTIEWTSPnDTRASNYiynvtvtnvtggvSWTQS-----TSKDETTFT 649
Cdd:NF038112 1269 PDTVTVLVRnvnraPVAVAGApaTVDERSTVTLDGSGTDA-DGDALTY-------------AWTQTsgpavTLTGATTAT 1334
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 650 ATRLQP---GDQyQLSVQSVTPEDTLSTPVEVTST---TNPSPV----TGLSVVNGTTQSLTIEWTRPTDTRASNYTYRV 719
Cdd:NF038112 1335 ATFTAPevtADT-QLTFTLTVSDGTASATDTVTVTvrnVNRAPVanagADQTVDERSTVTLSGSATDPDGDALTYAWTQT 1413
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 720 TVTNVT--GGVSWSKS------TSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPV-------------EVK---STT 775
Cdd:NF038112 1414 AGPTVTltGADTATASftapevAADTELTFQLTVSADGQASADVTVTVTVRNVNRAPVahagesitvdegsTVTldaSAT 1493
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 776 DP---------SPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNvTDGASST 824
Cdd:NF038112 1494 DPdgdtltyawTQVAGPSVTLTGADSAKLTFTAPEVSADTTLTFSLTVTD-GSGSSGP 1550
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
777-866 |
1.70e-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: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 777 PSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASST-TITSKGETTFTVTGLQPGDQYRLSVRSVTpE 855
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79
|
90
....*....|.
gi 1822521639 856 DTWSTPAQVTS 866
Cdd:cd00063 80 GGESPPSESVT 90
|
|
| PTP_PTEN-like |
cd14497 |
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ... |
1276-1360 |
2.39e-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: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1276 EPRTITQFHFT----SWPDHGVPkTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIA--LDYLLQRI-EKEAV 1348
Cdd:cd14497 52 EYDDDSKFEGRvlhyGFPDHHPP-PLGLLLEIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICayLLYYGQYStADEAL 130
|
90
....*....|..
gi 1822521639 1349 VDVYgivhNMRM 1360
Cdd:cd14497 131 EYFA----KKRF 138
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
33-109 |
3.33e-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: 49.15 E-value: 3.33e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 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 ... |
405-493 |
4.74e-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: 49.03 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 405 PSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRST-TVTSKGETAFTATGLQPGDQYQLSVQSVTP- 482
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVNGg 80
|
90
....*....|..
gi 1822521639 483 -EGTLSTPVEVT 493
Cdd:cd00063 81 gESPPSESVTVT 92
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
313-388 |
5.41e-07 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 48.57 E-value: 5.41e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521639 313 SPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTEST-SKGETTFTATGLQPGDQYQLSVQSVT 388
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
405-484 |
6.74e-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: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 405 PSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKG-ETAFTATGLQPGDQYQLSVQSVTPE 483
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPsSTSYTLTGLKPGTEYEFRVRAVNGA 80
|
.
gi 1822521639 484 G 484
Cdd:smart00060 81 G 81
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
592-667 |
7.62e-07 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 48.18 E-value: 7.62e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521639 592 SPVTGLSVVNGTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSW-TQSTSKDETTFTATRLQPGDQYQLSVQSVT 667
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
684-775 |
7.88e-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: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 684 PSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGvSWSK--STSKGETTFTATGLQPGDQYQLSVQSVTp 761
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSG-DWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVN- 78
|
90
....*....|....
gi 1822521639 762 EDTLSTPVEVKSTT 775
Cdd:cd00063 79 GGGESPPSESVTVT 92
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
112-649 |
1.03e-06 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 53.63 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 112 DTLSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTATGLQPG 191
Cdd:COG4625 24 GGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGTGGVGGGGGGGGGG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 192 DQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNK 271
Cdd:COG4625 104 GGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGGGGGGGGGGGGGGGGG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 272 GETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTN 351
Cdd:COG4625 184 GGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGNGGGGG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 352 VTGGvswtestskgeTTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTTQSLGIEWTSPTDT 431
Cdd:COG4625 264 AGGG-----------GGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 432 RASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTT 511
Cdd:COG4625 333 GAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGGAGGTGGGG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 512 QSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSKDETTFTATrlqpGDQYLLSVQSVTPEDTLSTPAQVTSTTNP 591
Cdd:COG4625 413 AGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGS----GGGAGAGGGSGSGAGTLTLTGNNTYTGTT 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 592 SPVTGLSVVNGTTESLTIEwtsPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDETTFT 649
Cdd:COG4625 489 TVNGGGNYTQSAGSTLAVE---VDAANSDRLVVTGTATLNGGTVVVLAGGYAPGTTYT 543
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
73-931 |
1.23e-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: 53.62 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 73 VAGGVSSITTTGKNET---TFTATGLQPGDQYLLSVRSVTPEDTLSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSP 149
Cdd:COG3210 805 TAAGTTAINVTGSGGTitiNTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGV 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 150 TDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTATGLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLTVVN 229
Cdd:COG3210 885 ATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAG 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 230 GTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTST 309
Cdd:COG3210 965 DTGASSAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQN 1044
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 310 TNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTP 389
Cdd:COG3210 1045 GVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGT 1124
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 390 EDTLSTPEQVTNTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQP 469
Cdd:COG3210 1125 TTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDST 1204
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 470 GDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTS 549
Cdd:COG3210 1205 GGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGATATGS 1284
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 550 KDETTFTATRLQPGDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNGTTESLTIEWTSPNDTRASNYIYNVTVT 629
Cdd:COG3210 1285 TVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNGATDSAAG 1364
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 630 NVTGGVSWTQSTSKDETTFTATRLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTiewTRPTD 709
Cdd:COG3210 1365 AGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGG---TGNTT 1441
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 710 TRASNYTYRVTVTNVTGGVSWSKSTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVKSTTDPSPVTGLSVVNST 789
Cdd:COG3210 1442 GTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAEVAK 1521
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 790 TQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSKGETTFTVTGLQPGDQYRLSVRSVTPEDTWSTPAQVTSTSN 869
Cdd:COG3210 1522 ASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNTATLTLSL 1601
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822521639 870 PSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAIDTGPGVTTFTVTN 931
Cdd:COG3210 1602 AEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNG 1663
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
34-109 |
1.50e-06 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 47.41 E-value: 1.50e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521639 34 SPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSIT-TTGKNETTFTATGLQPGDQYLLSVRSVT 109
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEiTVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
499-574 |
1.53e-06 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 47.41 E-value: 1.53e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521639 499 SPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSW-TQSTSKDETTFTATRLQPGDQYLLSVQSVT 574
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 |
2.83e-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: 47.11 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 126 PSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGvSWTK--STNKDKTTFTATGLQPGDQYQLSVRSVTp 203
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSG-DWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVN- 78
|
90
....*....|....
gi 1822521639 204 EDTLSTPVEVTNTT 217
Cdd:cd00063 79 GGGESPPSESVTVT 92
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
591-682 |
3.09e-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: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 591 PSPVTGLSVVNGTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGvSWTQ--STSKDETTFTATRLQPGDQYQLSVQSVTp 668
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSG-DWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVN- 78
|
90
....*....|....
gi 1822521639 669 EDTLSTPVEVTSTT 682
Cdd:cd00063 79 GGGESPPSESVTVT 92
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
406-481 |
5.49e-06 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 45.87 E-value: 5.49e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521639 406 SPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVT-SKGETAFTATGLQPGDQYQLSVQSVT 481
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
312-388 |
5.82e-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: 5.82e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521639 312 PSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWT-ESTSKGETTFTATGLQPGDQYQLSVQSVT 388
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
|
|
| PRK15375 |
PRK15375 |
type III secretion system effector GTPase-activating protein SptP; |
1201-1335 |
6.02e-06 |
|
type III secretion system effector GTPase-activating protein SptP;
Pssm-ID: 185273 [Multi-domain] Cd Length: 535 Bit Score: 50.57 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1201 PNTVVDFWRMVWEQKTKVIVMLTNcveQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEW-TTRKFNVKKTGCPEPRT 1279
Cdd:PRK15375 346 PDALEAHMKMLLEKECSCLVVLTS---EDQMQAKQLPPYFRGSYTFGEVHTNSQKVSSASQGeAIDQYNMQLSCGEKRYT 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521639 1280 ITQFHFTSWPDHGVPKTTDKLLQFQRMMRdylNKNRAG----------LPVVHCSAGVGRTGTLIA 1335
Cdd:PRK15375 423 IPVLHVKNWPDHQPLPSTDQLEYLADRVK---NSNQNGapgrsssdkhLPMIHCLGGVGRTGTMAA 485
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
498-589 |
7.73e-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: 45.57 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 498 PSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGvSWTQ--STSKDETTFTATRLQPGDQYLLSVQSVTp 575
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSG-DWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVN- 78
|
90
....*....|....
gi 1822521639 576 EDTLSTPAQVTSTT 589
Cdd:cd00063 79 GGGESPPSESVTVT 92
|
|
| PTP_PTPDC1 |
cd14506 |
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ... |
1283-1376 |
8.03e-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: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1283 FHFTSWPDHGVPkTTDKLLQFQRMMRDYLNKnrAGLPVVHCSAGVGRTGTLIA--LDYLLQRIEKEAVVDVygivhnmRM 1360
Cdd:cd14506 79 FYNFGWKDYGVP-SLTTILDIVKVMAFALQE--GGKVAVHCHAGLGRTGVLIAcyLVYALRMSADQAIRLV-------RS 148
|
90
....*....|....*.
gi 1822521639 1361 SRTCMVQTENQYIFLH 1376
Cdd:cd14506 149 KRPNSIQTRGQVLCVR 164
|
|
| PTP_VSP_TPTE |
cd14510 |
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ... |
1289-1376 |
8.82e-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: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1289 PDHGVPkTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIA---LDYLLQRIEKEAvVDVYGivhNMRMSRTCM 1365
Cdd:cd14510 82 DDHNVP-TLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCawlIYSGQFESAKEA-LEYFG---ERRTDKSVS 156
|
90
....*....|....*.
gi 1822521639 1366 -----VQTENQYIFLH 1376
Cdd:cd14510 157 skfqgVETPSQSRYVG 172
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
665-1041 |
1.18e-05 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 50.00 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 665 SVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTrptdtrASNYTYRVTVTNVTGGVSWSKSTSKGETTFTAT 744
Cdd:COG3401 30 GGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTG------GRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 745 GLQPGDQYQLSVQSVTPEDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASST 824
Cdd:COG3401 104 GGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 825 TITSKGETTFTVTG-LQPGDQYRLSVRSVTPEDTWSTPAQV---TSTSNPSPVSGLTVVNRTTVSIEVTWAAPTDARAPE 900
Cdd:COG3401 184 SLTVTSTTLVDGGGdIEPGTTYYYRVAATDTGGESAPSNEVsvtTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 901 YT-YRITLANVTRRGRGAIDTgpgvTTFTVTNLVPGVEYELRLQSVTPAGTRSSP----ETVRNATIPAAISDFRCSGST 975
Cdd:COG3401 264 YRvYRSNSGDGPFTKVATVTT----TSYTDTGLTNGTTYYYRVTAVDAAGNESAPsnvvSVTTDLTPPAAPSGLTATAVG 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 976 GYMVEAKWSQPNGQFSMFKALTYDGEQLISNLSLGK--EERSLTVDNLQPGRTYTLRV--VTESGNTSSQ 1041
Cdd:COG3401 340 SSSITLSWTASSDADVTGYNVYRSTSGGGTYTKIAEtvTTTSYTDTGLTPGTTYYYKVtaVDAAGNESAP 409
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
127-202 |
2.14e-05 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 44.33 E-value: 2.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521639 127 SPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSW-TKSTNKDKTTFTATGLQPGDQYQLSVRSVT 202
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
|
|
| COG4733 |
COG4733 |
Phage-related protein, tail protein J [Mobilome: prophages, transposons]; |
824-1039 |
7.12e-05 |
|
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 47.63 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 824 TTITSKGETTFTVTGLQPGDQYRLSVRSVTPEDTWSTPAQVTSTSNPSpvsgLTVVNRTTV--SIEVTWAAPTDARAPEY 901
Cdd:COG4733 494 VSIEENEDGTYTITAVQHAPEKYAAIDAGAFDDVPPQWPPVNVTTSES----LSVVAQGTAvtTLTVSWDAPAGAVAYEV 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 902 TYRITLANVTRRGRgaidtgPGVTTFTVTNLVPGvEYELRLQSVTPAGTRSSPETVRNATI------PAAISDFRCSGST 975
Cdd:COG4733 570 EWRRDDGNWVSVPR------TSGTSFEVPGIYAG-DYEVRVRAINALGVSSAWAASSETTVtgktapPPAPTGLTATGGL 642
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 976 GyMVEAKWSQPNG----QFSMFKALTYDGEQLISNLSLGKeERSLTVDNLQPGRTYTLRV--VTESGNTS 1039
Cdd:COG4733 643 G-GITLSWSFPVDadtlRTEIRYSTTGDWASATVAQALYP-GNTYTLAGLKAGQTYYYRAraVDRSGNVS 710
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
112-838 |
9.93e-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: 47.07 E-value: 9.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 112 DTLSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTATGLQPG 191
Cdd:COG3210 12 KTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGGIGAAAANTAGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 192 DQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNK 271
Cdd:COG3210 92 LETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNTNTNNSSSGT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 272 GETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTN 351
Cdd:COG3210 172 NIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGVISTGGTDISSL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 352 VTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTTqslgiewtsptdt 431
Cdd:COG3210 252 SVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAA------------- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 432 rasNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTT 511
Cdd:COG3210 319 ---GITTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNAS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 512 QSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTskdeTTFTATRLQPGDQYLLSVQSVTPEDTLSTPAQVTSTTNP 591
Cdd:COG3210 396 STTVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGV----LGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGT 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 592 SPVTGLSVVNGTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYQLSVQSVTPEDT 671
Cdd:COG3210 472 VTNSAGNTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 672 LSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSKSTSKGETTFTATGLQPGDQ 751
Cdd:COG3210 552 ASGTTAASGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGG 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 752 YQLSVQSVTPEDTLSTPVEVkSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSKGE 831
Cdd:COG3210 632 AGLTGSAVGAALSGTGSGTT-GTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTIST 710
|
....*..
gi 1822521639 832 TTFTVTG 838
Cdd:COG3210 711 GSITVTG 717
|
|
| DUSP23 |
cd14504 |
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ... |
1282-1335 |
1.34e-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: 1.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1822521639 1282 QFHFTSWPDHGVPkTTDKLLQFQRMMRDYLNKNRAGLpvVHCSAGVGRTGTLIA 1335
Cdd:cd14504 51 RYHHIPIEDYTPP-TLEQIDEFLDIVEEANAKNEAVL--VHCLAGKGRTGTMLA 101
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
177-598 |
2.07e-04 |
|
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: 46.06 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 177 NKDKTTFTATGLQPGDQYQLSVRSVTPEDTLSTPVEVTnttnpspvTGLTVVNGTTHSLRIEWTPPTDTR---------- 246
Cdd:pfam05109 312 SQDMPTNTTDITYVGDNATYSVPMVTSEDANSPNVTVT--------AFWAWPNNTETDFKCKWTLTSGTPsgcenisgaf 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 247 ATNYTYKVTVTNVAGGVSSTTITNKGETAFTATglqpgdqyQLSVQSVTPEDTLSTP-VEVTSTTNPSPVTGLSVVNGTT 325
Cdd:pfam05109 384 ASNRTFDITVSGLGTAPKTLIITRTATNATTTT--------HKVIFSKAPESTTTSPtLNTTGFAAPNTTTGLPSSTHVP 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 326 QSLTIEwTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNP 405
Cdd:pfam05109 456 TNLTAP-ASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNA 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 406 -SPVTGLSVVNGTTQSLGIEWTSPTDTrASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSVTpeG 484
Cdd:pfam05109 535 tSPTLGKTSPTSAVTTPTPNATSPTPA-VTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLG--G 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 485 TLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRP----------TDTRASNYTYNVTVTNVTGGVSWTQSTSKDETT 554
Cdd:pfam05109 612 TSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPssisetlspsTSDNSTSHMPLLTSAHPTGGENITQVTPASTST 691
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1822521639 555 FTATRLQPGDQYLLSVQSVTP--EDTLSTPAQVTSTTNPSPVTGLS 598
Cdd:pfam05109 692 HHVSTSSPAPRPGTTSQASGPgnSSTSTKPGEVNVTKGTPPKNATS 737
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
333-838 |
2.45e-04 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 45.54 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 333 TSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGLS 412
Cdd:COG4625 2 GGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 413 VVNGTTqSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSVTPEGTLSTPVEV 492
Cdd:COG4625 82 GGGGGG-GGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 493 TSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSkdETTFTATRLQPGDQYLLSVQS 572
Cdd:COG4625 161 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGG--GGGGGGGGGGGGGGGGGGGGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 573 VTPEDTLSTPAQVTSTTNPSPVTGLSVVNGTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDETTFTATR 652
Cdd:COG4625 239 GGGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 653 LQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSK 732
Cdd:COG4625 319 GGGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 733 STSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNV 812
Cdd:COG4625 399 GGGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTL 478
|
490 500
....*....|....*....|....*.
gi 1822521639 813 TVTNVTDGAssTTITSKGETTFTVTG 838
Cdd:COG4625 479 TGNNTYTGT--TTVNGGGNYTQSAGS 502
|
|
| CDC14_C |
cd14499 |
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ... |
1321-1342 |
3.12e-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: 3.12e-04
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
399-880 |
6.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 44.38 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 399 VTNTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQ 478
Cdd:COG4625 32 AGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGTGGVGGGGGGGGGGGGGGGGGG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 479 SVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSKDETTFTAT 558
Cdd:COG4625 112 GGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 559 RLQPGDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNGTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWT 638
Cdd:COG4625 192 GNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 639 QSTSKDETTFTATRLqpGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYR 718
Cdd:COG4625 272 GGGSGGGGGGGGGGG--SGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 719 VTVTNVTGGVSWSKSTSKGETTFTATGlqpgdqyqlSVQSVTPEDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSLRIEWT 798
Cdd:COG4625 350 AGGGGAGGGGGGGTGGGGGGGGGGGGG---------SGGGGAGGGGGSGGGGGGGAGGGGGGGGAGGTGGGGAGGGGGAA 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 799 TPNNIRASNYTYNVTVTNVTDGASSTTITSKGETTFTVTGLQPGDQyrlsvrsvtpeDTWSTPAQVTSTSNPSPVSGLTV 878
Cdd:COG4625 421 GGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAG-----------GGSGSGAGTLTLTGNNTYTGTTT 489
|
..
gi 1822521639 879 VN 880
Cdd:COG4625 490 VN 491
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
377-870 |
7.76e-04 |
|
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: 44.14 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 377 GDQYQLSVQSVTPEDTlstpeqvtNTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTR----------ASNYTYIVTVTNVT 446
Cdd:pfam05109 326 GDNATYSVPMVTSEDA--------NSPNVTVTAFWAWPNNTETDFKCKWTLTSGTPsgcenisgafASNRTFDITVSGLG 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 447 GGGRSTTVTSKGETAFTATglqpgdqyQLSVQSVTPEGTLSTP-VEVTSTTNPSPVTGLSvvngTTQSLTIEWTRPTDTR 525
Cdd:pfam05109 398 TAPKTLIITRTATNATTTT--------HKVIFSKAPESTTTSPtLNTTGFAAPNTTTGLP----SSTHVPTNLTAPASTG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 526 ASNYTYNVTV---TNVTGGVSWTQSTSKDETTFTATRLQPGDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTglsvVNG 602
Cdd:pfam05109 466 PTVSTADVTSptpAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPT----LGK 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 603 TTESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDET-TFTATRLQPGDQY-QLSVQSVTPEDTLSTPVEVTS 680
Cdd:pfam05109 542 TSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTpTPNATSPTVGETSpQANTTNHTLGGTSSTPVVTSP 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 681 TTNPSPVTGLSVVNGTTQSLTIEWTRP----------TDTRASNYTYRVTVTNVTGGVSWSKSTSKGETTFTATGLQPGD 750
Cdd:pfam05109 622 PKNATSAVTTGQHNITSSSTSSMSLRPssisetlspsTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAP 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 751 QYQLSVQSVTP--EDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITS 828
Cdd:pfam05109 702 RPGTTSQASGPgnSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTD 781
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1822521639 829 KGETTFT-------VTGLQPGDQYRLSVR---SVTPEDTWSTPAQVTSTSNP 870
Cdd:pfam05109 782 YGGDSTTprtrynaTTYLPPSTSSKLRPRwtfTSPPVTTAQATVPVPPTSQP 833
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
113-332 |
9.07e-04 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 43.59 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 113 TLSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTATGLQPGD 192
Cdd:COG3469 1 SSSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 193 QYQLSVRSVTPEDTLSTPVEVTNTTNP--SPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITN 270
Cdd:COG3469 81 TATAAAAAATSTSATLVATSTASGANTgtSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822521639 271 KGETAFTATGLQPGDQYQLSVQSVTPeDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEW 332
Cdd:COG3469 161 GGTTTTSTTTTTTSASTTPSATTTAT-ATTASGATTPSATTTATTTGPPTPGLPKHVLVGYW 221
|
|
| FhaB |
COG3210 |
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ... |
27-933 |
9.27e-04 |
|
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 43.99 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 27 SQNVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVR 106
Cdd:COG3210 278 TGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGT 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 107 SVTPEDTLSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTAT 186
Cdd:COG3210 358 GAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITG 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 187 GLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSST 266
Cdd:COG3210 438 NGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGI 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 267 TITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYN 346
Cdd:COG3210 518 TAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSG 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 347 VTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTTQSLGIEWT 426
Cdd:COG3210 598 GTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGT 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 427 SPTDTRASNYTYIVTVT-----------------NVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSVTPEGTLSTP 489
Cdd:COG3210 678 VTSGATGGTTGTTLNAAtggtlnnagntltistgSITVTGQIGALANANGDTVTFGNLGTGATLTLNAGVTITSGNAGTL 757
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 490 VEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYLLS 569
Cdd:COG3210 758 SIGLTANTTASGTTLTLANANGNTSAGATLDNAGAEISIDITADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTT 837
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 570 VQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNGTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDETTFT 649
Cdd:COG3210 838 SGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVT 917
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 650 ATRLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVS 729
Cdd:COG3210 918 ATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGIL 997
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 730 WSKSTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYT 809
Cdd:COG3210 998 VAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASN 1077
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 810 YNVTVTNVTDGASSTTITSKGETTFTVTGLQPGDQYRLSVRSVTPEDTWSTPAQVTSTSNPSPVSGLTVVNRTTVSIEVT 889
Cdd:COG3210 1078 GGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGG 1157
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 1822521639 890 WAAPTDARAPEYTYRITLANVTRRGRGAIDTGPGVTTFTVTNLV 933
Cdd:COG3210 1158 ASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGG 1201
|
|
| COG3979 |
COG3979 |
Chitodextrinase [Carbohydrate transport and metabolism]; |
403-745 |
1.24e-03 |
|
Chitodextrinase [Carbohydrate transport and metabolism];
Pssm-ID: 443178 [Multi-domain] Cd Length: 369 Bit Score: 42.84 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 403 TNPSPVTGLSVVNGTTQSLGIEWTSPTDTRAsnytyiVTVTNVTGGGrSTTVTSKGETAFTATGLQPGDQYQLSVQSVTP 482
Cdd:COG3979 1 QAPTAPTGLTASNVTSSSVSLSWDASTDNVG------VTGYDVYRGG-DQVATVTGLTAWTVTGLTPGTEYTFTVGACDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 483 EGTLST-PVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSKDETTFTATRLQ 561
Cdd:COG3979 74 AGNVSAaSGTSTAMFGGSSTTLGSAEGVADTSGNLAASGAFFGVTTPPTPSSTLVVDGTTTVNAAATANGGTGGSGGTTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 562 PGDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNGTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQST 641
Cdd:COG3979 154 IITTGVEGGGGSKTAQSLNAITAAGTAALNGGVVGGADEVLTCSAVKDDGSGGAGAGNTYWALNTLGVSDTPSGTTATGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 642 SKDETTFTATRLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTV 721
Cdd:COG3979 234 TVGITSAYGAGVSGNAAVNVNAGFVVGNVGGAAGNTGTTSGTATSDAATNDVGDAAVTGLNDGAANGPTGGYGATGTTVA 313
|
330 340
....*....|....*....|....
gi 1822521639 722 TNVTGGVSWSKSTSKGETTFTATG 745
Cdd:COG3979 314 GAAGVGGTKSGTGALGLSGAGGAG 337
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
206-412 |
1.24e-03 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 43.20 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 206 TLSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGD 285
Cdd:COG3469 1 SSSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 286 QYQLSV-------QSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSW 358
Cdd:COG3469 81 TATAAAaaatstsATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETAT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1822521639 359 TESTSKGETTFTATGLQPGDQYQlSVQSVTPEDTLSTPEQVTNTTNPSPVTGLS 412
Cdd:COG3469 161 GGTTTTSTTTTTTSASTTPSATT-TATATTASGATTPSATTTATTTGPPTPGLP 213
|
|
| AidA |
COG3468 |
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ... |
409-838 |
1.26e-03 |
|
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 43.40 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 409 TGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSVTPEGTLST 488
Cdd:COG3468 8 GATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSGGTGGN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 489 PVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYLL 568
Cdd:COG3468 88 STGGGGGNSGTGGTGGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGTGSGGGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 569 SVQSVTPEDTLSTPAQ----VTSTTNPSPVTGLSVVNGTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKD 644
Cdd:COG3468 168 SGGGGGAGGGGGGGAGgsggAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGGGSAGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 645 ETTFTATRLQPGdqyqlSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYrVTVTNV 724
Cdd:COG3468 248 TGGGGLTGGGAA-----GTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGG-GGGGSN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 725 TGGVSWSKSTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSlriewttpNNIR 804
Cdd:COG3468 322 AGGGSGGGGGGGGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSD--------GVGT 393
|
410 420 430
....*....|....*....|....*....|....
gi 1822521639 805 ASNYTYNVTVTNVTDGASSTTITSKGETTFTVTG 838
Cdd:COG3468 394 GLTTGGTGNNGGGGVGGGGGGGLTLTGGTLTVNG 427
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
238-461 |
1.45e-03 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 42.82 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 238 EWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTG 317
Cdd:COG3469 4 VSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 318 LSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTftatglqpgdqyqlSVQSVTPEDTLSTPE 397
Cdd:COG3469 84 AAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTT--------------TSGASATSSAGSTTT 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822521639 398 QVTNTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYtyivTVTNVTGGGRSTTVTSKGETA 461
Cdd:COG3469 150 TTTVSGTETATGGTTTTSTTTTTTSASTTPSATTTATAT----TASGATTPSATTTATTTGPPT 209
|
|
| PTP_PTEN |
cd14509 |
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ... |
1289-1359 |
1.54e-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: 1.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521639 1289 PDHGVPkTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALdYLLQRIE----KEAvVDVYGI--VHNMR 1359
Cdd:cd14509 68 DDHNPP-PLELIKPFCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICC-YLLYLGKfpsaKEA-LDFYGAkrTKNKK 141
|
|
| DSP_DUSP16 |
cd14646 |
dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual ... |
1274-1344 |
1.55e-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: 1.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822521639 1274 CPEPRTITQFHFTSWPDHGvpKTTDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTlIALDYLLQRIE 1344
Cdd:cd14646 39 CPKPDFIPESHFLRVPVND--SFCEKILPWLDKSVDFIEKAKAsnGRVLVHCLAGISRSAT-IAIAYIMKRMD 108
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
965-1041 |
1.82e-03 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 38.94 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 965 AISDFRCSGSTGYMVEAKWSQP---NGQFSMFKaLTY---DGEQLISNLSLGKEERSLTVDNLQPGRTYTLRVVTESGNT 1038
Cdd:pfam00041 2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYE-VEYrpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
|
...
gi 1822521639 1039 SSQ 1041
Cdd:pfam00041 81 EGP 83
|
|
| COG4625 |
COG4625 |
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ... |
54-465 |
1.90e-03 |
|
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];
Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 42.84 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 54 TSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTPEDTLSTPVEVTSTTNPSPVIGLS 133
Cdd:COG4625 101 GGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGGGGGGGGGGGGGG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 134 VVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDkTTFTATGLQPGDQYQLSVRSVTPEDTLSTPVEV 213
Cdd:COG4625 181 GGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGG-GGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGNG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 214 TNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQS 293
Cdd:COG4625 260 GGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGG 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 294 VTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATG 373
Cdd:COG4625 340 SGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGGAGGTGGGGAGGGGGA 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 374 LQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTT 453
Cdd:COG4625 420 AGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNTYTGTTTVNGGGNYTQS 499
|
410
....*....|..
gi 1822521639 454 VTSKGETAFTAT 465
Cdd:COG4625 500 AGSTLAVEVDAA 511
|
|
| DSPc |
smart00195 |
Dual specificity phosphatase, catalytic domain; |
1296-1377 |
2.36e-03 |
|
Dual specificity phosphatase, catalytic domain;
Pssm-ID: 214551 [Multi-domain] Cd Length: 138 Bit Score: 39.96 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1296 TTDKLLQFQRMMRDYLN--KNRAGLPVVHCSAGVGRTGTLIALdYLLQRiEKEAVVDVYGIVhnmRMSRTCMVQTENqyi 1373
Cdd:smart00195 56 TETKISPYFPEAVEFIEdaESKGGKVLVHCQAGVSRSATLIIA-YLMKT-RNMSLNDAYDFV---KDRRPIISPNFG--- 127
|
....
gi 1822521639 1374 FLHQ 1377
Cdd:smart00195 128 FLRQ 131
|
|
| DSPc |
pfam00782 |
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ... |
1296-1377 |
3.32e-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: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1296 TTDKLLQFQRMMRDYLN--KNRAGLPVVHCSAGVGRTGTLIALdYLLQRiEKEAVVDVYGIVhnmRMSRTCMVQTENqyi 1373
Cdd:pfam00782 47 HETNISKYLEEAVEFIDdaRQKGGKVLVHCQAGISRSATLIIA-YLMKT-RNLSLNEAYSFV---KERRPGISPNFG--- 118
|
....
gi 1822521639 1374 FLHQ 1377
Cdd:pfam00782 119 FKRQ 122
|
|
| TpbA-like |
cd14529 |
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ... |
1277-1361 |
3.68e-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: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1277 PRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDylnKNRAGlPVV-HCSAGVGRTGTLIALdYLlqriekeavvDVYG-- 1353
Cdd:cd14529 53 AAKIDGVKYVNLPLSATRPTESDVQSFLLIMDL---KLAPG-PVLiHCKHGKDRTGLVSAL-YR----------IVYGgs 117
|
90
....*....|.
gi 1822521639 1354 ---IVHNMRMS 1361
Cdd:cd14529 118 keeANEDYRLS 128
|
|
| DSP_MKP |
cd14512 |
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ... |
1272-1342 |
4.64e-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: 4.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822521639 1272 TGCPEPRTITQFHFTSWP--DHgvpkTTDKLLQFQRMMRDYLN--KNRAGLPVVHCSAGVGRTGTlIALDYLLQR 1342
Cdd:cd14512 35 NTCPNPDFIGLFHYKRIPvnDS----FCQNISPWFDEAIEFIEeaKASNGGVLVHCLAGISRSAT-IAIAYLMKR 104
|
|
| DSP_DUSP11 |
cd17665 |
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ... |
1289-1334 |
5.52e-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: 5.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1822521639 1289 PDHGVPKTtDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTLI 1334
Cdd:cd17665 85 PGHQVPDD-KTIQSFKDAVKDFLEKNKDndKLIGVHCTHGLNRTGYLI 131
|
|
| DSP_MKP_classIII |
cd14568 |
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ... |
1268-1359 |
6.35e-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: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521639 1268 NVKKTgCPEPRTITQFHFTSWPDHGVPKttDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTlIALDYLLQRIeK 1345
Cdd:cd14568 32 NVSNT-CPKPDFIPDSHFLRIPVNDSYC--EKLLPWLDKAVEFIEKARAsnKRVLVHCLAGISRSAT-IAIAYIMKHM-R 106
|
90
....*....|....
gi 1822521639 1346 EAVVDVYGIVHNMR 1359
Cdd:cd14568 107 MSLDDAYRFVKEKR 120
|
|
| |
