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Conserved domains on  [gi|2067662268|ref|NP_001382445|]
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transmembrane protease serine 9 [Rattus norvegicus]

Protein Classification

LDL receptor domain-containing protein; serine protease( domain architecture ID 12018001)

Low Density Lipoprotein (LDL) receptor class A domain is a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism| trypsin-like serine protease catalyzes the cleavage of specific peptide bonds in protein substrates using an active site serine as the nucleophile; contains C-terminal DNA polymerase III subunits gamma and tau

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
864-1089 1.09e-93

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 298.04  E-value: 1.09e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  864 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPMQWAAFLGTPFLSSTE--GQLERVARIYRH 941
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  942 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGPTR-PPEGARCVITGWGSLREGGSMARQLQKAAVRVLSEQTCRRFY 1020
Cdd:cd00190     80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2067662268 1021 --PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGQWVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWI 1089
Cdd:cd00190    160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
238-467 1.81e-93

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


:

Pssm-ID: 214473  Cd Length: 229  Bit Score: 297.67  E-value: 1.81e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268   238 RIVGGAEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEaSAVRARVLRIAK 316
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGE-EGQVIKVSKVII 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268   317 HPAYNADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPRKKCLISGWGYLKEDFLVKPEVLQKATVELLDQNLCSS 396
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2067662268   397 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGVVSWGIGCAEARRPGVYTRVTRLRDWI 467
Cdd:smart00020  159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
540-767 1.76e-87

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 281.47  E-value: 1.76e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  540 IVGGISAVSGEVPWQASLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKLEQVQAHLGTVSLLGVGGSPVKLGLRSVALHP 618
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  619 RYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGnATKPDILQKASVGIIEQKMCGALY 698
Cdd:cd00190     81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2067662268  699 --NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACeETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 767
Cdd:cd00190    160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVC-NDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
190-225 1.38e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 51.44  E-value: 1.38e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2067662268  190 CPGNAFSCQNSQCVSKENpECDDRVDCSDGSDEAQC 225
Cdd:cd00112      1 CPPNEFRCANGRCIPSSW-VCDGEDDCGDGSDEENC 35
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
68-148 2.30e-05

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


:

Pssm-ID: 460188  Cd Length: 100  Bit Score: 44.15  E-value: 2.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268   68 VRFTSLLQQENSDFYRLLTPALQTLFVRSFQKTELESSCTGCTVLSYRDGNSSVIVHFRLHFllralQPLSLDQEADILQ 147
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVF-----RFPSTEPALDREK 86

                   .
gi 2067662268  148 K 148
Cdd:pfam01390   87 L 87
PHA03247 super family cl33720
large tegument protein UL36; Provisional
463-539 7.82e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 7.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  463 LRDWILEVTSSADTP---VVPTEAPAPITPSTPWPTSPESRVPNTTAKP-TVAPTPAPLHPSTAAKPQECGARPAMDKPT 538
Cdd:PHA03247  2688 ARPTVGSLTSLADPPpppPTPEPAPHALVSATPLPPGPAAARQASPALPaAPAPPAVPAGPATPGGPARPARPPTTAGPP 2767

                   .
gi 2067662268  539 R 539
Cdd:PHA03247  2768 A 2768
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
864-1089 1.09e-93

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 298.04  E-value: 1.09e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  864 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPMQWAAFLGTPFLSSTE--GQLERVARIYRH 941
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  942 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGPTR-PPEGARCVITGWGSLREGGSMARQLQKAAVRVLSEQTCRRFY 1020
Cdd:cd00190     80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2067662268 1021 --PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGQWVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWI 1089
Cdd:cd00190    160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
238-467 1.81e-93

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 297.67  E-value: 1.81e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268   238 RIVGGAEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEaSAVRARVLRIAK 316
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGE-EGQVIKVSKVII 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268   317 HPAYNADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPRKKCLISGWGYLKEDFLVKPEVLQKATVELLDQNLCSS 396
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2067662268   397 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGVVSWGIGCAEARRPGVYTRVTRLRDWI 467
Cdd:smart00020  159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
239-467 1.46e-92

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 295.34  E-value: 1.46e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  239 IVGGAEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEASAVRARVLRIAKH 317
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  318 PAYNADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPRKKCLISGWGYLKEDfLVKPEVLQKATVELLDQNLCSSL 397
Cdd:cd00190     80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRA 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2067662268  398 YGHS--LTDRMVCAGYLDGKVDSCQGDSGGPLVCEEPsGRFFLAGVVSWGIGCAEARRPGVYTRVTRLRDWI 467
Cdd:cd00190    159 YSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
863-1089 1.29e-91

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 292.66  E-value: 1.29e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268   863 RIVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPMQWAAFLGTPFLSSTE-GQLERVARIYRH 941
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEeGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268   942 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGP-TRPPEGARCVITGWGSLREG-GSMARQLQKAAVRVLSEQTCRRF 1019
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2067662268  1020 YPVQ--ISSRMLCAGFPQGGVDSCSGDAGGPLACRepSGQWVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWI 1089
Cdd:smart00020  160 YSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
540-767 1.76e-87

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 281.47  E-value: 1.76e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  540 IVGGISAVSGEVPWQASLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKLEQVQAHLGTVSLLGVGGSPVKLGLRSVALHP 618
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  619 RYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGnATKPDILQKASVGIIEQKMCGALY 698
Cdd:cd00190     81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2067662268  699 --NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACeETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 767
Cdd:cd00190    160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVC-NDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
539-767 3.94e-87

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 280.33  E-value: 3.94e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268   539 RIVGGISAVSGEVPWQASLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKLEQVQAHLGTVSLLgVGGSPVKLGLRSVALH 617
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268   618 PRYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKASVGIIEQKMCGAL 697
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2067662268   698 Y--NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACEEtpGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 767
Cdd:smart00020  160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
239-467 2.66e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 241.96  E-value: 2.66e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  239 IVGGAEAAPGEFPWQVSL-RENHEHFCGATIIGARWLVSAAHCFNefqDPAQWAAQAGSVHLSGSEASAVRARVLRIAKH 317
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  318 PAYNADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPRKKCLISGWGYLKEDflVKPEVLQKATVELLDQNLCSSL 397
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  398 YGHSLTDRMVCAGYldGKVDSCQGDSGGPLVCEEPsgrfFLAGVVSWGIGCAEARRPGVYTRVTRLRDWI 467
Cdd:pfam00089  156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
835-1095 8.72e-70

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 233.77  E-value: 8.72e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  835 TRRQTPAPGTTVFSHLPDCGLAPPGALTRIVGGSAASLGEWPWQVSLWLR--RREHRCGAVLVAERWLLSAAHCFDVYGd 912
Cdd:COG5640      2 RRRRLLAALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDG- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  913 PMQWAAFLGTPFLSSTEGQLERVARIYRHPFYNIYTLDYDVALLELAGPVRRsrlVRPICLPGPTRPPE-GARCVITGWG 991
Cdd:COG5640     81 PSDLRVVIGSTDLSTSGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAApGTPATVAGWG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  992 SLREG-GSMARQLQKAAVRVLSEQTCRRfYPVQISSRMLCAGFPQGGVDSCSGDAGGPLAcREPSGQWVLTGVTSWGYGC 1070
Cdd:COG5640    158 RTSEGpGSQSGTLRKADVPVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGP 235
                          250       260
                   ....*....|....*....|....*
gi 2067662268 1071 GRPHFPGVYTRVAAVLGWIGQNIRE 1095
Cdd:COG5640    236 CAAGYPGVYTRVSAYRDWIKSTAGG 260
Trypsin pfam00089
Trypsin;
864-1089 1.30e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 231.95  E-value: 1.30e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  864 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvygDPMQWAAFLGTPFLSSTEG--QLERVARIYRH 941
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGgeQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  942 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGPTR-PPEGARCVITGWGSLREGGSmARQLQKAAVRVLSEQTCRRFY 1020
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSdLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2067662268 1021 PVQISSRMLCAGFpqGGVDSCSGDAGGPLACrepSGQwVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWI 1089
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVC---SDG-ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Trypsin pfam00089
Trypsin;
540-767 4.19e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 230.41  E-value: 4.19e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  540 IVGGISAVSGEVPWQASLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKleQVQAHLGTVSLLGVGGSPVKLGLRSVALHP 618
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGAS--DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  619 RYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNatKPDILQKASVGIIEQKMCGALY 698
Cdd:pfam00089   79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2067662268  699 NFSLTDRMLCAGFleGRVDSCQGDSGGPLACEETpgvfYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 767
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
230-475 3.23e-66

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 224.14  E-value: 3.23e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  230 QPAWRSAGRIVGGAEAAPGEFPWQVSLREN---HEHFCGATIIGARWLVSAAHCFNEfQDPAQWAAQAGSVHLSGSEAsa 306
Cdd:COG5640     22 APAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGG-- 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  307 VRARVLRIAKHPAYNADTADFDVAVLELARPLPFgryVQPACLPAATHVFPPRKKCLISGWGYLKEDFLVKPEVLQKATV 386
Cdd:COG5640     99 TVVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADV 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  387 ELLDQNLCSSlYGHSLTDRMVCAGYLDGKVDSCQGDSGGPLVcEEPSGRFFLAGVVSWGIGCAEARRPGVYTRVTRLRDW 466
Cdd:COG5640    176 PVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                   ....*....
gi 2067662268  467 ILEVTSSAD 475
Cdd:COG5640    254 IKSTAGGLG 262
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
529-775 6.64e-60

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 206.04  E-value: 6.64e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  529 GARPAMDKPTRIVGGISAVSGEVPWQASL---KEGSRHFCGATVVGDRWLLSAAHCFNHTKLEQVQAHLGTVSLLGVGGs 605
Cdd:COG5640     20 AAAPAADAAPAIVGGTPATVGEYPWMVALqssNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGG- 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  606 pVKLGLRSVALHPRYNPGILDFDVALLELAQPLvfnKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKAS 685
Cdd:COG5640     99 -TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  686 VGIIEQKMCGALYNFsLTDRMLCAGFLEGRVDSCQGDSGGPLAcEETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKD 765
Cdd:COG5640    175 VPVVSDATCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252
                          250
                   ....*....|
gi 2067662268  766 WILKAMSSDP 775
Cdd:COG5640    253 WIKSTAGGLG 262
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
190-225 1.38e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 51.44  E-value: 1.38e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2067662268  190 CPGNAFSCQNSQCVSKENpECDDRVDCSDGSDEAQC 225
Cdd:cd00112      1 CPPNEFRCANGRCIPSSW-VCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
190-222 5.65e-08

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 49.55  E-value: 5.65e-08
                            10        20        30
                    ....*....|....*....|....*....|...
gi 2067662268   190 CPGNAFSCQNSQCVSKENpECDDRVDCSDGSDE 222
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSW-VCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
190-225 7.94e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 46.47  E-value: 7.94e-07
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2067662268  190 CPGNAFSCQNSQCVSKeNPECDDRVDCSDGSDEAQC 225
Cdd:pfam00057    3 CSPNEFQCGSGECIPR-SWVCDGDPDCGDGSDEENC 37
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
68-148 2.30e-05

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


Pssm-ID: 460188  Cd Length: 100  Bit Score: 44.15  E-value: 2.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268   68 VRFTSLLQQENSDFYRLLTPALQTLFVRSFQKTELESSCTGCTVLSYRDGNSSVIVHFRLHFllralQPLSLDQEADILQ 147
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVF-----RFPSTEPALDREK 86

                   .
gi 2067662268  148 K 148
Cdd:pfam01390   87 L 87
PHA03247 PHA03247
large tegument protein UL36; Provisional
463-539 7.82e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 7.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  463 LRDWILEVTSSADTP---VVPTEAPAPITPSTPWPTSPESRVPNTTAKP-TVAPTPAPLHPSTAAKPQECGARPAMDKPT 538
Cdd:PHA03247  2688 ARPTVGSLTSLADPPpppPTPEPAPHALVSATPLPPGPAAARQASPALPaAPAPPAVPAGPATPGGPARPARPPTTAGPP 2767

                   .
gi 2067662268  539 R 539
Cdd:PHA03247  2768 A 2768
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
473-536 5.19e-03

Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442381 [Multi-domain]  Cd Length: 140  Bit Score: 38.60  E-value: 5.19e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2067662268  473 SADTPVVPTEAPAPITPSTPWPTSPESRVPNTTAKPTVAP-TPAPLhPSTAAKPQECGARPAMDK 536
Cdd:COG3147      2 AEEAAAAPAAAAAPAAPAAAAAPAPAAAAAAAAPKPAAKPaAPKPA-AAAAAAPAAKAAAPAGGG 65
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
864-1089 1.09e-93

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 298.04  E-value: 1.09e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  864 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPMQWAAFLGTPFLSSTE--GQLERVARIYRH 941
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEggGQVIKVKKVIVH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  942 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGPTR-PPEGARCVITGWGSLREGGSMARQLQKAAVRVLSEQTCRRFY 1020
Cdd:cd00190     80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2067662268 1021 --PVQISSRMLCAGFPQGGVDSCSGDAGGPLACREPsGQWVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWI 1089
Cdd:cd00190    160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
238-467 1.81e-93

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 297.67  E-value: 1.81e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268   238 RIVGGAEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEaSAVRARVLRIAK 316
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGE-EGQVIKVSKVII 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268   317 HPAYNADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPRKKCLISGWGYLKEDFLVKPEVLQKATVELLDQNLCSS 396
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRR 158
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2067662268   397 LYG--HSLTDRMVCAGYLDGKVDSCQGDSGGPLVCEepSGRFFLAGVVSWGIGCAEARRPGVYTRVTRLRDWI 467
Cdd:smart00020  159 AYSggGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
239-467 1.46e-92

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 295.34  E-value: 1.46e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  239 IVGGAEAAPGEFPWQVSLR-ENHEHFCGATIIGARWLVSAAHCFNEFqDPAQWAAQAGSVHLSGSEASAVRARVLRIAKH 317
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  318 PAYNADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPRKKCLISGWGYLKEDfLVKPEVLQKATVELLDQNLCSSL 397
Cdd:cd00190     80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRA 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2067662268  398 YGHS--LTDRMVCAGYLDGKVDSCQGDSGGPLVCEEPsGRFFLAGVVSWGIGCAEARRPGVYTRVTRLRDWI 467
Cdd:cd00190    159 YSYGgtITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
863-1089 1.29e-91

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 292.66  E-value: 1.29e-91
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268   863 RIVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvYGDPMQWAAFLGTPFLSSTE-GQLERVARIYRH 941
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEeGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268   942 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGP-TRPPEGARCVITGWGSLREG-GSMARQLQKAAVRVLSEQTCRRF 1019
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2067662268  1020 YPVQ--ISSRMLCAGFPQGGVDSCSGDAGGPLACRepSGQWVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWI 1089
Cdd:smart00020  160 YSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
540-767 1.76e-87

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 281.47  E-value: 1.76e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  540 IVGGISAVSGEVPWQASLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKLEQVQAHLGTVSLLGVGGSPVKLGLRSVALHP 618
Cdd:cd00190      1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  619 RYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGnATKPDILQKASVGIIEQKMCGALY 698
Cdd:cd00190     81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG-GPLPDVLQEVNVPIVSNAECKRAY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2067662268  699 --NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACeETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 767
Cdd:cd00190    160 syGGTITDNMLCAGGLEGGKDACQGDSGGPLVC-NDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
539-767 3.94e-87

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 280.33  E-value: 3.94e-87
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268   539 RIVGGISAVSGEVPWQASLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKLEQVQAHLGTVSLLgVGGSPVKLGLRSVALH 617
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQyGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLS-SGEEGQVIKVSKVIIH 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268   618 PRYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKASVGIIEQKMCGAL 697
Cdd:smart00020   80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2067662268   698 Y--NFSLTDRMLCAGFLEGRVDSCQGDSGGPLACEEtpGVFYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 767
Cdd:smart00020  160 YsgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCND--GRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
239-467 2.66e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 241.96  E-value: 2.66e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  239 IVGGAEAAPGEFPWQVSL-RENHEHFCGATIIGARWLVSAAHCFNefqDPAQWAAQAGSVHLSGSEASAVRARVLRIAKH 317
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  318 PAYNADTADFDVAVLELARPLPFGRYVQPACLPAATHVFPPRKKCLISGWGYLKEDflVKPEVLQKATVELLDQNLCSSL 397
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRSA 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  398 YGHSLTDRMVCAGYldGKVDSCQGDSGGPLVCEEPsgrfFLAGVVSWGIGCAEARRPGVYTRVTRLRDWI 467
Cdd:pfam00089  156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
835-1095 8.72e-70

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 233.77  E-value: 8.72e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  835 TRRQTPAPGTTVFSHLPDCGLAPPGALTRIVGGSAASLGEWPWQVSLWLR--RREHRCGAVLVAERWLLSAAHCFDVYGd 912
Cdd:COG5640      2 RRRRLLAALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDG- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  913 PMQWAAFLGTPFLSSTEGQLERVARIYRHPFYNIYTLDYDVALLELAGPVRRsrlVRPICLPGPTRPPE-GARCVITGWG 991
Cdd:COG5640     81 PSDLRVVIGSTDLSTSGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAApGTPATVAGWG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  992 SLREG-GSMARQLQKAAVRVLSEQTCRRfYPVQISSRMLCAGFPQGGVDSCSGDAGGPLAcREPSGQWVLTGVTSWGYGC 1070
Cdd:COG5640    158 RTSEGpGSQSGTLRKADVPVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGP 235
                          250       260
                   ....*....|....*....|....*
gi 2067662268 1071 GRPHFPGVYTRVAAVLGWIGQNIRE 1095
Cdd:COG5640    236 CAAGYPGVYTRVSAYRDWIKSTAGG 260
Trypsin pfam00089
Trypsin;
864-1089 1.30e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 231.95  E-value: 1.30e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  864 IVGGSAASLGEWPWQVSLWLRRREHRCGAVLVAERWLLSAAHCFDvygDPMQWAAFLGTPFLSSTEG--QLERVARIYRH 941
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGAHNIVLREGgeQKFDVEKIIVH 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  942 PFYNIYTLDYDVALLELAGPVRRSRLVRPICLPGPTR-PPEGARCVITGWGSLREGGSmARQLQKAAVRVLSEQTCRRFY 1020
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSdLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2067662268 1021 PVQISSRMLCAGFpqGGVDSCSGDAGGPLACrepSGQwVLTGVTSWGYGCGRPHFPGVYTRVAAVLGWI 1089
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVC---SDG-ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
Trypsin pfam00089
Trypsin;
540-767 4.19e-69

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 230.41  E-value: 4.19e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  540 IVGGISAVSGEVPWQASLK-EGSRHFCGATVVGDRWLLSAAHCFNHTKleQVQAHLGTVSLLGVGGSPVKLGLRSVALHP 618
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGAS--DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  619 RYNPGILDFDVALLELAQPLVFNKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNatKPDILQKASVGIIEQKMCGALY 698
Cdd:pfam00089   79 NYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2067662268  699 NFSLTDRMLCAGFleGRVDSCQGDSGGPLACEETpgvfYLAGIVSWGIGCAQAKKPGVYARITRLKDWI 767
Cdd:pfam00089  157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
230-475 3.23e-66

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 224.14  E-value: 3.23e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  230 QPAWRSAGRIVGGAEAAPGEFPWQVSLREN---HEHFCGATIIGARWLVSAAHCFNEfQDPAQWAAQAGSVHLSGSEAsa 306
Cdd:COG5640     22 APAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGG-- 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  307 VRARVLRIAKHPAYNADTADFDVAVLELARPLPFgryVQPACLPAATHVFPPRKKCLISGWGYLKEDFLVKPEVLQKATV 386
Cdd:COG5640     99 TVVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADV 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  387 ELLDQNLCSSlYGHSLTDRMVCAGYLDGKVDSCQGDSGGPLVcEEPSGRFFLAGVVSWGIGCAEARRPGVYTRVTRLRDW 466
Cdd:COG5640    176 PVVSDATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                   ....*....
gi 2067662268  467 ILEVTSSAD 475
Cdd:COG5640    254 IKSTAGGLG 262
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
529-775 6.64e-60

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 206.04  E-value: 6.64e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  529 GARPAMDKPTRIVGGISAVSGEVPWQASL---KEGSRHFCGATVVGDRWLLSAAHCFNHTKLEQVQAHLGTVSLLGVGGs 605
Cdd:COG5640     20 AAAPAADAAPAIVGGTPATVGEYPWMVALqssNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGG- 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  606 pVKLGLRSVALHPRYNPGILDFDVALLELAQPLvfnKYIQPVCLPLAIHKFPVGRKCMISGWGNMQEGNATKPDILQKAS 685
Cdd:COG5640     99 -TVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  686 VGIIEQKMCGALYNFsLTDRMLCAGFLEGRVDSCQGDSGGPLAcEETPGVFYLAGIVSWGIGCAQAKKPGVYARITRLKD 765
Cdd:COG5640    175 VPVVSDATCAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252
                          250
                   ....*....|
gi 2067662268  766 WILKAMSSDP 775
Cdd:COG5640    253 WIKSTAGGLG 262
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
190-225 1.38e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 51.44  E-value: 1.38e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2067662268  190 CPGNAFSCQNSQCVSKENpECDDRVDCSDGSDEAQC 225
Cdd:cd00112      1 CPPNEFRCANGRCIPSSW-VCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
190-222 5.65e-08

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 49.55  E-value: 5.65e-08
                            10        20        30
                    ....*....|....*....|....*....|...
gi 2067662268   190 CPGNAFSCQNSQCVSKENpECDDRVDCSDGSDE 222
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSW-VCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
190-225 7.94e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 46.47  E-value: 7.94e-07
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2067662268  190 CPGNAFSCQNSQCVSKeNPECDDRVDCSDGSDEAQC 225
Cdd:pfam00057    3 CSPNEFQCGSGECIPR-SWVCDGDPDCGDGSDEENC 37
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
560-745 5.04e-06

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 48.52  E-value: 5.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  560 GSRHFCGATVVGDRWLLSAAHCFNHTklEQVQAHLGTVSLLGVGGSP-VKLGLRSVALHPRY-NPGILDFDVALLELAQP 637
Cdd:COG3591      9 GGGGVCTGTLIGPNLVLTAGHCVYDG--AGGGWATNIVFVPGYNGGPyGTATATRFRVPPGWvASGDAGYDYALLRLDEP 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  638 LVFnkyiQPVCLPLAI-HKFPVGRKCMISGWGnmqegnATKPDILQKASVGIIeqkmcgalynFSLTDRmlcagFLEGRV 716
Cdd:COG3591     87 LGD----TTGWLGLAFnDAPLAGEPVTIIGYP------GDRPKDLSLDCSGRV----------TGVQGN-----RLSYDC 141
                          170       180
                   ....*....|....*....|....*....
gi 2067662268  717 DSCQGDSGGPLaCEETPGVFYLAGIVSWG 745
Cdd:COG3591    142 DTTGGSSGSPV-LDDSDGGGRVVGVHSAG 169
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
262-445 5.19e-06

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 48.52  E-value: 5.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  262 HFCGATIIGARWLVSAAHCFNEFQD---PAQWAAQAGsvhLSGSEASAVRARVLRIakHPAYNADT-ADFDVAVLELARP 337
Cdd:COG3591     12 GVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPG---YNGGPYGTATATRFRV--PPGWVASGdAGYDYALLRLDEP 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  338 LPfgryvqpaclpaathvfpprkkcliSGWGYLKEDFLVKPEVLQKATVelldqnlcsslYGHSLTDRMVCAGYLDGKV- 416
Cdd:COG3591     87 LG-------------------------DTTGWLGLAFNDAPLAGEPVTI-----------IGYPGDRPKDLSLDCSGRVt 130
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2067662268  417 -----------DSCQGDSGGPLVCEEpSGRFFLAGVVSWG 445
Cdd:COG3591    131 gvqgnrlsydcDTTGGSSGSPVLDDS-DGGGRVVGVHSAG 169
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
68-148 2.30e-05

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


Pssm-ID: 460188  Cd Length: 100  Bit Score: 44.15  E-value: 2.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268   68 VRFTSLLQQENSDFYRLLTPALQTLFVRSFQKTELESSCTGCTVLSYRDGNSSVIVHFRLHFllralQPLSLDQEADILQ 147
Cdd:pfam01390   12 LQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVF-----RFPSTEPALDREK 86

                   .
gi 2067662268  148 K 148
Cdd:pfam01390   87 L 87
PHA03247 PHA03247
large tegument protein UL36; Provisional
463-539 7.82e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 7.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  463 LRDWILEVTSSADTP---VVPTEAPAPITPSTPWPTSPESRVPNTTAKP-TVAPTPAPLHPSTAAKPQECGARPAMDKPT 538
Cdd:PHA03247  2688 ARPTVGSLTSLADPPpppPTPEPAPHALVSATPLPPGPAAARQASPALPaAPAPPAVPAGPATPGGPARPARPPTTAGPP 2767

                   .
gi 2067662268  539 R 539
Cdd:PHA03247  2768 A 2768
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
473-536 5.19e-03

Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442381 [Multi-domain]  Cd Length: 140  Bit Score: 38.60  E-value: 5.19e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2067662268  473 SADTPVVPTEAPAPITPSTPWPTSPESRVPNTTAKPTVAP-TPAPLhPSTAAKPQECGARPAMDK 536
Cdd:COG3147      2 AEEAAAAPAAAAAPAAPAAAAAPAPAAAAAAAAPKPAAKPaAPKPA-AAAAAAPAAKAAAPAGGG 65
COG5373 COG5373
Uncharacterized membrane protein [Function unknown];
436-527 6.84e-03

Uncharacterized membrane protein [Function unknown];


Pssm-ID: 444140 [Multi-domain]  Cd Length: 854  Bit Score: 40.37  E-value: 6.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067662268  436 FFLAGVVSWGIGCAEARRPGVYTRVTRLRDWILEVTSSADTPVVPT-EAPAPITPSTPWP-TSPESRVPNTTAKPTVAPT 513
Cdd:COG5373      6 ILIGLLVLALLVGLLGRVARLRRRVEELEAELAEAAEAASAPAEPEpEAAAAATAAAPEAaPAPVPEAPAAPPAAAEAPA 85
                           90
                   ....*....|....
gi 2067662268  514 PAPLHPSTAAKPQE 527
Cdd:COG5373     86 PAAAAPPAEAEPAA 99
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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