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Conserved domains on  [gi|24643047|ref|NP_573298|]
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uncharacterized protein Dmel_CG15046 [Drosophila melanogaster]

Protein Classification

serine protease family protein; serine protease( domain architecture ID 10653444)

trypsin-like serine protease family protein| 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
CLIP smart00680
Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, ...
 168-215 2.34e-07

Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, Drosophila Easter and silkworm prophenoloxidase-activating enzyme.


:

Pssm-ID: 197829  Cd Length: 52  Bit Score: 47.50  E-value: 2.34e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 24643047    168 CTAP-LYEGQCRAVSACPSVEPLLSQG---RLRDEDFTTCREGTHEEIICCP 215
Cdd:smart00680   1 CRTPdGERGTCVPISDCPSLLSLLKKDppeDLNFLRKSQCGFGNREPLVCCP 52
CLIP smart00680
Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, ...
 35-82 1.15e-06

Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, Drosophila Easter and silkworm prophenoloxidase-activating enzyme.


:

Pssm-ID: 197829  Cd Length: 52  Bit Score: 45.58  E-value: 1.15e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 24643047     35 CPTVN-YRSRCQALEDCETLASHLKTG---RLTLRAVMNCGFTTRSEKICCP 82
Cdd:smart00680   1 CRTPDgERGTCVPISDCPSLLSLLKKDppeDLNFLRKSQCGFGNREPLVCCP 52
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 274-379 4.69e-04

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.


The actual alignment was detected with superfamily member cd00190:

Pssm-ID: 473915 [Multi-domain]  Cd Length: 232  Bit Score: 41.88  E-value: 4.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643047 274 FDGHLHHCAALVLTPQLLVSAAGCERPSHA-----VFGVADLRDVDADEDYLaDIVRLVQ--------FQKDLSLIRLQD 340
Cdd:cd00190  20 YTGGRHFCGGSLISPRWVLTAAHCVYSSAPsnytvRLGSHDLSSNEGGGQVI-KVKKVIVhpnynpstYDNDIALLKLKR 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 24643047 341 PLRLGSqtsanvSVAPICtqfeltrLQRSGSLVAV-------GWGK 379
Cdd:cd00190  99 PVTLSD------NVRPIC-------LPSSGYNLPAgttctvsGWGR 131
 
Name Accession Description Interval E-value
CLIP smart00680
Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, ...
 168-215 2.34e-07

Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, Drosophila Easter and silkworm prophenoloxidase-activating enzyme.


Pssm-ID: 197829  Cd Length: 52  Bit Score: 47.50  E-value: 2.34e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 24643047    168 CTAP-LYEGQCRAVSACPSVEPLLSQG---RLRDEDFTTCREGTHEEIICCP 215
Cdd:smart00680   1 CRTPdGERGTCVPISDCPSLLSLLKKDppeDLNFLRKSQCGFGNREPLVCCP 52
CLIP smart00680
Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, ...
 35-82 1.15e-06

Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, Drosophila Easter and silkworm prophenoloxidase-activating enzyme.


Pssm-ID: 197829  Cd Length: 52  Bit Score: 45.58  E-value: 1.15e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 24643047     35 CPTVN-YRSRCQALEDCETLASHLKTG---RLTLRAVMNCGFTTRSEKICCP 82
Cdd:smart00680   1 CRTPDgERGTCVPISDCPSLLSLLKKDppeDLNFLRKSQCGFGNREPLVCCP 52
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 274-379 4.69e-04

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: 41.88  E-value: 4.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643047 274 FDGHLHHCAALVLTPQLLVSAAGCERPSHA-----VFGVADLRDVDADEDYLaDIVRLVQ--------FQKDLSLIRLQD 340
Cdd:cd00190  20 YTGGRHFCGGSLISPRWVLTAAHCVYSSAPsnytvRLGSHDLSSNEGGGQVI-KVKKVIVhpnynpstYDNDIALLKLKR 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 24643047 341 PLRLGSqtsanvSVAPICtqfeltrLQRSGSLVAV-------GWGK 379
Cdd:cd00190  99 PVTLSD------NVRPIC-------LPSSGYNLPAgttctvsGWGR 131
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 274-426 8.21e-04

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: 41.12  E-value: 8.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643047    274 FDGHLHHCAALVLTPQLLVSAAGCERPSHA-----VFGVADLRDVDADEDYLADIVRL------VQFQKDLSLIRLQDPL 342
Cdd:smart00020  21 YGGGRHFCGGSLISPRWVLTAAHCVRGSDPsnirvRLGSHDLSSGEEGQVIKVSKVIIhpnynpSTYDNDIALLKLKEPV 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643047    343 RLGSqtsanvSVAPICTQFELTRLQRSGSLVAVGWGKGEDTDCPLFEMPMRLR----PTWACgdLPNYGGVQDLGSSHLC 418
Cdd:smart00020 101 TLSD------NVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNvpivSNATC--RRAYSGGGAITDNMLC 172


                   ....*...
gi 24643047    419 VEPMDGER 426
Cdd:smart00020 173 AGGLEGGK 180
 
Name Accession Description Interval E-value
CLIP smart00680
Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, ...
 168-215 2.34e-07

Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, Drosophila Easter and silkworm prophenoloxidase-activating enzyme.


Pssm-ID: 197829  Cd Length: 52  Bit Score: 47.50  E-value: 2.34e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 24643047    168 CTAP-LYEGQCRAVSACPSVEPLLSQG---RLRDEDFTTCREGTHEEIICCP 215
Cdd:smart00680   1 CRTPdGERGTCVPISDCPSLLSLLKKDppeDLNFLRKSQCGFGNREPLVCCP 52
CLIP smart00680
Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, ...
 35-82 1.15e-06

Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, Drosophila Easter and silkworm prophenoloxidase-activating enzyme.


Pssm-ID: 197829  Cd Length: 52  Bit Score: 45.58  E-value: 1.15e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 24643047     35 CPTVN-YRSRCQALEDCETLASHLKTG---RLTLRAVMNCGFTTRSEKICCP 82
Cdd:smart00680   1 CRTPDgERGTCVPISDCPSLLSLLKKDppeDLNFLRKSQCGFGNREPLVCCP 52
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 274-379 4.69e-04

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: 41.88  E-value: 4.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643047 274 FDGHLHHCAALVLTPQLLVSAAGCERPSHA-----VFGVADLRDVDADEDYLaDIVRLVQ--------FQKDLSLIRLQD 340
Cdd:cd00190  20 YTGGRHFCGGSLISPRWVLTAAHCVYSSAPsnytvRLGSHDLSSNEGGGQVI-KVKKVIVhpnynpstYDNDIALLKLKR 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 24643047 341 PLRLGSqtsanvSVAPICtqfeltrLQRSGSLVAV-------GWGK 379
Cdd:cd00190  99 PVTLSD------NVRPIC-------LPSSGYNLPAgttctvsGWGR 131
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 274-426 8.21e-04

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: 41.12  E-value: 8.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643047    274 FDGHLHHCAALVLTPQLLVSAAGCERPSHA-----VFGVADLRDVDADEDYLADIVRL------VQFQKDLSLIRLQDPL 342
Cdd:smart00020  21 YGGGRHFCGGSLISPRWVLTAAHCVRGSDPsnirvRLGSHDLSSGEEGQVIKVSKVIIhpnynpSTYDNDIALLKLKEPV 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643047    343 RLGSqtsanvSVAPICTQFELTRLQRSGSLVAVGWGKGEDTDCPLFEMPMRLR----PTWACgdLPNYGGVQDLGSSHLC 418
Cdd:smart00020 101 TLSD------NVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNvpivSNATC--RRAYSGGGAITDNMLC 172


                   ....*...
gi 24643047    419 VEPMDGER 426
Cdd:smart00020 173 AGGLEGGK 180
 
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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