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Conserved domains on  [gi|471012806|ref|NP_001264176|]
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acrosin isoform 4 precursor [Mus musculus]

Protein Classification

S1 family serine peptidase( domain architecture ID 12184331)

S1 family trypsin-like serine peptidase such as snake venom serine proteases and trypsin, which preferentially cleaves peptide bonds after arginine and lysine residues

CATH:  2.40.10.10
EC:  3.4.-.-
Gene Ontology:  GO:0008236|GO:0006508
MEROPS:  S1
SCOP:  3000114

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
27-244 3.39e-88

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: 266.47  E-value: 3.39e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806    27 RRYHACGGSLLNSHWVLTAAHCFDNKKKvYDWRLVFGAQEIEYGrnkpvkEPQQERYVQKIVIHEKYNVVTEGNDIALLK 106
Cdd:smart00020  23 GGRHFCGGSLISPRWVLTAAHCVRGSDP-SNIRVRLGSHDLSSG------EEGQVIKVSKVIIHPNYNPSTYDNDIALLK 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806   107 ITPPVTCGNFIGPCCLPHFKAGPPQiPHTCYVTGWGYIKEKAPRPSPVLMEARVDLIDLDLCNSTQWYNGRVTSTNVCAG 186
Cdd:smart00020  96 LKEPVTLSDNVRPICLPSSNYNVPA-GTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGGGAITDNMLCAG 174
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 471012806   187 YPEGKIDTCQGDSGGPLMCRDNVdspFVVVGITSWGVGCARAKRPGVYTATWDYLDWI 244
Cdd:smart00020 175 GLEGGKDACQGDSGGPLVCNDGR---WVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
27-244 3.39e-88

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: 266.47  E-value: 3.39e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806    27 RRYHACGGSLLNSHWVLTAAHCFDNKKKvYDWRLVFGAQEIEYGrnkpvkEPQQERYVQKIVIHEKYNVVTEGNDIALLK 106
Cdd:smart00020  23 GGRHFCGGSLISPRWVLTAAHCVRGSDP-SNIRVRLGSHDLSSG------EEGQVIKVSKVIIHPNYNPSTYDNDIALLK 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806   107 ITPPVTCGNFIGPCCLPHFKAGPPQiPHTCYVTGWGYIKEKAPRPSPVLMEARVDLIDLDLCNSTQWYNGRVTSTNVCAG 186
Cdd:smart00020  96 LKEPVTLSDNVRPICLPSSNYNVPA-GTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGGGAITDNMLCAG 174
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 471012806   187 YPEGKIDTCQGDSGGPLMCRDNVdspFVVVGITSWGVGCARAKRPGVYTATWDYLDWI 244
Cdd:smart00020 175 GLEGGKDACQGDSGGPLVCNDGR---WVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
26-247 7.13e-84

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: 255.28  E-value: 7.13e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806  26 DRRYHACGGSLLNSHWVLTAAHCFDNKKkVYDWRLVFGaqeiEYGRNKPvKEPQQERYVQKIVIHEKYNVVTEGNDIALL 105
Cdd:cd00190   21 TGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLG----SHDLSSN-EGGGQVIKVKKVIVHPNYNPSTYDNDIALL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806 106 KITPPVTCGNFIGPCCLPHFKAGPPQiPHTCYVTGWGYIKEKAPRPSpVLMEARVDLIDLDLCNSTQWYNGRVTSTNVCA 185
Cdd:cd00190   95 KLKRPVTLSDNVRPICLPSSGYNLPA-GTTCTVSGWGRTSEGGPLPD-VLQEVNVPIVSNAECKRAYSYGGTITDNMLCA 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 471012806 186 GYPEGKIDTCQGDSGGPLMCRDNvdSPFVVVGITSWGVGCARAKRPGVYTATWDYLDWIASK 247
Cdd:cd00190  173 GGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
27-244 1.54e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 220.78  E-value: 1.54e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806   27 RRYHACGGSLLNSHWVLTAAHCFDNKKkvyDWRLVFGAQEIEYGRnkpvkEPQQERYVQKIVIHEKYNVVTEGNDIALLK 106
Cdd:pfam00089  22 SGKHFCGGSLISENWVLTAAHCVSGAS---DVKVVLGAHNIVLRE-----GGEQKFDVEKIIVHPNYNPDTLDNDIALLK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806  107 ITPPVTCGNFIGPCCLPHFKAgPPQIPHTCYVTGWGYIKEKapRPSPVLMEARVDLIDLDLCNStqWYNGRVTSTNVCAG 186
Cdd:pfam00089  94 LESPVTLGDTVRPICLPDASS-DLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRS--AYGGTVTDTMICAG 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 471012806  187 YpeGKIDTCQGDSGGPLMCRDNvdspfVVVGITSWGVGCARAKRPGVYTATWDYLDWI 244
Cdd:pfam00089 169 A--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
28-249 6.24e-60

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 194.87  E-value: 6.24e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806  28 RYHACGGSLLNSHWVLTAAHCFDNKKKVyDWRLVfgaqeieYGRNKPVKEPQQERYVQKIVIHEKYNVVTEGNDIALLKI 107
Cdd:COG5640   55 SGQFCGGTLIAPRWVLTAAHCVDGDGPS-DLRVV-------IGSTDLSTSGGTVVKVARIVVHPDYDPATPGNDIALLKL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806 108 TPPVTcgnFIGPCCLP----HFKAGPPQIphtcyVTGWGYIKEKAPRPSPVLMEARVDLIDLDLCNStqwYNGRVTSTNV 183
Cdd:COG5640  127 ATPVP---GVAPAPLAtsadAAAPGTPAT-----VAGWGRTSEGPGSQSGTLRKADVPVVSDATCAA---YGGFDGGTML 195
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 471012806 184 CAGYPEGKIDTCQGDSGGPLMcrDNVDSPFVVVGITSWGVGCARAKRPGVYTATWDYLDWIASKIG 249
Cdd:COG5640  196 CAGYPEGGKDACQGDSGGPLV--VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAG 259
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
27-244 3.39e-88

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: 266.47  E-value: 3.39e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806    27 RRYHACGGSLLNSHWVLTAAHCFDNKKKvYDWRLVFGAQEIEYGrnkpvkEPQQERYVQKIVIHEKYNVVTEGNDIALLK 106
Cdd:smart00020  23 GGRHFCGGSLISPRWVLTAAHCVRGSDP-SNIRVRLGSHDLSSG------EEGQVIKVSKVIIHPNYNPSTYDNDIALLK 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806   107 ITPPVTCGNFIGPCCLPHFKAGPPQiPHTCYVTGWGYIKEKAPRPSPVLMEARVDLIDLDLCNSTQWYNGRVTSTNVCAG 186
Cdd:smart00020  96 LKEPVTLSDNVRPICLPSSNYNVPA-GTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGGGAITDNMLCAG 174
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 471012806   187 YPEGKIDTCQGDSGGPLMCRDNVdspFVVVGITSWGVGCARAKRPGVYTATWDYLDWI 244
Cdd:smart00020 175 GLEGGKDACQGDSGGPLVCNDGR---WVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
26-247 7.13e-84

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: 255.28  E-value: 7.13e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806  26 DRRYHACGGSLLNSHWVLTAAHCFDNKKkVYDWRLVFGaqeiEYGRNKPvKEPQQERYVQKIVIHEKYNVVTEGNDIALL 105
Cdd:cd00190   21 TGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLG----SHDLSSN-EGGGQVIKVKKVIVHPNYNPSTYDNDIALL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806 106 KITPPVTCGNFIGPCCLPHFKAGPPQiPHTCYVTGWGYIKEKAPRPSpVLMEARVDLIDLDLCNSTQWYNGRVTSTNVCA 185
Cdd:cd00190   95 KLKRPVTLSDNVRPICLPSSGYNLPA-GTTCTVSGWGRTSEGGPLPD-VLQEVNVPIVSNAECKRAYSYGGTITDNMLCA 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 471012806 186 GYPEGKIDTCQGDSGGPLMCRDNvdSPFVVVGITSWGVGCARAKRPGVYTATWDYLDWIASK 247
Cdd:cd00190  173 GGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
27-244 1.54e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 220.78  E-value: 1.54e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806   27 RRYHACGGSLLNSHWVLTAAHCFDNKKkvyDWRLVFGAQEIEYGRnkpvkEPQQERYVQKIVIHEKYNVVTEGNDIALLK 106
Cdd:pfam00089  22 SGKHFCGGSLISENWVLTAAHCVSGAS---DVKVVLGAHNIVLRE-----GGEQKFDVEKIIVHPNYNPDTLDNDIALLK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806  107 ITPPVTCGNFIGPCCLPHFKAgPPQIPHTCYVTGWGYIKEKapRPSPVLMEARVDLIDLDLCNStqWYNGRVTSTNVCAG 186
Cdd:pfam00089  94 LESPVTLGDTVRPICLPDASS-DLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRS--AYGGTVTDTMICAG 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 471012806  187 YpeGKIDTCQGDSGGPLMCRDNvdspfVVVGITSWGVGCARAKRPGVYTATWDYLDWI 244
Cdd:pfam00089 169 A--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
28-249 6.24e-60

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 194.87  E-value: 6.24e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806  28 RYHACGGSLLNSHWVLTAAHCFDNKKKVyDWRLVfgaqeieYGRNKPVKEPQQERYVQKIVIHEKYNVVTEGNDIALLKI 107
Cdd:COG5640   55 SGQFCGGTLIAPRWVLTAAHCVDGDGPS-DLRVV-------IGSTDLSTSGGTVVKVARIVVHPDYDPATPGNDIALLKL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806 108 TPPVTcgnFIGPCCLP----HFKAGPPQIphtcyVTGWGYIKEKAPRPSPVLMEARVDLIDLDLCNStqwYNGRVTSTNV 183
Cdd:COG5640  127 ATPVP---GVAPAPLAtsadAAAPGTPAT-----VAGWGRTSEGPGSQSGTLRKADVPVVSDATCAA---YGGFDGGTML 195
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 471012806 184 CAGYPEGKIDTCQGDSGGPLMcrDNVDSPFVVVGITSWGVGCARAKRPGVYTATWDYLDWIASKIG 249
Cdd:COG5640  196 CAGYPEGGKDACQGDSGGPLV--VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAG 259
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
26-224 2.93e-13

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 67.78  E-value: 2.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806  26 DRRYHACGGSLLNSHWVLTAAHCFDNKKK---VYDWRLVFGAQEIEYGRNKpvkepqqeryVQKIVIHEKYNVVT-EGND 101
Cdd:COG3591    8 DGGGGVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPGYNGGPYGTAT----------ATRFRVPPGWVASGdAGYD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806 102 IALLKITPPVtcGNFIGPccLPHFKAGPPQIPHTCYVTGWGYIKEKAPrpspvlmearvdlidldlcnsTQWYNGRVTST 181
Cdd:COG3591   78 YALLRLDEPL--GDTTGW--LGLAFNDAPLAGEPVTIIGYPGDRPKDL---------------------SLDCSGRVTGV 132
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 471012806 182 NvcAGYPEGKIDTCQGDSGGPLMcrDNVDSPFVVVGITSWGVG 224
Cdd:COG3591  133 Q--GNRLSYDCDTTGGSSGSPVL--DDSDGGGRVVGVHSAGGA 171
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
168-243 7.73e-07

alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and similar proteins; This family represents the catalytic domain of alpha-lytic protease (alpha-LP) and its closely-related homologs. Alpha-lytic protease (EC 3.4.21.12; also called alpha-lytic endopeptidase), originally isolated from the myxobacterium Lysobacter enzymogenes, belongs to the MEROPS peptidase family S1, subfamily S1E (streptogrisin A subfamily). It is synthesized as a pro-enzyme, thus having two domains; the N-terminal pro-domain acts as a foldase, required transiently for the correct folding of the protease domain, and also acts as a potent inhibitor of the mature enzyme, while the C-terminal domain catalyzes the cleavage of peptide bonds. Members of the alpha-lytic protease subfamily include Nocardiopsis alba protease (NAPase), a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis, streptogrisins (SPG-A, SPG-B, SPG-C, and SPG-D), and Thermobifida fusca protease A (TFPA). These serine proteases have characteristic kinetic stability, exhibited by their extremely slow unfolding kinetics. The active site, characteristic of serine proteases, contains the catalytic triad consisting of serine acting as a nucleophile, aspartate as an electrophile, and histidine as a base, all required for activity. This model represents the C-terminal catalytic domain of alpha-lytic proteases.


Pssm-ID: 411050  Cd Length: 188  Bit Score: 49.23  E-value: 7.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012806 168 CNS---TQWYNGRVTSTNVCAGYPEGKI------DTC--QGDSGGPLMcrdnvdSPFVVVGITSWGVG-CARAKRPGVYT 235
Cdd:cd21112  105 CKSgrtTGWTCGTVTAVNVTVNYPGGTVtgltrtNACaePGDSGGPVF------SGTQALGITSGGSGnCGSGGGTSYFQ 178

                 ....*...
gi 471012806 236 ATWDYLDW 243
Cdd:cd21112  179 PVNPVLSA 186
 
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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