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Conserved domains on  [gi|471012474|ref|NP_001264175|]
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acrosin isoform 3 [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 ...
1-230 2.29e-90

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: 271.47  E-value: 2.29e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474     1 MVSLQIftshnSRRYHACGGSLLNSHWVLTAAHCFDNKKKvYDWRLVFGAQEIEYGrnkpvkEPQQERYVQKIVIHEKYN 80
Cdd:smart00020  16 QVSLQY-----GGGRHFCGGSLISPRWVLTAAHCVRGSDP-SNIRVRLGSHDLSSG------EEGQVIKVSKVIIHPNYN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474    81 VVTEGNDIALLKITPPVTCGNFIGPCCLPHFKAGPPQiPHTCYVTGWGYIKEKAPRPSPVLMEARVDLIDLDLCNSTQWY 160
Cdd:smart00020  84 PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPA-GTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYSG 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474   161 NGRVTSTNVCAGYPEGKIDTCQGDSGGPLMCRDNVdspFVVVGITSWGVGCARAKRPGVYTATWDYLDWI 230
Cdd:smart00020 163 GGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR---WVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-230 2.29e-90

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: 271.47  E-value: 2.29e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474     1 MVSLQIftshnSRRYHACGGSLLNSHWVLTAAHCFDNKKKvYDWRLVFGAQEIEYGrnkpvkEPQQERYVQKIVIHEKYN 80
Cdd:smart00020  16 QVSLQY-----GGGRHFCGGSLISPRWVLTAAHCVRGSDP-SNIRVRLGSHDLSSG------EEGQVIKVSKVIIHPNYN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474    81 VVTEGNDIALLKITPPVTCGNFIGPCCLPHFKAGPPQiPHTCYVTGWGYIKEKAPRPSPVLMEARVDLIDLDLCNSTQWY 160
Cdd:smart00020  84 PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPA-GTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYSG 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474   161 NGRVTSTNVCAGYPEGKIDTCQGDSGGPLMCRDNVdspFVVVGITSWGVGCARAKRPGVYTATWDYLDWI 230
Cdd:smart00020 163 GGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR---WVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-233 4.67e-86

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: 260.29  E-value: 4.67e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474   1 MVSLQiftshNSRRYHACGGSLLNSHWVLTAAHCFDNKKkVYDWRLVFGaqeiEYGRNKPvKEPQQERYVQKIVIHEKYN 80
Cdd:cd00190   15 QVSLQ-----YTGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLG----SHDLSSN-EGGGQVIKVKKVIVHPNYN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474  81 VVTEGNDIALLKITPPVTCGNFIGPCCLPHFKAGPPQiPHTCYVTGWGYIKEKAPRPSpVLMEARVDLIDLDLCNSTQWY 160
Cdd:cd00190   84 PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPA-GTTCTVSGWGRTSEGGPLPD-VLQEVNVPIVSNAECKRAYSY 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 471012474 161 NGRVTSTNVCAGYPEGKIDTCQGDSGGPLMCRDNvdSPFVVVGITSWGVGCARAKRPGVYTATWDYLDWIASK 233
Cdd:cd00190  162 GGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
1-230 3.07e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 224.63  E-value: 3.07e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474    1 MVSLQIftshnSRRYHACGGSLLNSHWVLTAAHCFDNKKkvyDWRLVFGAQEIEYGRnkpvkEPQQERYVQKIVIHEKYN 80
Cdd:pfam00089  15 QVSLQL-----SSGKHFCGGSLISENWVLTAAHCVSGAS---DVKVVLGAHNIVLRE-----GGEQKFDVEKIIVHPNYN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474   81 VVTEGNDIALLKITPPVTCGNFIGPCCLPHFKAgPPQIPHTCYVTGWGYIKEKapRPSPVLMEARVDLIDLDLCNStqWY 160
Cdd:pfam00089  82 PDTLDNDIALLKLESPVTLGDTVRPICLPDASS-DLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRS--AY 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474  161 NGRVTSTNVCAGYpeGKIDTCQGDSGGPLMCRDNvdspfVVVGITSWGVGCARAKRPGVYTATWDYLDWI 230
Cdd:pfam00089 157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-235 8.21e-63

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 201.80  E-value: 8.21e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474   1 MVSLQiftSHNSRRYHACGGSLLNSHWVLTAAHCFDNKKKVyDWRLVfgaqeieYGRNKPVKEPQQERYVQKIVIHEKYN 80
Cdd:COG5640   45 MVALQ---SSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPS-DLRVV-------IGSTDLSTSGGTVVKVARIVVHPDYD 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474  81 VVTEGNDIALLKITPPVTcgnFIGPCCLP----HFKAGPPQIphtcyVTGWGYIKEKAPRPSPVLMEARVDLIDLDLCNS 156
Cdd:COG5640  114 PATPGNDIALLKLATPVP---GVAPAPLAtsadAAAPGTPAT-----VAGWGRTSEGPGSQSGTLRKADVPVVSDATCAA 185
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 471012474 157 tqwYNGRVTSTNVCAGYPEGKIDTCQGDSGGPLMcrDNVDSPFVVVGITSWGVGCARAKRPGVYTATWDYLDWIASKIG 235
Cdd:COG5640  186 ---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV--VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAG 259
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-230 2.29e-90

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: 271.47  E-value: 2.29e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474     1 MVSLQIftshnSRRYHACGGSLLNSHWVLTAAHCFDNKKKvYDWRLVFGAQEIEYGrnkpvkEPQQERYVQKIVIHEKYN 80
Cdd:smart00020  16 QVSLQY-----GGGRHFCGGSLISPRWVLTAAHCVRGSDP-SNIRVRLGSHDLSSG------EEGQVIKVSKVIIHPNYN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474    81 VVTEGNDIALLKITPPVTCGNFIGPCCLPHFKAGPPQiPHTCYVTGWGYIKEKAPRPSPVLMEARVDLIDLDLCNSTQWY 160
Cdd:smart00020  84 PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPA-GTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYSG 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474   161 NGRVTSTNVCAGYPEGKIDTCQGDSGGPLMCRDNVdspFVVVGITSWGVGCARAKRPGVYTATWDYLDWI 230
Cdd:smart00020 163 GGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR---WVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-233 4.67e-86

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: 260.29  E-value: 4.67e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474   1 MVSLQiftshNSRRYHACGGSLLNSHWVLTAAHCFDNKKkVYDWRLVFGaqeiEYGRNKPvKEPQQERYVQKIVIHEKYN 80
Cdd:cd00190   15 QVSLQ-----YTGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLG----SHDLSSN-EGGGQVIKVKKVIVHPNYN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474  81 VVTEGNDIALLKITPPVTCGNFIGPCCLPHFKAGPPQiPHTCYVTGWGYIKEKAPRPSpVLMEARVDLIDLDLCNSTQWY 160
Cdd:cd00190   84 PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPA-GTTCTVSGWGRTSEGGPLPD-VLQEVNVPIVSNAECKRAYSY 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 471012474 161 NGRVTSTNVCAGYPEGKIDTCQGDSGGPLMCRDNvdSPFVVVGITSWGVGCARAKRPGVYTATWDYLDWIASK 233
Cdd:cd00190  162 GGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
1-230 3.07e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 224.63  E-value: 3.07e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474    1 MVSLQIftshnSRRYHACGGSLLNSHWVLTAAHCFDNKKkvyDWRLVFGAQEIEYGRnkpvkEPQQERYVQKIVIHEKYN 80
Cdd:pfam00089  15 QVSLQL-----SSGKHFCGGSLISENWVLTAAHCVSGAS---DVKVVLGAHNIVLRE-----GGEQKFDVEKIIVHPNYN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474   81 VVTEGNDIALLKITPPVTCGNFIGPCCLPHFKAgPPQIPHTCYVTGWGYIKEKapRPSPVLMEARVDLIDLDLCNStqWY 160
Cdd:pfam00089  82 PDTLDNDIALLKLESPVTLGDTVRPICLPDASS-DLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRETCRS--AY 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474  161 NGRVTSTNVCAGYpeGKIDTCQGDSGGPLMCRDNvdspfVVVGITSWGVGCARAKRPGVYTATWDYLDWI 230
Cdd:pfam00089 157 GGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-235 8.21e-63

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 201.80  E-value: 8.21e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474   1 MVSLQiftSHNSRRYHACGGSLLNSHWVLTAAHCFDNKKKVyDWRLVfgaqeieYGRNKPVKEPQQERYVQKIVIHEKYN 80
Cdd:COG5640   45 MVALQ---SSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPS-DLRVV-------IGSTDLSTSGGTVVKVARIVVHPDYD 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474  81 VVTEGNDIALLKITPPVTcgnFIGPCCLP----HFKAGPPQIphtcyVTGWGYIKEKAPRPSPVLMEARVDLIDLDLCNS 156
Cdd:COG5640  114 PATPGNDIALLKLATPVP---GVAPAPLAtsadAAAPGTPAT-----VAGWGRTSEGPGSQSGTLRKADVPVVSDATCAA 185
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 471012474 157 tqwYNGRVTSTNVCAGYPEGKIDTCQGDSGGPLMcrDNVDSPFVVVGITSWGVGCARAKRPGVYTATWDYLDWIASKIG 235
Cdd:COG5640  186 ---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV--VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAG 259
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
18-210 5.96e-13

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 67.01  E-value: 5.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474  18 CGGSLLNSHWVLTAAHCFDNKKK---VYDWRLVFGAQEIEYGRNKpvkepqqeryVQKIVIHEKYNVVT-EGNDIALLKI 93
Cdd:COG3591   14 CTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPGYNGGPYGTAT----------ATRFRVPPGWVASGdAGYDYALLRL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474  94 TPPVtcGNFIGPccLPHFKAGPPQIPHTCYVTGWGYIKEKAPrpspvlmearvdlidldlcnsTQWYNGRVTSTNvcAGY 173
Cdd:COG3591   84 DEPL--GDTTGW--LGLAFNDAPLAGEPVTIIGYPGDRPKDL---------------------SLDCSGRVTGVQ--GNR 136
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 471012474 174 PEGKIDTCQGDSGGPLMcrDNVDSPFVVVGITSWGVG 210
Cdd:COG3591  137 LSYDCDTTGGSSGSPVL--DDSDGGGRVVGVHSAGGA 171
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
154-229 7.56e-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: 7.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471012474 154 CNS---TQWYNGRVTSTNVCAGYPEGKI------DTC--QGDSGGPLMcrdnvdSPFVVVGITSWGVG-CARAKRPGVYT 221
Cdd:cd21112  105 CKSgrtTGWTCGTVTAVNVTVNYPGGTVtgltrtNACaePGDSGGPVF------SGTQALGITSGGSGnCGSGGGTSYFQ 178

                 ....*...
gi 471012474 222 ATWDYLDW 229
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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