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Conserved domains on  [gi|459212753|ref|NP_001264010|]
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kallikrein-15 isoform 5 preproprotein [Homo sapiens]

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 ...
24-248 4.07e-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: 273.40  E-value: 4.07e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753    24 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNlRKRDGPEQLRTTSRVIPHPRYE 98
Cdd:smart00020   5 GSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHD-LSSGEEGQVIKVSKVIIHPNYN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753    99 ARSHRNDIMLLRLVQPARLNPQVRPAVLPTR--CPHPGEACVVSGWGLVSHNEPgtagsprsqvSLPDTLHCANISIISD 176
Cdd:smart00020  84 PSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAG----------SLPDTLQEVNVPIVSN 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 459212753   177 TSCDKSYPGR--LTNTMVCAGAEGRGAESCEGDSGGPLVCG---GILQGIVSWGdVPCDNTTKPGVYTKVCHYLEWI 248
Cdd:smart00020 154 ATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWG-SGCARPGKPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-248 4.07e-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: 273.40  E-value: 4.07e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753    24 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNlRKRDGPEQLRTTSRVIPHPRYE 98
Cdd:smart00020   5 GSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHD-LSSGEEGQVIKVSKVIIHPNYN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753    99 ARSHRNDIMLLRLVQPARLNPQVRPAVLPTR--CPHPGEACVVSGWGLVSHNEPgtagsprsqvSLPDTLHCANISIISD 176
Cdd:smart00020  84 PSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAG----------SLPDTLQEVNVPIVSN 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 459212753   177 TSCDKSYPGR--LTNTMVCAGAEGRGAESCEGDSGGPLVCG---GILQGIVSWGdVPCDNTTKPGVYTKVCHYLEWI 248
Cdd:smart00020 154 ATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWG-SGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
24-251 1.34e-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: 272.23  E-value: 1.34e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753  24 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYE 98
Cdd:cd00190    4 GSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753  99 ARSHRNDIMLLRLVQPARLNPQVRPAVLPT--RCPHPGEACVVSGWGLVShnepgtagsprSQVSLPDTLHCANISIISD 176
Cdd:cd00190   84 PSTYDNDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTS-----------EGGPLPDVLQEVNVPIVSN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753 177 TSCDKSY--PGRLTNTMVCAGAEGRGAESCEGDSGGPLVCG----GILQGIVSWGDVpCDNTTKPGVYTKVCHYLEWIRE 250
Cdd:cd00190  153 AECKRAYsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQK 231

                 .
gi 459212753 251 T 251
Cdd:cd00190  232 T 232
Trypsin pfam00089
Trypsin;
24-248 3.93e-82

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 245.43  E-value: 3.93e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753   24 GDECAPHSQPWQVALY-ERGRFNCGASLISPHWVLSAAHC--QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYEAR 100
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753  101 SHRNDIMLLRLVQPARLNPQVRPAVLPT--RCPHPGEACVVSGWGLVSHNEPgtagsprsqvslPDTLHCANISIISDTS 178
Cdd:pfam00089  84 TLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCTVSGWGNTKTLGP------------SDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 459212753  179 CDKSYPGRLTNTMVCAGAEGRGAesCEGDSGGPLVC-GGILQGIVSWGDvPCDNTTKPGVYTKVCHYLEWI 248
Cdd:pfam00089 152 CRSAYGGTVTDTMICAGAGGKDA--CQGDSGGPLVCsDGELIGIVSWGY-GCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
12-255 3.57e-60

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 190.63  E-value: 3.57e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753  12 ASTAQDGDKLLEGDECAPHSQPWQVALYERG---RFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGpeQ 84
Cdd:COG5640   22 APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSGG--T 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753  85 LRTTSRVIPHPRYEARSHRNDIMLLRLVQPArlnPQVRPAVLPTR--CPHPGEACVVSGWGLVSHNEPgtagsprsqvSL 162
Cdd:COG5640  100 VVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSadAAAPGTPATVAGWGRTSEGPG----------SQ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753 163 PDTLHCANISIISDTSCdKSYPGRLTNTMVCAGAEGRGAESCEGDSGGPLV----CGGILQGIVSWGDVPCDnTTKPGVY 238
Cdd:COG5640  167 SGTLRKADVPVVSDATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCA-AGYPGVY 244
                        250
                 ....*....|....*..
gi 459212753 239 TKVCHYLEWIRETMKRN 255
Cdd:COG5640  245 TRVSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-248 4.07e-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: 273.40  E-value: 4.07e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753    24 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNlRKRDGPEQLRTTSRVIPHPRYE 98
Cdd:smart00020   5 GSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHD-LSSGEEGQVIKVSKVIIHPNYN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753    99 ARSHRNDIMLLRLVQPARLNPQVRPAVLPTR--CPHPGEACVVSGWGLVSHNEPgtagsprsqvSLPDTLHCANISIISD 176
Cdd:smart00020  84 PSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAG----------SLPDTLQEVNVPIVSN 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 459212753   177 TSCDKSYPGR--LTNTMVCAGAEGRGAESCEGDSGGPLVCG---GILQGIVSWGdVPCDNTTKPGVYTKVCHYLEWI 248
Cdd:smart00020 154 ATCRRAYSGGgaITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWG-SGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
24-251 1.34e-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: 272.23  E-value: 1.34e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753  24 GDECAPHSQPWQVAL-YERGRFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYE 98
Cdd:cd00190    4 GSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753  99 ARSHRNDIMLLRLVQPARLNPQVRPAVLPT--RCPHPGEACVVSGWGLVShnepgtagsprSQVSLPDTLHCANISIISD 176
Cdd:cd00190   84 PSTYDNDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTS-----------EGGPLPDVLQEVNVPIVSN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753 177 TSCDKSY--PGRLTNTMVCAGAEGRGAESCEGDSGGPLVCG----GILQGIVSWGDVpCDNTTKPGVYTKVCHYLEWIRE 250
Cdd:cd00190  153 AECKRAYsyGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQK 231

                 .
gi 459212753 251 T 251
Cdd:cd00190  232 T 232
Trypsin pfam00089
Trypsin;
24-248 3.93e-82

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 245.43  E-value: 3.93e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753   24 GDECAPHSQPWQVALY-ERGRFNCGASLISPHWVLSAAHC--QSRFMRVRLGEHNLRKRDGPEQLRTTSRVIPHPRYEAR 100
Cdd:pfam00089   4 GDEAQPGSFPWQVSLQlSSGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753  101 SHRNDIMLLRLVQPARLNPQVRPAVLPT--RCPHPGEACVVSGWGLVSHNEPgtagsprsqvslPDTLHCANISIISDTS 178
Cdd:pfam00089  84 TLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCTVSGWGNTKTLGP------------SDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 459212753  179 CDKSYPGRLTNTMVCAGAEGRGAesCEGDSGGPLVC-GGILQGIVSWGDvPCDNTTKPGVYTKVCHYLEWI 248
Cdd:pfam00089 152 CRSAYGGTVTDTMICAGAGGKDA--CQGDSGGPLVCsDGELIGIVSWGY-GCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
12-255 3.57e-60

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 190.63  E-value: 3.57e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753  12 ASTAQDGDKLLEGDECAPHSQPWQVALYERG---RFNCGASLISPHWVLSAAHC----QSRFMRVRLGEHNLRKRDGpeQ 84
Cdd:COG5640   22 APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSGG--T 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753  85 LRTTSRVIPHPRYEARSHRNDIMLLRLVQPArlnPQVRPAVLPTR--CPHPGEACVVSGWGLVSHNEPgtagsprsqvSL 162
Cdd:COG5640  100 VVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSadAAAPGTPATVAGWGRTSEGPG----------SQ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753 163 PDTLHCANISIISDTSCdKSYPGRLTNTMVCAGAEGRGAESCEGDSGGPLV----CGGILQGIVSWGDVPCDnTTKPGVY 238
Cdd:COG5640  167 SGTLRKADVPVVSDATC-AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCA-AGYPGVY 244
                        250
                 ....*....|....*..
gi 459212753 239 TKVCHYLEWIRETMKRN 255
Cdd:COG5640  245 TRVSAYRDWIKSTAGGL 261
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
182-241 4.63e-05

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: 43.06  E-value: 4.63e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753 182 SYPGRLTNTMVCAGAEGRGaesceGDSGGPLVCGGILQGIVSWGDVPCDNTTKPGVYTKV 241
Cdd:cd21112  126 NYPGGTVTGLTRTNACAEP-----GDSGGPVFSGTQALGITSGGSGNCGSGGGTSYFQPV 180
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
41-232 2.40e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 40.82  E-value: 2.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753  41 RGRFNCGASLISPHWVLSAAHC--------QSRFMRVRLGEHNlrkrdGPEQLRTTSRVIPHPRYEARSH-RNDIMLLRL 111
Cdd:COG3591    9 GGGGVCTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGDaGYDYALLRL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753 112 vqPARLNPQVRP-AVLPTRCPHPGEACVVSGWGlvshnepgtAGSPRSQvslpdTLHCA-NISIISDT----SCDksypg 185
Cdd:COG3591   84 --DEPLGDTTGWlGLAFNDAPLAGEPVTIIGYP---------GDRPKDL-----SLDCSgRVTGVQGNrlsyDCD----- 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 459212753 186 rltntmvcagaegrgaeSCEGDSGGPLV----CGGILQGIVSWGDVPCDNT 232
Cdd:COG3591  143 -----------------TTGGSSGSPVLddsdGGGRVVGVHSAGGADRANT 176
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
33-132 1.13e-03

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 37.91  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459212753   33 PWQVALYERGRFNCGASLISPHWVLSAAHC------QSRFMRVRLGEH-NLRKRDGP-EQLRttsrviphpRYEARSH-- 102
Cdd:pfam09342   2 PWIAKVYLDGNMICSGVLIDASWVIVSGSClrdtnlRHQYISVVLGGAkTLKSIEGPyEQIV---------RVDCRHDip 72
                          90       100       110
                  ....*....|....*....|....*....|
gi 459212753  103 RNDIMLLRLVQPARLNPQVRPAVLPTRCPH 132
Cdd:pfam09342  73 ESEISLLHLASPASFSNHVLPTFVPETRNE 102
 
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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