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Conserved domains on  [gi|1805139917|ref|WP_162025831|]
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MULTISPECIES: signal peptidase I [unclassified Lentimonas]

Protein Classification

S26 family signal peptidase( domain architecture ID 11493928)

S26 family signal peptidase is a membrane-bound serine protease which frees proteins tethered to inner or mitochondrial membranes by cleaving off signal peptides during polypeptide translocation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 258-401 7.09e-32

signal peptidase I, bacterial type; This model represents signal peptidase I from most bacteria. Eukaryotic sequences are likely organellar. Several bacteria have multiple paralogs, but these represent isozymes of signal peptidase I. Virtually all known bacteria may be presumed to A related model finds a simlar protein in many archaea and a few bacteria, as well as a microsomal (endoplasmic reticulum) protein in eukaryotes. [Protein fate, Protein and peptide secretion and trafficking]


:

Pssm-ID: 274044 [Multi-domain]  Cd Length: 142  Bit Score: 117.72  E-value: 7.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805139917 258 GDALFVDRISYHFKRPKAGDPFVFRTnaireelgrltGDYTDKYYIKRIGGVGGETLEIVDSTLLVDGQPRDEVEAFGRN 337
Cdd:TIGR02227  20 GDRILVNKFAYRTSDPKRGDIVVFKD-----------PDTNKNIYVKRIIGLPGDKVEFRDGKLYINGKKIDEPYLKPNG 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805139917 338 AAREGEYSGYinhtllaegrkLKIPDDKFVALGDNSANSLDSRYWGFVPEKSVIGKAIFIYYPF 401
Cdd:TIGR02227  89 YLDTSEFNTP-----------VKVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYPF 141
 
Name Accession Description Interval E-value
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 258-401 7.09e-32

signal peptidase I, bacterial type; This model represents signal peptidase I from most bacteria. Eukaryotic sequences are likely organellar. Several bacteria have multiple paralogs, but these represent isozymes of signal peptidase I. Virtually all known bacteria may be presumed to A related model finds a simlar protein in many archaea and a few bacteria, as well as a microsomal (endoplasmic reticulum) protein in eukaryotes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274044 [Multi-domain]  Cd Length: 142  Bit Score: 117.72  E-value: 7.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805139917 258 GDALFVDRISYHFKRPKAGDPFVFRTnaireelgrltGDYTDKYYIKRIGGVGGETLEIVDSTLLVDGQPRDEVEAFGRN 337
Cdd:TIGR02227  20 GDRILVNKFAYRTSDPKRGDIVVFKD-----------PDTNKNIYVKRIIGLPGDKVEFRDGKLYINGKKIDEPYLKPNG 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805139917 338 AAREGEYSGYinhtllaegrkLKIPDDKFVALGDNSANSLDSRYWGFVPEKSVIGKAIFIYYPF 401
Cdd:TIGR02227  89 YLDTSEFNTP-----------VKVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYPF 141
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 258-399 2.38e-31

Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases which function in the processing of newly-synthesized secreted proteins. Peptidase S26 removes the hydrophobic, N-terminal, signal peptides as proteins are translocated across membranes. The active site residues take the form of a catalytic dyad that is Ser, Lys in subfamily S26A; the Ser is the nucleophile in catalysis, and the Lys is the general base.


Pssm-ID: 431321 [Multi-domain]  Cd Length: 162  Bit Score: 117.31  E-value: 2.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805139917 258 GDALFVDRISYHFKRPKAGDPFVFRTNAIReelgrltgdytDKYYIKRIGGVGGETLEIVDSTLLVDGQPRDEveafgrn 337
Cdd:pfam10502  40 GDYLIVNKFSYGLGEPKRGDIVVFRPPEGP-----------GVPLIKRVIGLPGDRVEYKDDQLYINGKPVGE------- 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805139917 338 aAREGEYSGYINHTLLAEGRKLKIPDDKFVALGDNSANSLDSRYWGFVPEKSVIGKAIFIYY 399
Cdd:pfam10502 102 -PYLADRKGRPTFDLPPWQGCRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVGRAVFPVW 162
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 276-400 3.98e-26

Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, chaperones, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443985 [Multi-domain]  Cd Length: 114  Bit Score: 101.53  E-value: 3.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805139917 276 GDPFVFR-TNAIREELGRLtgdYTDKYYIKRIGGVGGETLEIVDSTLLVDGQPRDEVEAFGRNAAREGEYSGyinhtlla 354
Cdd:COG4959     2 GDLVAFRpPEPLAAERGYL---PRGVPLIKRVAALPGDTVCIKGGQVYINGKPVAEALERDRAGRPLPVWQG-------- 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1805139917 355 egrKLKIPDDKFVALGDNSANSLDSRYWGFVPEKSVIGKAIFIYYP 400
Cdd:COG4959    71 ---CGVVPEGEYFLLGDNRPNSFDSRYFGPVPRSQIIGRAVPLWTP 113
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 258-394 3.03e-13

The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4.21.89) family members are essential membrane-bound serine proteases that function to cleave the amino-terminal signal peptide extension from proteins that are translocated across biological membranes. The bacterial signal peptidase I, which is the most intensively studied, has two N-terminal transmembrane segments inserted in the plasma membrane and a hydrophilic, C-terminal catalytic region that is located in the periplasmic space. Although the bacterial signal peptidase I is monomeric, signal peptidases of eukaryotic cells commonly function as oligomeric complexes containing two divergent copies of the catalytic monomer. These are the IMP1 and IMP2 signal peptidases of the mitochondrial inner membrane that remove leader peptides from nuclear- and mitochondrial-encoded proteins. Also, two components of the endoplasmic reticulum signal peptidase in mammals (18-kDa and 21-kDa) belong to this family and they process many proteins that enter the ER for retention or for export to the Golgi apparatus, secretory vesicles, plasma membranes or vacuole. An atypical member of the S26 SPase type I family is the TraF peptidase which has the remarkable activity of producing a cyclic protein of the Pseudomonas pilin system. The type I signal peptidases are unique serine proteases that utilize a serine/lysine catalytic dyad mechanism in place of the classical serine/histidine/aspartic acid catalytic triad mechanism.


Pssm-ID: 119398 [Multi-domain]  Cd Length: 85  Bit Score: 64.91  E-value: 3.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805139917 258 GDALFVDRISYHFKRPKAGDPFVFRTNaireelgrltgDYTDKYYIKRIGGVggetleivdstllvdgqprdeveafgrn 337
Cdd:cd06530    17 GDLVLVNKLSYGFREPKRGDVVVFKSP-----------GDPGKPIIKRVIGY---------------------------- 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1805139917 338 aaregeysgyinhtllaegrklkipddkFVaLGDNSANSLDSRYWGFVPEKSVIGKA 394
Cdd:cd06530    58 ----------------------------FV-LGDNRNNSLDSRYWGPVPEDDIVGKV 85
PRK10861 PRK10861
signal peptidase I;
361-406 1.21e-10

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 62.38  E-value: 1.21e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1805139917 361 IPDDKFVALGDNSANSLDSRYWGFVPEKSVIGKAIFIYYPFTKRWG 406
Cdd:PRK10861  264 VPPGQYFMMGDNRDNSADSRYWGFVPEANLVGKATAIWMSFEKQEG 309
 
Name Accession Description Interval E-value
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 258-401 7.09e-32

signal peptidase I, bacterial type; This model represents signal peptidase I from most bacteria. Eukaryotic sequences are likely organellar. Several bacteria have multiple paralogs, but these represent isozymes of signal peptidase I. Virtually all known bacteria may be presumed to A related model finds a simlar protein in many archaea and a few bacteria, as well as a microsomal (endoplasmic reticulum) protein in eukaryotes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274044 [Multi-domain]  Cd Length: 142  Bit Score: 117.72  E-value: 7.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805139917 258 GDALFVDRISYHFKRPKAGDPFVFRTnaireelgrltGDYTDKYYIKRIGGVGGETLEIVDSTLLVDGQPRDEVEAFGRN 337
Cdd:TIGR02227  20 GDRILVNKFAYRTSDPKRGDIVVFKD-----------PDTNKNIYVKRIIGLPGDKVEFRDGKLYINGKKIDEPYLKPNG 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805139917 338 AAREGEYSGYinhtllaegrkLKIPDDKFVALGDNSANSLDSRYWGFVPEKSVIGKAIFIYYPF 401
Cdd:TIGR02227  89 YLDTSEFNTP-----------VKVPPGHYFVLGDNRDNSLDSRYFGFVPIDQIIGKVSFVFYPF 141
Peptidase_S26 pfam10502
Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases ...
 258-399 2.38e-31

Signal peptidase, peptidase S26; This is a family of membrane signal serine endopeptidases which function in the processing of newly-synthesized secreted proteins. Peptidase S26 removes the hydrophobic, N-terminal, signal peptides as proteins are translocated across membranes. The active site residues take the form of a catalytic dyad that is Ser, Lys in subfamily S26A; the Ser is the nucleophile in catalysis, and the Lys is the general base.


Pssm-ID: 431321 [Multi-domain]  Cd Length: 162  Bit Score: 117.31  E-value: 2.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805139917 258 GDALFVDRISYHFKRPKAGDPFVFRTNAIReelgrltgdytDKYYIKRIGGVGGETLEIVDSTLLVDGQPRDEveafgrn 337
Cdd:pfam10502  40 GDYLIVNKFSYGLGEPKRGDIVVFRPPEGP-----------GVPLIKRVIGLPGDRVEYKDDQLYINGKPVGE------- 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805139917 338 aAREGEYSGYINHTLLAEGRKLKIPDDKFVALGDNSANSLDSRYWGFVPEKSVIGKAIFIYY 399
Cdd:pfam10502 102 -PYLADRKGRPTFDLPPWQGCRVVPEGEYFVMGDNRDNSLDSRYFGFVPASNIVGRAVFPVW 162
TraF COG4959
Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, ...
 276-400 3.98e-26

Type IV secretory pathway, protease TraF [Posttranslational modification, protein turnover, chaperones, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443985 [Multi-domain]  Cd Length: 114  Bit Score: 101.53  E-value: 3.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805139917 276 GDPFVFR-TNAIREELGRLtgdYTDKYYIKRIGGVGGETLEIVDSTLLVDGQPRDEVEAFGRNAAREGEYSGyinhtlla 354
Cdd:COG4959     2 GDLVAFRpPEPLAAERGYL---PRGVPLIKRVAALPGDTVCIKGGQVYINGKPVAEALERDRAGRPLPVWQG-------- 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1805139917 355 egrKLKIPDDKFVALGDNSANSLDSRYWGFVPEKSVIGKAIFIYYP 400
Cdd:COG4959    71 ---CGVVPEGEYFLLGDNRPNSFDSRYFGPVPRSQIIGRAVPLWTP 113
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 258-394 3.03e-13

The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4.21.89) family members are essential membrane-bound serine proteases that function to cleave the amino-terminal signal peptide extension from proteins that are translocated across biological membranes. The bacterial signal peptidase I, which is the most intensively studied, has two N-terminal transmembrane segments inserted in the plasma membrane and a hydrophilic, C-terminal catalytic region that is located in the periplasmic space. Although the bacterial signal peptidase I is monomeric, signal peptidases of eukaryotic cells commonly function as oligomeric complexes containing two divergent copies of the catalytic monomer. These are the IMP1 and IMP2 signal peptidases of the mitochondrial inner membrane that remove leader peptides from nuclear- and mitochondrial-encoded proteins. Also, two components of the endoplasmic reticulum signal peptidase in mammals (18-kDa and 21-kDa) belong to this family and they process many proteins that enter the ER for retention or for export to the Golgi apparatus, secretory vesicles, plasma membranes or vacuole. An atypical member of the S26 SPase type I family is the TraF peptidase which has the remarkable activity of producing a cyclic protein of the Pseudomonas pilin system. The type I signal peptidases are unique serine proteases that utilize a serine/lysine catalytic dyad mechanism in place of the classical serine/histidine/aspartic acid catalytic triad mechanism.


Pssm-ID: 119398 [Multi-domain]  Cd Length: 85  Bit Score: 64.91  E-value: 3.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805139917 258 GDALFVDRISYHFKRPKAGDPFVFRTNaireelgrltgDYTDKYYIKRIGGVggetleivdstllvdgqprdeveafgrn 337
Cdd:cd06530    17 GDLVLVNKLSYGFREPKRGDVVVFKSP-----------GDPGKPIIKRVIGY---------------------------- 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1805139917 338 aaregeysgyinhtllaegrklkipddkFVaLGDNSANSLDSRYWGFVPEKSVIGKA 394
Cdd:cd06530    58 ----------------------------FV-LGDNRNNSLDSRYWGPVPEDDIVGKV 85
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
256-407 1.47e-11

Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 62.95  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805139917 256 TL--GDALFVDRISYHFKRPKAGDPFVFRTnaireelgrlTGDyTDKYYIKRIGGVGGETLEIVDSTLLVDGQPRDEvea 333
Cdd:COG0681    46 TLlvGDRLLVNKLSYGFGEPKRGDIVVFKY----------PED-PSKDYIKRVIGLPGDTVEIRDGQVYVNGKPLNE--- 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805139917 334 fgrNAAREGEYSGYINHTLLAEGRKLKIPDDKFVALGDNSANSLDSRYWGFVPEKSVIGKAIFIYYPFTKRWGV 407
Cdd:COG0681   112 ---PYLEEYYYPVSVDGDVEVPPGEEEVPGGGGDNSNDSRSGDPDDGGGGVGVDGVGVGGVVDVVVPDVDSRLV 182
PRK10861 PRK10861
signal peptidase I;
361-406 1.21e-10

signal peptidase I;


Pssm-ID: 182787 [Multi-domain]  Cd Length: 324  Bit Score: 62.38  E-value: 1.21e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1805139917 361 IPDDKFVALGDNSANSLDSRYWGFVPEKSVIGKAIFIYYPFTKRWG 406
Cdd:PRK10861  264 VPPGQYFMMGDNRDNSADSRYWGFVPEANLVGKATAIWMSFEKQEG 309
TraF_Ti TIGR02771
conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding ...
 301-394 1.28e-06

conjugative transfer signal peptidase TraF; This protein is found in apparent operons encoding elements of conjugative transfer systems. This family is homologous to a broader family of signal (leader) peptidases such as lepB. This family is present in both Ti-type and I-type conjugative systems.


Pssm-ID: 131818 [Multi-domain]  Cd Length: 171  Bit Score: 48.24  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805139917 301 YYIKRIGGVGGETLEIVDSTLLVDGQPRD-----EVEAFGRNAARegeysgyinhtlLAEGRklkIPDdKFVALGDNSAN 375
Cdd:TIGR02771  83 PLLKRVLGLPGDRVTVRADVVAINGQLLPyskplATDSSGRPLPP------------FPEGV---IPP-GFFVVHDTSPT 146

                          90
                  ....*....|....*....
gi 1805139917 376 SLDSRYWGFVPEKSVIGKA 394
Cdd:TIGR02771 147 SFDSRYFGPISREQVIGRV 165
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 258-394 5.84e-04

The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal peptidase families. The S24 LexA protein domains include: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The S26 type I signal peptidase (SPase) family also includes mitochondrial inner membrane protease (IMP)-like members. SPases are essential membrane-bound proteases which function to cleave away the amino-terminal signal peptide from the translocated pre-protein, thus playing a crucial role in the transport of proteins across membranes in all living organisms. All members in this superfamily are unique serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases.


Pssm-ID: 119396 [Multi-domain]  Cd Length: 84  Bit Score: 38.40  E-value: 5.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805139917 258 GDALFVDRISYHFKRpkaGDPFVFRTNaireelgrltgdyTDKYYIKRIGGVGGEtleivdstllvdgqprdeveafgrn 337
Cdd:cd06462    17 GDLVLVDKSSYEPKR---GDIVVFRLP-------------GGELTVKRVIGLPGE------------------------- 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1805139917 338 aaregeysgyinhtllaegrklkipdDKFVALGDNSaNSLDSRYWGFvPEKSVIGKA 394
Cdd:cd06462    56 --------------------------GHYFLLGDNP-NSPDSRIDGP-PELDIVGVV 84
sod_Ni_protease TIGR02754
nickel-type superoxide dismutase maturation protease; Members of this protein family are ...
 350-394 2.69e-03

nickel-type superoxide dismutase maturation protease; Members of this protein family are apparent proteases encoded adjacent to the genes for a nickel-type superoxide dismutase. This family belongs to the same larger family (see pfam00717) as signal peptidase I, an unusual serine protease suggested to have a Ser/Lys catalytic dyad. [Cellular processes, Detoxification, Protein fate, Protein modification and repair]


Pssm-ID: 274282 [Multi-domain]  Cd Length: 90  Bit Score: 36.66  E-value: 2.69e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1805139917 350 HTLLAEGRKLK----IPDDKFVALGDNSANSLDSRYWGFVPEKSVIGKA 394
Cdd:TIGR02754  40 HPLQPYGLIIKrlaaVDDNGLFLLGDNPKASTDSRQLGPVPRSLLLGKV 88
PRK13838 PRK13838
conjugal transfer pilin processing protease TraF; Provisional
 303-400 4.00e-03

conjugal transfer pilin processing protease TraF; Provisional


Pssm-ID: 172365 [Multi-domain]  Cd Length: 176  Bit Score: 38.05  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805139917 303 IKRIGGVGGETLEIVDStLLVDGQPRdeveAFGRNAAREGEysgyinhtllaeGRKLK------IPDDkFVALGDNSANS 376
Cdd:PRK13838   89 IKTVAALAGQRVEIGGS-VSIDGRPL----PSSSVRRRDGE------------GRPLTpfpggvVPPG-HLFLHSSFAGS 150

                          90       100
                  ....*....|....*....|....*.
gi 1805139917 377 LDSRYWGFVPEKSVIGKA--IFIYYP 400
Cdd:PRK13838  151 YDSRYFGPVPASGLLGLArpVLTFDP 176
 
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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