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Conserved domains on  [gi|41281782|ref|NP_694533|]
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signal peptide peptidase-like 2B isoform 2 precursor [Homo sapiens]

Protein Classification

PA_hSPPL_like and Peptidase_A22B domain-containing protein( domain architecture ID 10114778)

PA_hSPPL_like and Peptidase_A22B domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_A22B pfam04258
Signal peptide peptidase; The members of this family are membrane proteins. In some proteins ...
 213-505 2.69e-124

Signal peptide peptidase; The members of this family are membrane proteins. In some proteins this region is found associated with pfam02225. This family corresponds with Merops subfamily A22B, the type example of which is signal peptide peptidase. There is a sequence-similarity relationship with pfam01080.


:

Pssm-ID: 282158  Cd Length: 286  Bit Score: 367.78  E-value: 2.69e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782   213 KQEDEAVDVTPVMTCVFVVMCCSMLVLLYYFYD-LLVYVVIGIFCLASATGLYSCLAPCVRRLPFGKCRIPNNSLPYFHK 291
Cdd:pfam04258   1 KSSDDFETITKIHAICFPITASCTLLLLYFFFKsLLVYVLTIYFCILGIIALAFCLSPFLTRLFFNKCPLKNIKLPFLPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782   292 RPQARMLLLALFCVAVSVVWGVFRNEdqwaWVLQDALGIAFCLYMLKTIRLPTFKACTLLLLVLFLYDIFFVFITPFltK 371
Cdd:pfam04258  81 RFSYSELVALLLCIVFAVWWALKRHE----WILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPY--I 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782   372 SGSSIMVEVATGPSDsaTREKLPMVLKVPRLnsSPLALCDRPFSLLGFGDILVPGLLVAYCHRFDIQVQSSR--VYFVAC 449
Cdd:pfam04258 155 FGTSVMVTVATGPSS--TGEDIPMKLVFPRL--SNMFDNWGPFSMLGLGDIVMPGLLIALCLRFDISKKKSThdIYFIST 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 41281782   450 TIAYGVGLLVTFVALALMQRGQPALLYLVPCTLVTSCAVALWRRELGVFWTGSGFA 505
Cdd:pfam04258 231 MIAYGLGLLITFVALNLFKAAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
 44-163 8.28e-68

PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like (hSPPL)-like. This group contains various PA domain-containing proteins similar to hSPPL2a and 2b. These SPPLs are GxGD aspartic proteases. SPPL2a is sorted to the late endosomes, SPPL2b to the plasma membrane. In activated dendritic cells, hSPPL2a and 2b catalyze the intramembrane proteolysis of tumor necrosis factor alpha triggering IL-12 production. hSPPL2a and 2b may have a broad substrate spectrum. The significance of the PA domain to these SPPLs has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


:

Pssm-ID: 239044 [Multi-domain]  Cd Length: 120  Bit Score: 215.72  E-value: 8.28e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782  44 YCILYNPQWAHLPHDLSKASFLQLRNWTASLLCSAADLPARGFSNQIPLVARGNCTFYEKVRLAQGSGARGLLIVSRERL 123
Cdd:cd02129   1 YCILYNSQWASLPSDLDKATLLPLRNLTSSVLCSASDVPPGGLKGKAVVVMRGNCTFYEKARLAQSLGAEGLLIVSRERL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 41281782 124 VPPGGNKTQYDEIGIPVALLSYKDMLDIFTRFGRTVRAAL 163
Cdd:cd02129  81 VPPSGNRSEYEKIDIPVALLSYKDMLDIQQTFGDSVKVAM 120
PHA03378 super family cl33729
EBNA-3B; Provisional
 520-590 1.49e-03

EBNA-3B; Provisional


The actual alignment was detected with superfamily member PHA03378:

Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.59  E-value: 1.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41281782  520 GPQPPKdSATPLSPQPPSEEPATSPWPAEQSpksrtseemGAGAPMREPGSPAESEGRDQAQPSPVTQPGA 590
Cdd:PHA03378 742 GRARPP-AAAPGRARPPAAAPGRARPPAAAP---------GAPTPQPPPQAPPAPQQRPRGAPTPQPPPQA 802
 
Name Accession Description Interval E-value
Peptidase_A22B pfam04258
Signal peptide peptidase; The members of this family are membrane proteins. In some proteins ...
 213-505 2.69e-124

Signal peptide peptidase; The members of this family are membrane proteins. In some proteins this region is found associated with pfam02225. This family corresponds with Merops subfamily A22B, the type example of which is signal peptide peptidase. There is a sequence-similarity relationship with pfam01080.


Pssm-ID: 282158  Cd Length: 286  Bit Score: 367.78  E-value: 2.69e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782   213 KQEDEAVDVTPVMTCVFVVMCCSMLVLLYYFYD-LLVYVVIGIFCLASATGLYSCLAPCVRRLPFGKCRIPNNSLPYFHK 291
Cdd:pfam04258   1 KSSDDFETITKIHAICFPITASCTLLLLYFFFKsLLVYVLTIYFCILGIIALAFCLSPFLTRLFFNKCPLKNIKLPFLPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782   292 RPQARMLLLALFCVAVSVVWGVFRNEdqwaWVLQDALGIAFCLYMLKTIRLPTFKACTLLLLVLFLYDIFFVFITPFltK 371
Cdd:pfam04258  81 RFSYSELVALLLCIVFAVWWALKRHE----WILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPY--I 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782   372 SGSSIMVEVATGPSDsaTREKLPMVLKVPRLnsSPLALCDRPFSLLGFGDILVPGLLVAYCHRFDIQVQSSR--VYFVAC 449
Cdd:pfam04258 155 FGTSVMVTVATGPSS--TGEDIPMKLVFPRL--SNMFDNWGPFSMLGLGDIVMPGLLIALCLRFDISKKKSThdIYFIST 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 41281782   450 TIAYGVGLLVTFVALALMQRGQPALLYLVPCTLVTSCAVALWRRELGVFWTGSGFA 505
Cdd:pfam04258 231 MIAYGLGLLITFVALNLFKAAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PSN smart00730
Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic ...
 217-492 7.50e-86

Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic membrane proteins, whose genes are mutated in some individuals with Alzheimer's disease. Distant homologues, present in eukaryotes and archaea, also contain conserved aspartic acid residues which are predicted to contribute to catalysis. At least one member of this family has been shown to possess signal peptide peptidase activity.


Pssm-ID: 214793  Cd Length: 249  Bit Score: 267.19  E-value: 7.50e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782    217 EAVDVTPVMTCVFVVMCCSMLVLLYYFYDLLVYVVIGIFCLASATGLYSCLAPCVRRLPFgkcripnnslpyfhkrpqAR 296
Cdd:smart00730   1 EYSLLNSLVAIVFPIVATFVLVLLYKFFKYLVIVLVIYFSSLGVLFLYSLLYPLEVFRVD------------------YP 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782    297 MLLLALFCVAVSVVWGVFRNedqWAWVLQDALGIAFCLYMLKTIRLPTFKACTLLLLVLFLYDIFFVFITPFltksGSSI 376
Cdd:smart00730  63 TLLILLLNFAVVGFWCIHRK---GAWIQQDLIGISLCMAILFILRLPSEWTAWILLGALFIYDIFAVFGTPG----PLRV 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782    377 MVEVATGPSDSAtrEKLPMVLKVPRLNSSPLALCDRPFSLLGFGDILVPGLLVAYCHRFDIQVQSSRVYFVACTIAYGVG 456
Cdd:smart00730 136 MVEVATGRDEPI--KVFPALLYVPRLVVSFEDDEEERFSMLGLGDIVFPGILVASAARFDVSVRSDSNYFLACFVAYGIG 213

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 41281782    457 LLVTFVALALMQRGQPALLYLVPCTLVTSCAVALWR 492
Cdd:smart00730 214 LILTLVLLALFKKAQPALPYLVPFTLVFYLLTALLR 249
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
 44-163 8.28e-68

PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like (hSPPL)-like. This group contains various PA domain-containing proteins similar to hSPPL2a and 2b. These SPPLs are GxGD aspartic proteases. SPPL2a is sorted to the late endosomes, SPPL2b to the plasma membrane. In activated dendritic cells, hSPPL2a and 2b catalyze the intramembrane proteolysis of tumor necrosis factor alpha triggering IL-12 production. hSPPL2a and 2b may have a broad substrate spectrum. The significance of the PA domain to these SPPLs has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239044 [Multi-domain]  Cd Length: 120  Bit Score: 215.72  E-value: 8.28e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782  44 YCILYNPQWAHLPHDLSKASFLQLRNWTASLLCSAADLPARGFSNQIPLVARGNCTFYEKVRLAQGSGARGLLIVSRERL 123
Cdd:cd02129   1 YCILYNSQWASLPSDLDKATLLPLRNLTSSVLCSASDVPPGGLKGKAVVVMRGNCTFYEKARLAQSLGAEGLLIVSRERL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 41281782 124 VPPGGNKTQYDEIGIPVALLSYKDMLDIFTRFGRTVRAAL 163
Cdd:cd02129  81 VPPSGNRSEYEKIDIPVALLSYKDMLDIQQTFGDSVKVAM 120
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
 76-151 4.84e-07

PA domain; The PA (Protease associated) domain is found as an insert domain in diverse proteases. The PA domain is also found in a plant vacuolar sorting receptor Swiss:O22925 and members of the RZF family Swiss:O43567. It has been suggested that this domain forms a lid-like structure that covers the active site in active proteases, and is involved in protein recognition in vacuolar sorting receptors.


Pssm-ID: 460499 [Multi-domain]  Cd Length: 91  Bit Score: 47.89  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782    76 CSAADLPARGFSNQIPLVARGNCTFYEKVRLAQGSGARGLLIVSRERLVPP----GGNKTQYDEIGIPVALLSYKDMLDI 151
Cdd:pfam02225  12 AGDGIPADFDVKGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNVEGLGGppgaGGNELYPDGIYIPAVGVSRADGEAL 91
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
 82-170 4.52e-04

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 43.49  E-value: 4.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782    82 PARGFSNQIPLVARGNCTFYEKVRLAQGSGARGLLIVSRERLVPP--GGNKTqydEIGIPVALLSYKDmldiftrfGRTV 159
Cdd:NF038112  540 NAAEVAGKIALIDRGTCDFTVKALNAQNAGAIGVIIANNAAGAAPglGGTDP---AVTIPALSITQAD--------GNAW 608

                          90
                  ....*....|.
gi 41281782   160 RAALyaPKEPV 170
Cdd:NF038112  609 KAAL--ANGPV 617
PHA03378 PHA03378
EBNA-3B; Provisional
 520-590 1.49e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.59  E-value: 1.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41281782  520 GPQPPKdSATPLSPQPPSEEPATSPWPAEQSpksrtseemGAGAPMREPGSPAESEGRDQAQPSPVTQPGA 590
Cdd:PHA03378 742 GRARPP-AAAPGRARPPAAAPGRARPPAAAP---------GAPTPQPPPQAPPAPQQRPRGAPTPQPPPQA 802
 
Name Accession Description Interval E-value
Peptidase_A22B pfam04258
Signal peptide peptidase; The members of this family are membrane proteins. In some proteins ...
 213-505 2.69e-124

Signal peptide peptidase; The members of this family are membrane proteins. In some proteins this region is found associated with pfam02225. This family corresponds with Merops subfamily A22B, the type example of which is signal peptide peptidase. There is a sequence-similarity relationship with pfam01080.


Pssm-ID: 282158  Cd Length: 286  Bit Score: 367.78  E-value: 2.69e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782   213 KQEDEAVDVTPVMTCVFVVMCCSMLVLLYYFYD-LLVYVVIGIFCLASATGLYSCLAPCVRRLPFGKCRIPNNSLPYFHK 291
Cdd:pfam04258   1 KSSDDFETITKIHAICFPITASCTLLLLYFFFKsLLVYVLTIYFCILGIIALAFCLSPFLTRLFFNKCPLKNIKLPFLPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782   292 RPQARMLLLALFCVAVSVVWGVFRNEdqwaWVLQDALGIAFCLYMLKTIRLPTFKACTLLLLVLFLYDIFFVFITPFltK 371
Cdd:pfam04258  81 RFSYSELVALLLCIVFAVWWALKRHE----WILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPY--I 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782   372 SGSSIMVEVATGPSDsaTREKLPMVLKVPRLnsSPLALCDRPFSLLGFGDILVPGLLVAYCHRFDIQVQSSR--VYFVAC 449
Cdd:pfam04258 155 FGTSVMVTVATGPSS--TGEDIPMKLVFPRL--SNMFDNWGPFSMLGLGDIVMPGLLIALCLRFDISKKKSThdIYFIST 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 41281782   450 TIAYGVGLLVTFVALALMQRGQPALLYLVPCTLVTSCAVALWRRELGVFWTGSGFA 505
Cdd:pfam04258 231 MIAYGLGLLITFVALNLFKAAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PSN smart00730
Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic ...
 217-492 7.50e-86

Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic membrane proteins, whose genes are mutated in some individuals with Alzheimer's disease. Distant homologues, present in eukaryotes and archaea, also contain conserved aspartic acid residues which are predicted to contribute to catalysis. At least one member of this family has been shown to possess signal peptide peptidase activity.


Pssm-ID: 214793  Cd Length: 249  Bit Score: 267.19  E-value: 7.50e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782    217 EAVDVTPVMTCVFVVMCCSMLVLLYYFYDLLVYVVIGIFCLASATGLYSCLAPCVRRLPFgkcripnnslpyfhkrpqAR 296
Cdd:smart00730   1 EYSLLNSLVAIVFPIVATFVLVLLYKFFKYLVIVLVIYFSSLGVLFLYSLLYPLEVFRVD------------------YP 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782    297 MLLLALFCVAVSVVWGVFRNedqWAWVLQDALGIAFCLYMLKTIRLPTFKACTLLLLVLFLYDIFFVFITPFltksGSSI 376
Cdd:smart00730  63 TLLILLLNFAVVGFWCIHRK---GAWIQQDLIGISLCMAILFILRLPSEWTAWILLGALFIYDIFAVFGTPG----PLRV 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782    377 MVEVATGPSDSAtrEKLPMVLKVPRLNSSPLALCDRPFSLLGFGDILVPGLLVAYCHRFDIQVQSSRVYFVACTIAYGVG 456
Cdd:smart00730 136 MVEVATGRDEPI--KVFPALLYVPRLVVSFEDDEEERFSMLGLGDIVFPGILVASAARFDVSVRSDSNYFLACFVAYGIG 213

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 41281782    457 LLVTFVALALMQRGQPALLYLVPCTLVTSCAVALWR 492
Cdd:smart00730 214 LILTLVLLALFKKAQPALPYLVPFTLVFYLLTALLR 249
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
 44-163 8.28e-68

PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like (hSPPL)-like. This group contains various PA domain-containing proteins similar to hSPPL2a and 2b. These SPPLs are GxGD aspartic proteases. SPPL2a is sorted to the late endosomes, SPPL2b to the plasma membrane. In activated dendritic cells, hSPPL2a and 2b catalyze the intramembrane proteolysis of tumor necrosis factor alpha triggering IL-12 production. hSPPL2a and 2b may have a broad substrate spectrum. The significance of the PA domain to these SPPLs has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239044 [Multi-domain]  Cd Length: 120  Bit Score: 215.72  E-value: 8.28e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782  44 YCILYNPQWAHLPHDLSKASFLQLRNWTASLLCSAADLPARGFSNQIPLVARGNCTFYEKVRLAQGSGARGLLIVSRERL 123
Cdd:cd02129   1 YCILYNSQWASLPSDLDKATLLPLRNLTSSVLCSASDVPPGGLKGKAVVVMRGNCTFYEKARLAQSLGAEGLLIVSRERL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 41281782 124 VPPGGNKTQYDEIGIPVALLSYKDMLDIFTRFGRTVRAAL 163
Cdd:cd02129  81 VPPSGNRSEYEKIDIPVALLSYKDMLDIQQTFGDSVKVAM 120
PA cd00538
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
 59-163 5.58e-16

PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases including, hSPPL2a and 2b which catalyze the intramembrane proteolysis of tumor necrosis factor alpha, ii) various proteins containing a C3H2C3 RING finger including, Arabidopsis ReMembR-H2 protein and various E3 ubiquitin ligases such as human GRAIL (gene related to anergy in lymphocytes), iii) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), iv) various plant vacuolar sorting receptors such as Pisum sativum BP-80, v) glutamate carboxypeptidase II (GCPII), vi) yeast aminopeptidase Y, vii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, viii) lactocepin (a cell envelope-associated protease from Lactobacillus paracasei subsp. paracasei NCDO 151), ix) various subtilisin-like proteases such as melon Cucumisin, and x) human TfR (transferrin receptor) 1 and 2.


Pssm-ID: 238300 [Multi-domain]  Cd Length: 126  Bit Score: 74.47  E-value: 5.58e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782  59 LSKASFLQLRNWTASLLCSAADL--PARGFSNQIPLVARGNCTFYEKVRLAQGSGARGLLIVSRE--RLVPPGGNKTQYD 134
Cdd:cd00538  16 FNPPSSPVGVVAGPLVGCGYGTTddSGADVKGKIVLVRRGGCSFSEKVKNAQKAGAKAVIIYNNGddPGPQMGSVGLEST 95

                        90       100       110
                ....*....|....*....|....*....|.
gi 41281782 135 EIGIPVALLSYKDMLDIFTRF--GRTVRAAL 163
Cdd:cd00538  96 DPSIPTVGISYADGEALLSLLeaGKTVTVDL 126
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
 76-151 4.84e-07

PA domain; The PA (Protease associated) domain is found as an insert domain in diverse proteases. The PA domain is also found in a plant vacuolar sorting receptor Swiss:O22925 and members of the RZF family Swiss:O43567. It has been suggested that this domain forms a lid-like structure that covers the active site in active proteases, and is involved in protein recognition in vacuolar sorting receptors.


Pssm-ID: 460499 [Multi-domain]  Cd Length: 91  Bit Score: 47.89  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782    76 CSAADLPARGFSNQIPLVARGNCTFYEKVRLAQGSGARGLLIVSRERLVPP----GGNKTQYDEIGIPVALLSYKDMLDI 151
Cdd:pfam02225  12 AGDGIPADFDVKGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNVEGLGGppgaGGNELYPDGIYIPAVGVSRADGEAL 91
PA_ScAPY_like cd02130
PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae ...
 72-147 5.81e-07

PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae aminopeptidase Y (ScAPY). This group contains various PA domain-containing proteins similar to the S. cerevisiae APY, including Trichophyton rubrum leucine aminopeptidase 1(LAP1). Proteins in this group belong to the peptidase M28 family. ScAPY hydrolyzes amino acid-4-methylcoumaryl-7-amides (MCAs). ScAPY more rapidly hydrolyzes dipeptidyl-MCAs. Hydrolysis of amino acid-MCAs or dipeptides is stimulated by Co2+ while the hydrolysis of dipeptidyl-MCAs, tripeptides, and longer peptides is inhibited by Co2+. ScAPY is vacuolar and is activated by proteolytic processing. LAP1 is a secreted leucine aminopeptidase. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239045 [Multi-domain]  Cd Length: 122  Bit Score: 48.41  E-value: 5.81e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41281782  72 ASLLCSAADLPARGfSNQIPLVARGNCTFYEKVRLAQGSGARGLLIVSRERLVPPGGNKTQYDEIGIPVALLSYKD 147
Cdd:cd02130  30 PNLGCDAADYPASV-AGNIALIERGECPFGDKSALAGAAGAAAAIIYNNVPAGGLSGTLGEPSGPYVPTVGISQED 104
PA_GO-like cd02132
PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on ...
 26-144 1.14e-06

PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on protein GRO10. This group contains various PA domain-containing proteins similar to the functionally uncharacterized Arabidopsis GRO10. The PA domain may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239047 [Multi-domain]  Cd Length: 139  Bit Score: 48.19  E-value: 1.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782  26 EYGMVHVVSQAGGPEGKDYCILYNPQWAHLPHDLSKAsfLQLRNWTASLLCSAADLPARgFSNQIPLVARGNCTFYEKVR 105
Cdd:cd02132   1 PFQLVKVQNWVDGDEGDELVGVTARFGASLPSKEDNA--NKTRAVLANPLDCCSPSTSK-LSGSIALVERGECAFTEKAK 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 41281782 106 LAQGSGARGLLIVS-RERLVPPGGNKTQYD-EIGIPVALLS 144
Cdd:cd02132  78 IAEAGGASALLIINdQEELYKMVCEDNDTSlNISIPVVMIP 118
PA_GRAIL_like cd02122
PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain ...
 90-131 2.03e-06

PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain containing E3 (ubiquitin ligases) similar to human GRAIL (gene related to anergy in lymphocytes) protein. Proteins in this group contain a C3H2C3 RING finger. E3 ubiquitin ligase is part of an enzymic cascade, the end result of which is the ubiquitination of proteins. In this cascade, E1 activates the ubiquitin, the activated ubiquitin is carried by E2, and E3 recognizes the acceptor protein as well as catalyzes the transfer of the activated ubiquitin from E2 to this acceptor. GRAIL, a transmembrane protein localized in the endosomes, controls the development of T cell clonal anergy, and may ubiquitinate membrane-associated targets for T cell activation. GRAIL1 is associated with, and regulated by, two isoforms of otubain 1 (the ubiquitin-specific protease). Additional E3s belonging to this group include human (h)Goliath and Xenopus GREUL1 (Goliath Related E3 Ubiquitin Ligase 1). hGoliath and GRAIL both have the property of self-ubiquitination. hGoliath is expressed in leukocytes; its expression and localization is not modified in leukemia. GREUL1 may play a role in the generation of anterior ectoderm. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239037 [Multi-domain]  Cd Length: 138  Bit Score: 47.29  E-value: 2.03e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 41281782  90 IPLVARGNCTFYEKVRLAQGSGARGLLIVSrerlVPPGGNKT 131
Cdd:cd02122  63 IALIQRGNCTFEEKIKLAAERNASAVVIYN----NPGTGNET 100
PA_C_RZF_like cd02123
PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA ...
 86-140 2.19e-05

PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA domain-containing proteins similar to C-RZF (chicken embryo RING zinc finger) protein. These proteins contain a C3H2C3 RING finger. C-RZF is expressed in embryo cells and is restricted mainly to brain and heart, it is localized to both the nucleus and endosomes. Additional C3H2C3 RING finger proteins belonging to this group, include Arabidopsis ReMembR-H2 protein and mouse sperizin. ReMembR-H2 is likely to be an integral membrane protein, and to traffic through the endosomal pathway. Sperizin is expressed in haploid germ cells and localized in the cytoplasm, it may participate in spermatogenesis. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239038 [Multi-domain]  Cd Length: 153  Bit Score: 44.64  E-value: 2.19e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41281782  86 FSNQIPLVARGNCTFYEKVRLAQGSGARGLLI--VSRERLVPPGGNKTQYDEIGIPV 140
Cdd:cd02123  66 SGSFIVLIRRGNCSFETKVRNAQRAGYKAAIVynDESNDLISMSGNDQEIKGIDIPS 122
PA_SaNapH_like cd04816
PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ...
 76-172 2.53e-05

PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus N-acetylpuromycin N-acetylhydrolase (SaNapH).This group contains various PA domain-containing proteins similar SaNapH. Proteins in this group belong to the peptidase M28 family. NapH is a terminal enzyme in the puromycin biosynthetic pathway; NapH hydrolyzes N-acetylpuromycin to the active antibiotic. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 240120 [Multi-domain]  Cd Length: 122  Bit Score: 43.85  E-value: 2.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782  76 CSAAD---LPARGfsnQIPLVARGNCTFYEKVRLAQGSGARGLLIVSRE-RLVPPGGNKTQYDEIGIPVALLSYKDmldi 151
Cdd:cd04816  32 CDASDydgLDVKG---AIVLVDRGGCPFADKQKVAAARGAVAVIVVNNSdGGGTAGTLGAPNIDLKVPVGVITKAA---- 104

                        90       100
                ....*....|....*....|.
gi 41281782 152 ftrfGRTVRAALYAPKEPVLD 172
Cdd:cd04816 105 ----GAALRRRLGAGETLELD 121
PA_subtilisin_1 cd04818
PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. ...
 76-153 2.90e-05

PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. A subgroup of PA domain-containing subtilisin-like proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following subtilisin-like proteases: i) melon cucumisin, ii) Arabidopsis thaliana Ara12, iii) Alnus glutinosa ag12, iv) members of the tomato P69 family, and v) tomato LeSBT2. However, these proteins belong to other subtilisin-like subgroups. Relatively little is known about proteins in this subgroup.


Pssm-ID: 240122 [Multi-domain]  Cd Length: 118  Bit Score: 43.47  E-value: 2.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782  76 CSAADLPARgFSNQIPLVARGNCTFYEKVRLAQGSGARGLLI---VSRERLVPPGGNKTQydeIGIPVALLSYKDMLDIF 152
Cdd:cd04818  30 CTAFTNAAA-FAGKIALIDRGTCNFTVKVLNAQNAGAIAVIVannVAGGAPITMGGDDPD---ITIPAVMISQADGDALK 105


                .
gi 41281782 153 T 153
Cdd:cd04818 106 A 106
PA_1 cd04813
PA_1: Protease-associated (PA) domain subgroup 1. A subgroup of PA-domain containing proteins. ...
 88-147 6.84e-05

PA_1: Protease-associated (PA) domain subgroup 1. A subgroup of PA-domain containing proteins. Proteins in this subgroup contain a RING-finger (Really Interesting New Gene) domain C-terminal to this PA domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins in this group contain a C-terminal RING-finger domain. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases: such as hSPPL2a and 2b, ii) various E3 ubiquitin ligases similar to human GRAIL (gene related to anergy in lymphocytes) protein, iii) various proteins containing a RING finger motif such as Arabidopsis ReMembR-H2 protein, iv) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), v) various plant vacuolar sorting receptors such as Pisum sativum BP-80, vi) prostate-specific membrane antigen (PSMA), vii) yeast aminopeptidase Y viii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, ix) various subtilisin-like proteases such as Cucumisin from the juice of melon fruits, and x) human TfR (transferrin receptor) 1 and human TfR2. The proteins listed above belong to other subgroups; relatively little is known about proteins in this subgroup.


Pssm-ID: 240117 [Multi-domain]  Cd Length: 117  Bit Score: 42.37  E-value: 6.84e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41281782  88 NQIPLVARGNCTFYEKVRLAQGSGARGLLIVSRErlvPPGGNKTQY-----DEIGIPVALLSYKD 147
Cdd:cd04813  40 GKVALVLRGGCGFLDKVMWAQRRGAKAVIVGDDE---PGRGLITMFsngdtDNVTIPAMFTSRTS 101
PA_EDEM3_like cd02126
PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This ...
 89-143 2.07e-04

PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This group contains various PA domain-containing proteins similar to mouse EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein). EDEM3 contains a region, similar to Class I alpha-mannosidases (gylcosyl hydrolase family 47), N-terminal to the PA domain. EDEM3 accelerates glycoprotein ERAD (ER-associated degradation). In transfected mammalian cells, overexpression of EDEM3 enhances the mannose trimming from the N-glycans, of a model misfolded protein [alpha1-antitrypsin null (Hong Kong)] as well as, from total glycoproteins. Mannose trimming appears to be involved in the selection of ERAD substrates. EDEM3 has a different specificity of trimming than ER alpha-mannosidase 1. The significance of the PA domain to EDEM3 has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239041 [Multi-domain]  Cd Length: 126  Bit Score: 41.58  E-value: 2.07e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41281782  89 QIPLVARGNCTFYEKVRLAQGSGARGLLIVSRErlvpPG------------GNKTQYDEIGIPVALL 143
Cdd:cd02126  42 KIAIMERGDCMFVEKARRVQKAGAIGGIVIDNN----EGsssdtapmfamsGDGDSTDDVTIPVVFL 104
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
 82-170 4.52e-04

myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes.


Pssm-ID: 468355 [Multi-domain]  Cd Length: 1597  Bit Score: 43.49  E-value: 4.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782    82 PARGFSNQIPLVARGNCTFYEKVRLAQGSGARGLLIVSRERLVPP--GGNKTqydEIGIPVALLSYKDmldiftrfGRTV 159
Cdd:NF038112  540 NAAEVAGKIALIDRGTCDFTVKALNAQNAGAIGVIIANNAAGAAPglGGTDP---AVTIPALSITQAD--------GNAW 608

                          90
                  ....*....|.
gi 41281782   160 RAALyaPKEPV 170
Cdd:NF038112  609 KAAL--ANGPV 617
PA_C5a_like cd02133
PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a ...
 90-147 6.25e-04

PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a peptidase. This group contains various PA domain-containing proteins similar to S. pyogenes C5a, including, i) Vpr, a minor extracellular serine protease from Bacillus subtilis, ii) a large molecular mass collagenolytic protease from Geobacillus collagenovorans MO-1, and iii) PrtS, a cell envelope protease from Streptococcus thermophilus CNRZ 385. Proteins in this group belong to the peptidase S8 family. C5a peptidase is a cell surface serine protease which specifically inactivates C5a [a chemotactic peptide, which attracts polymorphonuclear leukocytes (PMNs)], by cleaving it to release a 7-residue carboxy-terminal fragment which contains the PMN binding site. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239048 [Multi-domain]  Cd Length: 143  Bit Score: 40.35  E-value: 6.25e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 41281782  90 IPLVARGNCTFYEKVRLAQGSGARGLLIV-SRERLVPPggnkTQYDEIGIPVALLSYKD 147
Cdd:cd02133  50 IALIQRGEITFVEKIANAKAAGAVGVIIYnNVDGLIPG----TLGEAVFIPVVFISKED 104
PHA03378 PHA03378
EBNA-3B; Provisional
 520-590 1.49e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.59  E-value: 1.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41281782  520 GPQPPKdSATPLSPQPPSEEPATSPWPAEQSpksrtseemGAGAPMREPGSPAESEGRDQAQPSPVTQPGA 590
Cdd:PHA03378 742 GRARPP-AAAPGRARPPAAAPGRARPPAAAP---------GAPTPQPPPQAPPAPQQRPRGAPTPQPPPQA 802
PA_hPAP21_like cd02127
PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted ...
 83-163 5.66e-03

PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted glycoprotein hPAP21 (human protease-associated domain-containing protein, 21kDa). This group contains various PA domain-containing proteins similar to hPAP21. Complex N-glycosylation may be required for the secretion of hPAP21. The significance of the PA domain to hPAP21 has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.


Pssm-ID: 239042 [Multi-domain]  Cd Length: 118  Bit Score: 36.97  E-value: 5.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41281782  83 ARGFSNQIPLVARGNCTFYEKVRLAQGSGARGLLIVSRERlvppgGNKTQY---------DEIGIPVALLSYKDmldift 153
Cdd:cd02127  30 IHDINGNIALIERGGCSFLTKAINAQKAGALAVIITDVNN-----DSDEYYvemiqddssRRADIPAAFLLGKN------ 98

                        90
                ....*....|
gi 41281782 154 rfGRTVRAAL 163
Cdd:cd02127  99 --GYMIRKTL 106
PHA03378 PHA03378
EBNA-3B; Provisional
 522-591 6.88e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 6.88e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41281782  522 QPPKDSATPLSP--------QPPseEPATSPWPAEQSPKSRTSEEMGAGAPMREPGSPAESEGRDQAQPSPVTQPGAS 591
Cdd:PHA03378 695 QPPPRAPTPMRPpaappgraQRP--AAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAA 770
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 519-592 7.10e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 7.10e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41281782  519 DGPQPPKDSATPLSPQPPSEEPATSPWPAEQSPKSRTSEEMGAGAPMREPGSP-AESEGRDQAQPSPVTQPGASA 592
Cdd:PRK07764 410 PAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPsAQPAPAPAAAPEPTAAPAPAP 484
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 519-592 7.61e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.20  E-value: 7.61e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41281782  519 DGPQPPKDSATPlsPQPPSEEPATSPWPAEQSPKSRTSEEMGAGAPMREPGSPAESEGRDQAQPSPVTQPGASA 592
Cdd:PRK07764 433 PAPAPAPAPPSP--AGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPA 504
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 519-592 9.31e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 38.93  E-value: 9.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41281782  519 DGPQPPKDSATPLSPQPPSEEPATSPWPAEQSPKSRTSEEMGAGAPMREPGSPAesegrDQAQPSPVTQPGASA 592
Cdd:PRK14951 419 AAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAV-----ASAAPAPAAAPAAAR 487
 
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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