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Conserved domains on  [gi|222636272|gb|EEE66404|]
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hypothetical protein OsJ_22746 [Oryza sativa Japonica Group]

Protein Classification

A22B family peptidase( domain architecture ID 10114795)

A22B family peptidase catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein, resulting in the release of the fragment from the ER membrane into the cytoplasm

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 ...
238-522 3.84e-126

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: 370.48  E-value: 3.84e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  238 GSSSGMIDINVASAIMFVVVASCFLIMLYKMMSSWFVELLVVIFCVGGVEGLQTCLVALLSRWFRAAS-ESFFKVPFF-G 315
Cdd:pfam04258   1 KSSDDFETITKIHAICFPITASCTLLLLYFFFKSLLVYVLTIYFCILGIIALAFCLSPFLTRLFFNKCpLKNIKLPFLpG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  316 AVSYLTLAVSPFCIVFAVLWAVHRHftyAWIGQDILGIALIITVIQIVRVPNLKVGSVLLSCAFFYDIFWVFVSKRWFHE 395
Cdd:pfam04258  81 RFSYSELVALLLCIVFAVWWALKRH---EWILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPYIFGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  396 SVMIVVARGDKTDEDGVPMLLKIPR---MFDPWGGYSIIGFGDILLPGLLVAFALRYDWAAKKSLQTGYFLWSMVAYGSG 472
Cdd:pfam04258 158 SVMVTVATGPSSTGEDIPMKLVFPRlsnMFDNWGPFSMLGLGDIVMPGLLIALCLRFDISKKKSTHDIYFISTMIAYGLG 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 222636272  473 LLITYVALNLMDgHGQPALLYIVPFTLGALISLGWKRGELWNLWSKGEPE 522
Cdd:pfam04258 238 LLITFVALNLFK-AAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PA_GO-like cd02132
PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on ...
42-180 4.27e-82

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: 251.96  E-value: 4.27e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  42 DFILVKVQSWVNGKEDDEYVGVGARFGPQIVSKEKHANRTRLMLADPIDCCTSPKEKVSGDILLVQRGKCKFTKKAKFAE 121
Cdd:cd02132    1 PFQLVKVQNWVDGDEGDELVGVTARFGASLPSKEDNANKTRAVLANPLDCCSPSTSKLSGSIALVERGECAFTEKAKIAE 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222636272 122 AAGASGIIIINHVHELYKMVCEKNETDLDINIPAVLLPRDAGFALHTVLTSGNSVSVQQ 180
Cdd:cd02132   81 AGGASALLIINDQEELYKMVCEDNDTSLNISIPVVMIPQSAGDALNKSLDQGKKVEVLL 139
 
Name Accession Description Interval E-value
Peptidase_A22B pfam04258
Signal peptide peptidase; The members of this family are membrane proteins. In some proteins ...
238-522 3.84e-126

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: 370.48  E-value: 3.84e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  238 GSSSGMIDINVASAIMFVVVASCFLIMLYKMMSSWFVELLVVIFCVGGVEGLQTCLVALLSRWFRAAS-ESFFKVPFF-G 315
Cdd:pfam04258   1 KSSDDFETITKIHAICFPITASCTLLLLYFFFKSLLVYVLTIYFCILGIIALAFCLSPFLTRLFFNKCpLKNIKLPFLpG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  316 AVSYLTLAVSPFCIVFAVLWAVHRHftyAWIGQDILGIALIITVIQIVRVPNLKVGSVLLSCAFFYDIFWVFVSKRWFHE 395
Cdd:pfam04258  81 RFSYSELVALLLCIVFAVWWALKRH---EWILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPYIFGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  396 SVMIVVARGDKTDEDGVPMLLKIPR---MFDPWGGYSIIGFGDILLPGLLVAFALRYDWAAKKSLQTGYFLWSMVAYGSG 472
Cdd:pfam04258 158 SVMVTVATGPSSTGEDIPMKLVFPRlsnMFDNWGPFSMLGLGDIVMPGLLIALCLRFDISKKKSTHDIYFISTMIAYGLG 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 222636272  473 LLITYVALNLMDgHGQPALLYIVPFTLGALISLGWKRGELWNLWSKGEPE 522
Cdd:pfam04258 238 LLITFVALNLFK-AAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PA_GO-like cd02132
PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on ...
42-180 4.27e-82

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: 251.96  E-value: 4.27e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  42 DFILVKVQSWVNGKEDDEYVGVGARFGPQIVSKEKHANRTRLMLADPIDCCTSPKEKVSGDILLVQRGKCKFTKKAKFAE 121
Cdd:cd02132    1 PFQLVKVQNWVDGDEGDELVGVTARFGASLPSKEDNANKTRAVLANPLDCCSPSTSKLSGSIALVERGECAFTEKAKIAE 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222636272 122 AAGASGIIIINHVHELYKMVCEKNETDLDINIPAVLLPRDAGFALHTVLTSGNSVSVQQ 180
Cdd:cd02132   81 AGGASALLIINDQEELYKMVCEDNDTSLNISIPVVMIPQSAGDALNKSLDQGKKVEVLL 139
PSN smart00730
Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic ...
245-509 1.43e-71

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: 229.06  E-value: 1.43e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272   245 DINVASAIMFVVVASCFLIMLYKMMSSWFVeLLVVIFCVGGVEGLQTCLVALLSRwfraasesffkvpffgAVSYLTLAV 324
Cdd:smart00730   4 LLNSLVAIVFPIVATFVLVLLYKFFKYLVI-VLVIYFSSLGVLFLYSLLYPLEVF----------------RVDYPTLLI 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272   325 SPFCIVFAVLWAVHRHftYAWIGQDILGIALIITVIQIVRVPNLKVGSVLLSCAFFYDIFWVFVSKrwFHESVMIVVARG 404
Cdd:smart00730  67 LLLNFAVVGFWCIHRK--GAWIQQDLIGISLCMAILFILRLPSEWTAWILLGALFIYDIFAVFGTP--GPLRVMVEVATG 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272   405 DKTDEDGVPMLLKIPRM-----FDPWGGYSIIGFGDILLPGLLVAFALRYDWAAKKSLqtGYFLWSMVAYGSGLLITYVA 479
Cdd:smart00730 143 RDEPIKVFPALLYVPRLvvsfeDDEEERFSMLGLGDIVFPGILVASAARFDVSVRSDS--NYFLACFVAYGIGLILTLVL 220
                          250       260       270
                   ....*....|....*....|....*....|
gi 222636272   480 LNLMDgHGQPALLYIVPFTLGALISLGWKR 509
Cdd:smart00730 221 LALFK-KAQPALPYLVPFTLVFYLLTALLR 249
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
60-178 5.91e-16

T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131).


Pssm-ID: 468356 [Multi-domain]  Cd Length: 868  Bit Score: 81.24  E-value: 5.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  60 YVGVGARFGPQIVSKEKHANrtrLMLA-----DPIDCCTS--PKEKVSGDILLVQRGKCKFTKKAKFAEAAGASGIIIIN 132
Cdd:NF038113 424 YPGVRAGFGPRLPDAPITGD---LALAtdsspDPNDGCDPilNAAALAGKIAVIRRGSCEFAVKVLNAQNAGAIAVIIVN 500
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 222636272 133 HV-HELYKMvcEKNETDLDINIPAVLLPRDAGFALHTVLTSGNSVSV 178
Cdd:NF038113 501 NVpGEPIVM--GGGDTGPPITIPSIMISQADGEAIITALNNGETVNV 545
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
59-189 6.81e-12

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: 68.53  E-value: 6.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272   59 EYVGVGARFGPQ-------IVSKEKHANRTRlmladpiDCCT--SPKEKVSGDILLVQRGKCKFTKKAKFAEAAGASGII 129
Cdd:NF038112  502 VYEAGSASFGPQafdvtgdVVLAPDGTGSDT-------DGCTpfTNAAEVAGKIALIDRGTCDFTVKALNAQNAGAIGVI 574
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  130 IINHVHelyKMVCEKNETDLDINIPAVLLPRDAGFALHTVLTSGnSVSVQQYSpdRPVVD 189
Cdd:NF038112  575 IANNAA---GAAPGLGGTDPAVTIPALSITQADGNAWKAALANG-PVTVRLRR--EPALD 628
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
93-166 2.67e-10

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: 57.14  E-value: 2.67e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222636272   93 TSPKEKVSGDILLVQRGKCKFTKKAKFAEAAGASGIIIINHVHELY--KMVCEKNETDLDINIPAVLLPRDAGFAL 166
Cdd:pfam02225  16 IPADFDVKGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNVEGLGgpPGAGGNELYPDGIYIPAVGVSRADGEAL 91
 
Name Accession Description Interval E-value
Peptidase_A22B pfam04258
Signal peptide peptidase; The members of this family are membrane proteins. In some proteins ...
238-522 3.84e-126

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: 370.48  E-value: 3.84e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  238 GSSSGMIDINVASAIMFVVVASCFLIMLYKMMSSWFVELLVVIFCVGGVEGLQTCLVALLSRWFRAAS-ESFFKVPFF-G 315
Cdd:pfam04258   1 KSSDDFETITKIHAICFPITASCTLLLLYFFFKSLLVYVLTIYFCILGIIALAFCLSPFLTRLFFNKCpLKNIKLPFLpG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  316 AVSYLTLAVSPFCIVFAVLWAVHRHftyAWIGQDILGIALIITVIQIVRVPNLKVGSVLLSCAFFYDIFWVFVSKRWFHE 395
Cdd:pfam04258  81 RFSYSELVALLLCIVFAVWWALKRH---EWILQDILGIALCINVIEILRLPNLKVGTLLLSGLFFYDIFWVFGSPYIFGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  396 SVMIVVARGDKTDEDGVPMLLKIPR---MFDPWGGYSIIGFGDILLPGLLVAFALRYDWAAKKSLQTGYFLWSMVAYGSG 472
Cdd:pfam04258 158 SVMVTVATGPSSTGEDIPMKLVFPRlsnMFDNWGPFSMLGLGDIVMPGLLIALCLRFDISKKKSTHDIYFISTMIAYGLG 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 222636272  473 LLITYVALNLMDgHGQPALLYIVPFTLGALISLGWKRGELWNLWSKGEPE 522
Cdd:pfam04258 238 LLITFVALNLFK-AAQPALLYLVPCTLGTLLLLALWRGELKKLWNYGEST 286
PA_GO-like cd02132
PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on ...
42-180 4.27e-82

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: 251.96  E-value: 4.27e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  42 DFILVKVQSWVNGKEDDEYVGVGARFGPQIVSKEKHANRTRLMLADPIDCCTSPKEKVSGDILLVQRGKCKFTKKAKFAE 121
Cdd:cd02132    1 PFQLVKVQNWVDGDEGDELVGVTARFGASLPSKEDNANKTRAVLANPLDCCSPSTSKLSGSIALVERGECAFTEKAKIAE 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222636272 122 AAGASGIIIINHVHELYKMVCEKNETDLDINIPAVLLPRDAGFALHTVLTSGNSVSVQQ 180
Cdd:cd02132   81 AGGASALLIINDQEELYKMVCEDNDTSLNISIPVVMIPQSAGDALNKSLDQGKKVEVLL 139
PSN smart00730
Presenilin, signal peptide peptidase, family; Presenilin 1 and presenilin 2 are polytopic ...
245-509 1.43e-71

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: 229.06  E-value: 1.43e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272   245 DINVASAIMFVVVASCFLIMLYKMMSSWFVeLLVVIFCVGGVEGLQTCLVALLSRwfraasesffkvpffgAVSYLTLAV 324
Cdd:smart00730   4 LLNSLVAIVFPIVATFVLVLLYKFFKYLVI-VLVIYFSSLGVLFLYSLLYPLEVF----------------RVDYPTLLI 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272   325 SPFCIVFAVLWAVHRHftYAWIGQDILGIALIITVIQIVRVPNLKVGSVLLSCAFFYDIFWVFVSKrwFHESVMIVVARG 404
Cdd:smart00730  67 LLLNFAVVGFWCIHRK--GAWIQQDLIGISLCMAILFILRLPSEWTAWILLGALFIYDIFAVFGTP--GPLRVMVEVATG 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272   405 DKTDEDGVPMLLKIPRM-----FDPWGGYSIIGFGDILLPGLLVAFALRYDWAAKKSLqtGYFLWSMVAYGSGLLITYVA 479
Cdd:smart00730 143 RDEPIKVFPALLYVPRLvvsfeDDEEERFSMLGLGDIVFPGILVASAARFDVSVRSDS--NYFLACFVAYGIGLILTLVL 220
                          250       260       270
                   ....*....|....*....|....*....|
gi 222636272   480 LNLMDgHGQPALLYIVPFTLGALISLGWKR 509
Cdd:smart00730 221 LALFK-KAQPALPYLVPFTLVFYLLTALLR 249
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
60-178 5.91e-16

T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131).


Pssm-ID: 468356 [Multi-domain]  Cd Length: 868  Bit Score: 81.24  E-value: 5.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  60 YVGVGARFGPQIVSKEKHANrtrLMLA-----DPIDCCTS--PKEKVSGDILLVQRGKCKFTKKAKFAEAAGASGIIIIN 132
Cdd:NF038113 424 YPGVRAGFGPRLPDAPITGD---LALAtdsspDPNDGCDPilNAAALAGKIAVIRRGSCEFAVKVLNAQNAGAIAVIIVN 500
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 222636272 133 HV-HELYKMvcEKNETDLDINIPAVLLPRDAGFALHTVLTSGNSVSV 178
Cdd:NF038113 501 NVpGEPIVM--GGGDTGPPITIPSIMISQADGEAIITALNNGETVNV 545
PA_subtilisin_1 cd04818
PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. ...
63-178 4.09e-15

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: 71.59  E-value: 4.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  63 VGARFGPQIVSKEKHANRTRLMLADPIDCCTSPKEK--VSGDILLVQRGKCKFTKKAKFAEAAGASGIIIINHVhelykm 140
Cdd:cd04818    1 VSAGFGPALTNVTADVVLAGAAPASNTDGCTAFTNAaaFAGKIALIDRGTCNFTVKVLNAQNAGAIAVIVANNV------ 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 222636272 141 vcEKNE------TDLDINIPAVLLPRDAGFALHTVLTSGNSVSV 178
Cdd:cd04818   75 --AGGApitmggDDPDITIPAVMISQADGDALKAALAAGGTVTV 116
PA cd00538
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
95-179 5.48e-15

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: 71.39  E-value: 5.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  95 PKEKVSGDILLVQRGKCKFTKKAKFAEAAGASGIIIINHV-HELYKMVCEKNETDlDINIPAVLLPRDAGFALHTVLTSG 173
Cdd:cd00538   41 SGADVKGKIVLVRRGGCSFSEKVKNAQKAGAKAVIIYNNGdDPGPQMGSVGLEST-DPSIPTVGISYADGEALLSLLEAG 119

                 ....*.
gi 222636272 174 NSVSVQ 179
Cdd:cd00538  120 KTVTVD 125
PA_EDEM3_like cd02126
PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This ...
65-158 1.66e-14

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: 70.08  E-value: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  65 ARFGPQIvSKEKHAnRTRLMLADPIDCCTS--PKEKVSGDILLVQRGKCKFTKKAKFAEAAGASGIIIINHV-------H 135
Cdd:cd02126    5 AQFGMDL-TGDKAG-VGRVVKAKPYRACSEitNAEEVKGKIAIMERGDCMFVEKARRVQKAGAIGGIVIDNNegsssdtA 82
                         90       100
                 ....*....|....*....|...
gi 222636272 136 ELYKMVCEKNETDlDINIPAVLL 158
Cdd:cd02126   83 PMFAMSGDGDSTD-DVTIPVVFL 104
PA_hPAP21_like cd02127
PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted ...
67-176 3.31e-12

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: 63.55  E-value: 3.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  67 FGPQIVSKEKHanrTRLMLADPIDCCTSPK--EKVSGDILLVQRGKCKFTKKAKFAEAAGASGIII--INHVHELYKMVC 142
Cdd:cd02127    2 FGTIFNTRYKH---VPLVPADPLEACEELRniHDINGNIALIERGGCSFLTKAINAQKAGALAVIItdVNNDSDEYYVEM 78
                         90       100       110
                 ....*....|....*....|....*....|....
gi 222636272 143 EKNETDLDINIPAVLLPRDAGFALHTVLTSGNSV 176
Cdd:cd02127   79 IQDDSSRRADIPAAFLLGKNGYMIRKTLERLGLP 112
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
59-189 6.81e-12

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: 68.53  E-value: 6.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272   59 EYVGVGARFGPQ-------IVSKEKHANRTRlmladpiDCCT--SPKEKVSGDILLVQRGKCKFTKKAKFAEAAGASGII 129
Cdd:NF038112  502 VYEAGSASFGPQafdvtgdVVLAPDGTGSDT-------DGCTpfTNAAEVAGKIALIDRGTCDFTVKALNAQNAGAIGVI 574
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  130 IINHVHelyKMVCEKNETDLDINIPAVLLPRDAGFALHTVLTSGnSVSVQQYSpdRPVVD 189
Cdd:NF038112  575 IANNAA---GAAPGLGGTDPAVTIPALSITQADGNAWKAALANG-PVTVRLRR--EPALD 628
PA_C_RZF_like cd02123
PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA ...
58-166 1.59e-10

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: 59.66  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  58 DEYVGVGARFGPQIvskEKHANRTRLMLADPIDCCTS-----PKEKVSGD-ILLVQRGKCKFTKKAKFAEAAGASGIIII 131
Cdd:cd02123   22 DEFDDLPANFGPIP---PGSGLKGVLVVAEPLNACSPienppLNSNASGSfIVLIRRGNCSFETKVRNAQRAGYKAAIVY 98
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 222636272 132 NhVH--ELYKMVcEKNETDLDINIPAVLLPRDAGFAL 166
Cdd:cd02123   99 N-DEsnDLISMS-GNDQEIKGIDIPSVFVGKSTGEIL 133
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
93-166 2.67e-10

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: 57.14  E-value: 2.67e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222636272   93 TSPKEKVSGDILLVQRGKCKFTKKAKFAEAAGASGIIIINHVHELY--KMVCEKNETDLDINIPAVLLPRDAGFAL 166
Cdd:pfam02225  16 IPADFDVKGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNVEGLGgpPGAGGNELYPDGIYIPAVGVSRADGEAL 91
PA_C5a_like cd02133
PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a ...
99-182 3.59e-09

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: 55.37  E-value: 3.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  99 VSGDILLVQRGKCKFTKKAKFAEAAGASGIIIINHVHELYKMVcekneTDLDINIPAVLLPRDAGFALHTVLTSGNSVSV 178
Cdd:cd02133   46 VKGKIALIQRGEITFVEKIANAKAAGAVGVIIYNNVDGLIPGT-----LGEAVFIPVVFISKEDGEALKAALESSKKLTF 120

                 ....
gi 222636272 179 QQYS 182
Cdd:cd02133  121 NTKK 124
PA_SaNapH_like cd04816
PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ...
99-178 2.57e-07

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: 49.63  E-value: 2.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  99 VSGDILLVQRGKCKFTKKAKFAEAAGASGIIIINHVHElykmvcekNET-------DLDINIPAVLLPRDAGFALHTVLT 171
Cdd:cd04816   42 VKGAIVLVDRGGCPFADKQKVAAARGAVAVIVVNNSDG--------GGTagtlgapNIDLKVPVGVITKAAGAALRRRLG 113

                 ....*..
gi 222636272 172 SGNSVSV 178
Cdd:cd04816  114 AGETLEL 120
PA_VSR cd02125
PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This ...
103-178 3.72e-07

PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This group includes various PA domain-containing VSRs such as garden pea BP-80, pumpkin PV72, and various Arabidopsis VSRs including AtVSR1. In contrast to most eukaryotes, which only have one or two VSRs, plants have several. This may in part be a reflection of having a more complex vacuolar system with both lytic vacuoles and storage vacuoles. The lytic vacuole is thought to be equivalent to the mammalian lysosome and the yeast vacuole. Pea BP-80 is a type 1 transmembrane protein, involved in the targeting of proteins to the lytic vacuole; it has been suggested that this protein also mediates targeting to the storage vacuole. PV72 and AtVSR1 may mediate transport of seed storage proteins to protein storage vacuoles. The significance of the PA domain to VSRs 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: 239040 [Multi-domain]  Cd Length: 127  Bit Score: 49.02  E-value: 3.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272 103 ILLVQRGKCKFTKKAKFAEAAGASGIIIINHVHE-LYKMVCEKNETDLD----INIPAVLLPRDAGFALHTVLTSGNSVS 177
Cdd:cd02125   45 ILLLDRGGCFFTLKAWNAQQAGAAAVLVADNVDEpLLTMDTPEESGSADyiekITIPSALITKAFGEKLKKAISNGEMVV 124

                 .
gi 222636272 178 V 178
Cdd:cd02125  125 I 125
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
78-178 4.55e-07

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: 48.93  E-value: 4.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  78 ANRTRLMLADPIDcctSPKEKVSGDILLVQRGKCKFTKKAKFAEAAGASGIIIINHVHElykMVCEKNETDL-DINIPAV 156
Cdd:cd02129   25 RNLTSSVLCSASD---VPPGGLKGKAVVVMRGNCTFYEKARLAQSLGAEGLLIVSRERL---VPPSGNRSEYeKIDIPVA 98
                         90       100
                 ....*....|....*....|..
gi 222636272 157 LLpRDAGFaLHTVLTSGNSVSV 178
Cdd:cd02129   99 LL-SYKDM-LDIQQTFGDSVKV 118
PA_ScAPY_like cd02130
PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae ...
97-136 1.32e-06

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: 47.64  E-value: 1.32e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 222636272  97 EKVSGDILLVQRGKCKFTKKAKFAEAAGASGIIIINHVHE 136
Cdd:cd02130   41 ASVAGNIALIERGECPFGDKSALAGAAGAAAAIIYNNVPA 80
PA_GRAIL_like cd02122
PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain ...
103-132 3.24e-05

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: 43.83  E-value: 3.24e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 222636272 103 ILLVQRGKCKFTKKAKFAEAAGASGIIIIN 132
Cdd:cd02122   63 IALIQRGNCTFEEKIKLAAERNASAVVIYN 92
PA_VapT_like cd04817
PA_VapT_like: Protease-associated domain containing proteins like VapT from Vibrio ...
99-178 1.03e-04

PA_VapT_like: Protease-associated domain containing proteins like VapT from Vibrio metschnikovii strain RH530. This group contains various PA domain-containing proteins similar to V. metschnikovii VapT, including the serine alkaline protease SapSh from the psychotroph Shewanella strain Ac10 and the Apa1 protease from the psychrotroph Pseudoalteromonas Sp. As-11. VapT is a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease showing high activity over a broad pH range and temperature. SapSh has a high level of protease activity at low temperatures. Apa1 is also cold-adapted. 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: 240121  Cd Length: 139  Bit Score: 42.47  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  99 VSGDILLVQRGKCK-----FTKKAKFAEAAGASGIIIINHVHE---LYKMVCEKNEtdlDINIPAVLLPRDAGFALHTVL 170
Cdd:cd04817   55 MAGKICLIERGGNSksvypEIDKVKACQNAGAIAAIVYSNAALaglQNPFLVDTNN---DTTIPSVSVDRADGQALLAAL 131

                 ....*...
gi 222636272 171 TSGNSVSV 178
Cdd:cd04817  132 GQSTTVST 139
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
92-175 4.59e-04

PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This group contains various PA domain-containing subtilisin-like proteases including melon cucumisin, Arabidopsis thaliana Ara12, a nodule specific serine protease from Alnus glutinosa ag12, members of the tomato P69 family, and tomato LeSBT2. These proteins belong to the peptidase S8 family. Cucumisin from the juice of melon fruits is a thermostable serine peptidase, with a broad substrate specificity for oligopeptides and proteins. A. thaliana Ara12 is a thermostable, extracellular serine protease, found chiefly in silique tissue and stem tissue. Ara12 is stimulated by Ca2+ ions. A. glutinosa ag12 is expressed at high levels in the nodules, and at low levels in the shoot tips; it is implicated in both symbiotic and non-symbiotic processes in plant development. The tomato P69 protease family is comprised of various protein isoforms of approximately 69KDa. These isoforms accumulate extracellularly. Some of the P69 genes are tightly regulated in a tissue specific fashion, and by environmental and developmental signals. For example: infection with avirulent bacteria activates transcription of the genes for the P69 B and C isoforms, the P69 E transcript was detected only in roots, and the P69F transcript only in hydathodes. The Tomato LeSBT2 subtilase transcript was not detected in flowers and roots, but was present in cotyledons and leaves. 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: 239035 [Multi-domain]  Cd Length: 126  Bit Score: 40.09  E-value: 4.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  92 CTSP---KEKVSGDILLVQRGK-CKFTKKAKFAEAAGASGIIIINHVHELYkmvceknETDLDIN-IPAVLLPRDAGFAL 166
Cdd:cd02120   40 CLPGsldPSKVKGKIVLCDRGGnTSRVAKGDAVKAAGGAGMILANDPTDGL-------DVVADAHvLPAVHVDYEDGTAI 112

                 ....*....
gi 222636272 167 HTVLTSGNS 175
Cdd:cd02120  113 LSYINSTSN 121
PA_1 cd04813
PA_1: Protease-associated (PA) domain subgroup 1. A subgroup of PA-domain containing proteins. ...
90-160 1.41e-03

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: 38.52  E-value: 1.41e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 222636272  90 DCCTSPKEKVSGDILLVQRGKCKFTKKAKFAEAAGASGIIIINHVHE--LYKMVcEKNETDLdINIPAVLLPR 160
Cdd:cd04813   29 ACSLQEHAEIDGKVALVLRGGCGFLDKVMWAQRRGAKAVIVGDDEPGrgLITMF-SNGDTDN-VTIPAMFTSR 99
PA_PoS1_like cd02124
PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA ...
100-132 4.24e-03

PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA domain-containing proteins similar to Pleurotus ostreatus (Po)S1. PoSl, the main extracellular protease in P. ostreatus is a subtilisin-like serine protease belonging to the peptidase S8 family. Ca2+ and Mn2+ both stimulate the protease activity of (Po)S1. Ca2+ protects PoS1 from autolysis. PoS1 is a monomeric glycoprotein, which may play a role in the regulation of laccases in lignin formation. (Po)S1 participates in the degradation of POXA1b, and in the activation of POXA3, (POXA1b and POXA3 are laccase isoenzymes), but its effect may be indirect. The significance of the PA domain to PoS1 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: 239039  Cd Length: 129  Bit Score: 37.69  E-value: 4.24e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 222636272 100 SGDILLVQRGKCKFTKKAKFAEAAGASGIIIIN 132
Cdd:cd02124   55 SGYIVLVRRGTCTFATKAANAAAKGAKYVLIYN 87
PA_2 cd04819
PA_2: Protease-associated (PA) domain subgroup 2. A subgroup of PA-domain containing proteins. ...
99-178 4.66e-03

PA_2: Protease-associated (PA) domain subgroup 2. A subgroup of PA-domain containing proteins. 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: 240123 [Multi-domain]  Cd Length: 127  Bit Score: 37.37  E-value: 4.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222636272  99 VSGDILLVQRGKCKFTKKAKFAEA--AGASGIIIINHVH-ELYKMVCEKNETDLDINIPAVLLPRDAGFALHTVLTSGNS 175
Cdd:cd04819   43 LEGKIAVVKRDDPDVDRKEKYAKAvaAGAAAFVVVNTVPgVLPATGDEGTEDGPPSPIPAASVSGEDGLRLARVAERNDT 122

                 ...
gi 222636272 176 VSV 178
Cdd:cd04819  123 LVL 125
 
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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