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Conserved domains on  [gi|163310725|ref|NP_079467|]
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ER degradation-enhancing alpha-mannosidase-like protein 3 isoform 2 precursor [Homo sapiens]

Protein Classification

Glyco_hydro_47 and PA_EDEM3_like domain-containing protein( domain architecture ID 10479226)

Glyco_hydro_47 and PA_EDEM3_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
 59-498 6.25e-154

Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).


:

Pssm-ID: 460241  Cd Length: 453  Bit Score: 460.87  E-value: 6.25e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725   59 MFDHAYGNYMEHAYPADELMPLTCRGRvrgqepsrgdvdDALGKFSLTLIDSLDTLVVLNKTKEFEDAVRKVLRDVNLDN 138
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGN------------DTFGGWGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDK 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  139 DV-VVSVFETNIRVlggllgghsLAIMLkekGEYM--QWYNDELLQMAKQLGYKLLPAFNTTSGLPYPRINLKFGIRKPE 215
Cdd:pfam01532  69 DStEVSVFETTIRY---------LGGLL---SAYDlsGDGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGKGGNG 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  216 ARTGTetDTCTACAGTLILEFAALSRFTGATIFEEYARKALDFLWEKRQRSS--NLVGVTINIHTGDWVRKDSGVGAGID 293
Cdd:pfam01532 137 HVAGG--ASSLAEAGTLQLEFTRLSQLTGDPKYEDLAQKIMDVLWKNQSRTPlpGLVPIYIDPDTGKFVGSNIGLGARGD 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  294 SYYEYLLKAYVLLG--DDSFLERFNTHYDAIMRYI----SQPPLLLDVHIHKPMLNAR--TWMDALLAFFPGLQVL---- 361
Cdd:pfam01532 215 SYYEYLLKQYLLTGgtDPEYRDMYEEAMDAIKKHLlfrpSTPSDLLFIGELDSGGGGKlsPKMDHLSCFAGGMLALgatl 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  362 ----KGDIRPAIETHEMLYQVIK--KHNFLPEAF--------------TTDFRVHW--AQHPLRPEFAESTYFLYKATGD 419
Cdd:pfam01532 295 glprEGDLELAEKLTEGCYKTYDstPTGLGPEIFyfdpcdedcpwdedKWDFYVKIedPHYLLRPETIESLFYLYRATGD 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  420 PYYLEVGKTLIENLNKYARVPCGFAAMKDVR--TGSHEDRMDSFFLAEMFKYLYLLFADKEDIifDIEDYIFTTEAHLLP 497
Cdd:pfam01532 375 PKYREWGWEIFQAIEKYTRTECGYSGLQDVTspPGEKEDNMESFWLAETLKYLYLLFSDDDLL--SLDEWVFNTEAHPLP 452


                  .
gi 163310725  498 L 498
Cdd:pfam01532 453 V 453
PA_EDEM3_like cd02126
PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This ...
 664-789 9.74e-77

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: 246.12  E-value: 9.74e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 664 TAGPAQFGLDLSKHKETRGFVASSKPSNGCSELTNPEAVMGKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEGSSSD 743
Cdd:cd02126    1 TAGPAQFGMDLTGDKAGVGRVVKAKPYRACSEITNAEEVKGKIAIMERGDCMFVEKARRVQKAGAIGGIVIDNNEGSSSD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 163310725 744 TAPLFQMAGDGKDTDDIKIPMLFLFSKEGSIILDAIREYEEVEVLL 789
Cdd:cd02126   81 TAPMFAMSGDGDSTDDVTIPVVFLFSKEGSKLLAAIKEHQNVEVLL 126
DMP1 super family cl25845
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 783-902 2.66e-05

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


The actual alignment was detected with superfamily member pfam07263:

Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 48.00  E-value: 2.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  783 EEVEvllSDKAKDRDPE-------MENEEQPSSENDSQNQSGEQ-------ISSSSQEVDLVDQESSEEnslnSHPESLS 848
Cdd:pfam07263 288 EEVK---SDSTESTSSKeaglsqsREDSKSESQEDSEESQSQEDsqnsqdpSSESSQEADLPSQESSSE----SQEEVVS 360

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 163310725  849 LADMDNAASISPSEQTSNPTENHETTNLNgectDLDNQLQEQSETEEDSNPNVS 902
Cdd:pfam07263 361 ESRGDNPDNTSSSEEDQEDSDSSEEDSLS----TFSSSESESREEQADSESNES 410
 
Name Accession Description Interval E-value
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
 59-498 6.25e-154

Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).


Pssm-ID: 460241  Cd Length: 453  Bit Score: 460.87  E-value: 6.25e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725   59 MFDHAYGNYMEHAYPADELMPLTCRGRvrgqepsrgdvdDALGKFSLTLIDSLDTLVVLNKTKEFEDAVRKVLRDVNLDN 138
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGN------------DTFGGWGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDK 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  139 DV-VVSVFETNIRVlggllgghsLAIMLkekGEYM--QWYNDELLQMAKQLGYKLLPAFNTTSGLPYPRINLKFGIRKPE 215
Cdd:pfam01532  69 DStEVSVFETTIRY---------LGGLL---SAYDlsGDGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGKGGNG 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  216 ARTGTetDTCTACAGTLILEFAALSRFTGATIFEEYARKALDFLWEKRQRSS--NLVGVTINIHTGDWVRKDSGVGAGID 293
Cdd:pfam01532 137 HVAGG--ASSLAEAGTLQLEFTRLSQLTGDPKYEDLAQKIMDVLWKNQSRTPlpGLVPIYIDPDTGKFVGSNIGLGARGD 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  294 SYYEYLLKAYVLLG--DDSFLERFNTHYDAIMRYI----SQPPLLLDVHIHKPMLNAR--TWMDALLAFFPGLQVL---- 361
Cdd:pfam01532 215 SYYEYLLKQYLLTGgtDPEYRDMYEEAMDAIKKHLlfrpSTPSDLLFIGELDSGGGGKlsPKMDHLSCFAGGMLALgatl 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  362 ----KGDIRPAIETHEMLYQVIK--KHNFLPEAF--------------TTDFRVHW--AQHPLRPEFAESTYFLYKATGD 419
Cdd:pfam01532 295 glprEGDLELAEKLTEGCYKTYDstPTGLGPEIFyfdpcdedcpwdedKWDFYVKIedPHYLLRPETIESLFYLYRATGD 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  420 PYYLEVGKTLIENLNKYARVPCGFAAMKDVR--TGSHEDRMDSFFLAEMFKYLYLLFADKEDIifDIEDYIFTTEAHLLP 497
Cdd:pfam01532 375 PKYREWGWEIFQAIEKYTRTECGYSGLQDVTspPGEKEDNMESFWLAETLKYLYLLFSDDDLL--SLDEWVFNTEAHPLP 452


                  .
gi 163310725  498 L 498
Cdd:pfam01532 453 V 453
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
 42-498 6.20e-77

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 260.81  E-value: 6.20e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  42 EPMSREEKQ---------KLGNQVLEMFDHAYGNYMEHAYPADELMPLTCRGRvrgqepsrgdvddALGKFSLTLIDSLD 112
Cdd:PTZ00470  53 NPFNKIDEVyyqneklniKRRESVREAMKHAWEGYKEYAWGHDELRPLTKRHH-------------EWFGLGLTIIDSLD 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 113 TLVVLNKTKEFEDAVRKVLRDVNLDNDV--VVSVFETNIRVLGGLLGGHSLAimlkekgeymqwyNDEL-LQMAKQLGYK 189
Cdd:PTZ00470 120 TLKIMGLKKEYKEGRDWVANNLKQSKDTglGVSVFETTIRVLGGLLSAYDLT-------------GDEMyLEKAREIADR 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 190 LLPAFNTTSGLPYPRINLKFGIRKPEARTGTetDTCTACAGTLILEFAALSRFTGATIFEEYARKALDFLWEKRQRSSNL 269
Cdd:PTZ00470 187 LLPAFNEDTGFPASEINLATGRKSYPGWAGG--CSILSEVGTLQLEFNYLSEITGDPKYAEYVDKVMDALFSMKPAINGL 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 270 VGVTINIHTGDWVRKDSGVGAGIDSYYEYLLKAYVLL--GDDSFLERFNTHYDAIMR-----------YISQppLLLDVH 336
Cdd:PTZ00470 265 YPIFLNPDAGRFCGNHISLGALGDSYYEYLLKQWLYTngREERYRRLFVESAKGIIEhlykrspkgltYIAE--MDGGSL 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 337 IHKpmlnartwMDALLAFFPGLQVLKGDIRPA---------IETHEML----YQV--IKKHNFLPEAFTTD-------FR 394
Cdd:PTZ00470 343 TNK--------MEHLACFAGGMFALGAAINITpddeksaryMEVGEEVtktcYETyaTSPTGLGPEIFHFDpnsgdisPN 414

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 395 VHWAQHPLRPEFAESTYFLYKATGDPYYLEVGKTLIENLNKYARVPCGFAAMKDVRT--GSHEDRMDSFFLAEMFKYLYL 472
Cdd:PTZ00470 415 VHDSHYILRPETVESIFILYRLTGDPKYREWAWKIFQAIEKHCKTENGYSGLKNVLTvhPQQDDFQESFFLAETLKYLYL 494

                        490       500
                 ....*....|....*....|....*.
gi 163310725 473 LFADKEDIIFDieDYIFTTEAHLLPL 498
Cdd:PTZ00470 495 LFQPDHVIPLD--KYVFNTEAHPIPI 518
PA_EDEM3_like cd02126
PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This ...
 664-789 9.74e-77

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: 246.12  E-value: 9.74e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 664 TAGPAQFGLDLSKHKETRGFVASSKPSNGCSELTNPEAVMGKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEGSSSD 743
Cdd:cd02126    1 TAGPAQFGMDLTGDKAGVGRVVKAKPYRACSEITNAEEVKGKIAIMERGDCMFVEKARRVQKAGAIGGIVIDNNEGSSSD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 163310725 744 TAPLFQMAGDGKDTDDIKIPMLFLFSKEGSIILDAIREYEEVEVLL 789
Cdd:cd02126   81 TAPMFAMSGDGDSTDDVTIPVVFLFSKEGSKLLAAIKEHQNVEVLL 126
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
 667-791 7.81e-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: 82.39  E-value: 7.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 667 PAQFGLDLSKHKETRGFV----ASSKPSNGCSELTNPEAVMGKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEGSss 742
Cdd:NF038113 428 RAGFGPRLPDAPITGDLAlatdSSPDPNDGCDPILNAAALAGKIAVIRRGSCEFAVKVLNAQNAGAIAVIIVNNVPGE-- 505

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 163310725 743 dtaPLFQMAGDgkDTDDIKIPMLFLFSKEGSIILDAIREYEEVEVLLSD 791
Cdd:NF038113 506 ---PIVMGGGD--TGPPITIPSIMISQADGEAIITALNNGETVNVTLKD 549
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
 682-775 1.40e-14

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: 69.85  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  682 GFVASSKPSNGCSELTNPEAVMGKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEGSSSDTaplfQMAGDGKDTDDIK 761
Cdd:pfam02225   2 GPLVLAPGCYAGDGIPADFDVKGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNVEGLGGPP----GAGGNELYPDGIY 77

                          90
                  ....*....|....
gi 163310725  762 IPMLFLFSKEGSII 775
Cdd:pfam02225  78 IPAVGVSRADGEAL 91
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
 662-803 1.60e-14

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: 78.55  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  662 VLTAGPAQFG---LDLskhkeTRGFV----ASSKPSNGCSELTNPEAVMGKIALIQRGQCMFAEKARNIQNAGAIGGIVI 734
Cdd:NF038112  502 VYEAGSASFGpqaFDV-----TGDVVlapdGTGSDTDGCTPFTNAAEVAGKIALIDRGTCDFTVKALNAQNAGAIGVIIA 576

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 163310725  735 DDNEGSSSDTAplfqmagdGKDTdDIKIPMLFLFSKEGsiilDAIR---EYEEVEV-LLSDKAKDRDPEMENE 803
Cdd:NF038112  577 NNAAGAAPGLG--------GTDP-AVTIPALSITQADG----NAWKaalANGPVTVrLRREPALDRDGTLDNG 636
DMP1 pfam07263
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 783-902 2.66e-05

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 48.00  E-value: 2.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  783 EEVEvllSDKAKDRDPE-------MENEEQPSSENDSQNQSGEQ-------ISSSSQEVDLVDQESSEEnslnSHPESLS 848
Cdd:pfam07263 288 EEVK---SDSTESTSSKeaglsqsREDSKSESQEDSEESQSQEDsqnsqdpSSESSQEADLPSQESSSE----SQEEVVS 360

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 163310725  849 LADMDNAASISPSEQTSNPTENHETTNLNgectDLDNQLQEQSETEEDSNPNVS 902
Cdd:pfam07263 361 ESRGDNPDNTSSSEEDQEDSDSSEEDSLS----TFSSSESESREEQADSESNES 410
PRK08581 PRK08581
amidase domain-containing protein;
804-920 1.58e-04

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 45.55  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 804 EQPSSENDSQNQSGEQISSSSQEVDlvDQESSEENSLNSHPESLSLADMDNAASISP-SEQTSNPTENHETTNLNGECTD 882
Cdd:PRK08581 137 EQPRNSEKSTNDSNKNSDSSIKNDT--DTQSSKQDKADNQKAPSSNNTKPSTSNKQPnSPKPTQPNQSNSQPASDDTANQ 214

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 163310725 883 LDNQlqEQSETEEDSnpnvswgkkvqPIDSILADWNED 920
Cdd:PRK08581 215 KSSS--KDNQSMSDS-----------ALDSILDQYSED 239
LanM-like cd04792
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
 236-328 2.48e-03

Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.


Pssm-ID: 271200 [Multi-domain]  Cd Length: 836  Bit Score: 41.53  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 236 FAALSRFTGATIFEEYARKALdflwekrqrssNLVGVTINIHTGDWVRKDSGVGAGIDSYYEYLLKAYVLLGDDSFLERF 315
Cdd:cd04792  503 LAALAALTGDEKYRDLARKAL-----------RPLRKLLRDLAADPRSLGIGGFTGLGSILYALSHLARLLGDPELLEDA 571

                         90
                 ....*....|...
gi 163310725 316 NTHYDAIMRYISQ 328
Cdd:cd04792  572 LELADLLTEAIIE 584
 
Name Accession Description Interval E-value
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
 59-498 6.25e-154

Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).


Pssm-ID: 460241  Cd Length: 453  Bit Score: 460.87  E-value: 6.25e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725   59 MFDHAYGNYMEHAYPADELMPLTCRGRvrgqepsrgdvdDALGKFSLTLIDSLDTLVVLNKTKEFEDAVRKVLRDVNLDN 138
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGN------------DTFGGWGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDK 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  139 DV-VVSVFETNIRVlggllgghsLAIMLkekGEYM--QWYNDELLQMAKQLGYKLLPAFNTTSGLPYPRINLKFGIRKPE 215
Cdd:pfam01532  69 DStEVSVFETTIRY---------LGGLL---SAYDlsGDGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGKGGNG 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  216 ARTGTetDTCTACAGTLILEFAALSRFTGATIFEEYARKALDFLWEKRQRSS--NLVGVTINIHTGDWVRKDSGVGAGID 293
Cdd:pfam01532 137 HVAGG--ASSLAEAGTLQLEFTRLSQLTGDPKYEDLAQKIMDVLWKNQSRTPlpGLVPIYIDPDTGKFVGSNIGLGARGD 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  294 SYYEYLLKAYVLLG--DDSFLERFNTHYDAIMRYI----SQPPLLLDVHIHKPMLNAR--TWMDALLAFFPGLQVL---- 361
Cdd:pfam01532 215 SYYEYLLKQYLLTGgtDPEYRDMYEEAMDAIKKHLlfrpSTPSDLLFIGELDSGGGGKlsPKMDHLSCFAGGMLALgatl 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  362 ----KGDIRPAIETHEMLYQVIK--KHNFLPEAF--------------TTDFRVHW--AQHPLRPEFAESTYFLYKATGD 419
Cdd:pfam01532 295 glprEGDLELAEKLTEGCYKTYDstPTGLGPEIFyfdpcdedcpwdedKWDFYVKIedPHYLLRPETIESLFYLYRATGD 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  420 PYYLEVGKTLIENLNKYARVPCGFAAMKDVR--TGSHEDRMDSFFLAEMFKYLYLLFADKEDIifDIEDYIFTTEAHLLP 497
Cdd:pfam01532 375 PKYREWGWEIFQAIEKYTRTECGYSGLQDVTspPGEKEDNMESFWLAETLKYLYLLFSDDDLL--SLDEWVFNTEAHPLP 452


                  .
gi 163310725  498 L 498
Cdd:pfam01532 453 V 453
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
 42-498 6.20e-77

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 260.81  E-value: 6.20e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  42 EPMSREEKQ---------KLGNQVLEMFDHAYGNYMEHAYPADELMPLTCRGRvrgqepsrgdvddALGKFSLTLIDSLD 112
Cdd:PTZ00470  53 NPFNKIDEVyyqneklniKRRESVREAMKHAWEGYKEYAWGHDELRPLTKRHH-------------EWFGLGLTIIDSLD 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 113 TLVVLNKTKEFEDAVRKVLRDVNLDNDV--VVSVFETNIRVLGGLLGGHSLAimlkekgeymqwyNDEL-LQMAKQLGYK 189
Cdd:PTZ00470 120 TLKIMGLKKEYKEGRDWVANNLKQSKDTglGVSVFETTIRVLGGLLSAYDLT-------------GDEMyLEKAREIADR 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 190 LLPAFNTTSGLPYPRINLKFGIRKPEARTGTetDTCTACAGTLILEFAALSRFTGATIFEEYARKALDFLWEKRQRSSNL 269
Cdd:PTZ00470 187 LLPAFNEDTGFPASEINLATGRKSYPGWAGG--CSILSEVGTLQLEFNYLSEITGDPKYAEYVDKVMDALFSMKPAINGL 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 270 VGVTINIHTGDWVRKDSGVGAGIDSYYEYLLKAYVLL--GDDSFLERFNTHYDAIMR-----------YISQppLLLDVH 336
Cdd:PTZ00470 265 YPIFLNPDAGRFCGNHISLGALGDSYYEYLLKQWLYTngREERYRRLFVESAKGIIEhlykrspkgltYIAE--MDGGSL 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 337 IHKpmlnartwMDALLAFFPGLQVLKGDIRPA---------IETHEML----YQV--IKKHNFLPEAFTTD-------FR 394
Cdd:PTZ00470 343 TNK--------MEHLACFAGGMFALGAAINITpddeksaryMEVGEEVtktcYETyaTSPTGLGPEIFHFDpnsgdisPN 414

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 395 VHWAQHPLRPEFAESTYFLYKATGDPYYLEVGKTLIENLNKYARVPCGFAAMKDVRT--GSHEDRMDSFFLAEMFKYLYL 472
Cdd:PTZ00470 415 VHDSHYILRPETVESIFILYRLTGDPKYREWAWKIFQAIEKHCKTENGYSGLKNVLTvhPQQDDFQESFFLAETLKYLYL 494

                        490       500
                 ....*....|....*....|....*.
gi 163310725 473 LFADKEDIIFDieDYIFTTEAHLLPL 498
Cdd:PTZ00470 495 LFQPDHVIPLD--KYVFNTEAHPIPI 518
PA_EDEM3_like cd02126
PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This ...
 664-789 9.74e-77

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: 246.12  E-value: 9.74e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 664 TAGPAQFGLDLSKHKETRGFVASSKPSNGCSELTNPEAVMGKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEGSSSD 743
Cdd:cd02126    1 TAGPAQFGMDLTGDKAGVGRVVKAKPYRACSEITNAEEVKGKIAIMERGDCMFVEKARRVQKAGAIGGIVIDNNEGSSSD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 163310725 744 TAPLFQMAGDGKDTDDIKIPMLFLFSKEGSIILDAIREYEEVEVLL 789
Cdd:cd02126   81 TAPMFAMSGDGDSTDDVTIPVVFLFSKEGSKLLAAIKEHQNVEVLL 126
PA_C_RZF_like cd02123
PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA ...
 667-792 1.25e-21

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: 92.40  E-value: 1.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 667 PAQFGLDLSKHKEtRGFVASSKPSNGCSELTNPEAVMG----KIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEGSss 742
Cdd:cd02123   28 PANFGPIPPGSGL-KGVLVVAEPLNACSPIENPPLNSNasgsFIVLIRRGNCSFETKVRNAQRAGYKAAIVYNDESND-- 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 163310725 743 dtapLFQMAGDGKDTDDIKIPMLFLfSKEGSIILDAIREYEEVEVLLSDK 792
Cdd:cd02123  105 ----LISMSGNDQEIKGIDIPSVFV-GKSTGEILKKYASYEKGVILIPDL 149
PA cd00538
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ...
 662-789 1.56e-21

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: 91.04  E-value: 1.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 662 VLTAGPAQFGLDLSKHKETRGFVASSKPSNGCSELT---NPEAVMGKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDne 738
Cdd:cd00538    2 VILATTGYAGSALLFNPPSSPVGVVAGPLVGCGYGTtddSGADVKGKIVLVRRGGCSFSEKVKNAQKAGAKAVIIYNN-- 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 163310725 739 gsssDTAPLFQMAGDGKDTDDIKIPMLFLFSKEGSIILDAIREYEEVEVLL 789
Cdd:cd00538   80 ----GDDPGPQMGSVGLESTDPSIPTVGISYADGEALLSLLEAGKTVTVDL 126
PA_subtilisin_1 cd04818
PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. ...
 666-789 4.38e-19

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: 83.92  E-value: 4.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 666 GPAQFGLDLSKhkETRGFV----ASSKPSNGCSELTNPEAVMGKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEGss 741
Cdd:cd04818    1 VSAGFGPALTN--VTADVVlagaAPASNTDGCTAFTNAAAFAGKIALIDRGTCNFTVKVLNAQNAGAIAVIVANNVAG-- 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 163310725 742 sdtAPLFQMAGDGkdtDDIKIPMLFLFSKEGSIILDAIREYEEVEVLL 789
Cdd:cd04818   77 ---GAPITMGGDD---PDITIPAVMISQADGDALKAALAAGGTVTVTL 118
PA_hPAP21_like cd02127
PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted ...
 689-781 8.85e-17

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: 77.03  E-value: 8.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 689 PSNGCSELTNPEAVMGKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEGSSSDTaplFQMAGDgKDTDDIKIPMLFLF 768
Cdd:cd02127   20 PLEACEELRNIHDINGNIALIERGGCSFLTKAINAQKAGALAVIITDVNNDSDEYY---VEMIQD-DSSRRADIPAAFLL 95

                         90
                 ....*....|...
gi 163310725 769 SKEGSIILDAIRE 781
Cdd:cd02127   96 GKNGYMIRKTLER 108
PA_GO-like cd02132
PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on ...
 663-789 3.71e-16

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: 75.92  E-value: 3.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 663 LTAGPAQFGLDL--SKHKETRGFVASSKPSNGCSELTNPeaVMGKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEgs 740
Cdd:cd02132   19 LVGVTARFGASLpsKEDNANKTRAVLANPLDCCSPSTSK--LSGSIALVERGECAFTEKAKIAEAGGASALLIINDQE-- 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 163310725 741 ssdtaPLFQMAGDGKDTD-DIKIPMLFLFSKEGSIILDAIREYEEVEVLL 789
Cdd:cd02132   95 -----ELYKMVCEDNDTSlNISIPVVMIPQSAGDALNKSLDQGKKVEVLL 139
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
 667-791 7.81e-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: 82.39  E-value: 7.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 667 PAQFGLDLSKHKETRGFV----ASSKPSNGCSELTNPEAVMGKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEGSss 742
Cdd:NF038113 428 RAGFGPRLPDAPITGDLAlatdSSPDPNDGCDPILNAAALAGKIAVIRRGSCEFAVKVLNAQNAGAIAVIIVNNVPGE-- 505

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 163310725 743 dtaPLFQMAGDgkDTDDIKIPMLFLFSKEGSIILDAIREYEEVEVLLSD 791
Cdd:NF038113 506 ---PIVMGGGD--TGPPITIPSIMISQADGEAIITALNNGETVNVTLKD 549
PA pfam02225
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ...
 682-775 1.40e-14

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: 69.85  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  682 GFVASSKPSNGCSELTNPEAVMGKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEGSSSDTaplfQMAGDGKDTDDIK 761
Cdd:pfam02225   2 GPLVLAPGCYAGDGIPADFDVKGKIVLVRCTFGFRAEKVRNAQAAGAAGVIIYNNVEGLGGPP----GAGGNELYPDGIY 77

                          90
                  ....*....|....
gi 163310725  762 IPMLFLFSKEGSII 775
Cdd:pfam02225  78 IPAVGVSRADGEAL 91
myxo_dep_M36 NF038112
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
 662-803 1.60e-14

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: 78.55  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  662 VLTAGPAQFG---LDLskhkeTRGFV----ASSKPSNGCSELTNPEAVMGKIALIQRGQCMFAEKARNIQNAGAIGGIVI 734
Cdd:NF038112  502 VYEAGSASFGpqaFDV-----TGDVVlapdGTGSDTDGCTPFTNAAEVAGKIALIDRGTCDFTVKALNAQNAGAIGVIIA 576

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 163310725  735 DDNEGSSSDTAplfqmagdGKDTdDIKIPMLFLFSKEGsiilDAIR---EYEEVEV-LLSDKAKDRDPEMENE 803
Cdd:NF038112  577 NNAAGAAPGLG--------GTDP-AVTIPALSITQADG----NAWKaalANGPVTVrLRREPALDRDGTLDNG 636
PA_C5a_like cd02133
PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a ...
 702-787 4.33e-11

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: 61.53  E-value: 4.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 702 VMGKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEGsssdtapLFQMAGDGKdtddIKIPMLFLfSKE-GSIILDAIR 780
Cdd:cd02133   46 VKGKIALIQRGEITFVEKIANAKAAGAVGVIIYNNVDG-------LIPGTLGEA----VFIPVVFI-SKEdGEALKAALE 113


                 ....*..
gi 163310725 781 EYEEVEV 787
Cdd:cd02133  114 SSKKLTF 120
PA_1 cd04813
PA_1: Protease-associated (PA) domain subgroup 1. A subgroup of PA-domain containing proteins. ...
 686-779 1.32e-10

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: 59.32  E-value: 1.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 686 SSKPSNGCSELTNPEaVMGKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEGSssdtaPLFQMAGDGkDTDDIKIPML 765
Cdd:cd04813   23 KVSPTDACSLQEHAE-IDGKVALVLRGGCGFLDKVMWAQRRGAKAVIVGDDEPGR-----GLITMFSNG-DTDNVTIPAM 95

                         90
                 ....*....|....
gi 163310725 766 FLfSKEGSIILDAI 779
Cdd:cd04813   96 FT-SRTSYHLLSSL 108
PA_ScAPY_like cd02130
PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae ...
 689-744 1.29e-09

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: 56.88  E-value: 1.29e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 163310725 689 PSNGCSELTNPEAVMGKIALIQRGQCMFAEKARNIQNAGAIGGIVID-DNEGSSSDT 744
Cdd:cd02130   30 PNLGCDAADYPASVAGNIALIERGECPFGDKSALAGAAGAAAAIIYNnVPAGGLSGT 86
PA_GRAIL_like cd02122
PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain ...
 670-755 1.05e-07

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: 51.92  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 670 FGLDlSKHKETRGFVASSKPSN---GCSELTNPEAVMGK---IALIQRGQCMFAEKARNIQNAGAiGGIVIDDNEGSSSD 743
Cdd:cd02122   22 YGEH-SPKEEAKGLVVVPDPPNdhyGCDPDTRFPIPPNGepwIALIQRGNCTFEEKIKLAAERNA-SAVVIYNNPGTGNE 99

                         90
                 ....*....|..
gi 163310725 744 TaplFQMAGDGK 755
Cdd:cd02122  100 T---VKMSHPGT 108
PA_VSR cd02125
PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This ...
 703-789 1.20e-06

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: 48.63  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 703 MGKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEgsssdtAPLFQM-----AGDGKDTDDIKIPMLFLFSKEGSIILD 777
Cdd:cd02125   42 RPVILLLDRGGCFFTLKAWNAQQAGAAAVLVADNVD------EPLLTMdtpeeSGSADYIEKITIPSALITKAFGEKLKK 115

                         90
                 ....*....|..
gi 163310725 778 AIREYEEVEVLL 789
Cdd:cd02125  116 AISNGEMVVIKL 127
PA_hSPPL_like cd02129
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ...
 699-767 1.66e-05

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: 45.07  E-value: 1.66e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163310725 699 PEAVMGKIALIQRGQCMFAEKARNIQNAGAiGGIVIDDNEGsssdtapLFQMAGDGKDTDDIKIPMLFL 767
Cdd:cd02129   40 PGGLKGKAVVVMRGNCTFYEKARLAQSLGA-EGLLIVSRER-------LVPPSGNRSEYEKIDIPVALL 100
DMP1 pfam07263
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 783-902 2.66e-05

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 48.00  E-value: 2.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725  783 EEVEvllSDKAKDRDPE-------MENEEQPSSENDSQNQSGEQ-------ISSSSQEVDLVDQESSEEnslnSHPESLS 848
Cdd:pfam07263 288 EEVK---SDSTESTSSKeaglsqsREDSKSESQEDSEESQSQEDsqnsqdpSSESSQEADLPSQESSSE----SQEEVVS 360

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 163310725  849 LADMDNAASISPSEQTSNPTENHETTNLNgectDLDNQLQEQSETEEDSNPNVS 902
Cdd:pfam07263 361 ESRGDNPDNTSSSEEDQEDSDSSEEDSLS----TFSSSESESREEQADSESNES 410
PA_PoS1_like cd02124
PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA ...
 686-787 6.32e-05

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: 43.47  E-value: 6.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 686 SSKPSNGCSELtnPEAVM---GKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEGSssdtaplfqMAGDGKDTDDIKI 762
Cdd:cd02124   37 TSVADDACQPL--PDDTPdlsGYIVLVRRGTCTFATKAANAAAKGAKYVLIYNNGSGP---------TDQVGSDADSIIA 105

                         90       100
                 ....*....|....*....|....*
gi 163310725 763 PMLflfSKEGSIILDAIREYEEVEV 787
Cdd:cd02124  106 AVT---PEDGEAWIDALAAGSNVTV 127
PRK08581 PRK08581
amidase domain-containing protein;
804-920 1.58e-04

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 45.55  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 804 EQPSSENDSQNQSGEQISSSSQEVDlvDQESSEENSLNSHPESLSLADMDNAASISP-SEQTSNPTENHETTNLNGECTD 882
Cdd:PRK08581 137 EQPRNSEKSTNDSNKNSDSSIKNDT--DTQSSKQDKADNQKAPSSNNTKPSTSNKQPnSPKPTQPNQSNSQPASDDTANQ 214

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 163310725 883 LDNQlqEQSETEEDSnpnvswgkkvqPIDSILADWNED 920
Cdd:PRK08581 215 KSSS--KDNQSMSDS-----------ALDSILDQYSED 239
PA_subtilisin_like cd02120
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ...
 693-781 1.80e-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: 42.02  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 693 CSELT-NPEAVMGKIALIQRGQ-CMFAEKARNIQNAGAIGGIVIDDNEGsssdtaplfqmaGDGKDTDDIKIPMLFLFSK 770
Cdd:cd02120   40 CLPGSlDPSKVKGKIVLCDRGGnTSRVAKGDAVKAAGGAGMILANDPTD------------GLDVVADAHVLPAVHVDYE 107

                         90
                 ....*....|.
gi 163310725 771 EGSIILDAIRE 781
Cdd:cd02120  108 DGTAILSYINS 118
PA_SaNapH_like cd04816
PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ...
 702-787 3.22e-04

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: 41.54  E-value: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 702 VMGKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEGSSsdTAPLFqmagdGKDTDDIKIPMLFLFSKEGSIILDAIRE 781
Cdd:cd04816   42 VKGAIVLVDRGGCPFADKQKVAAARGAVAVIVVNNSDGGG--TAGTL-----GAPNIDLKVPVGVITKAAGAALRRRLGA 114


                 ....*.
gi 163310725 782 YEEVEV 787
Cdd:cd04816  115 GETLEL 120
LanM-like cd04792
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
 236-328 2.48e-03

Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.


Pssm-ID: 271200 [Multi-domain]  Cd Length: 836  Bit Score: 41.53  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163310725 236 FAALSRFTGATIFEEYARKALdflwekrqrssNLVGVTINIHTGDWVRKDSGVGAGIDSYYEYLLKAYVLLGDDSFLERF 315
Cdd:cd04792  503 LAALAALTGDEKYRDLARKAL-----------RPLRKLLRDLAADPRSLGIGGFTGLGSILYALSHLARLLGDPELLEDA 571

                         90
                 ....*....|...
gi 163310725 316 NTHYDAIMRYISQ 328
Cdd:cd04792  572 LELADLLTEAIIE 584
 
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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