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Conserved domains on  [gi|11545918|ref|NP_071447|]
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tubulointerstitial nephritis antigen-like isoform 1 precursor [Homo sapiens]

Protein Classification

C1 family peptidase( domain architecture ID 10243665)

C1 family peptidase such as cathepsin B, an endopeptidase that catalyzes the hydrolysis of proteins with broad specificity for peptide bonds; it preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
204-455 7.22e-102

Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial nephritis antigen (TIN-Ag). Cathepsin B is a lysosomal papain-like cysteine peptidase which is expressed in all tissues and functions primarily as an exopeptidase through its carboxydipeptidyl activity. Together with other cathepsins, it is involved in the degradation of proteins, proenzyme activation, Ag processing, metabolism and apoptosis. Cathepsin B has been implicated in a number of human diseases such as cancer, rheumatoid arthritis, osteoporosis and Alzheimer's disease. The unique carboxydipeptidyl activity of cathepsin B is attributed to the presence of an occluding loop in its active site which favors the binding of the C-termini of substrate proteins. Some members of this group do not possess the occluding loop. TIN-Ag is an extracellular matrix basement protein which was originally identified as a target Ag involved in anti-tubular basement membrane antibody-mediated interstitial nephritis. It plays a role in renal tubulogenesis and is defective in hereditary tubulointerstitial disorders. TIN-Ag is exclusively expressed in kidney tissues.


:

Pssm-ID: 239111 [Multi-domain]  Cd Length: 236  Bit Score: 304.19  E-value: 7.22e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 204 PTAFEASEKWPNLIH--EPLDQGNCAGSWAFSTAAVASDRVSIHSLGHMTPVLSPQNLLSCDTHQQQGCRGGRLDGAWWF 281
Cdd:cd02620   1 PESFDAREKWPNCISigEIRDQGNCGSCWAFSAVEAFSDRLCIQSNGKENVLLSAQDLLSCCSGCGDGCNGGYPDAAWKY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 282 LRRRGVVSDHCYPFsgrerdeagPAPPC--MMHSRAMGRGKRQATAHCPNSY--VNNNDIYQVTPVYRLGSNDKEIMKEL 357
Cdd:cd02620  81 LTTTGVVTGGCQPY---------TIPPCghHPEGPPPCCGTPYCTPKCQDGCekTYEEDKHKGKSAYSVPSDETDIMKEI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 358 MENGPVQALMEVHEDFFLYKGGIYSHTpvslgrpeRYRRHGTHSVKITGWGEEtlpdgRTLKYWTAANSWGPAWGERGHF 437
Cdd:cd02620 152 MTNGPVQAAFTVYEDFLYYKSGVYQHT--------SGKQLGGHAVKIIGWGVE-----NGVPYWLAANSWGTDWGENGYF 218
                       250
                ....*....|....*...
gi 11545918 438 RIVRGVNECDIESFVLGV 455
Cdd:cd02620 219 RILRGSNECGIESEVVAG 236
Somatomedin_B super family cl02508
Somatomedin B domain;
54-94 6.66e-03

Somatomedin B domain;


The actual alignment was detected with superfamily member smart00201:

Pssm-ID: 470596  Cd Length: 43  Bit Score: 34.66  E-value: 6.66e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 11545918     54 CCRGRADDcaLPYLGAICYCDLFCNRTvSDCCPDFWDFCLG 94
Cdd:smart00201   4 SCKGRCGE--SFNEGNACRCDALCLSY-GDCCTDYESVCKK 41
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
105-140 7.54e-03

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


The actual alignment was detected with superfamily member smart00214:

Pssm-ID: 450195  Cd Length: 59  Bit Score: 34.80  E-value: 7.54e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 11545918    105 CMHGGRIYPVLGTYWDN-CNRCTCQENRQWQCDQEPC 140
Cdd:smart00214   1 CVHNGRVYNDGETWKPDpCQICTCLDGTTVLCDPVEC 37
 
Name Accession Description Interval E-value
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
204-455 7.22e-102

Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial nephritis antigen (TIN-Ag). Cathepsin B is a lysosomal papain-like cysteine peptidase which is expressed in all tissues and functions primarily as an exopeptidase through its carboxydipeptidyl activity. Together with other cathepsins, it is involved in the degradation of proteins, proenzyme activation, Ag processing, metabolism and apoptosis. Cathepsin B has been implicated in a number of human diseases such as cancer, rheumatoid arthritis, osteoporosis and Alzheimer's disease. The unique carboxydipeptidyl activity of cathepsin B is attributed to the presence of an occluding loop in its active site which favors the binding of the C-termini of substrate proteins. Some members of this group do not possess the occluding loop. TIN-Ag is an extracellular matrix basement protein which was originally identified as a target Ag involved in anti-tubular basement membrane antibody-mediated interstitial nephritis. It plays a role in renal tubulogenesis and is defective in hereditary tubulointerstitial disorders. TIN-Ag is exclusively expressed in kidney tissues.


Pssm-ID: 239111 [Multi-domain]  Cd Length: 236  Bit Score: 304.19  E-value: 7.22e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 204 PTAFEASEKWPNLIH--EPLDQGNCAGSWAFSTAAVASDRVSIHSLGHMTPVLSPQNLLSCDTHQQQGCRGGRLDGAWWF 281
Cdd:cd02620   1 PESFDAREKWPNCISigEIRDQGNCGSCWAFSAVEAFSDRLCIQSNGKENVLLSAQDLLSCCSGCGDGCNGGYPDAAWKY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 282 LRRRGVVSDHCYPFsgrerdeagPAPPC--MMHSRAMGRGKRQATAHCPNSY--VNNNDIYQVTPVYRLGSNDKEIMKEL 357
Cdd:cd02620  81 LTTTGVVTGGCQPY---------TIPPCghHPEGPPPCCGTPYCTPKCQDGCekTYEEDKHKGKSAYSVPSDETDIMKEI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 358 MENGPVQALMEVHEDFFLYKGGIYSHTpvslgrpeRYRRHGTHSVKITGWGEEtlpdgRTLKYWTAANSWGPAWGERGHF 437
Cdd:cd02620 152 MTNGPVQAAFTVYEDFLYYKSGVYQHT--------SGKQLGGHAVKIIGWGVE-----NGVPYWLAANSWGTDWGENGYF 218
                       250
                ....*....|....*...
gi 11545918 438 RIVRGVNECDIESFVLGV 455
Cdd:cd02620 219 RILRGSNECGIESEVVAG 236
Peptidase_C1 pfam00112
Papain family cysteine protease;
203-455 4.01e-55

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 182.74  E-value: 4.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918   203 LPTAFEASEKwpNLIHEPLDQGNCAGSWAFSTAAVASDRVSIHSlgHMTPVLSPQNLLSCDTHQQqGCRGGRLDGAW-WF 281
Cdd:pfam00112   1 LPESFDWREK--GAVTPVKDQGQCGSCWAFSAVGALEGRYCIKT--GKLVSLSEQQLVDCDTFNN-GCNGGLPDNAFeYI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918   282 LRRRGVVSDHCYPFSGRERdeagpapPCmmhsramgrgkrqatahcpNSYVNNNDIYQVTPVYRLGSND-KEIMKELMEN 360
Cdd:pfam00112  76 KKNGGIVTESDYPYTAKDG-------TC-------------------KFKKSNSKVAKIKGYGDVPYNDeEALQAALAKN 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918   361 GPVQALMEV-HEDFFLYKGGIYSHTPVSlgrperyrRHGTHSVKITGWGEEtlpDGrtLKYWTAANSWGPAWGERGHFRI 439
Cdd:pfam00112 130 GPVSVAIDAyERDFQLYKSGVYKHTECG--------GELNHAVLLVGYGTE---NG--VPYWIVKNSWGTDWGENGYFRI 196
                         250
                  ....*....|....*..
gi 11545918   440 VRGVN-ECDIESFVLGV 455
Cdd:pfam00112 197 ARGVNnECGIASEASYP 213
Pept_C1 smart00645
Papain family cysteine protease;
203-456 5.68e-43

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 149.66  E-value: 5.68e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918    203 LPTAFEASEKWPNLIHEplDQGNCAGSWAFSTAAVASDRVSIHSLGHMTpvLSPQNLLSCDTHQQQGCRGGRLDGAWWFL 282
Cdd:smart00645   1 LPESFDWRKKGAVTPVK--DQGQCGSCWAFSATGALEGRYCIKTGKLVS--LSEQQLVDCSGGGNCGCNGGLPDNAFEYI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918    283 RRRGVV-SDHCYPFSGrerdeagpappcmmhsramgrgkrqatahcpnsyvnnndiyqvtpvyrlgsndkeimkelmeng 361
Cdd:smart00645  77 KKNGGLeTESCYPYTG---------------------------------------------------------------- 92
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918    362 pvqALMEVHEDFFLYKGGIYSHTPVSLGRPeryrrhgTHSVKITGWGEEtLPDGRtlKYWTAANSWGPAWGERGHFRIVR 441
Cdd:smart00645  93 ---SVAIDASDFQFYKSGIYDHPGCGSGTL-------DHAVLIVGYGTE-VENGK--DYWIVKNSWGTDWGENGYFRIAR 159
                          250
                   ....*....|....*.
gi 11545918    442 GV-NECDIESFVLGVW 456
Cdd:smart00645 160 GKnNECGIEASVASYP 175
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
203-439 3.00e-27

Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 113.31  E-value: 3.00e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 203 LPTAFEASEKWPnlihEPLDQGNCaGS-WAFSTAAVA-SDRVSIHSLGHMTPVLSPQNLLSCdTHQQQGCRGGRLDGAWW 280
Cdd:COG4870   4 LPSSVDLRGYVT----PVKDQGSL-GScWAFATAAALeSYLKKQAGAPGTSLDLSELFLYNQ-ARNGDGTEGTDDGGSSL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 281 -----FLRRRGVVSDHCYPFSGRERDEAGPAppcmmhsramgrgkrqatahcpnSYVNNNDIYQVTPVYRL----GSNDK 351
Cdd:COG4870  78 rdalkLLRWSGVVPESDWPYDDSDFTSQPSA-----------------------AAYADARNYKIQDYYRLpgggGATDL 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 352 EIMKE-LMENGPVQALMEVHEDFFLYKGGIYSHTPvslgrpeRYRRHGTHSVKITGWGeetlpDGRTLKYWTAANSWGPA 430
Cdd:COG4870 135 DAIKQaLAEGGPVVFGFYVYESFYNYTGGVYYPTP-------GDASLGGHAVAIVGYD-----DNYSDGAFIIKNSWGTG 202

                ....*....
gi 11545918 431 WGERGHFRI 439
Cdd:COG4870 203 WGDNGYFWI 211
PTZ00200 PTZ00200
cysteine proteinase; Provisional
222-451 1.12e-23

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 103.24  E-value: 1.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918  222 DQG-NCAGSWAFST-AAVAS-----DRVSIHslghmtpvLSPQNLLSCDThQQQGCRGGRLDGAWWFLRRRGVVSDHCYP 294
Cdd:PTZ00200 251 DQGlNCGSCWAFSSvGSVESlykiyRDKSVD--------LSEQELVNCDT-KSQGCSGGYPDTALEYVKNKGLSSSSDVP 321
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918  295 FSGRERdeagpapPCMMHSRamgrGKRqatahcpnsYVNNndiYQVTpvyrlgsNDKEIMKELMENGPVQALMEVHEDFF 374
Cdd:PTZ00200 322 YLAKDG-------KCVVSST----KKV---------YIDS---YLVA-------KGKDVLNKSLVISPTVVYIAVSRELL 371
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918  375 LYKGGIYS-HTPVSLgrperyrrhgTHSVKITGWG--EETlpdgrTLKYWTAANSWGPAWGERGHFRIVR---GVNECDI 448
Cdd:PTZ00200 372 KYKSGVYNgECGKSL----------NHAVLLVGEGydEKT-----KKRYWIIKNSWGTDWGENGYMRLERtneGTDKCGI 436

                 ...
gi 11545918  449 ESF 451
Cdd:PTZ00200 437 LTV 439
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
54-94 6.66e-03

Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.


Pssm-ID: 197571  Cd Length: 43  Bit Score: 34.66  E-value: 6.66e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 11545918     54 CCRGRADDcaLPYLGAICYCDLFCNRTvSDCCPDFWDFCLG 94
Cdd:smart00201   4 SCKGRCGE--SFNEGNACRCDALCLSY-GDCCTDYESVCKK 41
VWC smart00214
von Willebrand factor (vWF) type C domain;
105-140 7.54e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 34.80  E-value: 7.54e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 11545918    105 CMHGGRIYPVLGTYWDN-CNRCTCQENRQWQCDQEPC 140
Cdd:smart00214   1 CVHNGRVYNDGETWKPDpCQICTCLDGTTVLCDPVEC 37
 
Name Accession Description Interval E-value
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
204-455 7.22e-102

Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial nephritis antigen (TIN-Ag). Cathepsin B is a lysosomal papain-like cysteine peptidase which is expressed in all tissues and functions primarily as an exopeptidase through its carboxydipeptidyl activity. Together with other cathepsins, it is involved in the degradation of proteins, proenzyme activation, Ag processing, metabolism and apoptosis. Cathepsin B has been implicated in a number of human diseases such as cancer, rheumatoid arthritis, osteoporosis and Alzheimer's disease. The unique carboxydipeptidyl activity of cathepsin B is attributed to the presence of an occluding loop in its active site which favors the binding of the C-termini of substrate proteins. Some members of this group do not possess the occluding loop. TIN-Ag is an extracellular matrix basement protein which was originally identified as a target Ag involved in anti-tubular basement membrane antibody-mediated interstitial nephritis. It plays a role in renal tubulogenesis and is defective in hereditary tubulointerstitial disorders. TIN-Ag is exclusively expressed in kidney tissues.


Pssm-ID: 239111 [Multi-domain]  Cd Length: 236  Bit Score: 304.19  E-value: 7.22e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 204 PTAFEASEKWPNLIH--EPLDQGNCAGSWAFSTAAVASDRVSIHSLGHMTPVLSPQNLLSCDTHQQQGCRGGRLDGAWWF 281
Cdd:cd02620   1 PESFDAREKWPNCISigEIRDQGNCGSCWAFSAVEAFSDRLCIQSNGKENVLLSAQDLLSCCSGCGDGCNGGYPDAAWKY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 282 LRRRGVVSDHCYPFsgrerdeagPAPPC--MMHSRAMGRGKRQATAHCPNSY--VNNNDIYQVTPVYRLGSNDKEIMKEL 357
Cdd:cd02620  81 LTTTGVVTGGCQPY---------TIPPCghHPEGPPPCCGTPYCTPKCQDGCekTYEEDKHKGKSAYSVPSDETDIMKEI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 358 MENGPVQALMEVHEDFFLYKGGIYSHTpvslgrpeRYRRHGTHSVKITGWGEEtlpdgRTLKYWTAANSWGPAWGERGHF 437
Cdd:cd02620 152 MTNGPVQAAFTVYEDFLYYKSGVYQHT--------SGKQLGGHAVKIIGWGVE-----NGVPYWLAANSWGTDWGENGYF 218
                       250
                ....*....|....*...
gi 11545918 438 RIVRGVNECDIESFVLGV 455
Cdd:cd02620 219 RILRGSNECGIESEVVAG 236
Peptidase_C1 pfam00112
Papain family cysteine protease;
203-455 4.01e-55

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 182.74  E-value: 4.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918   203 LPTAFEASEKwpNLIHEPLDQGNCAGSWAFSTAAVASDRVSIHSlgHMTPVLSPQNLLSCDTHQQqGCRGGRLDGAW-WF 281
Cdd:pfam00112   1 LPESFDWREK--GAVTPVKDQGQCGSCWAFSAVGALEGRYCIKT--GKLVSLSEQQLVDCDTFNN-GCNGGLPDNAFeYI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918   282 LRRRGVVSDHCYPFSGRERdeagpapPCmmhsramgrgkrqatahcpNSYVNNNDIYQVTPVYRLGSND-KEIMKELMEN 360
Cdd:pfam00112  76 KKNGGIVTESDYPYTAKDG-------TC-------------------KFKKSNSKVAKIKGYGDVPYNDeEALQAALAKN 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918   361 GPVQALMEV-HEDFFLYKGGIYSHTPVSlgrperyrRHGTHSVKITGWGEEtlpDGrtLKYWTAANSWGPAWGERGHFRI 439
Cdd:pfam00112 130 GPVSVAIDAyERDFQLYKSGVYKHTECG--------GELNHAVLLVGYGTE---NG--VPYWIVKNSWGTDWGENGYFRI 196
                         250
                  ....*....|....*..
gi 11545918   440 VRGVN-ECDIESFVLGV 455
Cdd:pfam00112 197 ARGVNnECGIASEASYP 213
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
222-452 1.89e-45

Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) similar to papain, including the mammalian CPs (cathepsins B, C, F, H, L, K, O, S, V, X and W). Papain is an endopeptidase with specific substrate preferences, primarily for bulky hydrophobic or aromatic residues at the S2 subsite, a hydrophobic pocket in papain that accommodates the P2 sidechain of the substrate (the second residue away from the scissile bond). Most members of the papain subfamily are endopeptidases. Some exceptions to this rule can be explained by specific details of the catalytic domains like the occluding loop in cathepsin B which confers an additional carboxydipeptidyl activity and the mini-chain of cathepsin H resulting in an N-terminal exopeptidase activity. Papain-like CPs have different functions in various organisms. Plant CPs are used to mobilize storage proteins in seeds. Parasitic CPs act extracellularly to help invade tissues and cells, to hatch or to evade the host immune system. Mammalian CPs are primarily lysosomal enzymes with the exception of cathepsin W, which is retained in the endoplasmic reticulum. They are responsible for protein degradation in the lysosome. Papain-like CPs are synthesized as inactive proenzymes with N-terminal propeptide regions, which are removed upon activation. In addition to its inhibitory role, the propeptide is required for proper folding of the newly synthesized enzyme and its stabilization in denaturing pH conditions. Residues within the propeptide region also play a role in the transport of the proenzyme to lysosomes or acidified vesicles. Also included in this subfamily are proteins classified as non-peptidase homologs, which lack peptidase activity or have missing active site residues.


Pssm-ID: 239068 [Multi-domain]  Cd Length: 210  Bit Score: 157.40  E-value: 1.89e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 222 DQGNCAGSWAFSTAAVASDRVSIHslGHMTPVLSPQNLLSCDTHQQQGCRGGRLDGAWWFLRRRGVVSDHCYPFSGRERD 301
Cdd:cd02248  17 DQGSCGSCWAFSTVGALEGAYAIK--TGKLVSLSEQQLVDCSTSGNNGCNGGNPDNAFEYVKNGGLASESDYPYTGKDGT 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 302 eagpappCMmhsramgRGKRQATAHCpnsyvnnNDIYQVTPvyrlgSNDKEIMKELMENGPVQALMEVHEDFFLYKGGIY 381
Cdd:cd02248  95 -------CK-------YNSSKVGAKI-------TGYSNVPP-----GDEEALKAALANYGPVSVAIDASSSFQFYKGGIY 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11545918 382 SHtpvslgrPERYRRHGTHSVKITGWGEEtlpDGRtlKYWTAANSWGPAWGERGHFRIVRGVNECDIESFV 452
Cdd:cd02248 149 SG-------PCCSNTNLNHAVLLVGYGTE---NGV--DYWIVKNSWGTSWGEKGYIRIARGSNLCGIASYA 207
Pept_C1 smart00645
Papain family cysteine protease;
203-456 5.68e-43

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 149.66  E-value: 5.68e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918    203 LPTAFEASEKWPNLIHEplDQGNCAGSWAFSTAAVASDRVSIHSLGHMTpvLSPQNLLSCDTHQQQGCRGGRLDGAWWFL 282
Cdd:smart00645   1 LPESFDWRKKGAVTPVK--DQGQCGSCWAFSATGALEGRYCIKTGKLVS--LSEQQLVDCSGGGNCGCNGGLPDNAFEYI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918    283 RRRGVV-SDHCYPFSGrerdeagpappcmmhsramgrgkrqatahcpnsyvnnndiyqvtpvyrlgsndkeimkelmeng 361
Cdd:smart00645  77 KKNGGLeTESCYPYTG---------------------------------------------------------------- 92
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918    362 pvqALMEVHEDFFLYKGGIYSHTPVSLGRPeryrrhgTHSVKITGWGEEtLPDGRtlKYWTAANSWGPAWGERGHFRIVR 441
Cdd:smart00645  93 ---SVAIDASDFQFYKSGIYDHPGCGSGTL-------DHAVLIVGYGTE-VENGK--DYWIVKNSWGTDWGENGYFRIAR 159
                          250
                   ....*....|....*.
gi 11545918    442 GV-NECDIESFVLGVW 456
Cdd:smart00645 160 GKnNECGIEASVASYP 175
Peptidase_C1A_CathepsinC cd02621
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ...
203-454 3.63e-36

Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine peptidase with chloride dependency and dipeptidyl aminopeptidase activity, resulting from its tetrameric structure which limits substrate access. Each subunit of the tetramer is composed of three peptides: the heavy and light chains, which together adopts the papain fold and forms the catalytic domain; and the residual propeptide region, which forms a beta barrel and points towards the substrate's N-terminus. The subunit composition is the result of the unique characteristic of procathepsin C maturation involving the cleavage of the catalytic domain and the non-autocatalytic excision of an activation peptide within its propeptide region. By removing N-terminal dipeptide extensions, cathepsin C activates granule serine peptidases (granzymes) involved in cell-mediated apoptosis, inflammation and tissue remodelling. Loss-of-function mutations in cathepsin C are associated with Papillon-Lefevre and Haim-Munk syndromes, rare diseases characterized by hyperkeratosis and early-onset periodontitis. Cathepsin C is widely expressed in many tissues with high levels in lung, kidney and placenta. It is also highly expressed in cytotoxic lymphocytes and mature myeloid cells.


Pssm-ID: 239112 [Multi-domain]  Cd Length: 243  Bit Score: 133.67  E-value: 3.63e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 203 LPTAFEASEKWP--NLIHEPLDQGNCAGSWAFSTAAVASDRVSIHS----LGHMTPVLSPQNLLSCDTHQQqGCRGGRLD 276
Cdd:cd02621   1 LPKSFDWGDVNNgfNYVSPVRNQGGCGSCYAFASVYALEARIMIASnktdPLGQQPILSPQHVLSCSQYSQ-GCDGGFPF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 277 GAWWFLRRRGVVSDHCYPFSGrERDEAGPAPPcmmhsramgrgkrqatahcpnsyvNNNDIYQVTPVYRLGS-----NDK 351
Cdd:cd02621  80 LVGKFAEDFGIVTEDYFPYTA-DDDRPCKASP------------------------SECRRYYFSDYNYVGGcygctNED 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 352 EIMKELMENGPVQALMEVHEDFFLYKGGIYSHTP----VSLGRPER-YRRHGTHSVKITGWGEETLpdgRTLKYWTAANS 426
Cdd:cd02621 135 EMKWEIYRNGPIVVAFEVYSDFDFYKEGVYHHTDndevSDGDNDNFnPFELTNHAVLLVGWGEDEI---KGEKYWIVKNS 211
                       250       260
                ....*....|....*....|....*...
gi 11545918 427 WGPAWGERGHFRIVRGVNECDIESFVLG 454
Cdd:cd02621 212 WGSSWGEKGYFKIRRGTNECGIESQAVF 239
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
203-439 3.00e-27

Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 113.31  E-value: 3.00e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 203 LPTAFEASEKWPnlihEPLDQGNCaGS-WAFSTAAVA-SDRVSIHSLGHMTPVLSPQNLLSCdTHQQQGCRGGRLDGAWW 280
Cdd:COG4870   4 LPSSVDLRGYVT----PVKDQGSL-GScWAFATAAALeSYLKKQAGAPGTSLDLSELFLYNQ-ARNGDGTEGTDDGGSSL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 281 -----FLRRRGVVSDHCYPFSGRERDEAGPAppcmmhsramgrgkrqatahcpnSYVNNNDIYQVTPVYRL----GSNDK 351
Cdd:COG4870  78 rdalkLLRWSGVVPESDWPYDDSDFTSQPSA-----------------------AAYADARNYKIQDYYRLpgggGATDL 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 352 EIMKE-LMENGPVQALMEVHEDFFLYKGGIYSHTPvslgrpeRYRRHGTHSVKITGWGeetlpDGRTLKYWTAANSWGPA 430
Cdd:COG4870 135 DAIKQaLAEGGPVVFGFYVYESFYNYTGGVYYPTP-------GDASLGGHAVAIVGYD-----DNYSDGAFIIKNSWGTG 202

                ....*....
gi 11545918 431 WGERGHFRI 439
Cdd:COG4870 203 WGDNGYFWI 211
Peptidase_C1A_CathepsinX cd02698
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ...
226-443 1.62e-25

Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase activity. It can also act as a carboxydipeptidase, like cathepsin B, but has been shown to preferentially cleave substrates through a monopeptidyl carboxypeptidase pathway. The propeptide region of cathepsin X, the shortest among papain-like peptidases, is covalently attached to the active site cysteine in the inactive form of the enzyme. Little is known about the biological function of cathepsin X. Some studies point to a role in early tumorigenesis. A more recent study indicates that cathepsin X expression is restricted to immune cells suggesting a role in phagocytosis and the regulation of the immune response.


Pssm-ID: 239149  Cd Length: 239  Bit Score: 104.42  E-value: 1.62e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 226 CAGSWAFSTAAVASDRVSIHSLGHMTPV-LSPQNLLSCDthQQQGCRGGRLDGAWWFLRRRGVVSDHCYPFSGRErDEAG 304
Cdd:cd02698  28 CGSCWAHGSTSALADRINIARKGAWPSVyLSVQVVIDCA--GGGSCHGGDPGGVYEYAHKHGIPDETCNPYQAKD-GECN 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 305 PAPPCmmhSRAMGRGKRQATAHCPNSYVNNndiyqvtpvYRLGSNDKEIMKELMENGPVQALMEVHEDFFLYKGGIYsHT 384
Cdd:cd02698 105 PFNRC---GTCNPFGECFAIKNYTLYFVSD---------YGSVSGRDKMMAEIYARGPISCGIMATEALENYTGGVY-KE 171
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 11545918 385 PVSLGRPeryrrhgTHSVKITGWGEetlpDGRTLKYWTAANSWGPAWGERGHFRIVRGV 443
Cdd:cd02698 172 YVQDPLI-------NHIISVAGWGV----DENGVEYWIVRNSWGEPWGERGWFRIVTSS 219
PTZ00200 PTZ00200
cysteine proteinase; Provisional
222-451 1.12e-23

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 103.24  E-value: 1.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918  222 DQG-NCAGSWAFST-AAVAS-----DRVSIHslghmtpvLSPQNLLSCDThQQQGCRGGRLDGAWWFLRRRGVVSDHCYP 294
Cdd:PTZ00200 251 DQGlNCGSCWAFSSvGSVESlykiyRDKSVD--------LSEQELVNCDT-KSQGCSGGYPDTALEYVKNKGLSSSSDVP 321
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918  295 FSGRERdeagpapPCMMHSRamgrGKRqatahcpnsYVNNndiYQVTpvyrlgsNDKEIMKELMENGPVQALMEVHEDFF 374
Cdd:PTZ00200 322 YLAKDG-------KCVVSST----KKV---------YIDS---YLVA-------KGKDVLNKSLVISPTVVYIAVSRELL 371
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918  375 LYKGGIYS-HTPVSLgrperyrrhgTHSVKITGWG--EETlpdgrTLKYWTAANSWGPAWGERGHFRIVR---GVNECDI 448
Cdd:PTZ00200 372 KYKSGVYNgECGKSL----------NHAVLLVGEGydEKT-----KKRYWIIKNSWGTDWGENGYMRLERtneGTDKCGI 436

                 ...
gi 11545918  449 ESF 451
Cdd:PTZ00200 437 LTV 439
Peptidase_C1 cd02619
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
219-439 1.88e-23

C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; composed of two subfamilies of cysteine peptidases (CPs), C1A (papain) and C1B (bleomycin hydrolase). Papain-like enzymes are mostly endopeptidases with some exceptions like cathepsins B, C, H and X, which are exopeptidases. Papain-like CPs have different functions in various organisms. Plant CPs are used to mobilize storage proteins in seeds while mammalian CPs are primarily lysosomal enzymes responsible for protein degradation in the lysosome. Papain-like CPs are synthesized as inactive proenzymes with N-terminal propeptide regions, which are removed upon activation. Bleomycin hydrolase (BH) is a CP that detoxifies bleomycin by hydrolysis of an amide group. It acts as a carboxypeptidase on its C-terminus to convert itself into an aminopeptidase and peptide ligase. BH is found in all tissues in mammals as well as in many other eukaryotes. It forms a hexameric ring barrel structure with the active sites imbedded in the central channel. Some members of the C1 family are proteins classified as non-peptidase homologs which lack peptidase activity or have missing active site residues.


Pssm-ID: 239110 [Multi-domain]  Cd Length: 223  Bit Score: 98.36  E-value: 1.88e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 219 EPLDQGNCAGSWAFSTAAVASDRVSIHSLGHMTPVLSPQNLLSCDTHQQQGCRGGRLDGAWW-----FLRRRGVVSDHCY 293
Cdd:cd02619  11 PVKNQGSRGSCWAFASAYALESAYRIKGGEDEYVDLSPQYLYICANDECLGINGSCDGGGPLsallkLVALKGIPPEEDY 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918 294 PFSgrERDEAGPAPPCMMHSramgrgkrqatahcpNSYVNNNDIYQVtpvyrLGSNDKEIMKELMENGPVQALMEVHEDF 373
Cdd:cd02619  91 PYG--AESDGEEPKSEAALN---------------AAKVKLKDYRRV-----LKNNIEDIKEALAKGGPVVAGFDVYSGF 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11545918 374 FLYKGGIYSHTPVSLGRPERYRrhGTHSVKITGWGEETLPDGrtlKYWTAANSWGPAWGERGHFRI 439
Cdd:cd02619 149 DRLKEGIIYEEIVYLLYEDGDL--GGHAVVIVGYDDNYVEGK---GAFIVKNSWGTDWGDNGYGRI 209
PTZ00049 PTZ00049
cathepsin C-like protein; Provisional
203-450 1.29e-22

cathepsin C-like protein; Provisional


Pssm-ID: 240244 [Multi-domain]  Cd Length: 693  Bit Score: 101.18  E-value: 1.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918  203 LPTAFEASEKWPNLIHEP--LDQGNCAGSWAFSTAAVASDRVSI--------HSLGHMTPVLSPQNLLSCDTHQQqGCRG 272
Cdd:PTZ00049 381 LPKNFTWGDPFNNNTREYdvTNQLLCGSCYIASQMYAFKRRIEIaltknldkKYLNNFDDLLSIQTVLSCSFYDQ-GCNG 459
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918  273 GRLDGAWWFLRRRGVVSDHCYPFSGRER------DEAGPAPPCMMHSR---AMGRGKR-----QATAHCPNSYVNN---- 334
Cdd:PTZ00049 460 GFPYLVSKMAKLQGIPLDKVFPYTATEQtcpyqvDQSANSMNGSANLRqinAVFFSSEtqsdmHADFEAPISSEPArwya 539
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918  335 NDIYQVTPVYRLG--SNDKEIMKELMENGPVQALMEVHEDFFLYKGGIY-----SHTPV-SLGRPER---YRRHG----T 399
Cdd:PTZ00049 540 KDYNYIGGCYGCNqcNGEKIMMNEIYRNGPIVASFEASPDFYDYADGVYyvedfPHARRcTVDLPKHngvYNITGwekvN 619
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 11545918  400 HSVKITGWGEETLpDGRTLKYWTAANSWGPAWGERGHFRIVRGVNECDIES 450
Cdd:PTZ00049 620 HAIVLVGWGEEEI-NGKLYKYWIGRNSWGKNWGKEGYFKIIRGKNFSGIES 669
PTZ00203 PTZ00203
cathepsin L protease; Provisional
222-451 1.71e-20

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 92.46  E-value: 1.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918  222 DQGNCAGSWAFStaAVASDRVSIHSLGHMTPVLSPQNLLSCDtHQQQGCRGGRLDGAW-WFLRRRG--VVSDHCYPF-SG 297
Cdd:PTZ00203 143 NQGACGSCWAFS--AVGNIESQWAVAGHKLVRLSEQQLVSCD-HVDNGCGGGLMLQAFeWVLRNMNgtVFTEKSYPYvSG 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918  298 RerdeaGPAPPCMMHSRAMgrgkrqatahcPNSYVnnnDIYQVTPvyrlgSNDKEIMKELMENGPVQALMEVhEDFFLYK 377
Cdd:PTZ00203 220 N-----GDVPECSNSSELA-----------PGARI---DGYVSME-----SSERVMAAWLAKNGPISIAVDA-SSFMSYH 274
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11545918  378 GGIYSHTPvslgrpERYRRHGTHSVKITGWGEetlpdgrtLKYWTAANSWGPAWGERGHFRIVRGVNECDIESF 451
Cdd:PTZ00203 275 SGVLTSCI------GEQLNHGVLLVGYNMTGE--------VPYWVIKNSWGEDWGEKGYVRVTMGVNACLLTGY 334
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
197-460 1.17e-16

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381 [Multi-domain]  Cd Length: 548  Bit Score: 82.25  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918  197 LNPGEVLPTAFEasekWPNL-----IHEPLDQG---NCAGSWAFSTAAVASDRVSIHS-----LGHMTpVLSPQNLLSCD 263
Cdd:PTZ00364 199 HQLGDPPPAAWS----WGDVggasfLPAAPPASpgrGCNSSYVEAALAAMMARVMVASnrtdpLGQQT-FLSARHVLDCS 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918  264 THQQqGCRGGRLDGAWWFLRRRGVVSDHCYPFSGRERDeagpappCMMHSRAMGRGKRQatahcpnsyvnnndiYQVTPV 343
Cdd:PTZ00364 274 QYGQ-GCAGGFPEEVGKFAETFGILTTDSYYIPYDSGD-------GVERACKTRRPSRR---------------YYFTNY 330
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918  344 YRLGS------NDKEIMKELMENGPVQALMEVHEDFFLYKGGIY---------SHTPVSLGRPER--YRRHGTHSVKITG 406
Cdd:PTZ00364 331 GPLGGyygavtDPDEIIWEIYRHGPVPASVYANSDWYNCDENSTedvryvsldDYSTASADRPLRhyFASNVNHTVLIIG 410
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 11545918  407 WGEetlpDGRTLKYWTAANSWG--PAWGERGHFRIVRGVNECDIESFVLGV-WGRVG 460
Cdd:PTZ00364 411 WGT----DENGGDYWLVLDPWGsrRSWCDGGTRKIARGVNAYNIESEVVVMyWAPYP 463
PTZ00021 PTZ00021
falcipain-2; Provisional
222-439 1.92e-14

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 75.19  E-value: 1.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918  222 DQGNCAGSWAFSTAAVASDRVSIHSLGHMTpvLSPQNLLSCDThQQQGCRGGRLDGAWW-FLRRRGVVSDHCYPFsgrer 300
Cdd:PTZ00021 283 DQKNCGSCWAFSTVGVVESQYAIRKNELVS--LSEQELVDCSF-KNNGCYGGLIPNAFEdMIELGGLCSEDDYPY----- 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11545918  301 deAGPAPPCMMHSRamgrgkrqatahCPNSYVNNNdiYQVTPVYRLgsndKEIMKELmenGPVQALMEVHEDFFLYKGGI 380
Cdd:PTZ00021 355 --VSDTPELCNIDR------------CKEKYKIKS--YVSIPEDKF----KEAIRFL---GPISVSIAVSDDFAFYKGGI 411
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11545918  381 YSHtpvSLGRPEryrrhgTHSVKITGWGEETL--PDGRTLK---YWTAANSWGPAWGERGHFRI 439
Cdd:PTZ00021 412 FDG---ECGEEP------NHAVILVGYGMEEIynSDTKKMEkryYYIIKNSWGESWGEKGFIRI 466
PTZ00462 PTZ00462
Serine-repeat antigen protein; Provisional
400-439 5.06e-06

Serine-repeat antigen protein; Provisional


Pssm-ID: 185641 [Multi-domain]  Cd Length: 1004  Bit Score: 49.29  E-value: 5.06e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 11545918   400 HSVKITGWGEETLPDGRTLKYWTAANSWGPAWGERGHFRI 439
Cdd:PTZ00462  723 HAVNIVGYGNYINDEDEKKSYWIVRNSWGKYWGDEGYFKV 762
SO smart00201
Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from ...
54-94 6.66e-03

Somatomedin B -like domains; Somatomedin-B is a peptide, proteolytically excised from vitronectin, that is a growth hormone-dependent serum factor with protease-inhibiting activity.


Pssm-ID: 197571  Cd Length: 43  Bit Score: 34.66  E-value: 6.66e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 11545918     54 CCRGRADDcaLPYLGAICYCDLFCNRTvSDCCPDFWDFCLG 94
Cdd:smart00201   4 SCKGRCGE--SFNEGNACRCDALCLSY-GDCCTDYESVCKK 41
VWC smart00214
von Willebrand factor (vWF) type C domain;
105-140 7.54e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 34.80  E-value: 7.54e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 11545918    105 CMHGGRIYPVLGTYWDN-CNRCTCQENRQWQCDQEPC 140
Cdd:smart00214   1 CVHNGRVYNDGETWKPDpCQICTCLDGTTVLCDPVEC 37
 
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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