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Conserved domains on  [gi|442631480|ref|NP_001261668|]
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TBP-associated factor 2, isoform B [Drosophila melanogaster]

Protein Classification

transcription initiation factor TFIID subunit 2( domain architecture ID 10177047)

transcription initiation factor TFIID subunit 2 is a component of transcription factor TFIID, which is one of the general factors required for accurate and regulated initiation by RNA polymerase II

Gene Ontology:  GO:0005669|GO:0006357

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
M1_like_TAF2 cd09839
TATA binding protein (TBP) associated factor 2; This family includes TATA binding protein (TBP) ...
17-526 0e+00

TATA binding protein (TBP) associated factor 2; This family includes TATA binding protein (TBP) associated factor 2 (TAF2, TBP-associated factor TAFII150, transcription initiation factor TFIID subunit 2, RNA polymerase II TBP-associated factor subunit B), and has homology to the M1 gluzincin family. TAF2 is part of the TFIID multidomain subunit complex essential for transcription of most protein-encoded genes by RNA polymerase II. TAF2 is known to interact with the initiator element (Inr) found at the transcription start site of many genes, thus possibly playing a key role in promoter binding as well as start-site selection. Image analysis has shown TAF2 to form a complex with TAF1 and TBP, inferring its role in promoter recognition. Peptidases in the M1 family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile on activation during catalysis. TAF2, however, lacks these active site residues.


:

Pssm-ID: 341074 [Multi-domain]  Cd Length: 531  Bit Score: 564.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   17 LAHQVVSLTgISFERRSIIGVVELTIVPNSENLRLIRLNAKQLRIYSVVLNDVcQADFTYFDPFQNICYKEHKSRALEVY 96
Cdd:cd09839     1 VAHQKVELD-VDFANRSIIGYTEITIVPTSPDLRTIRLNCRQCKIKSVTVNGV-EAEFTYNDPLQNLDLSDNTDVNAHHE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   97 SKHHLTAAQYtDPDVNNGELLIQVPPEGYSMIQEGQG-------------------LRIRIEFSLENPKCGVHFVIPPAS 157
Cdd:cd09839    79 LKRKLAAALA-EPDEGNEELVISLPPSVKIELQDPNSastqattsspdtsedeftpLTIRIEYSLKNPRDGLHFVGPDEG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  158 TDEetqmNSSHMFT--NCYENSSRLWFPCVDSFADPCTWRLEFTVDK-----------------------------NMTA 206
Cdd:cd09839   158 GDK----RYPHVYTtnSPLPGSARCWFPCVDSLWERCTWELEITVPRtlgdagrpplagskededdddlteedkelEMVV 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  207 VSCGELLEVIMTP-DLRKKTFHYSVSTPVCAPNIALAVGQFEIYVDP-------------HMHEVTHFCLPGLLPLLKNT 272
Cdd:cd09839   234 VCSGDLVEQVVHPeDPSKKTFSFSLSNPTSAQHIGFAVGPFEIVPLPefreseeddklgsSAVEVTGFCLPGRLEELRNT 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  273 VRYLHEAFEFYEETlSTRYPFSCYKQVFVDELDTDISAYATMSIASVNLLHSIAIIDQTYISRTFMSRAVAEQFFGCFIT 352
Cdd:cd09839   314 CSFLHKAMDFFEEE-YGSYPFSSYKQVFVDDLPEDVSSFASLSICSSRLLYPPDIIDQAYETRRKLAHALASQWFGINII 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  353 SHHWSDTWLAKGIAEYLCGLYSRKCFGNNEYRAWVQSELARVVRYEeqyggiildcsqppaplpvsgtnqsaasskqqei 432
Cdd:cd09839   393 PKTWSDTWLVIGIAGYMTGLFLKKLFGNNEYRFRIKKDADRVCELD---------------------------------- 438
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  433 VHYFPIKSLHT---VSPKYVEAMRRKAHFVIRMLENRIGQELLIQVFNKQLALASSAATTkigaGLWSQLLISTNIFIKA 509
Cdd:cd09839   439 IGRPPLAQPGFilpLDPSELEFMALKAPLVLFILDRRLTKTGGSFGLSRVLPKIFLQAMS----GDLSNNALSTSHFLRT 514
                         570
                  ....*....|....*..
gi 442631480  510 IFTVTGKDMSVFMDQWV 526
Cdd:cd09839   515 CEKVSGNKLESFFDQWV 531
 
Name Accession Description Interval E-value
M1_like_TAF2 cd09839
TATA binding protein (TBP) associated factor 2; This family includes TATA binding protein (TBP) ...
17-526 0e+00

TATA binding protein (TBP) associated factor 2; This family includes TATA binding protein (TBP) associated factor 2 (TAF2, TBP-associated factor TAFII150, transcription initiation factor TFIID subunit 2, RNA polymerase II TBP-associated factor subunit B), and has homology to the M1 gluzincin family. TAF2 is part of the TFIID multidomain subunit complex essential for transcription of most protein-encoded genes by RNA polymerase II. TAF2 is known to interact with the initiator element (Inr) found at the transcription start site of many genes, thus possibly playing a key role in promoter binding as well as start-site selection. Image analysis has shown TAF2 to form a complex with TAF1 and TBP, inferring its role in promoter recognition. Peptidases in the M1 family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile on activation during catalysis. TAF2, however, lacks these active site residues.


Pssm-ID: 341074 [Multi-domain]  Cd Length: 531  Bit Score: 564.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   17 LAHQVVSLTgISFERRSIIGVVELTIVPNSENLRLIRLNAKQLRIYSVVLNDVcQADFTYFDPFQNICYKEHKSRALEVY 96
Cdd:cd09839     1 VAHQKVELD-VDFANRSIIGYTEITIVPTSPDLRTIRLNCRQCKIKSVTVNGV-EAEFTYNDPLQNLDLSDNTDVNAHHE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   97 SKHHLTAAQYtDPDVNNGELLIQVPPEGYSMIQEGQG-------------------LRIRIEFSLENPKCGVHFVIPPAS 157
Cdd:cd09839    79 LKRKLAAALA-EPDEGNEELVISLPPSVKIELQDPNSastqattsspdtsedeftpLTIRIEYSLKNPRDGLHFVGPDEG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  158 TDEetqmNSSHMFT--NCYENSSRLWFPCVDSFADPCTWRLEFTVDK-----------------------------NMTA 206
Cdd:cd09839   158 GDK----RYPHVYTtnSPLPGSARCWFPCVDSLWERCTWELEITVPRtlgdagrpplagskededdddlteedkelEMVV 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  207 VSCGELLEVIMTP-DLRKKTFHYSVSTPVCAPNIALAVGQFEIYVDP-------------HMHEVTHFCLPGLLPLLKNT 272
Cdd:cd09839   234 VCSGDLVEQVVHPeDPSKKTFSFSLSNPTSAQHIGFAVGPFEIVPLPefreseeddklgsSAVEVTGFCLPGRLEELRNT 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  273 VRYLHEAFEFYEETlSTRYPFSCYKQVFVDELDTDISAYATMSIASVNLLHSIAIIDQTYISRTFMSRAVAEQFFGCFIT 352
Cdd:cd09839   314 CSFLHKAMDFFEEE-YGSYPFSSYKQVFVDDLPEDVSSFASLSICSSRLLYPPDIIDQAYETRRKLAHALASQWFGINII 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  353 SHHWSDTWLAKGIAEYLCGLYSRKCFGNNEYRAWVQSELARVVRYEeqyggiildcsqppaplpvsgtnqsaasskqqei 432
Cdd:cd09839   393 PKTWSDTWLVIGIAGYMTGLFLKKLFGNNEYRFRIKKDADRVCELD---------------------------------- 438
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  433 VHYFPIKSLHT---VSPKYVEAMRRKAHFVIRMLENRIGQELLIQVFNKQLALASSAATTkigaGLWSQLLISTNIFIKA 509
Cdd:cd09839   439 IGRPPLAQPGFilpLDPSELEFMALKAPLVLFILDRRLTKTGGSFGLSRVLPKIFLQAMS----GDLSNNALSTSHFLRT 514
                         570
                  ....*....|....*..
gi 442631480  510 IFTVTGKDMSVFMDQWV 526
Cdd:cd09839   515 CEKVSGNKLESFFDQWV 531
PepN COG0308
Aminopeptidase N, contains DUF3458 domain [Amino acid transport and metabolism];
13-713 2.41e-43

Aminopeptidase N, contains DUF3458 domain [Amino acid transport and metabolism];


Pssm-ID: 440077 [Multi-domain]  Cd Length: 609  Bit Score: 167.90  E-value: 2.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   13 RPFKLAHQVVSLTgISFERRSIIGVVELTIVPNSENLRLIRLNAKQLRIYSVVLNDVcQADFTYfdpfqnicykehksra 92
Cdd:COG0308    13 PGYDVTHYDLDLD-LDPATTRLSGTATITFTATEAPLDSLVLDLKGLEVTSVTVDGK-PLDFTR---------------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   93 levyskhhltaaqytdpdvNNGELLIQVPPEgysmIQEGQGLRIRIEFS--LENPKCGVHFVIPPASTDeetqmnsSHMF 170
Cdd:COG0308    75 -------------------DGERLTITLPKP----LAPGETFTLEIEYSgkPSNGGEGLYRSGDPPDGP-------PYLY 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  171 TNCYENSSRLWFPCVDSFADPCTWRLEFTVDKNMTAVSCGELLEVIMTPDLRkKTFHYSVSTPVcaPN--IALAVGQFEI 248
Cdd:COG0308   125 TQCEPEGARRWFPCFDHPDDKATFTLTVTVPAGWVAVSNGNLVSETELGDGR-TTWHWADTQPI--PTylFALAAGDYAV 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  249 YVDPHMH--EVTHFCLPGLLPLLKNTVRYLHEAFEFYEETLSTRYPFSCYKQVFVDeldtDISAYAtMSIASVNLLHSIA 326
Cdd:COG0308   202 VEDTFASgvPLRVYVRPGLADKAKEAFESTKRMLDFFEELFGVPYPFDKYDQVAVP----DFNFGA-MENQGLVTFGEKV 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  327 IIDQTYISRTFMSRA------VAEQFFGCFITSHHWSDTWLAKGIAEYLCGLYSRKCFGNNEYRAWVQSELARvvryeeq 400
Cdd:COG0308   277 LADETATDADYERREsviaheLAHQWFGNLVTCADWDDLWLNEGFATYMEQLFSEDLYGKDAADRIFVGALRS------- 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  401 yggIILDCSQPPAPLPVSGTNQSAASSKQQEIVhyfpikslhtvspkYVeamrrKAHFVIRMLENRIGQElliqVFNKQL 480
Cdd:COG0308   350 ---YAFAEDAGPNAHPIRPDDYPEIENFFDGIV--------------YE-----KGALVLHMLRTLLGDE----AFRAGL 403
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  481 AL-----ASSAATTKigaglwsQllistniFIKAIFTVTGKDMSVFMDQWVRTGGHAKFSLTSVFNRKRNTiELEIRQD- 554
Cdd:COG0308   404 RLyfarhAGGNATTE-------D-------FLAALEEASGRDLSAFFDQWLYQAGLPTLEVEYEYDADGKV-TLTLRQTp 468
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  555 YVNQRgirkYNGPLMVQLqeLDGTFKHTlqiestlvksditchsksrrnkkkkIPLCTGEEVDMDLSAmddSPVLWIRLD 634
Cdd:COG0308   469 PRPHP----FHIPLEVGL--LGGKLTAR-------------------------TVLLDGEQTELVAKP---DPVLLLRLD 514
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442631480  635 PEMILLrdliieqpdfqwqyqLRHERDVTAQFQAIQALQKYPTNATRLALTDTIESercFYQVRCEAAHSLTKVANQMV 713
Cdd:COG0308   515 DELAFL---------------LAHDSDPFNRWEALQALWRDGEADYLDALRALADT---DPAVRAEALALLGSDQLALA 575
Peptidase_M1 pfam01433
Peptidase family M1 domain; Members of this family are aminopeptidases. The members differ ...
278-525 6.77e-07

Peptidase family M1 domain; Members of this family are aminopeptidases. The members differ widely in specificity, hydrolysing acidic, basic or neutral N-terminal residues. This family includes leukotriene-A4 hydrolase, this enzyme also has an aminopeptidase activity.


Pssm-ID: 426262 [Multi-domain]  Cd Length: 219  Bit Score: 51.52  E-value: 6.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   278 EAFEFYEETLSTRYPFSCYKQVFVDELdtdisAYATMSIASVNLLHSIAIIDQTYISRTFMSRAVAE--------QFFGC 349
Cdd:pfam01433    8 KLLEFYEDYFNIPYPLPKYDLVALPDF-----SAGAMENWGLITYRETLLLYDPGNSSTSDKQRVASviahelahQWFGN 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   350 FITSHHWSDTWLAKGIAEYLCGLYSRKCFGNNEYRAWVQseLARVVRYEEqyggiiLDCSQPPAPLpvsgtnqsaasskQ 429
Cdd:pfam01433   83 LVTMKWWDDLWLNEGFATYMEYLGTDALFPEWNIWEQFL--LDEVQNAMA------RDALDSSHPI-------------T 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   430 QEIVHYFPIKSLHTVSPKYveamrrKAHFVIRMLENRIGQElliqVFNKQLAL------ASSAATTKigagLWSQLLIST 503
Cdd:pfam01433  142 QNVNDPSEIDDIFDAIPYE------KGASVLRMLETLLGEE----VFQKGLRSylkkfqYGNATTED----LWDALSEAS 207
                          250       260
                   ....*....|....*....|..
gi 442631480   504 NifikaiftvtGKDMSVFMDQW 525
Cdd:pfam01433  208 G----------PLDVDSFMDTW 219
 
Name Accession Description Interval E-value
M1_like_TAF2 cd09839
TATA binding protein (TBP) associated factor 2; This family includes TATA binding protein (TBP) ...
17-526 0e+00

TATA binding protein (TBP) associated factor 2; This family includes TATA binding protein (TBP) associated factor 2 (TAF2, TBP-associated factor TAFII150, transcription initiation factor TFIID subunit 2, RNA polymerase II TBP-associated factor subunit B), and has homology to the M1 gluzincin family. TAF2 is part of the TFIID multidomain subunit complex essential for transcription of most protein-encoded genes by RNA polymerase II. TAF2 is known to interact with the initiator element (Inr) found at the transcription start site of many genes, thus possibly playing a key role in promoter binding as well as start-site selection. Image analysis has shown TAF2 to form a complex with TAF1 and TBP, inferring its role in promoter recognition. Peptidases in the M1 family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile on activation during catalysis. TAF2, however, lacks these active site residues.


Pssm-ID: 341074 [Multi-domain]  Cd Length: 531  Bit Score: 564.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   17 LAHQVVSLTgISFERRSIIGVVELTIVPNSENLRLIRLNAKQLRIYSVVLNDVcQADFTYFDPFQNICYKEHKSRALEVY 96
Cdd:cd09839     1 VAHQKVELD-VDFANRSIIGYTEITIVPTSPDLRTIRLNCRQCKIKSVTVNGV-EAEFTYNDPLQNLDLSDNTDVNAHHE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   97 SKHHLTAAQYtDPDVNNGELLIQVPPEGYSMIQEGQG-------------------LRIRIEFSLENPKCGVHFVIPPAS 157
Cdd:cd09839    79 LKRKLAAALA-EPDEGNEELVISLPPSVKIELQDPNSastqattsspdtsedeftpLTIRIEYSLKNPRDGLHFVGPDEG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  158 TDEetqmNSSHMFT--NCYENSSRLWFPCVDSFADPCTWRLEFTVDK-----------------------------NMTA 206
Cdd:cd09839   158 GDK----RYPHVYTtnSPLPGSARCWFPCVDSLWERCTWELEITVPRtlgdagrpplagskededdddlteedkelEMVV 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  207 VSCGELLEVIMTP-DLRKKTFHYSVSTPVCAPNIALAVGQFEIYVDP-------------HMHEVTHFCLPGLLPLLKNT 272
Cdd:cd09839   234 VCSGDLVEQVVHPeDPSKKTFSFSLSNPTSAQHIGFAVGPFEIVPLPefreseeddklgsSAVEVTGFCLPGRLEELRNT 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  273 VRYLHEAFEFYEETlSTRYPFSCYKQVFVDELDTDISAYATMSIASVNLLHSIAIIDQTYISRTFMSRAVAEQFFGCFIT 352
Cdd:cd09839   314 CSFLHKAMDFFEEE-YGSYPFSSYKQVFVDDLPEDVSSFASLSICSSRLLYPPDIIDQAYETRRKLAHALASQWFGINII 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  353 SHHWSDTWLAKGIAEYLCGLYSRKCFGNNEYRAWVQSELARVVRYEeqyggiildcsqppaplpvsgtnqsaasskqqei 432
Cdd:cd09839   393 PKTWSDTWLVIGIAGYMTGLFLKKLFGNNEYRFRIKKDADRVCELD---------------------------------- 438
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  433 VHYFPIKSLHT---VSPKYVEAMRRKAHFVIRMLENRIGQELLIQVFNKQLALASSAATTkigaGLWSQLLISTNIFIKA 509
Cdd:cd09839   439 IGRPPLAQPGFilpLDPSELEFMALKAPLVLFILDRRLTKTGGSFGLSRVLPKIFLQAMS----GDLSNNALSTSHFLRT 514
                         570
                  ....*....|....*..
gi 442631480  510 IFTVTGKDMSVFMDQWV 526
Cdd:cd09839   515 CEKVSGNKLESFFDQWV 531
PepN COG0308
Aminopeptidase N, contains DUF3458 domain [Amino acid transport and metabolism];
13-713 2.41e-43

Aminopeptidase N, contains DUF3458 domain [Amino acid transport and metabolism];


Pssm-ID: 440077 [Multi-domain]  Cd Length: 609  Bit Score: 167.90  E-value: 2.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   13 RPFKLAHQVVSLTgISFERRSIIGVVELTIVPNSENLRLIRLNAKQLRIYSVVLNDVcQADFTYfdpfqnicykehksra 92
Cdd:COG0308    13 PGYDVTHYDLDLD-LDPATTRLSGTATITFTATEAPLDSLVLDLKGLEVTSVTVDGK-PLDFTR---------------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   93 levyskhhltaaqytdpdvNNGELLIQVPPEgysmIQEGQGLRIRIEFS--LENPKCGVHFVIPPASTDeetqmnsSHMF 170
Cdd:COG0308    75 -------------------DGERLTITLPKP----LAPGETFTLEIEYSgkPSNGGEGLYRSGDPPDGP-------PYLY 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  171 TNCYENSSRLWFPCVDSFADPCTWRLEFTVDKNMTAVSCGELLEVIMTPDLRkKTFHYSVSTPVcaPN--IALAVGQFEI 248
Cdd:COG0308   125 TQCEPEGARRWFPCFDHPDDKATFTLTVTVPAGWVAVSNGNLVSETELGDGR-TTWHWADTQPI--PTylFALAAGDYAV 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  249 YVDPHMH--EVTHFCLPGLLPLLKNTVRYLHEAFEFYEETLSTRYPFSCYKQVFVDeldtDISAYAtMSIASVNLLHSIA 326
Cdd:COG0308   202 VEDTFASgvPLRVYVRPGLADKAKEAFESTKRMLDFFEELFGVPYPFDKYDQVAVP----DFNFGA-MENQGLVTFGEKV 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  327 IIDQTYISRTFMSRA------VAEQFFGCFITSHHWSDTWLAKGIAEYLCGLYSRKCFGNNEYRAWVQSELARvvryeeq 400
Cdd:COG0308   277 LADETATDADYERREsviaheLAHQWFGNLVTCADWDDLWLNEGFATYMEQLFSEDLYGKDAADRIFVGALRS------- 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  401 yggIILDCSQPPAPLPVSGTNQSAASSKQQEIVhyfpikslhtvspkYVeamrrKAHFVIRMLENRIGQElliqVFNKQL 480
Cdd:COG0308   350 ---YAFAEDAGPNAHPIRPDDYPEIENFFDGIV--------------YE-----KGALVLHMLRTLLGDE----AFRAGL 403
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  481 AL-----ASSAATTKigaglwsQllistniFIKAIFTVTGKDMSVFMDQWVRTGGHAKFSLTSVFNRKRNTiELEIRQD- 554
Cdd:COG0308   404 RLyfarhAGGNATTE-------D-------FLAALEEASGRDLSAFFDQWLYQAGLPTLEVEYEYDADGKV-TLTLRQTp 468
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  555 YVNQRgirkYNGPLMVQLqeLDGTFKHTlqiestlvksditchsksrrnkkkkIPLCTGEEVDMDLSAmddSPVLWIRLD 634
Cdd:COG0308   469 PRPHP----FHIPLEVGL--LGGKLTAR-------------------------TVLLDGEQTELVAKP---DPVLLLRLD 514
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442631480  635 PEMILLrdliieqpdfqwqyqLRHERDVTAQFQAIQALQKYPTNATRLALTDTIESercFYQVRCEAAHSLTKVANQMV 713
Cdd:COG0308   515 DELAFL---------------LAHDSDPFNRWEALQALWRDGEADYLDALRALADT---DPAVRAEALALLGSDQLALA 575
M1_APN_like cd09603
Peptidase M1 family similar to aminopeptidase N catalytic domain; This family contains mostly ...
15-527 5.24e-41

Peptidase M1 family similar to aminopeptidase N catalytic domain; This family contains mostly bacterial and some archaeal M1 peptidases with smilarity to the catalytic domain of aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.


Pssm-ID: 341066 [Multi-domain]  Cd Length: 410  Bit Score: 156.59  E-value: 5.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   15 FKLAHQVVSLTgISFERRSIIGVVELTIVPNsENLRLIRLNAKQLRIYSVVLNDVCQADFTYfdpfqnicykehksrale 94
Cdd:cd09603     1 YDVLHYDLDLD-YDPATKSLSGTATITFRAT-QDLDSLQLDLVGLTVSSVTVDGVPAAFFTH------------------ 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   95 vyskhhltaaqytdpdvNNGELLIQVPpegySMIQEGQGLRIRIEFSlenpkcGVHFVIPPASTDEETQMNSSH-MFTNC 173
Cdd:cd09603    61 -----------------DGDKLVITLP----RPLAAGETFTVTVRYS------GKPRPAGYPPGDGGGWEEGDDgVWTAG 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  174 YENSSRLWFPCVDSFADPCTWRLEFTVDKNMTAVSCGELLEVIMTPDlRKKTFHYSVSTPVCAPNIALAVGQFEIYVDPH 253
Cdd:cd09603   114 QPEGASTWFPCNDHPDDKATYDITVTVPAGLTVVSNGRLVSTTTNGG-GTTTWHWKMDYPIATYLVTLAVGRYAVVEDGS 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  254 MH--EVTHFCLPGLLPLLKNTVRYLHEAFEFYEETLsTRYPFSCYKQVFVDELdtdisAYA----TMSIASVNLLHsiai 327
Cdd:cd09603   193 GGgiPLRYYVPPGDAAKAKASFARTPEMLDFFEELF-GPYPFEKYGQVVVPDL-----GGGmehqTATTYGNNFLN---- 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  328 IDQTYISrtFMSRAVAEQFFGCFITSHHWSDTWLAKGIAEYLCGLYSRKCFGNNEYRAWVQSELARVVRYEEQYGGiild 407
Cdd:cd09603   263 GDRGSER--LIAHELAHQWFGDSVTCADWADIWLNEGFATYAEWLWSEHKGGADAYRAYLAGQRQDYLNADPGPGR---- 336
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  408 csqPPAPLPVSGTNqsaasskqqeivhyfpikslhtvspkyveaMRRKAHFVIRMLENRIGQEL---LIQVFNKQLALAS 484
Cdd:cd09603   337 ---PPDPDDLFDRD------------------------------VYQKGALVLHMLRNLLGDEAffaALRAYLARYAHGN 383
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 442631480  485 saattkigaglwsqllISTNIFIKAIFTVTGKDMSVFMDQWVR 527
Cdd:cd09603   384 ----------------VTTEDFIAAAEEVSGRDLTWFFDQWLY 410
M1 cd09595
Peptidase M1 family includes the catalytic domains of aminopeptidase N and leukotriene A4 ...
27-414 2.20e-15

Peptidase M1 family includes the catalytic domains of aminopeptidase N and leukotriene A4 hydrolase; The model represents the catalytic domains of M1 peptidase family members including aminopeptidase N (APN) and leukotriene A4 hydrolase (LTA4H). All peptidases in this family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile upon activation during catalysis. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types. APN expression is dysregulated in many inflammatory diseases and is enhanced in numerous tumor cells, making it a lead target in the development of anti-cancer and anti-inflammatory drugs. LTA4H is a bifunctional enzyme, possessing an aminopeptidase as well as an epoxide hydrolase activity. The two activities occupy different, but overlapping sites. The activity and physiological relevance of the aminopeptidase in LTA4H is as yet unknown, while the epoxide hydrolase converts leukotriene A4 (LTA4) into leukotriene B4 (LTB4), a potent chemotaxin that is fundamental to the inflammatory response of mammals.


Pssm-ID: 341058 [Multi-domain]  Cd Length: 413  Bit Score: 79.80  E-value: 2.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   27 ISFERRSIIGVVELTiVPNSENLRLIRLNAKQLRIYSVVLNDvcqadftyfdpfqnicykehksralevyskhhlTAAQY 106
Cdd:cd09595     9 VDFTTKTLNGTETLT-VDASQVGRELVLDLVGLTIHSVSVNG---------------------------------AAVDF 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  107 TDPDVNNGELLIQVPPEgysmiQEGQGLRIRIEFSLENPKCGVHFVIPPASTDEEtqmnsSHMFTNCYENSSRLWFPCVD 186
Cdd:cd09595    55 GEREHYDGEKLTIPGPK-----PPGQTFTVRISFEAKPSKNLLGWLWEQTAGKEK-----PYLFTQFEATHARRIFPCID 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  187 SFADPCTWRLEFTVDKNMTAVSCGELLEVIMTPDLRkKTFHYSVSTPVCAPNIALAVGQFE----IYVDPHMHEVTHFCL 262
Cdd:cd09595   125 HPAVKATFTVTITTPKKDLLASNGALVGEETGANGR-KTYRFEDTPPIPTYLVAVVVGDLEfkyvTVKSQPRVGLSVYSE 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  263 PGLLPLLKNTVRYLHEAFEFYEETLSTRYPFSCYKQVFVDELDTDISAYATMSIASVNLLHSIAIIDQTYISRT-FMSRA 341
Cdd:cd09595   204 PLQVDQAQYAFDATRAALAWFEDYFGGPYPLPKYDLLAVPDFNSGAMENPGLITFRTTYLLRSKVTDTGARSIEnVIAHE 283
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442631480  342 VAEQFFGCFITSHHWSDTWLAKGIAEYLCGLYSRKCFGNN--EYRAWVQSELARVVRYEEQYGGIILDCSQPPAP 414
Cdd:cd09595   284 LAHQWFGNLVTMRWWNDLWLNEGFAVYYENRIMDATFGTSsrHLDQLSGSSDLNTEQLLEDSSPTSTPVRSPADP 358
GluZincin cd09594
Gluzincin Peptidase family (thermolysin-like proteinases, TLPs) which includes peptidases M1, ...
275-372 1.39e-12

Gluzincin Peptidase family (thermolysin-like proteinases, TLPs) which includes peptidases M1, M2, M3, M4, M13, M32 and M36 (fungalysins); The Gluzincin family (thermolysin-like peptidases or TLPs) includes several zinc-dependent metallopeptidases such as M1, M2, M3, M4, M13, M32, M36 peptidases (MEROPS classification), which contain the HEXXH motif as part of their active site. Peptidases in this family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile on activation during catalysis. The M1 family includes aminopeptidase N (APN) and leukotriene A4 hydrolase (LTA4H). APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types. LTA4H is a bifunctional enzyme, possessing an aminopeptidase as well as an epoxide hydrolase activity such that the two activities occupy different, but overlapping sites. The M3_like peptidases include the M2_ACE, M3 or neurolysin-like family (subfamilies M3B_PepF and M3A) and M32_Taq peptidases. The M2 peptidase angiotensin converting enzyme (ACE, EC 3.4.15.1) catalyzes the conversion of decapeptide angiotensin I to the potent vasopressor octapeptide angiotensin II. ACE is a key component of the renin-angiotensin system that regulates blood pressure, thus ACE inhibitors are important for the treatment of hypertension. M3A includes thimet oligopeptidase (TOP; endopeptidase 3.4.24.15), neurolysin (3.4.24.16), and the mitochondrial intermediate peptidase; and M3B includes oligopeptidase F. The M32 family includes eukaryotic enzymes from protozoa Trypanosoma cruzi, a causative agent of Chagas' disease, and from Leishmania major, a parasite that causes leishmaniasis, making these enzymes attractive targets for drug development. The M4 family includes secreted protease thermolysin (EC 3.4.24.27), pseudolysin, aureolysin, and neutral protease as well as bacillolysin (EC 3.4.24.28) that degrade extracellular proteins and peptides for bacterial nutrition, especially prior to sporulation. Thermolysin is widely used as a nonspecific protease to obtain fragments for peptide sequencing as well as in production of the artificial sweetener aspartame. The M13 family includes neprilysin (EC 3.4.24.11) and endothelin-converting enzyme I (ECE-1, EC 3.4.24.71), which fulfill a broad range of physiological roles due to the greater variation in the S2' subsite allowing substrate specificity and are prime therapeutic targets for selective inhibition. The peptidase M36 fungalysin family includes endopeptidases from pathogenic fungi. Fungalysin hydrolyzes extracellular matrix proteins such as elastin and keratin. Aspergillus fumigatus causes the pulmonary disease aspergillosis by invading the lungs of immuno-compromised animals and secreting fungalysin that possibly breaks down proteinaceous structural barriers.


Pssm-ID: 341057 [Multi-domain]  Cd Length: 105  Bit Score: 65.20  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  275 YLHEAFEFYEETLST---RYPFSCYKQVFVDELDTDISAYATMSIASVNLLHSIAIIDQTYISRTFMSRAVAEQFFGCFI 351
Cdd:cd09594     3 YAHETYKYYEELLGRtsfRYPVSPIYSLLVYPAYVEVNAYNAMWIPSTNIFYGAGILDTLSGTIDVLAHELTHAFTGQFS 82
                          90       100
                  ....*....|....*....|..
gi 442631480  352 TSHH-WSDTWLAKGIAEYLCGL 372
Cdd:cd09594    83 NLMYsWSSGWLNEGISDYFGGL 104
M1_LTA4H cd09599
Peptidase M1 family including Leukotriene A4 hydrolase catalytic domain; This model represents ...
27-247 1.03e-11

Peptidase M1 family including Leukotriene A4 hydrolase catalytic domain; This model represents the N-terminal catalytic domain of leukotriene A4 hydrolase (LTA4H; E.C. 3.3.2.6) and the close homolog cold-active aminopeptidase (Colwellia psychrerythraea-type peptidase; ColAP), both members of the aminopeptidase M1 family. LTA4H is a bifunctional enzyme, possessing an aminopeptidase as well as an epoxide hydrolase activity. The two activities occupy different, but overlapping sites. The activity and physiological relevance of the aminopeptidase is poorly understood while the epoxide hydrolase converts leukotriene A4 (LTA4) into leukotriene B4 (LTB4), a potent chemotaxin that is fundamental to the inflammatory response of mammals. It accepts a variety of substrates, including some opioid, di- and tripeptides, as well as chromogenic aminoacyl-p-nitroanilide derivatives. The aminopeptidase activity of LTA4H is possibly involved in the processing of peptides related to inflammation and host defense. Kinetic analysis shows that LTA4H hydrolyzes arginyl tripeptides with high efficiency and specificity, indicating its function as an arginyl aminopeptidase. Thermodynamic characterization using different biophysical methods shows that structurally distinct inhibitors of the LTA4H occupy different regions of the binding site; while some (RB202, ARM1 and SC57461A) bind to the hydrophobic hydrolase side, both bestatin and captopril are located at the hydrophilic peptidase side. LTB4H overexpression is associated with different pathological conditions and diseases such as cystic fibrosis, coronary heart disease, sepsis, shock, connective tissue disease, and chronic obstructive pulmonary disease. It is also overexpressed in certain human cancers, and has been identified as a functionally important target for mediating anticancer properties of resveratrol, a well-known red wine polyphenolic compound with cancer chemopreventive activity.


Pssm-ID: 341062 [Multi-domain]  Cd Length: 442  Bit Score: 68.64  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   27 ISFERRSIIGVVELTIVPNSENLRLIRLNAKQLRIYSVVLNDVCQADFTYFDPfqnicyKEHKSRALEvyskhhltaaqy 106
Cdd:cd09599    22 VDFDKKTISGSATLTLEVLQDGADELVLDTRDLDISSVTVNGGKELKFELGPR------DPVLGSALT------------ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  107 tdpdvnngellIQVPPEgysmIQEGQGLRIRIEFSLeNPKC-GVHFvIPPASTDEETQmnsSHMFTNCYENSSRLWFPCV 185
Cdd:cd09599    84 -----------ITLPSP----LAKGDTFKVKIEYST-TPQAtALQW-LTPEQTAGKKH---PYLFTQCQAIHARSLFPCQ 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442631480  186 DSFADPCTWRLEFTVDKNMTAVSCGELLEVimTPDLRKKTFHYSVSTPVCAPNIALAVGQFE 247
Cdd:cd09599   144 DTPSVKSTYSATVTVPKGLTALMSALRTGE--KEEAGTGTYTFEQPVPIPSYLIAIAVGDLE 203
M1_APN-Q_like cd09601
Peptidase M1 aminopeptidase N catalytic domain family which includes aminopeptidase N (APN), ...
27-527 1.25e-08

Peptidase M1 aminopeptidase N catalytic domain family which includes aminopeptidase N (APN), aminopeptidase Q (APQ), tricorn interacting factor F3, and endoplasmic reticulum aminopeptidase 1 (ERAP1); This M1 peptidase family includes eukaryotic and bacterial members: the catalytic domains of aminopeptidase N (APN), aminopeptidase Q (APQ, laeverin), endoplasmic reticulum aminopeptidase 1 (ERAP1) as well as tricorn interacting factor F3. Aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease, preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is considered a marker of differentiation since it is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. ERAP1, also known as endoplasmic reticulum aminopeptidase associated with antigen processing (ERAAP), adipocyte derived leucine aminopeptidase (A-LAP), or aminopeptidase regulating tumor necrosis factor receptor I (THFRI) shedding (ARTS-1), associates with the closely related ER aminopeptidase ERAP2, for the final trimming of peptides within the ER for presentation by MHC class I molecules. ERAP1 is associated with ankylosing spondylitis (AS), an inflammatory arthritis that predominantly affects the spine. ERAP1 also aids in the shedding of membrane-bound cytokine receptors. The tricorn interacting factor F3, together with factors F1 and F2, degrades the tricorn protease products, producing free amino acids, thus completing the proteasomal degradation pathway. F3 is homologous to F2, but not F1, and shows a strong preference for glutamate in the P1' position. APQ, also known as laeverin, is specifically expressed in human embryo-derived extravillous trophoblasts (EVTs) that invade the uterus during early placentation. It cleaves the N-terminal amino acid of various peptides such as angiotensin III, endokinin C, and kisspeptin-10, all expressed in the placenta in large quantities. APN is a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs are also putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.


Pssm-ID: 341064 [Multi-domain]  Cd Length: 442  Bit Score: 58.75  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   27 ISFERRSIIGVVELTIVPNsENLRLIRLNAKQLRIYSVVLNDVCQADftyfdpfqnicykehksralevyskhhlTAAQY 106
Cdd:cd09601     9 PDLENFTFSGSVTITLEVL-EPTDTIVLHAKDLTITSASLTLKGGSG----------------------------IIEVT 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  107 TDPDVNNGELLIQVPpegySMIQEGQGLRIRIEFS--LENPKCGVHfvippASTDEETQMNSSHMF-TNCYENSSRLWFP 183
Cdd:cd09601    60 VVTDEETEFLTITLD----ETLPPGENYTLSIEFTgkLNDDLRGFY-----RSSYTDEDGETRYLAaTQFEPTDARRAFP 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  184 CVDsfaDP---CTWRLEFTVDKNMTAVSCGELLEVIMTPDLRKKT-FHYSV--STPVcapnIALAVGQFE---------- 247
Cdd:cd09601   131 CFD---EPafkATFDITITHPKGYTALSNMPPVESTELEDGWKTTtFETTPpmSTYL----VAFVVGDFEyiesttksgv 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  248 ---IYVDPHMHEVTHFCLpgllpllKNTVRYLheafEFYEETLSTRYPFScyKqvfvdeLDT----DISAYAT-----MS 315
Cdd:cd09601   204 pvrVYARPGKIEQGDFAL-------EVAPKIL----DFYEDYFGIPYPLP--K------LDLvaipDFAAGAMenwglIT 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  316 IASVNLLH---SIAIIDQTYISRTfMSRAVAEQFFGCFITSHHWSDTWLAKGIA---EYLCGLYSRKcfgnnEYRAWVQS 389
Cdd:cd09601   265 YRETALLYdpkTSSASDKQRVAEV-IAHELAHQWFGNLVTMKWWDDLWLNEGFAtymEYLAVDKLFP-----EWNMWDQF 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  390 ELarvvryEEQYGGIILDCSqppaplpvsgtnqsaASSKQQEivhyFPIKSLHTVSPKYVEAMRRKAHFVIRMLENRIGQ 469
Cdd:cd09601   339 VV------DELQSALELDSL---------------ASSHPIE----VPVESPSEISEIFDAISYSKGASVLRMLENFLGE 393
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442631480  470 ElliqVFNKQLAL-----ASSAATTKIgagLWSQLListnifiKAIFTVTGKDMSVFMDQWVR 527
Cdd:cd09601   394 E----VFRKGLRKylkkhAYGNATTDD---LWEALQ-------EASGESKPLDVKEIMDSWTL 442
Peptidase_M1 pfam01433
Peptidase family M1 domain; Members of this family are aminopeptidases. The members differ ...
278-525 6.77e-07

Peptidase family M1 domain; Members of this family are aminopeptidases. The members differ widely in specificity, hydrolysing acidic, basic or neutral N-terminal residues. This family includes leukotriene-A4 hydrolase, this enzyme also has an aminopeptidase activity.


Pssm-ID: 426262 [Multi-domain]  Cd Length: 219  Bit Score: 51.52  E-value: 6.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   278 EAFEFYEETLSTRYPFSCYKQVFVDELdtdisAYATMSIASVNLLHSIAIIDQTYISRTFMSRAVAE--------QFFGC 349
Cdd:pfam01433    8 KLLEFYEDYFNIPYPLPKYDLVALPDF-----SAGAMENWGLITYRETLLLYDPGNSSTSDKQRVASviahelahQWFGN 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   350 FITSHHWSDTWLAKGIAEYLCGLYSRKCFGNNEYRAWVQseLARVVRYEEqyggiiLDCSQPPAPLpvsgtnqsaasskQ 429
Cdd:pfam01433   83 LVTMKWWDDLWLNEGFATYMEYLGTDALFPEWNIWEQFL--LDEVQNAMA------RDALDSSHPI-------------T 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480   430 QEIVHYFPIKSLHTVSPKYveamrrKAHFVIRMLENRIGQElliqVFNKQLAL------ASSAATTKigagLWSQLLIST 503
Cdd:pfam01433  142 QNVNDPSEIDDIFDAIPYE------KGASVLRMLETLLGEE----VFQKGLRSylkkfqYGNATTED----LWDALSEAS 207
                          250       260
                   ....*....|....*....|..
gi 442631480   504 NifikaiftvtGKDMSVFMDQW 525
Cdd:pfam01433  208 G----------PLDVDSFMDTW 219
M1_APN cd09602
Peptidase M1 family including aminopeptidase N catalytic domain; This model represents the ...
135-303 3.74e-05

Peptidase M1 family including aminopeptidase N catalytic domain; This model represents the catalytic domain of bacterial and eukaryotic aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.


Pssm-ID: 341065 [Multi-domain]  Cd Length: 440  Bit Score: 47.51  E-value: 3.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  135 RIRIEFSLENPK--CGVHFVIPPAstDEETqmnssHMFTNCYENSSRLWFPCvdsFADP---CTWRLEFTVDKNMTAVSC 209
Cdd:cd09602    89 TVVVEFTAPYSSdgEGLHRFVDPA--DGET-----YLYTLFEPDDARRVFPC---FDQPdlkATFTLTVTAPADWTVISN 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631480  210 GELLEVIMTPDLRKKTFHysvSTPVCAPNI-ALAVGQFEIYVDPHMH-EVTHFCLPGLLPLLKNT--VRYLH-EAFEFYE 284
Cdd:cd09602   159 GPETSTEEAGGRKRWRFA---ETPPLSTYLfAFVAGPYHRVEDEHDGiPLGLYCRESLAEYERDAdeIFEVTkQGLDFYE 235
                         170
                  ....*....|....*....
gi 442631480  285 ETLSTRYPFSCYKQVFVDE 303
Cdd:cd09602   236 DYFGIPYPFGKYDQVFVPE 254
 
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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