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Conserved domains on  [gi|145559533|sp|Q6P1X5|]
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RecName: Full=Transcription initiation factor TFIID subunit 2; AltName: Full=150 kDa cofactor of initiator function; AltName: Full=RNA polymerase II TBP-associated factor subunit B; AltName: Full=TBP-associated factor 150 kDa; AltName: Full=Transcription initiation factor TFIID 150 kDa subunit; Short=TAF(II)150; Short=TAFII-150; Short=TAFII150

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

Graphical summary

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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) ...
28-523 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: 597.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533   28 LTHQVVCINnINFQRKSVVGFVELTIFPTVANLNRIKLNSKQCRIYRVRINDLEAAFIYNDPTLEVCHSESKQRNLNYFS 107
Cdd:cd09839     1 VAHQKVELD-VDFANRSIIGYTEITIVPTSPDLRTIRLNCRQCKIKSVTVNGVEAEFTYNDPLQNLDLSDNTDVNAHHEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  108 NAYAAAVSAvDPDAGNGELCIKVPSELWKHV-------------------DELKVLKIHINFSLDQPKGGLHFVVPsvEG 168
Cdd:cd09839    80 KRKLAAALA-EPDEGNEELVISLPPSVKIELqdpnsastqattsspdtseDEFTPLTIRIEYSLKNPRDGLHFVGP--DE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  169 SMAERGAHVFSCG--YQNSTRFWFPCVDSYSELCTWKLEFTVDA-----------------------------AMVAVSN 217
Cdd:cd09839   157 GGDKRYPHVYTTNspLPGSARCWFPCVDSLWERCTWELEITVPRtlgdagrpplagskededdddlteedkelEMVVVCS 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  218 GDLVETVYT-HDMRKKTFHYMLTIPTAASNISLAIGPFEILVDP-------------YMHEVTHFCLPQLLPLLKHTTSY 283
Cdd:cd09839   237 GDLVEQVVHpEDPSKKTFSFSLSNPTSAQHIGFAVGPFEIVPLPefreseeddklgsSAVEVTGFCLPGRLEELRNTCSF 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  284 LHEVFEFYEEiLTCRYPYSCFKTVFIDEAYVEVAAYASMSIFSTNLLHSAMIIDETPLTRRCLAQSLAQQFFGCFISRMS 363
Cdd:cd09839   317 LHKAMDFFEE-EYGSYPFSSYKQVFVDDLPEDVSSFASLSICSSRLLYPPDIIDQAYETRRKLAHALASQWFGINIIPKT 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  364 WSDEWVLKGISGYIYGLWMKKTFGVNEYRHWIKEELDKIVAYElktggvllhpifgggkekdnpasHLHFSIKHPHT--- 440
Cdd:cd09839   396 WSDTWLVIGIAGYMTGLFLKKLFGNNEYRFRIKKDADRVCELD-----------------------IGRPPLAQPGFilp 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  441 LSWEYYSMFQCKAHLVMRLIENRISMEFMLQVFNKLLSLASTassqKFQSHMWSQMLVSTSGFLKSISNVSGKDIQPLIK 520
Cdd:cd09839   453 LDPSELEFMALKAPLVLFILDRRLTKTGGSFGLSRVLPKIFL----QAMSGDLSNNALSTSHFLRTCEKVSGNKLESFFD 528

                  ...
gi 145559533  521 QWV 523
Cdd:cd09839   529 QWV 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) ...
28-523 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: 597.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533   28 LTHQVVCINnINFQRKSVVGFVELTIFPTVANLNRIKLNSKQCRIYRVRINDLEAAFIYNDPTLEVCHSESKQRNLNYFS 107
Cdd:cd09839     1 VAHQKVELD-VDFANRSIIGYTEITIVPTSPDLRTIRLNCRQCKIKSVTVNGVEAEFTYNDPLQNLDLSDNTDVNAHHEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  108 NAYAAAVSAvDPDAGNGELCIKVPSELWKHV-------------------DELKVLKIHINFSLDQPKGGLHFVVPsvEG 168
Cdd:cd09839    80 KRKLAAALA-EPDEGNEELVISLPPSVKIELqdpnsastqattsspdtseDEFTPLTIRIEYSLKNPRDGLHFVGP--DE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  169 SMAERGAHVFSCG--YQNSTRFWFPCVDSYSELCTWKLEFTVDA-----------------------------AMVAVSN 217
Cdd:cd09839   157 GGDKRYPHVYTTNspLPGSARCWFPCVDSLWERCTWELEITVPRtlgdagrpplagskededdddlteedkelEMVVVCS 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  218 GDLVETVYT-HDMRKKTFHYMLTIPTAASNISLAIGPFEILVDP-------------YMHEVTHFCLPQLLPLLKHTTSY 283
Cdd:cd09839   237 GDLVEQVVHpEDPSKKTFSFSLSNPTSAQHIGFAVGPFEIVPLPefreseeddklgsSAVEVTGFCLPGRLEELRNTCSF 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  284 LHEVFEFYEEiLTCRYPYSCFKTVFIDEAYVEVAAYASMSIFSTNLLHSAMIIDETPLTRRCLAQSLAQQFFGCFISRMS 363
Cdd:cd09839   317 LHKAMDFFEE-EYGSYPFSSYKQVFVDDLPEDVSSFASLSICSSRLLYPPDIIDQAYETRRKLAHALASQWFGINIIPKT 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  364 WSDEWVLKGISGYIYGLWMKKTFGVNEYRHWIKEELDKIVAYElktggvllhpifgggkekdnpasHLHFSIKHPHT--- 440
Cdd:cd09839   396 WSDTWLVIGIAGYMTGLFLKKLFGNNEYRFRIKKDADRVCELD-----------------------IGRPPLAQPGFilp 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  441 LSWEYYSMFQCKAHLVMRLIENRISMEFMLQVFNKLLSLASTassqKFQSHMWSQMLVSTSGFLKSISNVSGKDIQPLIK 520
Cdd:cd09839   453 LDPSELEFMALKAPLVLFILDRRLTKTGGSFGLSRVLPKIFL----QAMSGDLSNNALSTSHFLRTCEKVSGNKLESFFD 528

                  ...
gi 145559533  521 QWV 523
Cdd:cd09839   529 QWV 531
PepN COG0308
Aminopeptidase N, contains DUF3458 domain [Amino acid transport and metabolism];
11-581 8.78e-33

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


Pssm-ID: 440077 [Multi-domain]  Cd Length: 609  Bit Score: 135.93  E-value: 8.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533   11 MNRKKGDKGFeSPRPYKLTHQVVCINnINFQRKSVVGFVELTIFPTVANLNRIKLNSKQCRIYRVRINDLEAAFIYNDPT 90
Cdd:COG0308     1 MKRLTRLEAY-RPPGYDVTHYDLDLD-LDPATTRLSGTATITFTATEAPLDSLVLDLKGLEVTSVTVDGKPLDFTRDGER 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533   91 LEVchseskqrnlnYFSNAYAAAVSAVdpdagngelcikvpselwkhvdelkvlkIHINFSLDQPKG--GLHFVVPSVEG 168
Cdd:COG0308    79 LTI-----------TLPKPLAPGETFT----------------------------LEIEYSGKPSNGgeGLYRSGDPPDG 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  169 SmaergAHVFSCGYQNSTRFWFPCVDSYSELCTWKLEFTVDAAMVAVSNGDLVETVyTHDMRKKTFHYMLTIPTAASNIS 248
Cdd:COG0308   120 P-----PYLYTQCEPEGARRWFPCFDHPDDKATFTLTVTVPAGWVAVSNGNLVSET-ELGDGRTTWHWADTQPIPTYLFA 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  249 LAIGPFEILVDPYMH--EVTHFCLPQLLPLLKHTTSYLHEVFEFYEEILTCRYPYSCFKTVFIDEaYVEVA-AYASMSIF 325
Cdd:COG0308   194 LAAGDYAVVEDTFASgvPLRVYVRPGLADKAKEAFESTKRMLDFFEELFGVPYPFDKYDQVAVPD-FNFGAmENQGLVTF 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  326 STNLLHSAMIIDETPLTRRCL-AQSLAQQFFGCFISRMSWSDEWvLK-GISGYIYGLWMKKTFGVNEYRHWIKEELDKIv 403
Cdd:COG0308   273 GEKVLADETATDADYERRESViAHELAHQWFGNLVTCADWDDLW-LNeGFATYMEQLFSEDLYGKDAADRIFVGALRSY- 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  404 AYELKtGGVLLHPIFGggkeKDNPASHLHFSikhPHTlsweYYsmfqcKAHLVMRLIENRISMEfmlqVFNKLLSLAsta 483
Cdd:COG0308   351 AFAED-AGPNAHPIRP----DDYPEIENFFD---GIV----YE-----KGALVLHMLRTLLGDE----AFRAGLRLY--- 406
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  484 ssqkFQSHMWSqmLVSTSGFLKSISNVSGKDIQPLIKQWVDQSGVVKFYGSFAFNRKRNVlELEIKQdyTSPGTQKYVGP 563
Cdd:COG0308   407 ----FARHAGG--NATTEDFLAALEEASGRDLSAFFDQWLYQAGLPTLEVEYEYDADGKV-TLTLRQ--TPPRPHPFHIP 477
                         570
                  ....*....|....*...
gi 145559533  564 LKVTVqeLDGSFNHTLQI 581
Cdd:COG0308   478 LEVGL--LGGKLTARTVL 493
 
Name Accession Description Interval E-value
M1_like_TAF2 cd09839
TATA binding protein (TBP) associated factor 2; This family includes TATA binding protein (TBP) ...
28-523 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: 597.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533   28 LTHQVVCINnINFQRKSVVGFVELTIFPTVANLNRIKLNSKQCRIYRVRINDLEAAFIYNDPTLEVCHSESKQRNLNYFS 107
Cdd:cd09839     1 VAHQKVELD-VDFANRSIIGYTEITIVPTSPDLRTIRLNCRQCKIKSVTVNGVEAEFTYNDPLQNLDLSDNTDVNAHHEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  108 NAYAAAVSAvDPDAGNGELCIKVPSELWKHV-------------------DELKVLKIHINFSLDQPKGGLHFVVPsvEG 168
Cdd:cd09839    80 KRKLAAALA-EPDEGNEELVISLPPSVKIELqdpnsastqattsspdtseDEFTPLTIRIEYSLKNPRDGLHFVGP--DE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  169 SMAERGAHVFSCG--YQNSTRFWFPCVDSYSELCTWKLEFTVDA-----------------------------AMVAVSN 217
Cdd:cd09839   157 GGDKRYPHVYTTNspLPGSARCWFPCVDSLWERCTWELEITVPRtlgdagrpplagskededdddlteedkelEMVVVCS 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  218 GDLVETVYT-HDMRKKTFHYMLTIPTAASNISLAIGPFEILVDP-------------YMHEVTHFCLPQLLPLLKHTTSY 283
Cdd:cd09839   237 GDLVEQVVHpEDPSKKTFSFSLSNPTSAQHIGFAVGPFEIVPLPefreseeddklgsSAVEVTGFCLPGRLEELRNTCSF 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  284 LHEVFEFYEEiLTCRYPYSCFKTVFIDEAYVEVAAYASMSIFSTNLLHSAMIIDETPLTRRCLAQSLAQQFFGCFISRMS 363
Cdd:cd09839   317 LHKAMDFFEE-EYGSYPFSSYKQVFVDDLPEDVSSFASLSICSSRLLYPPDIIDQAYETRRKLAHALASQWFGINIIPKT 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  364 WSDEWVLKGISGYIYGLWMKKTFGVNEYRHWIKEELDKIVAYElktggvllhpifgggkekdnpasHLHFSIKHPHT--- 440
Cdd:cd09839   396 WSDTWLVIGIAGYMTGLFLKKLFGNNEYRFRIKKDADRVCELD-----------------------IGRPPLAQPGFilp 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  441 LSWEYYSMFQCKAHLVMRLIENRISMEFMLQVFNKLLSLASTassqKFQSHMWSQMLVSTSGFLKSISNVSGKDIQPLIK 520
Cdd:cd09839   453 LDPSELEFMALKAPLVLFILDRRLTKTGGSFGLSRVLPKIFL----QAMSGDLSNNALSTSHFLRTCEKVSGNKLESFFD 528

                  ...
gi 145559533  521 QWV 523
Cdd:cd09839   529 QWV 531
GluZincin cd09594
Gluzincin Peptidase family (thermolysin-like proteinases, TLPs) which includes peptidases M1, ...
281-381 1.07e-36

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: 133.76  E-value: 1.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  281 TSYLHEVFEFYEEILTC---RYPYSCFKTVFIDEAYVEVAAYASMSIFSTNLLHSAMIIDETPLTRRCLAQSLAQQFFGC 357
Cdd:cd09594     1 TSYAHETYKYYEELLGRtsfRYPVSPIYSLLVYPAYVEVNAYNAMWIPSTNIFYGAGILDTLSGTIDVLAHELTHAFTGQ 80
                          90       100
                  ....*....|....*....|....*
gi 145559533  358 FISRM-SWSDEWVLKGISGYIYGLW 381
Cdd:cd09594    81 FSNLMySWSSGWLNEGISDYFGGLV 105
PepN COG0308
Aminopeptidase N, contains DUF3458 domain [Amino acid transport and metabolism];
11-581 8.78e-33

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


Pssm-ID: 440077 [Multi-domain]  Cd Length: 609  Bit Score: 135.93  E-value: 8.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533   11 MNRKKGDKGFeSPRPYKLTHQVVCINnINFQRKSVVGFVELTIFPTVANLNRIKLNSKQCRIYRVRINDLEAAFIYNDPT 90
Cdd:COG0308     1 MKRLTRLEAY-RPPGYDVTHYDLDLD-LDPATTRLSGTATITFTATEAPLDSLVLDLKGLEVTSVTVDGKPLDFTRDGER 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533   91 LEVchseskqrnlnYFSNAYAAAVSAVdpdagngelcikvpselwkhvdelkvlkIHINFSLDQPKG--GLHFVVPSVEG 168
Cdd:COG0308    79 LTI-----------TLPKPLAPGETFT----------------------------LEIEYSGKPSNGgeGLYRSGDPPDG 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  169 SmaergAHVFSCGYQNSTRFWFPCVDSYSELCTWKLEFTVDAAMVAVSNGDLVETVyTHDMRKKTFHYMLTIPTAASNIS 248
Cdd:COG0308   120 P-----PYLYTQCEPEGARRWFPCFDHPDDKATFTLTVTVPAGWVAVSNGNLVSET-ELGDGRTTWHWADTQPIPTYLFA 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  249 LAIGPFEILVDPYMH--EVTHFCLPQLLPLLKHTTSYLHEVFEFYEEILTCRYPYSCFKTVFIDEaYVEVA-AYASMSIF 325
Cdd:COG0308   194 LAAGDYAVVEDTFASgvPLRVYVRPGLADKAKEAFESTKRMLDFFEELFGVPYPFDKYDQVAVPD-FNFGAmENQGLVTF 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  326 STNLLHSAMIIDETPLTRRCL-AQSLAQQFFGCFISRMSWSDEWvLK-GISGYIYGLWMKKTFGVNEYRHWIKEELDKIv 403
Cdd:COG0308   273 GEKVLADETATDADYERRESViAHELAHQWFGNLVTCADWDDLW-LNeGFATYMEQLFSEDLYGKDAADRIFVGALRSY- 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  404 AYELKtGGVLLHPIFGggkeKDNPASHLHFSikhPHTlsweYYsmfqcKAHLVMRLIENRISMEfmlqVFNKLLSLAsta 483
Cdd:COG0308   351 AFAED-AGPNAHPIRP----DDYPEIENFFD---GIV----YE-----KGALVLHMLRTLLGDE----AFRAGLRLY--- 406
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  484 ssqkFQSHMWSqmLVSTSGFLKSISNVSGKDIQPLIKQWVDQSGVVKFYGSFAFNRKRNVlELEIKQdyTSPGTQKYVGP 563
Cdd:COG0308   407 ----FARHAGG--NATTEDFLAALEEASGRDLSAFFDQWLYQAGLPTLEVEYEYDADGKV-TLTLRQ--TPPRPHPFHIP 477
                         570
                  ....*....|....*...
gi 145559533  564 LKVTVqeLDGSFNHTLQI 581
Cdd:COG0308   478 LEVGL--LGGKLTARTVL 493
M1_APN_like cd09603
Peptidase M1 family similar to aminopeptidase N catalytic domain; This family contains mostly ...
38-421 1.87e-29

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: 122.31  E-value: 1.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533   38 INFQRKSVVGFVELTIFPTvANLNRIKLNSKQCRIYRVRINDLEAAFIYNDptlevchseskqrnlnyfsnayaaavsav 117
Cdd:cd09603    12 YDPATKSLSGTATITFRAT-QDLDSLQLDLVGLTVSSVTVDGVPAAFFTHD----------------------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  118 dpdagNGELCIKVPSELWKHvdelKVLKIHINFSlDQPKGGLHFVVPSVEGSMAERGahVFSCGYQNSTRFWFPCVDSYS 197
Cdd:cd09603    62 -----GDKLVITLPRPLAAG----ETFTVTVRYS-GKPRPAGYPPGDGGGWEEGDDG--VWTAGQPEGASTWFPCNDHPD 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  198 ELCTWKLEFTVDAAMVAVSNGDLVETVyTHDMRKKTFHYMLTIPTAASNISLAIGPFEILVDPYMH--EVTHFCLPQLLP 275
Cdd:cd09603   130 DKATYDITVTVPAGLTVVSNGRLVSTT-TNGGGTTTWHWKMDYPIATYLVTLAVGRYAVVEDGSGGgiPLRYYVPPGDAA 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  276 LLKHTTSYLHEVFEFYEEILtCRYPYSCFKTVFIDEAYV--EvaaYASMSIFSTNLLHSAMIIDETpltrrcLAQSLAQQ 353
Cdd:cd09603   209 KAKASFARTPEMLDFFEELF-GPYPFEKYGQVVVPDLGGgmE---HQTATTYGNNFLNGDRGSERL------IAHELAHQ 278
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145559533  354 FFGCFISRMSWSDEWVLKGISGYIYGLWMKKTFGVNEYRHWIKEELDKIVAYELKTGGVLLHPIFGGG 421
Cdd:cd09603   279 WFGDSVTCADWADIWLNEGFATYAEWLWSEHKGGADAYRAYLAGQRQDYLNADPGPGRPPDPDDLFDR 346
M1 cd09595
Peptidase M1 family includes the catalytic domains of aminopeptidase N and leukotriene A4 ...
187-387 5.59e-08

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: 56.68  E-value: 5.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  187 RFWFPCVDSYSELCTWKLEFTVDAAMVAVSNGDLVETVYTHDMRKK-TFHYMLTIPTAAsnISLAIGPFEILVDPYM--- 262
Cdd:cd09595   117 RRIFPCIDHPAVKATFTVTITTPKKDLLASNGALVGEETGANGRKTyRFEDTPPIPTYL--VAVVVGDLEFKYVTVKsqp 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  263 -HEVTHFCLPQLLPLLKHTTSYLHEVFEFYEEILTCRYPYSCFKTVFIDEAYVEVAAYASMSIFSTNLLHSAMIIDETPL 341
Cdd:cd09595   195 rVGLSVYSEPLQVDQAQYAFDATRAALAWFEDYFGGPYPLPKYDLLAVPDFNSGAMENPGLITFRTTYLLRSKVTDTGAR 274
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 145559533  342 TRRCL-AQSLAQQFFGCFISRMSWSDEWVLKGISGYIYGLWMKKTFG 387
Cdd:cd09595   275 SIENViAHELAHQWFGNLVTMRWWNDLWLNEGFAVYYENRIMDATFG 321
M1_APN-Q_like cd09601
Peptidase M1 aminopeptidase N catalytic domain family which includes aminopeptidase N (APN), ...
190-302 2.48e-03

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: 41.80  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145559533  190 FPCVDsysEL---CTWKLEFTVDAAMVAVSNGDLVETVYTHDMRKKT-FHYMLTIPTaaSNISLAIGPFEILVDPYMHEV 265
Cdd:cd09601   129 FPCFD---EPafkATFDITITHPKGYTALSNMPPVESTELEDGWKTTtFETTPPMST--YLVAFVVGDFEYIESTTKSGV 203
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 145559533  266 TH--FCLPQLLPLLKHTTSYLHEVFEFYEEILTCRYPYS 302
Cdd:cd09601   204 PVrvYARPGKIEQGDFALEVAPKILDFYEDYFGIPYPLP 242
 
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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