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Conserved domains on  [gi|60498984|ref|NP_033720|]
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amine oxidase [copper-containing] 2 isoform b [Homo sapiens]

Protein Classification

Cu_amine_oxidN2 and Cu_amine_oxid domain-containing protein( domain architecture ID 10497919)

protein containing domains Cu_amine_oxidN2, Cu_amine_oxidN3, and Cu_amine_oxid

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cu_amine_oxid pfam01179
Copper amine oxidase, enzyme domain; Copper amine oxidases are a ubiquitous and novel group of ...
307-713 2.24e-150

Copper amine oxidase, enzyme domain; Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ). This family corresponds to the catalytic domain of the enzyme.


:

Pssm-ID: 460100  Cd Length: 403  Bit Score: 444.21  E-value: 2.24e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   307 PLQFSPQGSQYSVQGNLVVSSLWSFTFGHGVFSGLRIFDVRFQGERIAYEVSVQECVSIYGADSPKTMLTRYLDSSF-GL 385
Cdd:pfam01179   1 PNIVQPEGPSFTVDGNYVEWQGWSFRVGFNPREGLVLHDVRYKGRRILYRLSLSEMVVPYGDPDPPHHRKAAFDSGEyGF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   386 GRNSRGLVRGVDCPYQATMVDIHILVGKGAVQLLPGAVCVFEEAQGlPLRRHHNYLQNHfYGGLASSALVVRSVSSVGNY 465
Cdd:pfam01179  81 GRLANSLVLGCDCPGNITYLDAVFADSDGEPVTIPNAICIHEEDAG-PLWKHTDFRTGR-AEVTRNRRLVVRSIATVGNY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   466 DYIWDFVLYPNGALEGRVHATGYINTAFLKGGEEGLLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDVVFKPV 545
Cdd:pfam01179 159 DYIFDWIFYQDGTIEVEVRATGILSTAAIDPGEDGSPYGTRVAPGVLGSNHQHFFNFRLDPDIDGTKNSVVEVDVVPWPV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   546 aAPWNPEHwlQRPQLTRQVLGKEDLTAFSLGSPLPRYLYLAS-NQTNAWGHQRGYRIQIHSPLGIHIPLESD-MERALSW 623
Cdd:pfam01179 239 -GPENPYG--NAFKVERTVLETEKEAARDLDPSNPRYWKIVNpNKKNKSGKPVGYKLVPGPAHQPLLADPDSsVAKRAAF 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   624 GRYQLVVTQRKEEESQSSSIYHqNDIWTPTVTFADFI-NNETLLGEDLVAWVTASFLHIPHAEDIPntVTLGNRVGFLLR 702
Cdd:pfam01179 316 ARHHLWVTKYKDDELYAAGDYN-NQSRGPPVGLAKWIaDNESIENEDIVLWVTFGLTHIPRPEDFP--VMPVEHSGFLLR 392
                         410
                  ....*....|.
gi 60498984   703 PYNFFDEDPSI 713
Cdd:pfam01179 393 PFNFFDRNPAL 403
Cu_amine_oxidN3 pfam02728
Copper amine oxidase, N3 domain; This domain is the second or third structural domain in ...
165-263 1.08e-35

Copper amine oxidase, N3 domain; This domain is the second or third structural domain in copper amine oxidases, it is known as the N3 domain. Its function is uncertain. The catalytic domain can be found in pfam01179. Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ).


:

Pssm-ID: 426941 [Multi-domain]  Cd Length: 100  Bit Score: 130.14  E-value: 1.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   165 RPVLRAEFTQMWRHLKEVELPKAPIFLSSTFNYNGSTLAAVHATPRGLRS-GDRATWMALYHNISGVGLFLHPVGLELLL 243
Cdd:pfam02728   1 PPVTAEEYADIEEVIKTDPLFKEQLKKRGIFNGDDVYCDPWTVGPRGEKSgGRRLTKALCYYRTGGVNFYLHPIELELLV 80
                          90       100
                  ....*....|....*....|
gi 60498984   244 DHRALDPAHWTVQQVFYLGH 263
Cdd:pfam02728  81 DHDAKDVIEITDQKVRYPGP 100
Cu_amine_oxidN2 pfam02727
Copper amine oxidase, N2 domain; This domain is the first or second structural domain in ...
62-148 2.66e-34

Copper amine oxidase, N2 domain; This domain is the first or second structural domain in copper amine oxidases, it is known as the N2 domain. Its function is uncertain. The catalytic domain can be found in pfam01179. Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ).


:

Pssm-ID: 397027 [Multi-domain]  Cd Length: 87  Bit Score: 125.59  E-value: 2.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984    62 EELTAVMRFLTQRLGPGLVDAAQAQPSDNCIFSVELQLPPKAAALAHLDRGSPPPAREALAIVLFGGQPQPNVSELVVGP 141
Cdd:pfam02727   1 HPLDPLTSFEINKVESILKSSALFTLKDNSFFTVELEEPDKKAVLQWLDKGGPPPPREARVVILFGGQPHENVVDLAVGP 80

                  ....*..
gi 60498984   142 LPHPSYM 148
Cdd:pfam02727  81 LPSPRYM 87
 
Name Accession Description Interval E-value
Cu_amine_oxid pfam01179
Copper amine oxidase, enzyme domain; Copper amine oxidases are a ubiquitous and novel group of ...
307-713 2.24e-150

Copper amine oxidase, enzyme domain; Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ). This family corresponds to the catalytic domain of the enzyme.


Pssm-ID: 460100  Cd Length: 403  Bit Score: 444.21  E-value: 2.24e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   307 PLQFSPQGSQYSVQGNLVVSSLWSFTFGHGVFSGLRIFDVRFQGERIAYEVSVQECVSIYGADSPKTMLTRYLDSSF-GL 385
Cdd:pfam01179   1 PNIVQPEGPSFTVDGNYVEWQGWSFRVGFNPREGLVLHDVRYKGRRILYRLSLSEMVVPYGDPDPPHHRKAAFDSGEyGF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   386 GRNSRGLVRGVDCPYQATMVDIHILVGKGAVQLLPGAVCVFEEAQGlPLRRHHNYLQNHfYGGLASSALVVRSVSSVGNY 465
Cdd:pfam01179  81 GRLANSLVLGCDCPGNITYLDAVFADSDGEPVTIPNAICIHEEDAG-PLWKHTDFRTGR-AEVTRNRRLVVRSIATVGNY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   466 DYIWDFVLYPNGALEGRVHATGYINTAFLKGGEEGLLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDVVFKPV 545
Cdd:pfam01179 159 DYIFDWIFYQDGTIEVEVRATGILSTAAIDPGEDGSPYGTRVAPGVLGSNHQHFFNFRLDPDIDGTKNSVVEVDVVPWPV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   546 aAPWNPEHwlQRPQLTRQVLGKEDLTAFSLGSPLPRYLYLAS-NQTNAWGHQRGYRIQIHSPLGIHIPLESD-MERALSW 623
Cdd:pfam01179 239 -GPENPYG--NAFKVERTVLETEKEAARDLDPSNPRYWKIVNpNKKNKSGKPVGYKLVPGPAHQPLLADPDSsVAKRAAF 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   624 GRYQLVVTQRKEEESQSSSIYHqNDIWTPTVTFADFI-NNETLLGEDLVAWVTASFLHIPHAEDIPntVTLGNRVGFLLR 702
Cdd:pfam01179 316 ARHHLWVTKYKDDELYAAGDYN-NQSRGPPVGLAKWIaDNESIENEDIVLWVTFGLTHIPRPEDFP--VMPVEHSGFLLR 392
                         410
                  ....*....|.
gi 60498984   703 PYNFFDEDPSI 713
Cdd:pfam01179 393 PFNFFDRNPAL 403
TynA COG3733
Cu2+-containing amine oxidase [Secondary metabolites biosynthesis, transport and catabolism];
35-713 5.25e-56

Cu2+-containing amine oxidase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442947 [Multi-domain]  Cd Length: 646  Bit Score: 203.16  E-value: 5.25e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  35 PHCPSVSHRAQPWPHPgqsqlFADLSREELTAVMRFLtqrlgpglvdAAQAQPSDNCIF-SVELQLPPKAAALAHlDRGS 113
Cdd:COG3733   4 TLTGDLSAQAAAVPHP-----LDPLTAEEITAAVAIL----------RAAGLLGETTRFaSVELAEPPKAEVLAF-EPGD 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984 114 PPPaREALAIVLFGGQPQpnVSELVVgplphpSYMRDVTVERHggPLPYHRRPVLRAEFTqmwrhlkEVElpkapiflss 193
Cdd:COG3733  68 PVD-RRAFVVLLDRATGA--TYEAVV------SLTAGEVVSWE--EIPGVQPPILLEEFE-------EAE---------- 119
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984 194 tfnyngstlAAVHATP--------RGLRSGDRA---TWMAlyhnisgvGLFLHP--VGLELLldhRALdpahwTVQQVFY 260
Cdd:COG3733 120 ---------EIVKADPrwqaalakRGITDFDLVmvdPWSA--------GYFGIPeeRGRRLL---RVL-----SFVRSDP 174
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984 261 LGHYYA----------DLGQLErefksgrleVVR------VPLPPPNGASSLRSRNSPG-PLPPLQFS-PQGSQYSVQGN 322
Cdd:COG3733 175 EDNPYAhpieglvavvDLNTME---------VVRvedhgvVPVPPEPGNYDPELVGPLRtDLKPLEITqPEGPSFTVDGN 245
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984 323 LVVSSLWSFTFGHGVFSGLRIFDVRFQG---ER-IAYEVSVQECVSIYGADSP----KTmltrYLDSS-FGLGRNSRGLV 393
Cdd:COG3733 246 EVSWQNWSFRVGFNPREGLVLHQVTYNDggrERpILYRASLSEMVVPYGDPSPthywKN----AFDAGeYGLGRLANSLE 321
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984 394 RGVDCPYQATMVDIHILVGKGAVQLLPGAVCVFEEAQGlPLRRHHNYLQNHFYGgLASSALVVRSVSSVGNYDYIWDFVL 473
Cdd:COG3733 322 LGCDCLGEIHYLDAVLADSDGEPVTIPNAICIHEEDYG-VLWKHTDFRTGRAEV-RRSRRLVVSFIATVGNYDYGFYWYF 399
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984 474 YPNGALEGRVHATGYINTAFLKGGEEGlLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDVVFKPVaAPWNPEH 553
Cdd:COG3733 400 YQDGTIEVEVKLTGIVFTGAVPPGEDP-PYGTLVAPGLYAPNHQHFFNARLDMDVDGERNSVYEVDTVAVPI-GPDNPYG 477
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984 554 ---WLQRPQLTRQVLGKEDLTAFSlgsplPRYLYLAS-NQTNAWGHQRGYRI----QIHSPLGihiPLESDMERAlSWGR 625
Cdd:COG3733 478 nafTTEATPLETESEAARDADPAT-----GRYWKIVNpNKTNRLGEPVGYKLvpggNPTLLAD---PDSSIAKRA-GFAT 548
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984 626 YQLVVTQRKEEESQSSSIY-HQNDiwtPTVTFADFI-NNETLLGEDLVAWVTASFLHIPHAEDIPntVTLGNRVGFLLRP 703
Cdd:COG3733 549 KHLWVTPYDPDERYAAGDYpNQSP---GGAGLPAWTaDDRSIENEDVVLWYTFGVTHVPRPEDWP--VMPVDYAGFKLKP 623
                       730
                ....*....|
gi 60498984 704 YNFFDEDPSI 713
Cdd:COG3733 624 VGFFDRNPAL 633
tynA PRK11504
primary-amine oxidase;
37-718 7.87e-42

primary-amine oxidase;


Pssm-ID: 236919 [Multi-domain]  Cd Length: 647  Bit Score: 162.38  E-value: 7.87e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   37 CPSVSHRAQPW-PHPgqsqlFADLSREELTAVMRFLtqrlgpglvdAAQAQPSDNCIF-SVELQLPPKAAALAHlDRGSP 114
Cdd:PRK11504   1 TVEMATTTAAAvSHP-----LDPLTAAEIEAAVAIL----------RAEGLLGESTRFvSIELAEPPKAEVLAF-DPGDP 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  115 PPaREALAIVLFGGQPqpNVSELVVgplphpSYMRDVTVERHggPLPYHRRPVLRAEFTqmwrhlkEVE--LPKAPIFLs 192
Cdd:PRK11504  65 ID-RRAFVVLYDRATG--KTYEAVV------SLTAGEVVSWE--EIPGVQPPILLEEFE-------ECEevVRADPRWQ- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  193 stfnyngstlAAVHAtpRGLRSGDRA---TWMAlyhnisgvGLFLHP--VGLELL--LDHRALDPAhwtvqqvfylGHYY 265
Cdd:PRK11504 126 ----------AALAK--RGITDFDLVmvdPWSA--------GYFGEPeeRGRRLArgLAFVRADPG----------DNGY 175
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  266 A----------DLGQLERefksgrLEVV---RVPLPPPNGASSLRSRNSPG-PLPPLQ-FSPQGSQYSVQGNLVVSSLWS 330
Cdd:PRK11504 176 ArpieglvavvDLNTMEV------LRVEdhgVVPIPAEDGNYDPEFIPPLRtDLKPLEiTQPEGPSFTVDGNEVEWQKWS 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  331 FTFGHGVFSGLRIFDVRFQ-GER---IAYEVSVQECVSIYGADSPktmlTRYLDSSF-----GLGRNSRGLVRGVDCPYQ 401
Cdd:PRK11504 250 FRVGFNPREGLVLHQVSYDdGGRerpILYRASLSEMVVPYGDPSP----THYWKNAFdageyGLGRLANSLELGCDCLGE 325
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  402 ATMVDIHILVGKGAVQLLPGAVCVFEEAQGLpLRRHHNYLQNHFYGgLASSALVVRSVSSVGNYDYIWDFVLYPNGALEG 481
Cdd:PRK11504 326 IRYFDAVLADSDGEPYTIKNAICMHEEDYGI-LWKHTDFRTGSAEV-RRSRRLVISFFATVGNYDYGFYWYFYQDGTIEF 403
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  482 RVHATGYINTAFLKGGEEGlLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDVVFKPVaAPWNPEH---WLQRP 558
Cdd:PRK11504 404 EVKLTGIVFTAAVPPGETP-PYGTLVAPGLYAPNHQHFFNARLDMDVDGPGNSVYEVNSVPVPM-GPDNPHGnafYTRET 481
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  559 QLTRQVLGKEDLtAFSLGsplpRYLYLAS-NQTNAWGHQRGYRIQIHSPLGIHIPLESDMERALSWGRYQLVVTQRKEEE 637
Cdd:PRK11504 482 LLETESEAARDA-DPSTG----RYWKIVNpNKKNRLGEPVAYKLVPGGNPPLLADPGSSIRQRAGFATHHLWVTPYDPDE 556
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  638 SQSSSIY---HQNDIWTPTVTFADfinnETLLGEDLVAWVTASFLHIPHAEDIPntVTLGNRVGFLLRPYNFFDEDPSIF 714
Cdd:PRK11504 557 RYAAGDYpnqSAGGDGLPAYIAAD----RSIENTDVVLWYTFGITHVPRPEDWP--VMPVDYAGFKLKPVGFFDRNPALD 630

                 ....
gi 60498984  715 SPGS 718
Cdd:PRK11504 631 LPPE 634
Cu_amine_oxidN3 pfam02728
Copper amine oxidase, N3 domain; This domain is the second or third structural domain in ...
165-263 1.08e-35

Copper amine oxidase, N3 domain; This domain is the second or third structural domain in copper amine oxidases, it is known as the N3 domain. Its function is uncertain. The catalytic domain can be found in pfam01179. Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ).


Pssm-ID: 426941 [Multi-domain]  Cd Length: 100  Bit Score: 130.14  E-value: 1.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   165 RPVLRAEFTQMWRHLKEVELPKAPIFLSSTFNYNGSTLAAVHATPRGLRS-GDRATWMALYHNISGVGLFLHPVGLELLL 243
Cdd:pfam02728   1 PPVTAEEYADIEEVIKTDPLFKEQLKKRGIFNGDDVYCDPWTVGPRGEKSgGRRLTKALCYYRTGGVNFYLHPIELELLV 80
                          90       100
                  ....*....|....*....|
gi 60498984   244 DHRALDPAHWTVQQVFYLGH 263
Cdd:pfam02728  81 DHDAKDVIEITDQKVRYPGP 100
Cu_amine_oxidN2 pfam02727
Copper amine oxidase, N2 domain; This domain is the first or second structural domain in ...
62-148 2.66e-34

Copper amine oxidase, N2 domain; This domain is the first or second structural domain in copper amine oxidases, it is known as the N2 domain. Its function is uncertain. The catalytic domain can be found in pfam01179. Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ).


Pssm-ID: 397027 [Multi-domain]  Cd Length: 87  Bit Score: 125.59  E-value: 2.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984    62 EELTAVMRFLTQRLGPGLVDAAQAQPSDNCIFSVELQLPPKAAALAHLDRGSPPPAREALAIVLFGGQPQPNVSELVVGP 141
Cdd:pfam02727   1 HPLDPLTSFEINKVESILKSSALFTLKDNSFFTVELEEPDKKAVLQWLDKGGPPPPREARVVILFGGQPHENVVDLAVGP 80

                  ....*..
gi 60498984   142 LPHPSYM 148
Cdd:pfam02727  81 LPSPRYM 87
 
Name Accession Description Interval E-value
Cu_amine_oxid pfam01179
Copper amine oxidase, enzyme domain; Copper amine oxidases are a ubiquitous and novel group of ...
307-713 2.24e-150

Copper amine oxidase, enzyme domain; Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ). This family corresponds to the catalytic domain of the enzyme.


Pssm-ID: 460100  Cd Length: 403  Bit Score: 444.21  E-value: 2.24e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   307 PLQFSPQGSQYSVQGNLVVSSLWSFTFGHGVFSGLRIFDVRFQGERIAYEVSVQECVSIYGADSPKTMLTRYLDSSF-GL 385
Cdd:pfam01179   1 PNIVQPEGPSFTVDGNYVEWQGWSFRVGFNPREGLVLHDVRYKGRRILYRLSLSEMVVPYGDPDPPHHRKAAFDSGEyGF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   386 GRNSRGLVRGVDCPYQATMVDIHILVGKGAVQLLPGAVCVFEEAQGlPLRRHHNYLQNHfYGGLASSALVVRSVSSVGNY 465
Cdd:pfam01179  81 GRLANSLVLGCDCPGNITYLDAVFADSDGEPVTIPNAICIHEEDAG-PLWKHTDFRTGR-AEVTRNRRLVVRSIATVGNY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   466 DYIWDFVLYPNGALEGRVHATGYINTAFLKGGEEGLLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDVVFKPV 545
Cdd:pfam01179 159 DYIFDWIFYQDGTIEVEVRATGILSTAAIDPGEDGSPYGTRVAPGVLGSNHQHFFNFRLDPDIDGTKNSVVEVDVVPWPV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   546 aAPWNPEHwlQRPQLTRQVLGKEDLTAFSLGSPLPRYLYLAS-NQTNAWGHQRGYRIQIHSPLGIHIPLESD-MERALSW 623
Cdd:pfam01179 239 -GPENPYG--NAFKVERTVLETEKEAARDLDPSNPRYWKIVNpNKKNKSGKPVGYKLVPGPAHQPLLADPDSsVAKRAAF 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   624 GRYQLVVTQRKEEESQSSSIYHqNDIWTPTVTFADFI-NNETLLGEDLVAWVTASFLHIPHAEDIPntVTLGNRVGFLLR 702
Cdd:pfam01179 316 ARHHLWVTKYKDDELYAAGDYN-NQSRGPPVGLAKWIaDNESIENEDIVLWVTFGLTHIPRPEDFP--VMPVEHSGFLLR 392
                         410
                  ....*....|.
gi 60498984   703 PYNFFDEDPSI 713
Cdd:pfam01179 393 PFNFFDRNPAL 403
TynA COG3733
Cu2+-containing amine oxidase [Secondary metabolites biosynthesis, transport and catabolism];
35-713 5.25e-56

Cu2+-containing amine oxidase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442947 [Multi-domain]  Cd Length: 646  Bit Score: 203.16  E-value: 5.25e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  35 PHCPSVSHRAQPWPHPgqsqlFADLSREELTAVMRFLtqrlgpglvdAAQAQPSDNCIF-SVELQLPPKAAALAHlDRGS 113
Cdd:COG3733   4 TLTGDLSAQAAAVPHP-----LDPLTAEEITAAVAIL----------RAAGLLGETTRFaSVELAEPPKAEVLAF-EPGD 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984 114 PPPaREALAIVLFGGQPQpnVSELVVgplphpSYMRDVTVERHggPLPYHRRPVLRAEFTqmwrhlkEVElpkapiflss 193
Cdd:COG3733  68 PVD-RRAFVVLLDRATGA--TYEAVV------SLTAGEVVSWE--EIPGVQPPILLEEFE-------EAE---------- 119
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984 194 tfnyngstlAAVHATP--------RGLRSGDRA---TWMAlyhnisgvGLFLHP--VGLELLldhRALdpahwTVQQVFY 260
Cdd:COG3733 120 ---------EIVKADPrwqaalakRGITDFDLVmvdPWSA--------GYFGIPeeRGRRLL---RVL-----SFVRSDP 174
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984 261 LGHYYA----------DLGQLErefksgrleVVR------VPLPPPNGASSLRSRNSPG-PLPPLQFS-PQGSQYSVQGN 322
Cdd:COG3733 175 EDNPYAhpieglvavvDLNTME---------VVRvedhgvVPVPPEPGNYDPELVGPLRtDLKPLEITqPEGPSFTVDGN 245
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984 323 LVVSSLWSFTFGHGVFSGLRIFDVRFQG---ER-IAYEVSVQECVSIYGADSP----KTmltrYLDSS-FGLGRNSRGLV 393
Cdd:COG3733 246 EVSWQNWSFRVGFNPREGLVLHQVTYNDggrERpILYRASLSEMVVPYGDPSPthywKN----AFDAGeYGLGRLANSLE 321
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984 394 RGVDCPYQATMVDIHILVGKGAVQLLPGAVCVFEEAQGlPLRRHHNYLQNHFYGgLASSALVVRSVSSVGNYDYIWDFVL 473
Cdd:COG3733 322 LGCDCLGEIHYLDAVLADSDGEPVTIPNAICIHEEDYG-VLWKHTDFRTGRAEV-RRSRRLVVSFIATVGNYDYGFYWYF 399
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984 474 YPNGALEGRVHATGYINTAFLKGGEEGlLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDVVFKPVaAPWNPEH 553
Cdd:COG3733 400 YQDGTIEVEVKLTGIVFTGAVPPGEDP-PYGTLVAPGLYAPNHQHFFNARLDMDVDGERNSVYEVDTVAVPI-GPDNPYG 477
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984 554 ---WLQRPQLTRQVLGKEDLTAFSlgsplPRYLYLAS-NQTNAWGHQRGYRI----QIHSPLGihiPLESDMERAlSWGR 625
Cdd:COG3733 478 nafTTEATPLETESEAARDADPAT-----GRYWKIVNpNKTNRLGEPVGYKLvpggNPTLLAD---PDSSIAKRA-GFAT 548
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984 626 YQLVVTQRKEEESQSSSIY-HQNDiwtPTVTFADFI-NNETLLGEDLVAWVTASFLHIPHAEDIPntVTLGNRVGFLLRP 703
Cdd:COG3733 549 KHLWVTPYDPDERYAAGDYpNQSP---GGAGLPAWTaDDRSIENEDVVLWYTFGVTHVPRPEDWP--VMPVDYAGFKLKP 623
                       730
                ....*....|
gi 60498984 704 YNFFDEDPSI 713
Cdd:COG3733 624 VGFFDRNPAL 633
tynA PRK11504
primary-amine oxidase;
37-718 7.87e-42

primary-amine oxidase;


Pssm-ID: 236919 [Multi-domain]  Cd Length: 647  Bit Score: 162.38  E-value: 7.87e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   37 CPSVSHRAQPW-PHPgqsqlFADLSREELTAVMRFLtqrlgpglvdAAQAQPSDNCIF-SVELQLPPKAAALAHlDRGSP 114
Cdd:PRK11504   1 TVEMATTTAAAvSHP-----LDPLTAAEIEAAVAIL----------RAEGLLGESTRFvSIELAEPPKAEVLAF-DPGDP 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  115 PPaREALAIVLFGGQPqpNVSELVVgplphpSYMRDVTVERHggPLPYHRRPVLRAEFTqmwrhlkEVE--LPKAPIFLs 192
Cdd:PRK11504  65 ID-RRAFVVLYDRATG--KTYEAVV------SLTAGEVVSWE--EIPGVQPPILLEEFE-------ECEevVRADPRWQ- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  193 stfnyngstlAAVHAtpRGLRSGDRA---TWMAlyhnisgvGLFLHP--VGLELL--LDHRALDPAhwtvqqvfylGHYY 265
Cdd:PRK11504 126 ----------AALAK--RGITDFDLVmvdPWSA--------GYFGEPeeRGRRLArgLAFVRADPG----------DNGY 175
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  266 A----------DLGQLERefksgrLEVV---RVPLPPPNGASSLRSRNSPG-PLPPLQ-FSPQGSQYSVQGNLVVSSLWS 330
Cdd:PRK11504 176 ArpieglvavvDLNTMEV------LRVEdhgVVPIPAEDGNYDPEFIPPLRtDLKPLEiTQPEGPSFTVDGNEVEWQKWS 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  331 FTFGHGVFSGLRIFDVRFQ-GER---IAYEVSVQECVSIYGADSPktmlTRYLDSSF-----GLGRNSRGLVRGVDCPYQ 401
Cdd:PRK11504 250 FRVGFNPREGLVLHQVSYDdGGRerpILYRASLSEMVVPYGDPSP----THYWKNAFdageyGLGRLANSLELGCDCLGE 325
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  402 ATMVDIHILVGKGAVQLLPGAVCVFEEAQGLpLRRHHNYLQNHFYGgLASSALVVRSVSSVGNYDYIWDFVLYPNGALEG 481
Cdd:PRK11504 326 IRYFDAVLADSDGEPYTIKNAICMHEEDYGI-LWKHTDFRTGSAEV-RRSRRLVISFFATVGNYDYGFYWYFYQDGTIEF 403
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  482 RVHATGYINTAFLKGGEEGlLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDVVFKPVaAPWNPEH---WLQRP 558
Cdd:PRK11504 404 EVKLTGIVFTAAVPPGETP-PYGTLVAPGLYAPNHQHFFNARLDMDVDGPGNSVYEVNSVPVPM-GPDNPHGnafYTRET 481
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  559 QLTRQVLGKEDLtAFSLGsplpRYLYLAS-NQTNAWGHQRGYRIQIHSPLGIHIPLESDMERALSWGRYQLVVTQRKEEE 637
Cdd:PRK11504 482 LLETESEAARDA-DPSTG----RYWKIVNpNKKNRLGEPVAYKLVPGGNPPLLADPGSSIRQRAGFATHHLWVTPYDPDE 556
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  638 SQSSSIY---HQNDIWTPTVTFADfinnETLLGEDLVAWVTASFLHIPHAEDIPntVTLGNRVGFLLRPYNFFDEDPSIF 714
Cdd:PRK11504 557 RYAAGDYpnqSAGGDGLPAYIAAD----RSIENTDVVLWYTFGITHVPRPEDWP--VMPVDYAGFKLKPVGFFDRNPALD 630

                 ....
gi 60498984  715 SPGS 718
Cdd:PRK11504 631 LPPE 634
tynA PRK14696
primary-amine oxidase;
285-713 9.84e-40

primary-amine oxidase;


Pssm-ID: 184793 [Multi-domain]  Cd Length: 721  Bit Score: 156.91  E-value: 9.84e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  285 VPLPPPNGASSLRSRNSPgPLPPLQFS-PQGSQYSVQGNLVVSSLWSFTFGHGVFSGLRIFDVRF--QGER--IAYEVSV 359
Cdd:PRK14696 278 VPVPMTARPYDGRDRVAP-AVKPLQIIePEGKNYTITGDTIHWRNWDFHLSLDSRVGPMLSTVTYndNGTKrkVMYEGSL 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  360 QECVSIYGADSPKTMLTRYLDS-SFGLGRNSRGLVRGVDCPYQATMVDIHILVGKGAVQLLPGAVCVFEEAQGlPLRRHH 438
Cdd:PRK14696 357 GGMIVPYGDPDIGWYFKAYLDSgDYGMGTLTSPIARGKDAPSNAVLLDETIADYTGVPMEIPRAIAVFERYAG-PEYKHQ 435
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  439 NYLQNHFygGLASSALVVRSVSSVGNYDYIWDFVLYPNGALEGRVHATGyinTAFLKG----------GEEGLLFGNRVG 508
Cdd:PRK14696 436 EMGQPNV--STERRELVVRWISTVGNYDYIFDWVFHENGTIGIDAGATG---IEAVKGvkaktmhdetAKEDTRYGTLID 510
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  509 ERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDVVFKPVAAPWNPEHWLQRPQltrQVLGKEDLTAFSLGSPLPRYLYlASN 588
Cdd:PRK14696 511 HNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNTAGGPRTSTMQVNQ---YNIGNEQDAAQKFDPGTIRLLS-NPN 586
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  589 QTNAWGHQRGYRIqIHSPLGIHiPLESDMERA--------LSWGRYQLVVTQRKEEESQSSSIYHQNDiwTPTVTFADFI 660
Cdd:PRK14696 587 KENRMGNPVSYQI-IPYAGGTH-PVAKGANFApdewiyhrLSFMDKQLWVTRYHPGERFPEGKYPNRS--THDTGLGQYS 662
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 60498984  661 -NNETLLGEDLVAWVTASFLHIPHAEDIPNTVTlgNRVGFLLRPYNFFDEDPSI 713
Cdd:PRK14696 663 kDNESLDNTDAVVWMTTGTTHVARAEEWPIMPT--EWVHTLLKPWNFFDETPTL 714
Cu_amine_oxidN3 pfam02728
Copper amine oxidase, N3 domain; This domain is the second or third structural domain in ...
165-263 1.08e-35

Copper amine oxidase, N3 domain; This domain is the second or third structural domain in copper amine oxidases, it is known as the N3 domain. Its function is uncertain. The catalytic domain can be found in pfam01179. Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ).


Pssm-ID: 426941 [Multi-domain]  Cd Length: 100  Bit Score: 130.14  E-value: 1.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   165 RPVLRAEFTQMWRHLKEVELPKAPIFLSSTFNYNGSTLAAVHATPRGLRS-GDRATWMALYHNISGVGLFLHPVGLELLL 243
Cdd:pfam02728   1 PPVTAEEYADIEEVIKTDPLFKEQLKKRGIFNGDDVYCDPWTVGPRGEKSgGRRLTKALCYYRTGGVNFYLHPIELELLV 80
                          90       100
                  ....*....|....*....|
gi 60498984   244 DHRALDPAHWTVQQVFYLGH 263
Cdd:pfam02728  81 DHDAKDVIEITDQKVRYPGP 100
Cu_amine_oxidN2 pfam02727
Copper amine oxidase, N2 domain; This domain is the first or second structural domain in ...
62-148 2.66e-34

Copper amine oxidase, N2 domain; This domain is the first or second structural domain in copper amine oxidases, it is known as the N2 domain. Its function is uncertain. The catalytic domain can be found in pfam01179. Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyze the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ).


Pssm-ID: 397027 [Multi-domain]  Cd Length: 87  Bit Score: 125.59  E-value: 2.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984    62 EELTAVMRFLTQRLGPGLVDAAQAQPSDNCIFSVELQLPPKAAALAHLDRGSPPPAREALAIVLFGGQPQPNVSELVVGP 141
Cdd:pfam02727   1 HPLDPLTSFEINKVESILKSSALFTLKDNSFFTVELEEPDKKAVLQWLDKGGPPPPREARVVILFGGQPHENVVDLAVGP 80

                  ....*..
gi 60498984   142 LPHPSYM 148
Cdd:pfam02727  81 LPSPRYM 87
PLN02566 PLN02566
amine oxidase (copper-containing)
95-711 5.02e-34

amine oxidase (copper-containing)


Pssm-ID: 215306 [Multi-domain]  Cd Length: 646  Bit Score: 138.85  E-value: 5.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984   95 VELQLPPKAAALAHL---DRGSPPPAREALAIVLFGGQPQpnvsELVVGpLPHPSYMRDVTVERHGGPlPYhrrpvlraE 171
Cdd:PLN02566  55 LDLEEPEKRDVLKWLssnPSNKSPPPRRAKVVVRAGGETY----ELIVD-LATGSITSSRVYTGHGYP-PL--------T 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  172 FTQMWRHLKeveLP-KAPIFLSSTFNyNGSTLAAVHATP-----RGLRSGDRATWMALYHNISGVGLFLHPV-GLELLLD 244
Cdd:PLN02566 121 FIELFQASK---LPlKYPKFKKSILR-RGLNISEVSCIPftvgwYGETVTKRALKISCFYRGGSVNVFARPIeGISILID 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  245 hraLDpahwTVQQVFYLGHYyadlgqlerefksgrlevvRVPLPPPNGaSSLRSRNSPGPLPplqFSPQGSQYSVQGNLV 324
Cdd:PLN02566 197 ---VD----SMQIIKYSDRF-------------------RAPLPKAEG-TDFRTKHKPFSFP---CNVSDSGFTILGHRV 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  325 VSSLWSFTFGHGVFSGLRI-----FDVRFQG-ERIAYEVSVQECVSIYGADSPKTMLTRYLD-SSFGLGRNSRGLVRGVD 397
Cdd:PLN02566 247 KWANWDFHVGFDARAGVTIstasvFDAKVKRfRRVLYRGHVSETFVPYMDPTSEWYFRTFMDiGEFGFGRSAVTLQPLID 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  398 CPYQATMVDIHILVGKGAVQLLPGAVCVFEEAQGLPLRRHH--NYLQNHFYGGLASSALVVRSVSSVGNYDYIWDFVLYP 475
Cdd:PLN02566 327 CPANAVYLDGYVAGADGQAQKMTNVICIFERYSGDVAFRHTeiNVPGRVIRSGEPEISLVVRMVATLGNYDYILDWEFKK 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  476 NGA------LEG--RVHATGYINTAFLKggEEglLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDVVFKPVAA 547
Cdd:PLN02566 407 SGSikvgvdLTGvlEMKATSYTNNDQIT--KD--VYGTLVAENTIAVNHDHFLTYYLDLDVDGNGNSFVKAKLQTARVTA 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  548 PWNPEHWLQRPQLTRQVLGKEDLTAFSLGSPLPRYLYLASNQTNAWGHQRGYRIQIHSPLGIHIPLESDMERALSWGRYQ 627
Cdd:PLN02566 483 VNASSPRKSYWTVVKETAKTEAEGRIRLGSEPAELLIVNPNKKTKLGNQVGYRLITGQPVTSLLSDDDYPQIRAAYTKYQ 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60498984  628 LVVTQRKEEESQSSSIY----HQND---IWTPtvtfadfiNNETLLGEDLVAWVTASFLHIPHAEDIPNTVTLGNrvGFL 700
Cdd:PLN02566 563 VWVTAYNKSERWAGGFYadrsRGDDglaVWSS--------RNREIENKDIVLWYTVGFHHIPYQEDFPVMPTLHG--GFE 632
                        650
                 ....*....|.
gi 60498984  701 LRPYNFFDEDP 711
Cdd:PLN02566 633 LRPANFFESNP 643
 
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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