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Conserved domains on  [gi|741963933|ref|XP_010814607|]
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primary amine oxidase, liver isozyme isoform X2 [Bos taurus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cu_amine_oxid super family cl38029
Copper amine oxidase, enzyme domain; Copper amine oxidases are a ubiquitous and novel group of ...
 296-479 1.06e-62

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.


The actual alignment was detected with superfamily member pfam01179:

Pssm-ID: 460100  Cd Length: 403  Bit Score: 211.16  E-value: 1.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933  296 GLENWVWAEDMafvpmvVPWSP---EHQIQRLQVTRKQLETEEQAAFPLGGPSPRYLYLAS-NQSNKWGHPRGYRIQTVS 371
Cdd:pfam01179 223 GTKNSVVEVDV------VPWPVgpeNPYGNAFKVERTVLETEKEAARDLDPSNPRYWKIVNpNKKNKSGKPVGYKLVPGP 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933  372 FAGGPLPQNSS-MERAFSWARYQLAVTQRKEGEPSSTSIYNlNDPWSPTLDFSDFI-NNETIAGQDLVAWVTAGFLHIPH 449
Cdd:pfam01179 297 AHQPLLADPDSsVAKRAAFARHHLWVTKYKDDELYAAGDYN-NQSRGPPVGLAKWIaDNESIENEDIVLWVTFGLTHIPR 375

                         170       180       190
                  ....*....|....*....|....*....|
gi 741963933  450 AEDIPntVTVGNGVGFFLRPYNFFDQEPSM 479
Cdd:pfam01179 376 PEDFP--VMPVEHSGFLLRPFNFFDRNPAL 403
Cu_amine_oxidN3 pfam02728
Copper amine oxidase, N3 domain; This domain is the second or third structural domain in ...
 168-268 1.07e-36

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: 131.68  E-value: 1.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933  168 RPVLLREYLDIDQMIFNreLPQAAGVLHHCCSYKQGGQKLVTMNSAPRGVQS-GDRATWFGLYYNISGAGFFLHPVGLEL 246
Cdd:pfam02728   1 PPVTAEEYADIEEVIKT--DPLFKEQLKKRGIFNGDDVYCDPWTVGPRGEKSgGRRLTKALCYYRTGGVNFYLHPIELEL 78

                          90       100
                  ....*....|....*....|..
gi 741963933  247 LVDHKALDPAQWTIQKVFFQGR 268
Cdd:pfam02728  79 LVDHDAKDVIEITDQKVRYPGP 100
Cu_amine_oxidN2 pfam02727
Copper amine oxidase, N2 domain; This domain is the first or second structural domain in ...
 65-151 4.50e-35

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: 126.75  E-value: 4.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933   65 EELTAVMSFLTQQLGPDLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPPAREALAIVFFGKQPQPNVTELVVGP 144
Cdd:pfam02727   1 HPLDPLTSFEINKVESILKSSALFTLKDNSFFTVELEEPDKKAVLQWLDKGGPPPPREARVVILFGGQPHENVVDLAVGP 80


                  ....*..
gi 741963933  145 LPQPSYM 151
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 ...
 296-479 1.06e-62

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: 211.16  E-value: 1.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933  296 GLENWVWAEDMafvpmvVPWSP---EHQIQRLQVTRKQLETEEQAAFPLGGPSPRYLYLAS-NQSNKWGHPRGYRIQTVS 371
Cdd:pfam01179 223 GTKNSVVEVDV------VPWPVgpeNPYGNAFKVERTVLETEKEAARDLDPSNPRYWKIVNpNKKNKSGKPVGYKLVPGP 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933  372 FAGGPLPQNSS-MERAFSWARYQLAVTQRKEGEPSSTSIYNlNDPWSPTLDFSDFI-NNETIAGQDLVAWVTAGFLHIPH 449
Cdd:pfam01179 297 AHQPLLADPDSsVAKRAAFARHHLWVTKYKDDELYAAGDYN-NQSRGPPVGLAKWIaDNESIENEDIVLWVTFGLTHIPR 375

                         170       180       190
                  ....*....|....*....|....*....|
gi 741963933  450 AEDIPntVTVGNGVGFFLRPYNFFDQEPSM 479
Cdd:pfam01179 376 PEDFP--VMPVEHSGFLLRPFNFFDRNPAL 403
Cu_amine_oxidN3 pfam02728
Copper amine oxidase, N3 domain; This domain is the second or third structural domain in ...
 168-268 1.07e-36

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: 131.68  E-value: 1.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933  168 RPVLLREYLDIDQMIFNreLPQAAGVLHHCCSYKQGGQKLVTMNSAPRGVQS-GDRATWFGLYYNISGAGFFLHPVGLEL 246
Cdd:pfam02728   1 PPVTAEEYADIEEVIKT--DPLFKEQLKKRGIFNGDDVYCDPWTVGPRGEKSgGRRLTKALCYYRTGGVNFYLHPIELEL 78

                          90       100
                  ....*....|....*....|..
gi 741963933  247 LVDHKALDPAQWTIQKVFFQGR 268
Cdd:pfam02728  79 LVDHDAKDVIEITDQKVRYPGP 100
Cu_amine_oxidN2 pfam02727
Copper amine oxidase, N2 domain; This domain is the first or second structural domain in ...
 65-151 4.50e-35

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: 126.75  E-value: 4.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933   65 EELTAVMSFLTQQLGPDLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPPAREALAIVFFGKQPQPNVTELVVGP 144
Cdd:pfam02727   1 HPLDPLTSFEINKVESILKSSALFTLKDNSFFTVELEEPDKKAVLQWLDKGGPPPPREARVVILFGGQPHENVVDLAVGP 80


                  ....*..
gi 741963933  145 LPQPSYM 151
Cdd:pfam02727  81 LPSPRYM 87
TynA COG3733
Cu2+-containing amine oxidase [Secondary metabolites biosynthesis, transport and catabolism];
296-480 8.93e-16

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


Pssm-ID: 442947 [Multi-domain]  Cd Length: 646  Bit Score: 80.28  E-value: 8.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933 296 GLENWVwaEDMAFVPmvVPWSPEHQI-QRLQVTRKQLETEEQAAFPLGGPSPRYLYLAS-NQSNKWGHPRGYRIqtVSFA 373
Cdd:COG3733  455 GERNSV--YEVDTVA--VPIGPDNPYgNAFTTEATPLETESEAARDADPATGRYWKIVNpNKTNRLGEPVGYKL--VPGG 528

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933 374 GGPL---PQNSSMERAfSWARYQLAVTQRKEGEPSSTSIY-NLNDP------WSPtldfsdfiNNETIAGQDLVAWVTAG 443
Cdd:COG3733  529 NPTLladPDSSIAKRA-GFATKHLWVTPYDPDERYAAGDYpNQSPGgaglpaWTA--------DDRSIENEDVVLWYTFG 599

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 741963933 444 FLHIPHAEDIPntVTVGNGVGFFLRPYNFFDQEPSMD 480
Cdd:COG3733  600 VTHVPRPEDWP--VMPVDYAGFKLKPVGFFDRNPALD 634
tynA PRK14696
primary-amine oxidase;
324-479 8.24e-12

primary-amine oxidase;


Pssm-ID: 184793 [Multi-domain]  Cd Length: 721  Bit Score: 67.93  E-value: 8.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933 324 LQVTRKQLETEEQAAFPLGgPSPRYLYLASNQSNKWGHPRGYriQTVSFAGGPLP--------QNSSMERAFSWARYQLA 395
Cdd:PRK14696 557 MQVNQYNIGNEQDAAQKFD-PGTIRLLSNPNKENRMGNPVSY--QIIPYAGGTHPvakganfaPDEWIYHRLSFMDKQLW 633

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933 396 VTQRKEGEPSSTSIYnlndPWSPTLD--FSDFI-NNETIAGQDLVAWVTAGFLHIPHAEDIPNTVTvgNGVGFFLRPYNF 472
Cdd:PRK14696 634 VTRYHPGERFPEGKY----PNRSTHDtgLGQYSkDNESLDNTDAVVWMTTGTTHVARAEEWPIMPT--EWVHTLLKPWNF 707


                 ....*..
gi 741963933 473 FDQEPSM 479
Cdd:PRK14696 708 FDETPTL 714
 
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 ...
 296-479 1.06e-62

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: 211.16  E-value: 1.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933  296 GLENWVWAEDMafvpmvVPWSP---EHQIQRLQVTRKQLETEEQAAFPLGGPSPRYLYLAS-NQSNKWGHPRGYRIQTVS 371
Cdd:pfam01179 223 GTKNSVVEVDV------VPWPVgpeNPYGNAFKVERTVLETEKEAARDLDPSNPRYWKIVNpNKKNKSGKPVGYKLVPGP 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933  372 FAGGPLPQNSS-MERAFSWARYQLAVTQRKEGEPSSTSIYNlNDPWSPTLDFSDFI-NNETIAGQDLVAWVTAGFLHIPH 449
Cdd:pfam01179 297 AHQPLLADPDSsVAKRAAFARHHLWVTKYKDDELYAAGDYN-NQSRGPPVGLAKWIaDNESIENEDIVLWVTFGLTHIPR 375

                         170       180       190
                  ....*....|....*....|....*....|
gi 741963933  450 AEDIPntVTVGNGVGFFLRPYNFFDQEPSM 479
Cdd:pfam01179 376 PEDFP--VMPVEHSGFLLRPFNFFDRNPAL 403
Cu_amine_oxidN3 pfam02728
Copper amine oxidase, N3 domain; This domain is the second or third structural domain in ...
 168-268 1.07e-36

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: 131.68  E-value: 1.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933  168 RPVLLREYLDIDQMIFNreLPQAAGVLHHCCSYKQGGQKLVTMNSAPRGVQS-GDRATWFGLYYNISGAGFFLHPVGLEL 246
Cdd:pfam02728   1 PPVTAEEYADIEEVIKT--DPLFKEQLKKRGIFNGDDVYCDPWTVGPRGEKSgGRRLTKALCYYRTGGVNFYLHPIELEL 78

                          90       100
                  ....*....|....*....|..
gi 741963933  247 LVDHKALDPAQWTIQKVFFQGR 268
Cdd:pfam02728  79 LVDHDAKDVIEITDQKVRYPGP 100
Cu_amine_oxidN2 pfam02727
Copper amine oxidase, N2 domain; This domain is the first or second structural domain in ...
 65-151 4.50e-35

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: 126.75  E-value: 4.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933   65 EELTAVMSFLTQQLGPDLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPPAREALAIVFFGKQPQPNVTELVVGP 144
Cdd:pfam02727   1 HPLDPLTSFEINKVESILKSSALFTLKDNSFFTVELEEPDKKAVLQWLDKGGPPPPREARVVILFGGQPHENVVDLAVGP 80


                  ....*..
gi 741963933  145 LPQPSYM 151
Cdd:pfam02727  81 LPSPRYM 87
TynA COG3733
Cu2+-containing amine oxidase [Secondary metabolites biosynthesis, transport and catabolism];
296-480 8.93e-16

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


Pssm-ID: 442947 [Multi-domain]  Cd Length: 646  Bit Score: 80.28  E-value: 8.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933 296 GLENWVwaEDMAFVPmvVPWSPEHQI-QRLQVTRKQLETEEQAAFPLGGPSPRYLYLAS-NQSNKWGHPRGYRIqtVSFA 373
Cdd:COG3733  455 GERNSV--YEVDTVA--VPIGPDNPYgNAFTTEATPLETESEAARDADPATGRYWKIVNpNKTNRLGEPVGYKL--VPGG 528

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933 374 GGPL---PQNSSMERAfSWARYQLAVTQRKEGEPSSTSIY-NLNDP------WSPtldfsdfiNNETIAGQDLVAWVTAG 443
Cdd:COG3733  529 NPTLladPDSSIAKRA-GFATKHLWVTPYDPDERYAAGDYpNQSPGgaglpaWTA--------DDRSIENEDVVLWYTFG 599

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 741963933 444 FLHIPHAEDIPntVTVGNGVGFFLRPYNFFDQEPSMD 480
Cdd:COG3733  600 VTHVPRPEDWP--VMPVDYAGFKLKPVGFFDRNPALD 634
tynA PRK14696
primary-amine oxidase;
324-479 8.24e-12

primary-amine oxidase;


Pssm-ID: 184793 [Multi-domain]  Cd Length: 721  Bit Score: 67.93  E-value: 8.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933 324 LQVTRKQLETEEQAAFPLGgPSPRYLYLASNQSNKWGHPRGYriQTVSFAGGPLP--------QNSSMERAFSWARYQLA 395
Cdd:PRK14696 557 MQVNQYNIGNEQDAAQKFD-PGTIRLLSNPNKENRMGNPVSY--QIIPYAGGTHPvakganfaPDEWIYHRLSFMDKQLW 633

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933 396 VTQRKEGEPSSTSIYnlndPWSPTLD--FSDFI-NNETIAGQDLVAWVTAGFLHIPHAEDIPNTVTvgNGVGFFLRPYNF 472
Cdd:PRK14696 634 VTRYHPGERFPEGKY----PNRSTHDtgLGQYSkDNESLDNTDAVVWMTTGTTHVARAEEWPIMPT--EWVHTLLKPWNF 707


                 ....*..
gi 741963933 473 FDQEPSM 479
Cdd:PRK14696 708 FDETPTL 714
PLN02566 PLN02566
amine oxidase (copper-containing)
 326-477 4.20e-11

amine oxidase (copper-containing)


Pssm-ID: 215306 [Multi-domain]  Cd Length: 646  Bit Score: 65.66  E-value: 4.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933 326 VTRKQLETEEQAAFPLGGPSPRYLYLASNQSNKWGHPRGYRIQTVSFAGGPLPQNSSMERAFSWARYQLAVTQRKEGEPS 405
Cdd:PLN02566 495 VVKETAKTEAEGRIRLGSEPAELLIVNPNKKTKLGNQVGYRLITGQPVTSLLSDDDYPQIRAAYTKYQVWVTAYNKSERW 574

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 741963933 406 STSIY---NLNDP----WSPtldfsdfiNNETIAGQDLVAWVTAGFLHIPHAEDIPNTVTVGNgvGFFLRPYNFFDQEP 477
Cdd:PLN02566 575 AGGFYadrSRGDDglavWSS--------RNREIENKDIVLWYTVGFHHIPYQEDFPVMPTLHG--GFELRPANFFESNP 643
tynA PRK11504
primary-amine oxidase;
296-480 4.64e-11

primary-amine oxidase;


Pssm-ID: 236919 [Multi-domain]  Cd Length: 647  Bit Score: 65.31  E-value: 4.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933 296 GLENWVWAEDmaFVPmvVPWSPE--HQiQRLQVTRKQLETEEQAAFPLGGPSPRYLYLAS-NQSNKWGHPRGYRI----Q 368
Cdd:PRK11504 451 GPGNSVYEVN--SVP--VPMGPDnpHG-NAFYTRETLLETESEAARDADPSTGRYWKIVNpNKKNRLGEPVAYKLvpggN 525

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 741963933 369 TVSFAGgplPQNSSMERAfSWARYQLAVTQRKEGEpsstsIYnlndpwsPTLDF----------SDFI-NNETIAGQDLV 437
Cdd:PRK11504 526 PPLLAD---PGSSIRQRA-GFATHHLWVTPYDPDE-----RY-------AAGDYpnqsaggdglPAYIaADRSIENTDVV 589

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 741963933 438 AWVTAGFLHIPHAEDIPntVTVGNGVGFFLRPYNFFDQEPSMD 480
Cdd:PRK11504 590 LWYTFGITHVPRPEDWP--VMPVDYAGFKLKPVGFFDRNPALD 630
 
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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