NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1370472519|ref|XP_024306783|]
View 

membrane primary amine oxidase isoform X5 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 7-173 3.79e-61

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: 196.14  E-value: 3.79e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472519   7 AVPWSPEHQLQR---LQVTRKLLEMEEQAAFLVGSATPRYLYLAS-NHSNKWGHPRGYRIQMLSFAGEPLPQNSS-MARG 81
Cdd:pfam01179 233 VVPWPVGPENPYgnaFKVERTVLETEKEAARDLDPSNPRYWKIVNpNKKNKSGKPVGYKLVPGPAHQPLLADPDSsVAKR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472519  82 FSWERYQLAVTQRKEEEPSSSSVFNqNDPWAPTVDFSDFI-NNETIAGKDLVAWVTAGFLHIPHAEDIPntVTVGNGVGF 160
Cdd:pfam01179 313 AAFARHHLWVTKYKDDELYAAGDYN-NQSRGPPVGLAKWIaDNESIENEDIVLWVTFGLTHIPRPEDFP--VMPVEHSGF 389

                         170
                  ....*....|...
gi 1370472519 161 FLRPYNFFDEDPS 173
Cdd:pfam01179 390 LLRPFNFFDRNPA 402
 
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 ...
 7-173 3.79e-61

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: 196.14  E-value: 3.79e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472519   7 AVPWSPEHQLQR---LQVTRKLLEMEEQAAFLVGSATPRYLYLAS-NHSNKWGHPRGYRIQMLSFAGEPLPQNSS-MARG 81
Cdd:pfam01179 233 VVPWPVGPENPYgnaFKVERTVLETEKEAARDLDPSNPRYWKIVNpNKKNKSGKPVGYKLVPGPAHQPLLADPDSsVAKR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472519  82 FSWERYQLAVTQRKEEEPSSSSVFNqNDPWAPTVDFSDFI-NNETIAGKDLVAWVTAGFLHIPHAEDIPntVTVGNGVGF 160
Cdd:pfam01179 313 AAFARHHLWVTKYKDDELYAAGDYN-NQSRGPPVGLAKWIaDNESIENEDIVLWVTFGLTHIPRPEDFP--VMPVEHSGF 389

                         170
                  ....*....|...
gi 1370472519 161 FLRPYNFFDEDPS 173
Cdd:pfam01179 390 LLRPFNFFDRNPA 402
TynA COG3733
Cu2+-containing amine oxidase [Secondary metabolites biosynthesis, transport and catabolism];
7-173 1.15e-16

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


Pssm-ID: 442947 [Multi-domain]  Cd Length: 646  Bit Score: 77.97  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472519   7 AVPWSPEHQL-QRLQVTRKLLEMEEQAAFLVGSATPRYLYLAS-NHSNKWGHPRGYRI----QMLSFAGeplPQNSSMAR 80
Cdd:COG3733   467 AVPIGPDNPYgNAFTTEATPLETESEAARDADPATGRYWKIVNpNKTNRLGEPVGYKLvpggNPTLLAD---PDSSIAKR 543

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472519  81 -GFSweRYQLAVTQRKEEE--PSSSSVfNQNDPWA--PTvdfsdFI-NNETIAGKDLVAWVTAGFLHIPHAEDIPntVTV 154
Cdd:COG3733   544 aGFA--TKHLWVTPYDPDEryAAGDYP-NQSPGGAglPA-----WTaDDRSIENEDVVLWYTFGVTHVPRPEDWP--VMP 613

                         170
                  ....*....|....*....
gi 1370472519 155 GNGVGFFLRPYNFFDEDPS 173
Cdd:COG3733   614 VDYAGFKLKPVGFFDRNPA 632
tynA PRK11504
primary-amine oxidase;
7-174 3.28e-13

primary-amine oxidase;


Pssm-ID: 236919 [Multi-domain]  Cd Length: 647  Bit Score: 68.00  E-value: 3.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472519   7 AVPWSPEHQL-QRLQVTRKLLEMEEQAAFLVGSATPRYlYLASNHS--NKWGHPRGYRI----QMLSFAGEplpqNSSMA 79
Cdd:PRK11504  463 PVPMGPDNPHgNAFYTRETLLETESEAARDADPSTGRY-WKIVNPNkkNRLGEPVAYKLvpggNPPLLADP----GSSIR 537

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472519  80 R--GFSweRYQLAVTQRKEEEPSSSSVF-NQNDPWA--PtvdfsDFI-NNETIAGKDLVAWVTAGFLHIPHAEDIPntVT 153
Cdd:PRK11504  538 QraGFA--THHLWVTPYDPDERYAAGDYpNQSAGGDglP-----AYIaADRSIENTDVVLWYTFGITHVPRPEDWP--VM 608

                         170       180
                  ....*....|....*....|.
gi 1370472519 154 VGNGVGFFLRPYNFFDEDPSF 174
Cdd:PRK11504  609 PVDYAGFKLKPVGFFDRNPAL 629
Matonaviridae_RdRp cd23260
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Matonaviridae of ...
 110-147 5.26e-03

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Matonaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Matonaviridae, order Hepelivirales. Members of the family Matonaviridae have a (+)ssRNA genome enclosed by an icosahedral capsid. Matonaviridae has a single genus, Rubivirus, which contains three species: Rubivirus rubella (commonly called rubella virus), Rubivirus ruteetense (commonly called ruhugu virus), and Rubivirus strelense (commonly called rustrela virus). Rubella virus (RuV) is the etiologic agent of the disease rubella (also called German measles). RuV is transmitted only between humans via the respiratory route, and is the main cause of congenital rubella syndrome (severe congenital birth defects, miscarriage, and stillbirth) when infection occurs during the first trimester of pregnancy. In vitro studies with cell lines showed that RuV has an apoptotic effect on certain cell types; there is evidence for a p53-dependent mechanism. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438110  Cd Length: 257  Bit Score: 36.88  E-value: 5.26e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1370472519 110 PWAPTVDFSDFINNETIAGKDLVAWVTAGFLHIPHAED 147
Cdd:cd23260    78 PNAVEVDFTEFDMNQTLATRDVELEISASLLGLPSAED 115
 
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 ...
 7-173 3.79e-61

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: 196.14  E-value: 3.79e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472519   7 AVPWSPEHQLQR---LQVTRKLLEMEEQAAFLVGSATPRYLYLAS-NHSNKWGHPRGYRIQMLSFAGEPLPQNSS-MARG 81
Cdd:pfam01179 233 VVPWPVGPENPYgnaFKVERTVLETEKEAARDLDPSNPRYWKIVNpNKKNKSGKPVGYKLVPGPAHQPLLADPDSsVAKR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472519  82 FSWERYQLAVTQRKEEEPSSSSVFNqNDPWAPTVDFSDFI-NNETIAGKDLVAWVTAGFLHIPHAEDIPntVTVGNGVGF 160
Cdd:pfam01179 313 AAFARHHLWVTKYKDDELYAAGDYN-NQSRGPPVGLAKWIaDNESIENEDIVLWVTFGLTHIPRPEDFP--VMPVEHSGF 389

                         170
                  ....*....|...
gi 1370472519 161 FLRPYNFFDEDPS 173
Cdd:pfam01179 390 LLRPFNFFDRNPA 402
TynA COG3733
Cu2+-containing amine oxidase [Secondary metabolites biosynthesis, transport and catabolism];
7-173 1.15e-16

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


Pssm-ID: 442947 [Multi-domain]  Cd Length: 646  Bit Score: 77.97  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472519   7 AVPWSPEHQL-QRLQVTRKLLEMEEQAAFLVGSATPRYLYLAS-NHSNKWGHPRGYRI----QMLSFAGeplPQNSSMAR 80
Cdd:COG3733   467 AVPIGPDNPYgNAFTTEATPLETESEAARDADPATGRYWKIVNpNKTNRLGEPVGYKLvpggNPTLLAD---PDSSIAKR 543

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472519  81 -GFSweRYQLAVTQRKEEE--PSSSSVfNQNDPWA--PTvdfsdFI-NNETIAGKDLVAWVTAGFLHIPHAEDIPntVTV 154
Cdd:COG3733   544 aGFA--TKHLWVTPYDPDEryAAGDYP-NQSPGGAglPA-----WTaDDRSIENEDVVLWYTFGVTHVPRPEDWP--VMP 613

                         170
                  ....*....|....*....
gi 1370472519 155 GNGVGFFLRPYNFFDEDPS 173
Cdd:COG3733   614 VDYAGFKLKPVGFFDRNPA 632
tynA PRK11504
primary-amine oxidase;
7-174 3.28e-13

primary-amine oxidase;


Pssm-ID: 236919 [Multi-domain]  Cd Length: 647  Bit Score: 68.00  E-value: 3.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472519   7 AVPWSPEHQL-QRLQVTRKLLEMEEQAAFLVGSATPRYlYLASNHS--NKWGHPRGYRI----QMLSFAGEplpqNSSMA 79
Cdd:PRK11504  463 PVPMGPDNPHgNAFYTRETLLETESEAARDADPSTGRY-WKIVNPNkkNRLGEPVAYKLvpggNPPLLADP----GSSIR 537

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472519  80 R--GFSweRYQLAVTQRKEEEPSSSSVF-NQNDPWA--PtvdfsDFI-NNETIAGKDLVAWVTAGFLHIPHAEDIPntVT 153
Cdd:PRK11504  538 QraGFA--THHLWVTPYDPDERYAAGDYpNQSAGGDglP-----AYIaADRSIENTDVVLWYTFGITHVPRPEDWP--VM 608

                         170       180
                  ....*....|....*....|.
gi 1370472519 154 VGNGVGFFLRPYNFFDEDPSF 174
Cdd:PRK11504  609 PVDYAGFKLKPVGFFDRNPAL 629
tynA PRK14696
primary-amine oxidase;
19-173 1.54e-11

primary-amine oxidase;


Pssm-ID: 184793 [Multi-domain]  Cd Length: 721  Bit Score: 62.92  E-value: 1.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472519  19 LQVTRKLLEMEEQAAFLVGSATPRYLYlASNHSNKWGHPRGYriQMLSFAGEPLPqnssMARG--FSWERY--------- 87
Cdd:PRK14696  557 MQVNQYNIGNEQDAAQKFDPGTIRLLS-NPNKENRMGNPVSY--QIIPYAGGTHP----VAKGanFAPDEWiyhrlsfmd 629

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472519  88 -QLAVTQRKEEEPSSSSVFnqndPWAPTVD--FSDFI-NNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTvgNGVGFFLR 163
Cdd:PRK14696  630 kQLWVTRYHPGERFPEGKY----PNRSTHDtgLGQYSkDNESLDNTDAVVWMTTGTTHVARAEEWPIMPT--EWVHTLLK 703

                         170
                  ....*....|
gi 1370472519 164 PYNFFDEDPS 173
Cdd:PRK14696  704 PWNFFDETPT 713
PLN02566 PLN02566
amine oxidase (copper-containing)
 21-172 2.28e-11

amine oxidase (copper-containing)


Pssm-ID: 215306 [Multi-domain]  Cd Length: 646  Bit Score: 62.58  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472519  21 VTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHPRGYRIqmlsFAGEPL---------PQNSSmargfSWERYQLAV 91
Cdd:PLN02566  495 VVKETAKTEAEGRIRLGSEPAELLIVNPNKKTKLGNQVGYRL----ITGQPVtsllsdddyPQIRA-----AYTKYQVWV 565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370472519  92 TqrkeeepssssVFNQNDPWAPTVdFSD-----------FINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNgvGF 160
Cdd:PLN02566  566 T-----------AYNKSERWAGGF-YADrsrgddglavwSSRNREIENKDIVLWYTVGFHHIPYQEDFPVMPTLHG--GF 631

                         170
                  ....*....|..
gi 1370472519 161 FLRPYNFFDEDP 172
Cdd:PLN02566  632 ELRPANFFESNP 643
Matonaviridae_RdRp cd23260
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Matonaviridae of ...
 110-147 5.26e-03

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Matonaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Matonaviridae, order Hepelivirales. Members of the family Matonaviridae have a (+)ssRNA genome enclosed by an icosahedral capsid. Matonaviridae has a single genus, Rubivirus, which contains three species: Rubivirus rubella (commonly called rubella virus), Rubivirus ruteetense (commonly called ruhugu virus), and Rubivirus strelense (commonly called rustrela virus). Rubella virus (RuV) is the etiologic agent of the disease rubella (also called German measles). RuV is transmitted only between humans via the respiratory route, and is the main cause of congenital rubella syndrome (severe congenital birth defects, miscarriage, and stillbirth) when infection occurs during the first trimester of pregnancy. In vitro studies with cell lines showed that RuV has an apoptotic effect on certain cell types; there is evidence for a p53-dependent mechanism. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 438110  Cd Length: 257  Bit Score: 36.88  E-value: 5.26e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1370472519 110 PWAPTVDFSDFINNETIAGKDLVAWVTAGFLHIPHAED 147
Cdd:cd23260    78 PNAVEVDFTEFDMNQTLATRDVELEISASLLGLPSAED 115
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH