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Conserved domains on  [gi|13591971|ref|NP_112306|]
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histamine N-methyltransferase [Rattus norvegicus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10606006)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor similar to histamine N-methyltransferase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
32-218 1.47e-28

Methyltransferase domain; This family appears to be a methyltransferase domain.


:

Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 107.51  E-value: 1.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591971    32 MQEFMDKKLPGIIARIGET-KAEIKILSIGGGAGeIDLQILSKVQAQYPGICINNEVVEPNAEqivkykelvaktsnmeN 110
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKlPSPGRVLDFGCGTG-IFLRLLRAQGFSVTGVDPSPIAIERALL----------------N 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591971   111 IKFAWHKEtsseyqkrvVEEDEEPPKWDFIHMIQMLYYVKDIPATLKFFHGLLAANAKILIILVSGTSGWEKLWKKYGFR 190
Cdd:pfam13489  64 VRFDQFDE---------QEAAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYL 134
                         170       180
                  ....*....|....*....|....*...
gi 13591971   191 LPRDDLCQYVTSSDLAQILDDLGIKYEC 218
Cdd:pfam13489 135 RPRNGHISLFSARSLKRLLEEAGFEVVS 162
 
Name Accession Description Interval E-value
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
32-218 1.47e-28

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 107.51  E-value: 1.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591971    32 MQEFMDKKLPGIIARIGET-KAEIKILSIGGGAGeIDLQILSKVQAQYPGICINNEVVEPNAEqivkykelvaktsnmeN 110
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKlPSPGRVLDFGCGTG-IFLRLLRAQGFSVTGVDPSPIAIERALL----------------N 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591971   111 IKFAWHKEtsseyqkrvVEEDEEPPKWDFIHMIQMLYYVKDIPATLKFFHGLLAANAKILIILVSGTSGWEKLWKKYGFR 190
Cdd:pfam13489  64 VRFDQFDE---------QEAAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYL 134
                         170       180
                  ....*....|....*....|....*...
gi 13591971   191 LPRDDLCQYVTSSDLAQILDDLGIKYEC 218
Cdd:pfam13489 135 RPRNGHISLFSARSLKRLLEEAGFEVVS 162
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
55-174 1.36e-03

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 37.41  E-value: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591971  55 KILSIGGGAGEIDLQIlskvqAQYPGICInnEVVEPNAEQIVKYKELVAKtSNMENIKFawHKETSSEYQkrvveeDEEP 134
Cdd:cd02440   1 RVLDLGCGTGALALAL-----ASGPGARV--TGVDISPVALELARKAAAA-LLADNVEV--LKGDAEELP------PEAD 64
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 13591971 135 PKWDFIHMIQMLYYVK-DIPATLKFFHGLLAANAKILIILV 174
Cdd:cd02440  65 ESFDVIISDPPLHHLVeDLARFLEEARRLLKPGGVLVLTLV 105
 
Name Accession Description Interval E-value
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
32-218 1.47e-28

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 107.51  E-value: 1.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591971    32 MQEFMDKKLPGIIARIGET-KAEIKILSIGGGAGeIDLQILSKVQAQYPGICINNEVVEPNAEqivkykelvaktsnmeN 110
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKlPSPGRVLDFGCGTG-IFLRLLRAQGFSVTGVDPSPIAIERALL----------------N 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591971   111 IKFAWHKEtsseyqkrvVEEDEEPPKWDFIHMIQMLYYVKDIPATLKFFHGLLAANAKILIILVSGTSGWEKLWKKYGFR 190
Cdd:pfam13489  64 VRFDQFDE---------QEAAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYL 134
                         170       180
                  ....*....|....*....|....*...
gi 13591971   191 LPRDDLCQYVTSSDLAQILDDLGIKYEC 218
Cdd:pfam13489 135 RPRNGHISLFSARSLKRLLEEAGFEVVS 162
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
57-169 1.77e-04

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 40.04  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591971    57 LSIGGGAGeidlQILSKVQAQYPGIcinnEV--VEPNAEQIVKYKELVAktsnmENIKFAWHKETSSEYQkrvvEEDEEP 134
Cdd:pfam08242   1 LEIGCGTG----TLLRALLEALPGL----EYtgLDISPAALEAARERLA-----ALGLLNAVRVELFQLD----LGELDP 63
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 13591971   135 PKWDFIHMIQMLYYVKDIPATLKFFHGLLAANAKI 169
Cdd:pfam08242  64 GSFDVVVASNVLHHLADPRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
55-174 1.36e-03

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 37.41  E-value: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591971  55 KILSIGGGAGEIDLQIlskvqAQYPGICInnEVVEPNAEQIVKYKELVAKtSNMENIKFawHKETSSEYQkrvveeDEEP 134
Cdd:cd02440   1 RVLDLGCGTGALALAL-----ASGPGARV--TGVDISPVALELARKAAAA-LLADNVEV--LKGDAEELP------PEAD 64
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 13591971 135 PKWDFIHMIQMLYYVK-DIPATLKFFHGLLAANAKILIILV 174
Cdd:cd02440  65 ESFDVIISDPPLHHLVeDLARFLEEARRLLKPGGVLVLTLV 105
 
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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