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Conserved domains on  [gi|2445728481|ref|WP_273808454|]
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MULTISPECIES: nitrile hydratase subunit alpha [unclassified Pseudomonas]

Protein Classification

nitrile hydratase subunit alpha( domain architecture ID 12040854)

nitrile hydratase catalyzes the hydration of various nitrile compounds to the corresponding amides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NHase_alpha pfam02979
Nitrile hydratase, alpha chain;
28-205 2.19e-123

Nitrile hydratase, alpha chain;


:

Pssm-ID: 427091 [Multi-domain]  Cd Length: 178  Bit Score: 346.55  E-value: 2.19e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2445728481  28 VKALESLLLEKGLIDPVSMDALIDTYEHQIGPRNGAQVVAKAWADPEYRRRLLEDATTAIAELGFSGVQGEDMVVVENTP 107
Cdd:pfam02979   1 VRALESLLIEKGLITPAAVDAVIETYEAKVGPANGARVVARAWTDPAFKARLLADATAAIAELGFTGRQGEHLVVVENTP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2445728481 108 AVHNVTVCTLCSCYPWPTLGLPPAWYKSAPYRSRIVMDPRGVLAEFGLSIAADREIRVWDSSAELRYLVLPQRPDGTAGW 187
Cdd:pfam02979  81 EVHNVVVCTLCSCYPWPVLGLPPAWYKSPAYRSRAVREPRGVLAEFGVDLPEDVEVRVWDSTAEIRYLVLPMRPAGTEGW 160

                         170
                  ....*....|....*...
gi 2445728481 188 SEEQLAALVTRDSMIGTG 205
Cdd:pfam02979 161 SEEQLAALVTRDSMIGVA 178
 
Name Accession Description Interval E-value
NHase_alpha pfam02979
Nitrile hydratase, alpha chain;
28-205 2.19e-123

Nitrile hydratase, alpha chain;


Pssm-ID: 427091 [Multi-domain]  Cd Length: 178  Bit Score: 346.55  E-value: 2.19e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2445728481  28 VKALESLLLEKGLIDPVSMDALIDTYEHQIGPRNGAQVVAKAWADPEYRRRLLEDATTAIAELGFSGVQGEDMVVVENTP 107
Cdd:pfam02979   1 VRALESLLIEKGLITPAAVDAVIETYEAKVGPANGARVVARAWTDPAFKARLLADATAAIAELGFTGRQGEHLVVVENTP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2445728481 108 AVHNVTVCTLCSCYPWPTLGLPPAWYKSAPYRSRIVMDPRGVLAEFGLSIAADREIRVWDSSAELRYLVLPQRPDGTAGW 187
Cdd:pfam02979  81 EVHNVVVCTLCSCYPWPVLGLPPAWYKSPAYRSRAVREPRGVLAEFGVDLPEDVEVRVWDSTAEIRYLVLPMRPAGTEGW 160

                         170
                  ....*....|....*...
gi 2445728481 188 SEEQLAALVTRDSMIGTG 205
Cdd:pfam02979 161 SEEQLAALVTRDSMIGVA 178
nitrile_alph TIGR01323
nitrile hydratase, alpha subunit; This model describes both iron- and cobalt-containing ...
 22-210 2.51e-116

nitrile hydratase, alpha subunit; This model describes both iron- and cobalt-containing nitrile hydratase alpha chains. It excludes the thiocyanate hydrolase gamma subunit of Thiobacillus thioparus, a sequence that appears to have evolved from within the family of nitrile hydratase alpha subunits but which differs by several indels and a more rapid accumulation of point mutations. [Energy metabolism, Amino acids and amines]


Pssm-ID: 188130 [Multi-domain]  Cd Length: 189  Bit Score: 328.95  E-value: 2.51e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2445728481  22 EDVALRVKALESLLLEKGLIDPVSMDALIDTYEHQIGPRNGAQVVAKAWADPEYRRRLLEDATTAIAELGFSGVQGEDMV 101
Cdd:TIGR01323   1 ADSALRVRALESLLIEKGLITEAAVDGVIDTFENRMGPANGAKVVARAWTDPEFRERLLADGTAAIAELGYTGPQGEHMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2445728481 102 VVENTPAVHNVTVCTLCSCYPWPTLGLPPAWYKSAPYRSRIVMDPRGVLAEFGLSIAADREIRVWDSSAELRYLVLPQRP 181
Cdd:TIGR01323  81 AVENTPEVHNVIVCTLCSCYPWPVLGLPPYWYKSPEYRSRAVREPRGVLAEFGVELPEDVEVRVWDSSAETRYLVLPMRP 160

                         170       180
                  ....*....|....*....|....*....
gi 2445728481 182 DGTAGWSEEQLAALVTRDSMIGTGLALPP 210
Cdd:TIGR01323 161 AGTEGWSEEQLAELVTRDSMIGVALPKAP 189
 
Name Accession Description Interval E-value
NHase_alpha pfam02979
Nitrile hydratase, alpha chain;
28-205 2.19e-123

Nitrile hydratase, alpha chain;


Pssm-ID: 427091 [Multi-domain]  Cd Length: 178  Bit Score: 346.55  E-value: 2.19e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2445728481  28 VKALESLLLEKGLIDPVSMDALIDTYEHQIGPRNGAQVVAKAWADPEYRRRLLEDATTAIAELGFSGVQGEDMVVVENTP 107
Cdd:pfam02979   1 VRALESLLIEKGLITPAAVDAVIETYEAKVGPANGARVVARAWTDPAFKARLLADATAAIAELGFTGRQGEHLVVVENTP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2445728481 108 AVHNVTVCTLCSCYPWPTLGLPPAWYKSAPYRSRIVMDPRGVLAEFGLSIAADREIRVWDSSAELRYLVLPQRPDGTAGW 187
Cdd:pfam02979  81 EVHNVVVCTLCSCYPWPVLGLPPAWYKSPAYRSRAVREPRGVLAEFGVDLPEDVEVRVWDSTAEIRYLVLPMRPAGTEGW 160

                         170
                  ....*....|....*...
gi 2445728481 188 SEEQLAALVTRDSMIGTG 205
Cdd:pfam02979 161 SEEQLAALVTRDSMIGVA 178
nitrile_alph TIGR01323
nitrile hydratase, alpha subunit; This model describes both iron- and cobalt-containing ...
 22-210 2.51e-116

nitrile hydratase, alpha subunit; This model describes both iron- and cobalt-containing nitrile hydratase alpha chains. It excludes the thiocyanate hydrolase gamma subunit of Thiobacillus thioparus, a sequence that appears to have evolved from within the family of nitrile hydratase alpha subunits but which differs by several indels and a more rapid accumulation of point mutations. [Energy metabolism, Amino acids and amines]


Pssm-ID: 188130 [Multi-domain]  Cd Length: 189  Bit Score: 328.95  E-value: 2.51e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2445728481  22 EDVALRVKALESLLLEKGLIDPVSMDALIDTYEHQIGPRNGAQVVAKAWADPEYRRRLLEDATTAIAELGFSGVQGEDMV 101
Cdd:TIGR01323   1 ADSALRVRALESLLIEKGLITEAAVDGVIDTFENRMGPANGAKVVARAWTDPEFRERLLADGTAAIAELGYTGPQGEHMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2445728481 102 VVENTPAVHNVTVCTLCSCYPWPTLGLPPAWYKSAPYRSRIVMDPRGVLAEFGLSIAADREIRVWDSSAELRYLVLPQRP 181
Cdd:TIGR01323  81 AVENTPEVHNVIVCTLCSCYPWPVLGLPPYWYKSPEYRSRAVREPRGVLAEFGVELPEDVEVRVWDSSAETRYLVLPMRP 160

                         170       180
                  ....*....|....*....|....*....
gi 2445728481 182 DGTAGWSEEQLAALVTRDSMIGTGLALPP 210
Cdd:TIGR01323 161 AGTEGWSEEQLAELVTRDSMIGVALPKAP 189
TOMM_pelo TIGR03793
NHLP leader peptide domain; This model represents a domain that is conserved among a large ...
 131-195 2.99e-08

NHLP leader peptide domain; This model represents a domain that is conserved among a large number of putative ribosomal natural products (RNP) precursor, including the thiazole/oxazole-modified microcins (TOMMs). As a leader peptide domain, likely to be removed from the mature product, this domain is unusual in several ways. First, it is longer than most previously described RNP leader peptides. Second, most of the domain is homologous to nitrile hydratase alpha subunits. Finally, it appears that this domain correlates with a specific family of cleavage/export proteins while members undergo modifications by different classes of peptide maturase, including cyclodehydratases, lantibiotic synthases, radical SAM peptide maturases. This family is expanded especially in Pelotomaculum thermopropionicum SI. [Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274786 [Multi-domain]  Cd Length: 77  Bit Score: 49.23  E-value: 2.99e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2445728481 131 AWyKSAPYRSRIVMDPRGVLAEFGLSIAADREIRVWDSSAELRYLVLPQRPDGTAgwSEEQLAAL 195
Cdd:TIGR03793  13 AW-EDEAFKQALLTNPKEALEREGVQVPAEVEVKVVEESPTVLYLVLPVNPDGEL--TDEQLDAV 74
TOMM_pelo TIGR03793
NHLP leader peptide domain; This model represents a domain that is conserved among a large ...
 63-109 8.98e-06

NHLP leader peptide domain; This model represents a domain that is conserved among a large number of putative ribosomal natural products (RNP) precursor, including the thiazole/oxazole-modified microcins (TOMMs). As a leader peptide domain, likely to be removed from the mature product, this domain is unusual in several ways. First, it is longer than most previously described RNP leader peptides. Second, most of the domain is homologous to nitrile hydratase alpha subunits. Finally, it appears that this domain correlates with a specific family of cleavage/export proteins while members undergo modifications by different classes of peptide maturase, including cyclodehydratases, lantibiotic synthases, radical SAM peptide maturases. This family is expanded especially in Pelotomaculum thermopropionicum SI. [Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274786 [Multi-domain]  Cd Length: 77  Bit Score: 42.30  E-value: 8.98e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2445728481  63 AQVVAKAWADPEYRRRLLEDATTAIAELGFSGVQGEDMVVVENTPAV 109
Cdd:TIGR03793   7 EKIIAKAWEDEAFKQALLTNPKEALEREGVQVPAEVEVKVVEESPTV 53
 
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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