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Conserved domains on  [gi|2462546972|ref|XP_054235305|]
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nuclear pore complex-interacting protein family member A5 isoform X6 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NPIP super family cl05750
Nuclear pore complex interacting protein (NPIP); This family consists of a series of primate ...
 70-262 3.01e-106

Nuclear pore complex interacting protein (NPIP); This family consists of a series of primate specific nuclear pore complex interacting protein (NPIP) sequences. The function of this family is unknown but is well conserved from African apes to humans.


The actual alignment was detected with superfamily member pfam06409:

Pssm-ID: 461900 [Multi-domain]  Cd Length: 267  Bit Score: 309.36  E-value: 3.01e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546972  70 VINTLADHRHRGTDFGGSPWLLIITVFLRSYKFAISLCTSYLCVSFLKTIFPSQNGHDGSTDVQQRARRSNCRRQEGIKI 149
Cdd:pfam06409   1 MFCCLADERHRGGCFGGHPALLIITLADHRHKFADFGCSPWLCIIFLFLIFPKFAGHDCSSDLCQRALKSIFPRQEGHDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546972 150 VLEDIFTLWRQVETKVRAKIRKMKVTTKVNCHDKINGKRKTAKEHLRKLSMKEREHGEKERQVSEAEENGKLDMKEIHTY 229
Cdd:pfam06409  81 SLDDIFRARRQNERKQEAIICKLEDIFKLNRHDEIKGKAKIAKEHLRKKSMKEDEHGEKEKQAKEAEEKGKLDEKEHGEK 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462546972 230 MEMFQRAQALRRRAEDYYRCKITPSARKPLCNR 262
Cdd:pfam06409 161 EEMFQEAEALGKLAEDEIHCKIEMFARAPACNR 193
AFD_class_I super family cl17068
Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, ...
 2-41 1.30e-12

Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


The actual alignment was detected with superfamily member cd05928:

Pssm-ID: 473059 [Multi-domain]  Cd Length: 530  Bit Score: 67.49  E-value: 1.30e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462546972   2 VKLSIVLTPRFLSHDQGQLTKELQQHVKSVTCPCEYLRKV 41
Cdd:cd05928   467 VKAFVVLAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKV 506
 
Name Accession Description Interval E-value
NPIP pfam06409
Nuclear pore complex interacting protein (NPIP); This family consists of a series of primate ...
 70-262 3.01e-106

Nuclear pore complex interacting protein (NPIP); This family consists of a series of primate specific nuclear pore complex interacting protein (NPIP) sequences. The function of this family is unknown but is well conserved from African apes to humans.


Pssm-ID: 461900 [Multi-domain]  Cd Length: 267  Bit Score: 309.36  E-value: 3.01e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546972  70 VINTLADHRHRGTDFGGSPWLLIITVFLRSYKFAISLCTSYLCVSFLKTIFPSQNGHDGSTDVQQRARRSNCRRQEGIKI 149
Cdd:pfam06409   1 MFCCLADERHRGGCFGGHPALLIITLADHRHKFADFGCSPWLCIIFLFLIFPKFAGHDCSSDLCQRALKSIFPRQEGHDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546972 150 VLEDIFTLWRQVETKVRAKIRKMKVTTKVNCHDKINGKRKTAKEHLRKLSMKEREHGEKERQVSEAEENGKLDMKEIHTY 229
Cdd:pfam06409  81 SLDDIFRARRQNERKQEAIICKLEDIFKLNRHDEIKGKAKIAKEHLRKKSMKEDEHGEKEKQAKEAEEKGKLDEKEHGEK 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462546972 230 MEMFQRAQALRRRAEDYYRCKITPSARKPLCNR 262
Cdd:pfam06409 161 EEMFQEAEALGKLAEDEIHCKIEMFARAPACNR 193
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 2-41 1.30e-12

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 67.49  E-value: 1.30e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462546972   2 VKLSIVLTPRFLSHDQGQLTKELQQHVKSVTCPCEYLRKV 41
Cdd:cd05928   467 VKAFVVLAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKV 506
 
Name Accession Description Interval E-value
NPIP pfam06409
Nuclear pore complex interacting protein (NPIP); This family consists of a series of primate ...
 70-262 3.01e-106

Nuclear pore complex interacting protein (NPIP); This family consists of a series of primate specific nuclear pore complex interacting protein (NPIP) sequences. The function of this family is unknown but is well conserved from African apes to humans.


Pssm-ID: 461900 [Multi-domain]  Cd Length: 267  Bit Score: 309.36  E-value: 3.01e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546972  70 VINTLADHRHRGTDFGGSPWLLIITVFLRSYKFAISLCTSYLCVSFLKTIFPSQNGHDGSTDVQQRARRSNCRRQEGIKI 149
Cdd:pfam06409   1 MFCCLADERHRGGCFGGHPALLIITLADHRHKFADFGCSPWLCIIFLFLIFPKFAGHDCSSDLCQRALKSIFPRQEGHDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546972 150 VLEDIFTLWRQVETKVRAKIRKMKVTTKVNCHDKINGKRKTAKEHLRKLSMKEREHGEKERQVSEAEENGKLDMKEIHTY 229
Cdd:pfam06409  81 SLDDIFRARRQNERKQEAIICKLEDIFKLNRHDEIKGKAKIAKEHLRKKSMKEDEHGEKEKQAKEAEEKGKLDEKEHGEK 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462546972 230 MEMFQRAQALRRRAEDYYRCKITPSARKPLCNR 262
Cdd:pfam06409 161 EEMFQEAEALGKLAEDEIHCKIEMFARAPACNR 193
NPIP pfam06409
Nuclear pore complex interacting protein (NPIP); This family consists of a series of primate ...
 70-262 6.84e-106

Nuclear pore complex interacting protein (NPIP); This family consists of a series of primate specific nuclear pore complex interacting protein (NPIP) sequences. The function of this family is unknown but is well conserved from African apes to humans.


Pssm-ID: 461900 [Multi-domain]  Cd Length: 267  Bit Score: 308.59  E-value: 6.84e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546972  70 VINTLADHRHRGTDFGGSPWLLIITVFLRSYKFAISLCTSYLCVSFLKTIFPSQNGHDGSTDVQQRARRSNCRRQEGIKI 149
Cdd:pfam06409  22 LIITLADHRHKFADFGCSPWLCIIFLFLIFPKFAGHDCSSDLCQRALKSIFPRQEGHDGSLDDIFRARRQNERKQEAIIC 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462546972 150 VLEDIFTLWRQVETKVRAKIRKMKVTTKVNCHDKINGKRKTAKEHLRKLSMKEREHGEKERQVSEAEENGKLDMKEIHTY 229
Cdd:pfam06409 102 KLEDIFKLNRHDEIKGKAKIAKEHLRKKSMKEDEHGEKEKQAKEAEEKGKLDEKEHGEKEEMFQEAEALGKLAEDEIHCK 181

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462546972 230 MEMFQRAQALRRRAEDYYRCKITPSARKPLCNR 262
Cdd:pfam06409 182 IEMFARAPACNRRAEAAAECKHSPGAPKPLCLR 214
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 2-41 1.30e-12

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 67.49  E-value: 1.30e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462546972   2 VKLSIVLTPRFLSHDQGQLTKELQQHVKSVTCPCEYLRKV 41
Cdd:cd05928   467 VKAFVVLAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKV 506
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 1-54 1.24e-03

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 40.01  E-value: 1.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462546972   1 MVKLSIVLTPRFLSHDQgqLTKELQQHVKSVTCPCEYLRKVTLRN--PGSSGRKER 54
Cdd:cd05972   369 VVKAFVVLTSGYEPSEE--LAEELQGHVKKVLAPYKYPREIEFVEelPKTISGKIR 422
 
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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