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Conserved domains on  [gi|542133101|ref|NP_001269453|]
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nuclear pore complex-interacting protein family member B6 [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 ...
 41-300 1.53e-80

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: 249.27  E-value: 1.53e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133101   41 VINSLAVYRHRETDFG---------VGVRDHPGQ-HGKTPspqkldnLIIIIIGFLRRYTFNILFCTSCLCVSFLKTIFW 110
Cdd:pfam06409   1 MFCCLADERHRGGCFGghpalliitLADHRHKFAdFGCSP-------WLCIIFLFLIFPKFAGHDCSSDLCQRALKSIFP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133101  111 SRNGHDGSMDVQQRAWRSNRSRQkglrsicmhtkkrvssfRGNKIGLKDVITLRRHVETKVRAKIRKRKVTTKINRHDKI 190
Cdd:pfam06409  74 RQEGHDGSLDDIFRARRQNERKQ-----------------EAIICKLEDIFKLNRHDEIKGKAKIAKEHLRKKSMKEDEH 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133101  191 NGKRKTAR---------------KQKMFQRAQELRRRAEDYHKCKIPPSARKPLCNWVRMVAAEHRHSSGLPYWPYLTAE 255
Cdd:pfam06409 137 GEKEKQAKeaeekgkldekehgeKEEMFQEAEALGKLAEDEIHCKIEMFARAPACNRRAEAAAECKHSPGAPKPLCLRAE 216

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 542133101  256 TLKNRMGRQPPPPTQQHSITDNSLSLKTPTECLLTPLPPSVDDNI 300
Cdd:pfam06409 217 MAAAEHGHQPGLPTQPHLIADNLKNLKGHPECLLTPLHPIADNSA 261
AFD_class_I super family cl17068
Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, ...
 2-41 1.61e-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: 69.03  E-value: 1.61e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 542133101   2 VKLSIVLTPQFLSHDQSQLTKELQQHVKSVTCPCEYLRKV 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 ...
 41-300 1.53e-80

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: 249.27  E-value: 1.53e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133101   41 VINSLAVYRHRETDFG---------VGVRDHPGQ-HGKTPspqkldnLIIIIIGFLRRYTFNILFCTSCLCVSFLKTIFW 110
Cdd:pfam06409   1 MFCCLADERHRGGCFGghpalliitLADHRHKFAdFGCSP-------WLCIIFLFLIFPKFAGHDCSSDLCQRALKSIFP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133101  111 SRNGHDGSMDVQQRAWRSNRSRQkglrsicmhtkkrvssfRGNKIGLKDVITLRRHVETKVRAKIRKRKVTTKINRHDKI 190
Cdd:pfam06409  74 RQEGHDGSLDDIFRARRQNERKQ-----------------EAIICKLEDIFKLNRHDEIKGKAKIAKEHLRKKSMKEDEH 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133101  191 NGKRKTAR---------------KQKMFQRAQELRRRAEDYHKCKIPPSARKPLCNWVRMVAAEHRHSSGLPYWPYLTAE 255
Cdd:pfam06409 137 GEKEKQAKeaeekgkldekehgeKEEMFQEAEALGKLAEDEIHCKIEMFARAPACNRRAEAAAECKHSPGAPKPLCLRAE 216

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 542133101  256 TLKNRMGRQPPPPTQQHSITDNSLSLKTPTECLLTPLPPSVDDNI 300
Cdd:pfam06409 217 MAAAEHGHQPGLPTQPHLIADNLKNLKGHPECLLTPLHPIADNSA 261
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 2-41 1.61e-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: 69.03  E-value: 1.61e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 542133101   2 VKLSIVLTPQFLSHDQSQLTKELQQHVKSVTCPCEYLRKV 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 ...
 41-300 1.53e-80

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: 249.27  E-value: 1.53e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133101   41 VINSLAVYRHRETDFG---------VGVRDHPGQ-HGKTPspqkldnLIIIIIGFLRRYTFNILFCTSCLCVSFLKTIFW 110
Cdd:pfam06409   1 MFCCLADERHRGGCFGghpalliitLADHRHKFAdFGCSP-------WLCIIFLFLIFPKFAGHDCSSDLCQRALKSIFP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133101  111 SRNGHDGSMDVQQRAWRSNRSRQkglrsicmhtkkrvssfRGNKIGLKDVITLRRHVETKVRAKIRKRKVTTKINRHDKI 190
Cdd:pfam06409  74 RQEGHDGSLDDIFRARRQNERKQ-----------------EAIICKLEDIFKLNRHDEIKGKAKIAKEHLRKKSMKEDEH 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133101  191 NGKRKTAR---------------KQKMFQRAQELRRRAEDYHKCKIPPSARKPLCNWVRMVAAEHRHSSGLPYWPYLTAE 255
Cdd:pfam06409 137 GEKEKQAKeaeekgkldekehgeKEEMFQEAEALGKLAEDEIHCKIEMFARAPACNRRAEAAAECKHSPGAPKPLCLRAE 216

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 542133101  256 TLKNRMGRQPPPPTQQHSITDNSLSLKTPTECLLTPLPPSVDDNI 300
Cdd:pfam06409 217 MAAAEHGHQPGLPTQPHLIADNLKNLKGHPECLLTPLHPIADNSA 261
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 2-41 1.61e-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: 69.03  E-value: 1.61e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 542133101   2 VKLSIVLTPQFLSHDQSQLTKELQQHVKSVTCPCEYLRKV 41
Cdd:cd05928  467 VKAFVVLAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKV 506
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 1-41 1.30e-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: 40.78  E-value: 1.30e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 542133101   1 MVKLSIVLTPQFLshDQSQLTKELQQHVKSVTCPCEYLRKV 41
Cdd:cd05972  369 VVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREI 407
 
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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