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Conserved domains on  [gi|446542395|ref|WP_000619741|]
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MULTISPECIES: YfeK family protein [Leptospira]

Protein Classification

YfeK family protein( domain architecture ID 10013487)

YfeK family protein is a DUF5329 domain-containing protein, similar to Escherichia coli protein YfeK which may be a component of the sigmaE response and involved in maintaining cell envelope homeostasis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10318 PRK10318
hypothetical protein; Provisional
 2-128 1.84e-56

hypothetical protein; Provisional


:

Pssm-ID: 236672  Cd Length: 121  Bit Score: 171.47  E-value: 1.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446542395   2 IRKLIFLSIFLFCISIIAENDSNFRNDLNSLMNVL-ESCECKFIRNGSEHDSKEAREHMERKLKAVDGKIHTIQEFIDHI 80
Cdd:PRK10318   1 KKILCLLITLLFTLPAYAKLTAHEEARINAMLEGLaQKKDCTFVRNGDEHTCKEAVSHLRLKLGNTRNRIDTAEQFIDKV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446542395  81 GSKSSVSGKPYFVKFADGKTVESRVWLKEKWEEivnkksnSSKSIQNR 128
Cdd:PRK10318  81 ASSSSISGKPYIVKCPGKSDENAQPWLHALIAE-------TDKTVPAQ 121
 
Name Accession Description Interval E-value
PRK10318 PRK10318
hypothetical protein; Provisional
 2-128 1.84e-56

hypothetical protein; Provisional


Pssm-ID: 236672  Cd Length: 121  Bit Score: 171.47  E-value: 1.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446542395   2 IRKLIFLSIFLFCISIIAENDSNFRNDLNSLMNVL-ESCECKFIRNGSEHDSKEAREHMERKLKAVDGKIHTIQEFIDHI 80
Cdd:PRK10318   1 KKILCLLITLLFTLPAYAKLTAHEEARINAMLEGLaQKKDCTFVRNGDEHTCKEAVSHLRLKLGNTRNRIDTAEQFIDKV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446542395  81 GSKSSVSGKPYFVKFADGKTVESRVWLKEKWEEivnkksnSSKSIQNR 128
Cdd:PRK10318  81 ASSSSISGKPYIVKCPGKSDENAQPWLHALIAE-------TDKTVPAQ 121
DUF5329 pfam17263
Family of unknown function (DUF5329); This is a bacterial family of proteins with unknown ...
 23-114 2.80e-45

Family of unknown function (DUF5329); This is a bacterial family of proteins with unknown function.


Pssm-ID: 465394  Cd Length: 95  Bit Score: 142.43  E-value: 2.80e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446542395   23 SNFRNDLNSLMNVLESCECKFIRNGSEHDSKEAREHMERKLKAVDGK--IHTIQEFIDHIGSKSSVSGKPYFVKFADGKT 100
Cdd:pfam17263   1 PATEAEINALLSALESSGCEFIRNGSEHDAKEAREHLRRKYDYLRGKglISTAEDFIDRAASKSSISGKPYQVKCPGGAT 80

                          90
                  ....*....|....
gi 446542395  101 VESRVWLKEKWEEI 114
Cdd:pfam17263  81 VESGQWLTEELKRL 94
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
 23-55 4.11e-03

class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276872 [Multi-domain]  Cd Length: 669  Bit Score: 35.78  E-value: 4.11e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 446542395  23 SNFRNDLNSLMNVLESCECKFIRNGSEHDSKEA 55
Cdd:cd14907  579 SKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKA 611
 
Name Accession Description Interval E-value
PRK10318 PRK10318
hypothetical protein; Provisional
 2-128 1.84e-56

hypothetical protein; Provisional


Pssm-ID: 236672  Cd Length: 121  Bit Score: 171.47  E-value: 1.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446542395   2 IRKLIFLSIFLFCISIIAENDSNFRNDLNSLMNVL-ESCECKFIRNGSEHDSKEAREHMERKLKAVDGKIHTIQEFIDHI 80
Cdd:PRK10318   1 KKILCLLITLLFTLPAYAKLTAHEEARINAMLEGLaQKKDCTFVRNGDEHTCKEAVSHLRLKLGNTRNRIDTAEQFIDKV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446542395  81 GSKSSVSGKPYFVKFADGKTVESRVWLKEKWEEivnkksnSSKSIQNR 128
Cdd:PRK10318  81 ASSSSISGKPYIVKCPGKSDENAQPWLHALIAE-------TDKTVPAQ 121
DUF5329 pfam17263
Family of unknown function (DUF5329); This is a bacterial family of proteins with unknown ...
 23-114 2.80e-45

Family of unknown function (DUF5329); This is a bacterial family of proteins with unknown function.


Pssm-ID: 465394  Cd Length: 95  Bit Score: 142.43  E-value: 2.80e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446542395   23 SNFRNDLNSLMNVLESCECKFIRNGSEHDSKEAREHMERKLKAVDGK--IHTIQEFIDHIGSKSSVSGKPYFVKFADGKT 100
Cdd:pfam17263   1 PATEAEINALLSALESSGCEFIRNGSEHDAKEAREHLRRKYDYLRGKglISTAEDFIDRAASKSSISGKPYQVKCPGGAT 80

                          90
                  ....*....|....
gi 446542395  101 VESRVWLKEKWEEI 114
Cdd:pfam17263  81 VESGQWLTEELKRL 94
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
 23-55 4.11e-03

class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276872 [Multi-domain]  Cd Length: 669  Bit Score: 35.78  E-value: 4.11e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 446542395  23 SNFRNDLNSLMNVLESCECKFIRNGSEHDSKEA 55
Cdd:cd14907  579 SKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKA 611
 
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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