NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489915665|ref|WP_003819064|]
View 

MULTISPECIES: F0F1 ATP synthase subunit B [Bifidobacterium]

Protein Classification

F0F1 ATP synthase subunit B( domain architecture ID 11481619)

F0F1 ATP synthase subunit B is part of the membrane proton channel of the F-type ATPase that produces ATP from ADP in the presence of a proton gradient across the membrane

Gene Ontology:  GO:0015986|GO:0015078|GO:0045263
PubMed:  7961438|15473999|15078220

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 17-169 5.13e-46

F0F1 ATP synthase subunit B; Validated


:

Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 148.00  E-value: 5.13e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  17 YDIVWSLIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEAS 96
Cdd:PRK05759   5 GTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAKKRAA 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489915665  97 HIIADARSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKLeSDDVQSSMIDKMIDDL 169
Cdd:PRK05759  85 QIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGREL-DAAAQSDLIDKLIAEL 156
 
Name Accession Description Interval E-value
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 17-169 5.13e-46

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 148.00  E-value: 5.13e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  17 YDIVWSLIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEAS 96
Cdd:PRK05759   5 GTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAKKRAA 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489915665  97 HIIADARSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKLeSDDVQSSMIDKMIDDL 169
Cdd:PRK05759  85 QIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGREL-DAAAQSDLIDKLIAEL 156
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 17-169 2.86e-34

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 117.97  E-value: 2.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  17 YDIVWSLIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEAS 96
Cdd:COG0711    1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489915665  97 HIIADARSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKLeSDDVQSSMIDKMIDDL 169
Cdd:COG0711   81 AIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKEL-DAAAQAALVDRFIAEL 152
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 18-149 5.94e-34

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 116.38  E-value: 5.94e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  18 DIVWSLIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEASH 97
Cdd:cd06503    1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489915665  98 IIADARSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILG 149
Cdd:cd06503   81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKILG 132
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 19-149 7.19e-22

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 85.44  E-value: 7.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665   19 IVWSLIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEASHI 98
Cdd:pfam00430   2 LVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489915665   99 IADARSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILG 149
Cdd:pfam00430  82 KEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 23-169 7.93e-21

ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130214 [Multi-domain]  Cd Length: 147  Bit Score: 83.22  E-value: 7.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665   23 LIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEASHIIADA 102
Cdd:TIGR01144   2 LISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEEA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489915665  103 RSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKLEsDDVQSSMIDKMIDDL 169
Cdd:TIGR01144  82 KAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNID-KQAQKDLIDKLVAEL 147
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 46-163 6.84e-04

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 39.43  E-value: 6.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665   46 DERAAKIEGNIAKAEQSKKDADAAKSKyeaqlstARVEASKIRDDARA----------EASHIIADARSRAESDAAQ--- 112
Cdd:NF012221 1688 KDAVAKSEAGVAQGEQNQANAEQDIDD-------AKADAEKRKDDALAkqneaqqaesDANAAANDAQSRGEQDASAaen 1760

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489915665  113 ITANAQRSIESQQQQALVSlKGEVGTLATALAGKilGAKLESDDVQSSMID 163
Cdd:NF012221 1761 KANQAQADAKGAKQDESDK-PNRQGAAGSGLSGK--AYSVEGVAEPGSHIN 1808
growth_prot_Scy NF041483
polarized growth protein Scy;
57-129 2.13e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 37.88  E-value: 2.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489915665   57 AKAEQSKKDADAAKskyEAQLSTARVEASKIRDDARAEASHIIADARSRAESDAAQITANAQRSIESQQQQAL 129
Cdd:NF041483  993 TEAERVKAEAAAEA---ERLRTEAREEADRTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEAL 1062
 
Name Accession Description Interval E-value
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 17-169 5.13e-46

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 148.00  E-value: 5.13e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  17 YDIVWSLIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEAS 96
Cdd:PRK05759   5 GTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAKKRAA 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489915665  97 HIIADARSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKLeSDDVQSSMIDKMIDDL 169
Cdd:PRK05759  85 QIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGREL-DAAAQSDLIDKLIAEL 156
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 17-169 2.86e-34

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 117.97  E-value: 2.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  17 YDIVWSLIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEAS 96
Cdd:COG0711    1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489915665  97 HIIADARSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKLeSDDVQSSMIDKMIDDL 169
Cdd:COG0711   81 AIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKEL-DAAAQAALVDRFIAEL 152
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 18-149 5.94e-34

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 116.38  E-value: 5.94e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  18 DIVWSLIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEASH 97
Cdd:cd06503    1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489915665  98 IIADARSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILG 149
Cdd:cd06503   81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKILG 132
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 19-149 7.19e-22

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 85.44  E-value: 7.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665   19 IVWSLIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEASHI 98
Cdd:pfam00430   2 LVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489915665   99 IADARSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILG 149
Cdd:pfam00430  82 KEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
PRK14471 PRK14471
F0F1 ATP synthase subunit B; Provisional
 9-172 5.67e-21

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184695 [Multi-domain]  Cd Length: 164  Bit Score: 84.07  E-value: 5.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665   9 LKLFIPQVYDIVWSLIILVIVALFFHKF-FMPKFNAIfDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKI 87
Cdd:PRK14471   1 MDLLTPDFGLFFWQTILFLILLLLLAKFaWKPILGAV-KEREDSIKNALASAEEARKEMQNLQADNERLLKEARAERDAI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  88 RDDARAEASHIIADARSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKLESDDVQSSMIDKMID 167
Cdd:PRK14471  80 LKEAREIKEKMIADAKEEAQVEGDKMIEQAKASIESEKNAAMAEIKNQVANLSVEIAEKVLRKELSNKEKQHKLVEKMLG 159


                 ....*
gi 489915665 168 DLDTN 172
Cdd:PRK14471 160 DVKLN 164
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 23-169 7.93e-21

ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130214 [Multi-domain]  Cd Length: 147  Bit Score: 83.22  E-value: 7.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665   23 LIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEASHIIADA 102
Cdd:TIGR01144   2 LISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEEA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489915665  103 RSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKLEsDDVQSSMIDKMIDDL 169
Cdd:TIGR01144  82 KAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNID-KQAQKDLIDKLVAEL 147
PRK14472 PRK14472
F0F1 ATP synthase subunit B; Provisional
 19-172 2.93e-18

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172947 [Multi-domain]  Cd Length: 175  Bit Score: 77.54  E-value: 2.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  19 IVWSLIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEASHI 98
Cdd:PRK14472  21 IFWTAVTFVIVLLILKKIAWGPILSALEEREKGIQSSIDRAHSAKDEAEAILRKNRELLAKADAEADKIIREGKEYAEKL 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489915665  99 IADARSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKLESdDVQSSMIDKMIDDLDTN 172
Cdd:PRK14472 101 RAEITEKAHTEAKKMIASAKEEIEQEKRRALDVLRNEVADLAVKGAEKIIRTSLDA-DKQKKVVDSMIQDLSTK 173
PRK13460 PRK13460
F0F1 ATP synthase subunit B; Provisional
 1-170 5.69e-18

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 139585 [Multi-domain]  Cd Length: 173  Bit Score: 76.60  E-value: 5.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665   1 MTIAASDGLKLFIPQVYDIVWSLIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTA 80
Cdd:PRK13460   1 MVLLAAKGLSLLDVNPGLVVWTLVTFLVVVLVLKKFAWDVILKALDERASGVQNDINKASELRLEAEALLKDYEARLNSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  81 RVEASKIRDDARAEASHIIADARSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKLESDDVQsS 160
Cdd:PRK13460  81 KDEANAIVAEAKSDALKLKNKLLEETNNEVKAQKDQAVKEIELAKGKALSQLQNQIVEMTITIASKVLEKQLKKEDYK-A 159

                        170
                 ....*....|
gi 489915665 161 MIDKMIDDLD 170
Cdd:PRK13460 160 FIETELAKLG 169
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 23-172 2.68e-15

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 69.60  E-value: 2.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  23 LIILVIVaLFFHKFFMPKF-NAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEASHIIAD 101
Cdd:PRK07352  26 LINLAIV-IGLLYYFGRGFlGKILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIRAE 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489915665 102 ARSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKLEsDDVQSSMIDKMIDDLDTN 172
Cdd:PRK07352 105 IEKQAIEDMARLKQTAAADLSAEQERVIAQLRREAAELAIAKAESQLPGRLD-EDAQQRLIDRSIANLGGN 174
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
 36-151 9.99e-15

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 67.34  E-value: 9.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  36 FFMPKFNAIfDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEASHIIADARSRAESDAAQITA 115
Cdd:PRK07353  26 FYKPVGKVV-EEREDYIRTNRAEAKERLAEAEKLEAQYEQQLASARKQAQAVIAEAEAEADKLAAEALAEAQAEAQASKE 104

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489915665 116 NAQRSIESQQQQALVSLKGEVGTLATALAGKILGAK 151
Cdd:PRK07353 105 KARREIEQQKQAALAQLEQQVDALSRQILEKLLAAK 140
PRK13428 PRK13428
F0F1 ATP synthase subunit delta; Provisional
 27-170 3.84e-14

F0F1 ATP synthase subunit delta; Provisional


Pssm-ID: 184048 [Multi-domain]  Cd Length: 445  Bit Score: 68.99  E-value: 3.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  27 VIVALFFhKFFMPKFNAIFDERAAKIEGNIAKAEQSKK---DADAAKSKyeaQLSTARVEASKIRDDARAEASHIIADAR 103
Cdd:PRK13428  13 VIVFLVW-RFVVPPVRRLMAARQDTVRQQLAESATAADrlaEADQAHTK---AVEDAKAEAARVVEEAREDAERIAEQLR 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489915665 104 SRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKLESDDVQSSMIDKMIDDLD 170
Cdd:PRK13428  89 AQADAEAERIKVQGARQVQLLRAQLTRQLRLELGHESVRQAGELVRNHVADPAQQSATVDRFLDELD 155
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 9-170 8.61e-14

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 65.33  E-value: 8.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665   9 LKLFIPQVYDIVwsLIILVIVALFFHkffmPKFNAIfDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKI- 87
Cdd:PRK14473   8 LGLLIAQLINFL--LLIFLLRTFLYR----PVLNLL-NERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAKIv 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  88 ---RDDARAEASHIIADARsraeSDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKLESDDvQSSMIDK 164
Cdd:PRK14473  81 aqaQERARAQEAEIIAQAR----REAEKIKEEARAQAEQERQRMLSELKSQIADLVTLTASRVLGAELQARG-HDALIAE 155


                 ....*.
gi 489915665 165 MIDDLD 170
Cdd:PRK14473 156 SLAALG 161
PRK13461 PRK13461
F0F1 ATP synthase subunit B; Provisional
 19-150 3.54e-12

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184064 [Multi-domain]  Cd Length: 159  Bit Score: 60.83  E-value: 3.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  19 IVWSLIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEASHI 98
Cdd:PRK13461   8 IIATIINFIILLLILKHFFFDKIKAVIDSRQSEIDNKIEKADEDQKKARELKLKNERELKNAKEEGKKIVEEYKSKAENV 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489915665  99 IADARSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGA 150
Cdd:PRK13461  88 YEEIVKEAHEEADLIIERAKLEAQREKEKAEYEIKNQAVDLAVLLSSKALEE 139
atpG CHL00118
ATP synthase CF0 B' subunit; Validated
 23-149 8.82e-12

ATP synthase CF0 B' subunit; Validated


Pssm-ID: 214369 [Multi-domain]  Cd Length: 156  Bit Score: 60.00  E-value: 8.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  23 LIILVIVALFFHKffmpKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEASHIIADA 102
Cdd:CHL00118  33 LLLMVLLNIILYK----PLLKVLDERKEYIRKNLTKASEILAKANELTKQYEQELSKARKEAQLEITQSQKEAKEIVENE 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489915665 103 RSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILG 149
Cdd:CHL00118 109 LKQAQKYIDSLLNEATKQLEAQKEKALKSLEEQVDTLSDQIEEKLLI 155
PRK13454 PRK13454
F0F1 ATP synthase subunit B'; Provisional
 19-165 1.48e-11

F0F1 ATP synthase subunit B'; Provisional


Pssm-ID: 184061 [Multi-domain]  Cd Length: 181  Bit Score: 59.84  E-value: 1.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  19 IVWSLIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEASHI 98
Cdd:PRK13454  34 IFWLLVTLVAIYFVLTRVALPRIGAVLAERQGTITNDLAAAEELKQKAVEAEKAYNKALADARAEAQRIVAETRAEIQAE 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489915665  99 IADARSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAgKILGAKLESDDVQSSMIDKM 165
Cdd:PRK13454 114 LDVAIAKADAEIAAKAAESEKRIAEIRAGALESVEEVAKDTAEALV-AALGGKADAAAVDAAVAQRM 179
PRK13453 PRK13453
F0F1 ATP synthase subunit B; Provisional
 19-168 1.29e-10

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184060  Cd Length: 173  Bit Score: 57.23  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  19 IVWSLIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEA--- 95
Cdd:PRK13453  21 VIVTVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQArqq 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489915665  96 -SHIIADARSRAESdaaqITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKLESDDvQSSMIDKMIDD 168
Cdd:PRK13453 101 qEQIIHEANVRANG----MIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQD-QKALVDKYLKE 169
PRK06231 PRK06231
F0F1 ATP synthase subunit B; Validated
 12-174 3.90e-08

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180481 [Multi-domain]  Cd Length: 205  Bit Score: 50.61  E-value: 3.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  12 FIPQVYDIVWSLIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDA----DAAKSKYEAqlstARVEASKI 87
Cdd:PRK06231  44 LFPNFWVFIAHLIAFSILLLLGIFLFWKPTQRFLNKRKELIEAEINQANELKQQAqqllENAKQRHEN----ALAQAKEI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  88 RDDARAEASHIIADARSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKLESDDvQSSMIDKMID 167
Cdd:PRK06231 120 IDQANYEALQLKSELEKEANRQANLIIFQARQEIEKERRELKEQLQKESVELAMLAAEELIKKKVDRED-DDKLVDEFIR 198


                 ....*..
gi 489915665 168 DLDTNDK 174
Cdd:PRK06231 199 ELEANEK 205
PRK09174 PRK09174
F0F1 ATP synthase subunit B;
19-159 4.77e-08

F0F1 ATP synthase subunit B;


Pssm-ID: 169692 [Multi-domain]  Cd Length: 204  Bit Score: 50.57  E-value: 4.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  19 IVWSLIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEASHI 98
Cdd:PRK09174  56 LLWLAITFGLFYLFMSRVILPRIGGIIETRRDRIAQDLDQAARLKQEADAAVAAYEQELAQARAKAHSIAQAAREAAKAK 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489915665  99 IADARSRAESDAAQITANAQRSIESQQQQALvslkGEVGTLA----TALAGKILGAKLESDDVQS 159
Cdd:PRK09174 136 AEAERAAIEASLEKKLKEAEARIAAIKAKAM----ADVGSIAeetaAAIVEQLIGGTADKASVAA 196
atpF CHL00019
ATP synthase CF0 B subunit
 23-171 3.02e-07

ATP synthase CF0 B subunit


Pssm-ID: 176962 [Multi-domain]  Cd Length: 184  Bit Score: 47.94  E-value: 3.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  23 LIILVIVALFFHKFFmpkFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEASHIIADA 102
Cdd:CHL00019  34 LSVVLGVLIYFGKGV---LSDLLDNRKQTILNTIRNSEERREEAIEKLEKARARLRQAELEADEIRVNGYSEIEREKENL 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489915665 103 RSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKLeSDDVQSSMIDKMIDDLDT 171
Cdd:CHL00019 111 INQAKEDLERLENYKNETIRFEQQRAINQVRQQVFQLALQRALGTLNSCL-NNELHLRTINANIGLLGA 178
PRK02292 PRK02292
V-type ATP synthase subunit E; Provisional
 79-136 7.10e-07

V-type ATP synthase subunit E; Provisional


Pssm-ID: 235026 [Multi-domain]  Cd Length: 188  Bit Score: 46.91  E-value: 7.10e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489915665  79 TARVEASKIRDDARAEASHIIADARSRAESDAAQITANAQRSIESQQQQALVSLKGEV 136
Cdd:PRK02292  13 EARARASEIRAEADEEAEEIIAEAEADAEEILEDREAEAEREIEQLREQELSSAKLEA 70
PRK14475 PRK14475
F0F1 ATP synthase subunit B; Provisional
 24-152 1.12e-05

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184697 [Multi-domain]  Cd Length: 167  Bit Score: 43.39  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  24 IILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEASHIIADAR 103
Cdd:PRK14475  18 LLIFFGILIALKVLPKALAGALDAYAAKIQAELDEAQRLREEAQALLADVKAEREEAERQAAAMLAAAKADARRMEAEAK 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489915665 104 SRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKL 152
Cdd:PRK14475  98 EKLEEQIKRRAEMAERKIAQAEAQAAADVKAAAVDLAAQAAETVLAARL 146
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
 77-136 2.38e-04

Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 39.93  E-value: 2.38e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  77 LSTARVEASKIRDDARAEASHIIADARSRAESDAAQITANAQRSIESQQQQALVSLKGEV 136
Cdd:COG1390   12 LEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEA 71
PRK13455 PRK13455
F0F1 ATP synthase subunit B; Provisional
 18-171 4.92e-04

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184062 [Multi-domain]  Cd Length: 184  Bit Score: 39.01  E-value: 4.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  18 DIVWSLIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARVEASKIRDDARAEASH 97
Cdd:PRK13455  29 DFVVTLAFLLFIGILVYFKVPGMIGGMLDKRAEGIRSELEEARALREEAQTLLASYERKQREVQEQADRIVAAAKDEAQA 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489915665  98 IIADARSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKLESDDvQSSMIDKMIDDLDT 171
Cdd:PRK13455 109 AAEQAKADLEASIARRLAAAEDQIASAEAAAVKAVRDRAVSVAVAAAADVIAKQMTAAD-ANALIDEAIKEVEA 181
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 46-163 6.84e-04

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 39.43  E-value: 6.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665   46 DERAAKIEGNIAKAEQSKKDADAAKSKyeaqlstARVEASKIRDDARA----------EASHIIADARSRAESDAAQ--- 112
Cdd:NF012221 1688 KDAVAKSEAGVAQGEQNQANAEQDIDD-------AKADAEKRKDDALAkqneaqqaesDANAAANDAQSRGEQDASAaen 1760

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489915665  113 ITANAQRSIESQQQQALVSlKGEVGTLATALAGKilGAKLESDDVQSSMID 163
Cdd:NF012221 1761 KANQAQADAKGAKQDESDK-PNRQGAAGSGLSGK--AYSVEGVAEPGSHIN 1808
PRK08475 PRK08475
F0F1 ATP synthase subunit B; Validated
 15-158 7.37e-04

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 236272 [Multi-domain]  Cd Length: 167  Bit Score: 38.46  E-value: 7.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  15 QVYDIVWSLIILVIVALFFHKFFMPKFNAIFDERAAKIEGNIAKAEQSKKDADAAKSKYEAQLstarveaskirDDARAE 94
Cdd:PRK08475  21 EQYDIIERTINFLIFVGILWYFAAKPLKNFYKSRINKISKRLEEIQEKLKESKEKKEDALKKL-----------EEAKEK 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489915665  95 ASHIIADARSRAESDAAQITANAQRSIESQQQQALVSLKGEVGTLATALAGKILGAKLESDDVQ 158
Cdd:PRK08475  90 AELIVETAKKEAYILTQKIEKQTKDDIENLIKSFEELMEFEVRKMEREVVEEVLNELFESKKVS 153
growth_prot_Scy NF041483
polarized growth protein Scy;
57-129 2.13e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 37.88  E-value: 2.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489915665   57 AKAEQSKKDADAAKskyEAQLSTARVEASKIRDDARAEASHIIADARSRAESDAAQITANAQRSIESQQQQAL 129
Cdd:NF041483  993 TEAERVKAEAAAEA---ERLRTEAREEADRTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEAL 1062
PTZ00121 PTZ00121
MAEBL; Provisional
 47-128 4.21e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.04  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665   47 ERAAKIEGNIAKAEQSKKDADAAKSKYEAQLSTARV---EASKIRDDARAEASHIIADARSRAE----SDAAQITANAQR 119
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAakaEAEAAADEAEAAEEKAEAAEKKKEEakkkADAAKKKAEEKK 1391


                  ....*....
gi 489915665  120 SIESQQQQA 128
Cdd:PTZ00121 1392 KADEAKKKA 1400
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 46-126 6.46e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 36.34  E-value: 6.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489915665  46 DERAAKIEGNIAKAEQSKKDADAAKSKYEAQ----LSTARVEASKIRDDARAEASHIIADARSRAESDAAQItaNAQRSI 121
Cdd:PRK00409 533 EQKAEEAEALLKEAEKLKEELEEKKEKLQEEedklLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASV--KAHELI 610


                 ....*
gi 489915665 122 ESQQQ 126
Cdd:PRK00409 611 EARKR 615
PRK09098 PRK09098
HrpE/YscL family type III secretion apparatus protein;
66-119 8.92e-03

HrpE/YscL family type III secretion apparatus protein;


Pssm-ID: 181646 [Multi-domain]  Cd Length: 233  Bit Score: 35.55  E-value: 8.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489915665  66 ADAAKSKYEAQLSTARVEASKIRDDARAEASHIIADARSRAESDAAQITANAQR 119
Cdd:PRK09098  34 LAAVHAERDAVLAAARARAERIVAEARAQAEAILEAARREADRSARRGYAAGLR 87
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH