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Conserved domains on  [gi|15233789|ref|NP_194164|]
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hypothetical protein (DUF1682) [Arabidopsis thaliana]

Protein Classification

CCDC47 family protein( domain architecture ID 12085178)

CCDC47 family protein such as PAT complex subunit CCDC47 (Coiled-coil domain-containing protein 47), a component of the PAT complex that is part of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes

Gene Ontology:  GO:0016020|GO:0005509
PubMed:  32814900

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
150-467 6.58e-107

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


:

Pssm-ID: 462322  Cd Length: 323  Bit Score: 320.67  E-value: 6.58e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789   150 SYTVEIVCVSILIGYAINYFTGKRENENLALAWASKFglkDTIFEKNFSLLGVGEGEDSPLLLKEATNVFKFYASGRRYC 229
Cdd:pfam07946   1 DFKLEGIILAFLLLYVLNYFIGKRKNRRKAKKWFAAH---APLLESNFALVGFGDGKPSSLLIEDSPSEFTTYATGRRNC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789   230 HGLLATLELKSRHDLISRLFN--------SVVPCKDEISFEVYMNDEAMDHIVFAMARKKAAKTMHKELRDLqRFGGMVP 301
Cdd:pfam07946  78 AGLLVTLKLKKRQDLFSLLFElvlgfffdSVPPPKDRVEIDVYLFDGKMDPFVFAIVNKKEMKKLRKDRYDL-SLTKTKD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789   302 SPGgrkwVTEELAVVSESKEVAGDMITDVVLdqvfgdKSFEKFGKYFISMHFSDQHPGK--------HRKMLLFKFALP- 372
Cdd:pfam07946 157 NPK----LPEWLVVMSESAEITDALLTPELI------KALNKAGDLLEYLIITDQPSEKpetlkettPRKRLILSLRLPs 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789   373 DIKHMDDMVRLIALIPYYIDLIG-RYKLSSQARNKTDGARQKAAQEAYKELENVRQEALQ-RKKAEKKKILEEAQAKLSS 450
Cdd:pfam07946 227 SKSDYEALLPLLQLVLYLIDKLAkRAKLRPEALKKAKKTREEEIEKIKKAAEEERAEEAQeKKEEAKKKEREEKLAKLSP 306
                         330
                  ....*....|....*..
gi 15233789   451 EALRKKEAKERARQMKK 467
Cdd:pfam07946 307 EEQRKYEEKERKKEQRK 323
 
Name Accession Description Interval E-value
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
150-467 6.58e-107

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 320.67  E-value: 6.58e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789   150 SYTVEIVCVSILIGYAINYFTGKRENENLALAWASKFglkDTIFEKNFSLLGVGEGEDSPLLLKEATNVFKFYASGRRYC 229
Cdd:pfam07946   1 DFKLEGIILAFLLLYVLNYFIGKRKNRRKAKKWFAAH---APLLESNFALVGFGDGKPSSLLIEDSPSEFTTYATGRRNC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789   230 HGLLATLELKSRHDLISRLFN--------SVVPCKDEISFEVYMNDEAMDHIVFAMARKKAAKTMHKELRDLqRFGGMVP 301
Cdd:pfam07946  78 AGLLVTLKLKKRQDLFSLLFElvlgfffdSVPPPKDRVEIDVYLFDGKMDPFVFAIVNKKEMKKLRKDRYDL-SLTKTKD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789   302 SPGgrkwVTEELAVVSESKEVAGDMITDVVLdqvfgdKSFEKFGKYFISMHFSDQHPGK--------HRKMLLFKFALP- 372
Cdd:pfam07946 157 NPK----LPEWLVVMSESAEITDALLTPELI------KALNKAGDLLEYLIITDQPSEKpetlkettPRKRLILSLRLPs 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789   373 DIKHMDDMVRLIALIPYYIDLIG-RYKLSSQARNKTDGARQKAAQEAYKELENVRQEALQ-RKKAEKKKILEEAQAKLSS 450
Cdd:pfam07946 227 SKSDYEALLPLLQLVLYLIDKLAkRAKLRPEALKKAKKTREEEIEKIKKAAEEERAEEAQeKKEEAKKKEREEKLAKLSP 306
                         330
                  ....*....|....*..
gi 15233789   451 EALRKKEAKERARQMKK 467
Cdd:pfam07946 307 EEQRKYEEKERKKEQRK 323
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
410-464 3.47e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.99  E-value: 3.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15233789   410 ARQKAAQEAYKELEnvrQEALQRKKAEKKKILEEAQAKLSSEALRKKEAKERARQ 464
Cdd:TIGR02794 140 AERKAKEEAAKQAE---EEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKA 191
PTZ00121 PTZ00121
MAEBL; Provisional
398-473 1.19e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789   398 KLSSQARNKTDGARQKA-----AQEAYKELENVRQEALQRKKAEKKKILEEA-----QAKLSSEALRKKEAKERARQMKK 467
Cdd:PTZ00121 1411 KKAAAAKKKADEAKKKAeekkkADEAKKKAEEAKKADEAKKKAEEAKKAEEAkkkaeEAKKADEAKKKAEEAKKADEAKK 1490

                  ....*.
gi 15233789   468 SMPKVK 473
Cdd:PTZ00121 1491 KAEEAK 1496
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
410-469 5.46e-04

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: 40.11  E-value: 5.46e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789 410 ARQKAAQEAYKELENVRQEAlQRKKAEKKKILEEAQAKlsSEALRkKEAKERARQMKKSM 469
Cdd:cd06503  30 EREEKIAESLEEAEKAKEEA-EELLAEYEEKLAEARAE--AQEII-EEARKEAEKIKEEI 85
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
401-468 9.86e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 9.86e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789 401 SQARNKTDGARQK--AAQEAYKELEnVRQEALQRKKAEKKKILEEAQAKLsseALRKKEAKERARQMKKS 468
Cdd:COG3883  33 EAAQAELDALQAEleELNEEYNELQ-AELEALQAEIDKLQAEIAEAEAEI---EERREELGERARALYRS 98
 
Name Accession Description Interval E-value
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
150-467 6.58e-107

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 320.67  E-value: 6.58e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789   150 SYTVEIVCVSILIGYAINYFTGKRENENLALAWASKFglkDTIFEKNFSLLGVGEGEDSPLLLKEATNVFKFYASGRRYC 229
Cdd:pfam07946   1 DFKLEGIILAFLLLYVLNYFIGKRKNRRKAKKWFAAH---APLLESNFALVGFGDGKPSSLLIEDSPSEFTTYATGRRNC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789   230 HGLLATLELKSRHDLISRLFN--------SVVPCKDEISFEVYMNDEAMDHIVFAMARKKAAKTMHKELRDLqRFGGMVP 301
Cdd:pfam07946  78 AGLLVTLKLKKRQDLFSLLFElvlgfffdSVPPPKDRVEIDVYLFDGKMDPFVFAIVNKKEMKKLRKDRYDL-SLTKTKD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789   302 SPGgrkwVTEELAVVSESKEVAGDMITDVVLdqvfgdKSFEKFGKYFISMHFSDQHPGK--------HRKMLLFKFALP- 372
Cdd:pfam07946 157 NPK----LPEWLVVMSESAEITDALLTPELI------KALNKAGDLLEYLIITDQPSEKpetlkettPRKRLILSLRLPs 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789   373 DIKHMDDMVRLIALIPYYIDLIG-RYKLSSQARNKTDGARQKAAQEAYKELENVRQEALQ-RKKAEKKKILEEAQAKLSS 450
Cdd:pfam07946 227 SKSDYEALLPLLQLVLYLIDKLAkRAKLRPEALKKAKKTREEEIEKIKKAAEEERAEEAQeKKEEAKKKEREEKLAKLSP 306
                         330
                  ....*....|....*..
gi 15233789   451 EALRKKEAKERARQMKK 467
Cdd:pfam07946 307 EEQRKYEEKERKKEQRK 323
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
410-464 3.47e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.99  E-value: 3.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15233789   410 ARQKAAQEAYKELEnvrQEALQRKKAEKKKILEEAQAKLSSEALRKKEAKERARQ 464
Cdd:TIGR02794 140 AERKAKEEAAKQAE---EEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKA 191
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
409-468 9.46e-05

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 42.72  E-value: 9.46e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15233789   409 GARQKAAQEAYKEL-ENVRQEALQRKKAEKKKILEEAQAKLSSEALRKKEAKERARQMKKS 468
Cdd:pfam05672   3 SAGTTDAEEAARILaEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEA 63
PTZ00121 PTZ00121
MAEBL; Provisional
398-473 1.19e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789   398 KLSSQARNKTDGARQKA-----AQEAYKELENVRQEALQRKKAEKKKILEEA-----QAKLSSEALRKKEAKERARQMKK 467
Cdd:PTZ00121 1411 KKAAAAKKKADEAKKKAeekkkADEAKKKAEEAKKADEAKKKAEEAKKAEEAkkkaeEAKKADEAKKKAEEAKKADEAKK 1490

                  ....*.
gi 15233789   468 SMPKVK 473
Cdd:PTZ00121 1491 KAEEAK 1496
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
402-464 1.25e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 44.07  E-value: 1.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15233789   402 QARNKTDGARQKAAQEAYKELENVRQEALQRKKAEKKKILEEAQAKLSSEALRKKEAKERARQ 464
Cdd:TIGR02794  88 QARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK 150
PTZ00121 PTZ00121
MAEBL; Provisional
398-473 1.47e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789   398 KLSSQARNKTDGARQKA-----AQEAYKELENVRQEALQRKKAEKKKILEEA-----QAKLSSEALRKK-EAKERARQMK 466
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAeeakkAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkaeEAKKKADEAKKAaEAKKKADEAK 1516

                  ....*..
gi 15233789   467 KSMPKVK 473
Cdd:PTZ00121 1517 KAEEAKK 1523
PTZ00121 PTZ00121
MAEBL; Provisional
398-473 2.14e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 2.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15233789   398 KLSSQARNKTDGARQKAaQEAYKELENVRQEALQRKKAEKKKILEEAQaklSSEALRKKEAKERARQMKKSMPKVK 473
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKA-EEAKKKADEAKKAAEAKKKADEAKKAEEAK---KADEAKKAEEAKKADEAKKAEEKKK 1547
PTZ00121 PTZ00121
MAEBL; Provisional
398-473 2.39e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789   398 KLSSQARNKTDGARQKA-----AQEAYKELENVRQEALQRKKAEKKKILEEAQAKlSSEALRKKEAKERARQMKKSMPKV 472
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAeeakkADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEA 1502

                  .
gi 15233789   473 K 473
Cdd:PTZ00121 1503 K 1503
V-ATPase_G_2 pfam16999
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ...
402-460 2.58e-04

Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex


Pssm-ID: 339878 [Multi-domain]  Cd Length: 104  Bit Score: 40.11  E-value: 2.58e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15233789   402 QARNKTDGARQKAA---QEAYKELENVRQEALQRKKAEKKKILEEAQAKLSSEALRKKEAKE 460
Cdd:pfam16999  27 EAEREVEAAEAEAArilREAEAKAKALQAEYRQELAAETARIREEARARAEAEAQAVRTRAE 88
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
410-469 5.46e-04

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: 40.11  E-value: 5.46e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789 410 ARQKAAQEAYKELENVRQEAlQRKKAEKKKILEEAQAKlsSEALRkKEAKERARQMKKSM 469
Cdd:cd06503  30 EREEKIAESLEEAEKAKEEA-EELLAEYEEKLAEARAE--AQEII-EEARKEAEKIKEEI 85
PTZ00121 PTZ00121
MAEBL; Provisional
398-473 5.87e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 5.87e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15233789   398 KLSSQARNKTDGARQKAAQEAYKELENVRQ--EALQRKKAEKKKILEEAQAKlSSEALRKKEAKERARQMKKSMPKVK 473
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEkaEAAEKKKEEAKKKADAAKKK-AEEKKKADEAKKKAEEDKKKADELK 1411
PTZ00121 PTZ00121
MAEBL; Provisional
398-468 6.50e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 6.50e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233789   398 KLSSQARNKTDGARQKA-----AQEAYKELENVRQEALQ-RKKAEKKKILEEAQAKlSSEALRKKEAKERARQMKKS 468
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAeekkkADEAKKKAEEDKKKADElKKAAAAKKKADEAKKK-AEEKKKADEAKKKAEEAKKA 1446
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
410-464 6.63e-04

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 40.14  E-value: 6.63e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15233789  410 ARQKAAQ---EAYKELENVRQEALQRKKAEKKKILEEAQAKLSSEalrKKEAKERARQ 464
Cdd:PRK05759  68 ARAEAAEiieQAKKRAAQIIEEAKAEAEAEAARIKAQAQAEIEQE---RKRAREELRK 122
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
401-468 9.86e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 9.86e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789 401 SQARNKTDGARQK--AAQEAYKELEnVRQEALQRKKAEKKKILEEAQAKLsseALRKKEAKERARQMKKS 468
Cdd:COG3883  33 EAAQAELDALQAEleELNEEYNELQ-AELEALQAEIDKLQAEIAEAEAEI---EERREELGERARALYRS 98
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
412-469 1.09e-03

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: 39.39  E-value: 1.09e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15233789 412 QKAAQEAYKELENVRQEA---LQRKKAEKKKILEEAQAKLSSEALRKKE-AKERARQMKKSM 469
Cdd:COG0711  51 EAALAEYEEKLAEARAEAaeiIAEARKEAEAIAEEAKAEAEAEAERIIAqAEAEIEQERAKA 112
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
379-467 1.13e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789 379 DMVRLIALIPYYI----DLIGRYK--LSSQARNKTDGARQKAAQEAYKELENVRQEALQRKKAEKKKILEEAQAKLSSEA 452
Cdd:COG4942 133 DAVRRLQYLKYLAparrEQAEELRadLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
                        90
                ....*....|....*
gi 15233789 453 LRKKEAKERARQMKK 467
Cdd:COG4942 213 AELAELQQEAEELEA 227
PTZ00121 PTZ00121
MAEBL; Provisional
398-473 1.25e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15233789   398 KLSSQARNKTDGARQKaAQEAYKelenvRQEALQRKKAEKKKILEEAQAKLSSEALRKKEAKERARQMKKSMPKVK 473
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKK-AEEAKK-----AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
398-467 1.47e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 1.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15233789  398 KLSSQARNKTDgARQKAAQEAYKELE---NVRQEALQRKKAE---KKKILEEAQAKLSSEALRK--KEAKERARQMKK 467
Cdd:PRK09510 140 KAAAAAKAKAE-AEAKRAAAAAKKAAaeaKKKAEAEAAKKAAaeaKKKAEAEAAAKAAAEAKKKaeAEAKKKAAAEAK 216
PTZ00121 PTZ00121
MAEBL; Provisional
398-468 1.53e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15233789   398 KLSSQARNKTDGARQKAAQEAYKELENVRQEALQRKKAEKKKILEEAQAKLSSEA-----LRKKEAKE--RARQMKKS 468
Cdd:PTZ00121 1647 KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAkkaeeLKKKEAEEkkKAEELKKA 1724
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
411-477 1.90e-03

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.83  E-value: 1.90e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15233789 411 RQKAAQEaYKELENV--RQEALQRKKAEKKKILEEAQAKLSseALRKKEAKERARQMKKSMPKVKMSRG 477
Cdd:COG0497 326 AEELRAE-LAELENSdeRLEELEAELAEAEAELLEAAEKLS--AARKKAAKKLEKAVTAELADLGMPNA 391
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
398-473 2.00e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.56  E-value: 2.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15233789  398 KLSSQARNKTDGARQKAAQEAYK--ELENVRQEALQRKKAEKKKILEEAQAKLSSEALRKKEAKERARQMKKSMPKVK 473
Cdd:PRK09510 125 KQAALKQKQAEEAAAKAAAAAKAkaEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK 202
PTZ00121 PTZ00121
MAEBL; Provisional
402-473 2.31e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 2.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15233789   402 QARNKTDGARQKAAQEAYKELENVRQEALQRKKAEKKKILEEAQAKLSSEALRKKEAKERARQMKKSMPKVK 473
Cdd:PTZ00121 1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK 1431
PTZ00121 PTZ00121
MAEBL; Provisional
401-473 2.53e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789   401 SQARNKTDGARQKA-----AQEAYKELENVRQ--EALQRKKAEKKKILE--EAQAKLSSEALRKKEAKERARQMKKSMPK 471
Cdd:PTZ00121 1298 AEEKKKADEAKKKAeeakkADEAKKKAEEAKKkaDAAKKKAEEAKKAAEaaKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377

                  ..
gi 15233789   472 VK 473
Cdd:PTZ00121 1378 KK 1379
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
402-467 2.68e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.02  E-value: 2.68e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15233789 402 QARNKTDGARQKAAQEAyKELENVRQEALQRKKAEKKKILEEAQAKLssEALRKKEAKERARQMKK 467
Cdd:COG3064  41 EERLAELEAKRQAEEEA-REAKAEAEQRAAELAAEAAKKLAEAEKAA--AEAEKKAAAEKAKAAKE 103
AhaH TIGR02926
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
396-456 3.87e-03

ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The hydrophilic A1 "stalk" complex (AhaABCDEFG) is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex. It is unclear precisely where AhaH fits into these complexes.


Pssm-ID: 131972 [Multi-domain]  Cd Length: 85  Bit Score: 36.36  E-value: 3.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15233789   396 RYKLSSQARNKTDGARQKAAQEAYKELENVRQEALQRKKAEKKKILEEAQAKLssEALRKK 456
Cdd:TIGR02926  22 RKQRIAEAREEARELLEEAEEEASKLGEEIIKEAEEEIEKEAEKIREEGEKEI--EAMKSK 80
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
410-466 3.89e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 39.44  E-value: 3.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15233789   410 ARQKAAQEAYKELENVRQEALQRKKAEKKKILEEAQAKLSSEALRKKEAKERARQMK 466
Cdd:TIGR02794  74 EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAA 130
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
413-468 4.01e-03

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: 37.42  E-value: 4.01e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15233789 413 KAAQEAYKELENVRQEA---LQRKKAEKKKILEEAQA---KLSSEALrkKEAKERARQMKKS 468
Cdd:cd06503  40 EEAEKAKEEAEELLAEYeekLAEARAEAQEIIEEARKeaeKIKEEIL--AEAKEEAERILEQ 99
PTZ00121 PTZ00121
MAEBL; Provisional
398-468 4.20e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 4.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15233789   398 KLSSQARNKTDGARQKAaqEAYKELENVRQeALQRKKAEKKKILEEAQaklSSEALRKKEAKERARQMKKS 468
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAA--EAKKKADEAKK-AEEAKKADEAKKAEEAK---KADEAKKAEEKKKADELKKA 1554
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
401-464 4.41e-03

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: 37.42  E-value: 4.41e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15233789 401 SQARNKTDGARQKAAQEAYKELENVRQEAlqrkKAEKKKILEEAQAKLSSEalrKKEAKERARQ 464
Cdd:cd06503  61 AEARAEAQEIIEEARKEAEKIKEEILAEA----KEEAERILEQAKAEIEQE---KEKALAELRK 117
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
410-467 4.72e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 39.06  E-value: 4.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15233789   410 ARQKAAqEAYKELEnvrQEALQRKKAEKKKILEEAQAK-LSSEALRKKEAKERARQMKK 467
Cdd:TIGR02794 164 AKKKAE-EAKKKAE---AEAKAKAEAEAKAKAEEAKAKaEAAKAKAAAEAAAKAEAEAA 218
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
402-467 5.66e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.02  E-value: 5.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15233789  402 QARNKTDGARQKAAQEAYKELENVRQEA-LQRKKAE--KKKILEEAQAKLSSEALRKKEAKERARQMKK 467
Cdd:PRK09510 100 QERLKQLEKERLAAQEQKKQAEEAAKQAaLKQKQAEeaAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAK 168
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
410-467 6.32e-03

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: 37.07  E-value: 6.32e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15233789 410 ARQKAAQEAYKELENVRQEAlQRKKAEKKKILEEAQAKlsSEALRkKEAKERARQMKK 467
Cdd:COG0711  31 ERQEKIADGLAEAERAKEEA-EAALAEYEEKLAEARAE--AAEII-AEARKEAEAIAE 84
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
411-462 6.34e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 38.63  E-value: 6.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15233789  411 RQKAAQEAYKELENVRQEALQRKK---------AEKKKILEEAQAKLSSEALRKKEAKERA 462
Cdd:PRK09510  95 KQAAEQERLKQLEKERLAAQEQKKqaeeaakqaALKQKQAEEAAAKAAAAAKAKAEAEAKR 155
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
398-464 6.36e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 38.67  E-value: 6.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233789   398 KLSSQARNKTdgARQKAAQEAYKELENVRQEALQRKKAEKKKILEEAQAKLSSEAlRKKEAKERARQ 464
Cdd:TIGR02794  72 KLEQQAEEAE--KQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEA-KAKQAAEAKAK 135
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
379-467 9.45e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 36.40  E-value: 9.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233789   379 DMVRLIALIPYYIDLIGRYKLSSQARNKTDGARQKAAQEAYKELENV----------RQEALQRKKAEkkkiLEEAQAKL 448
Cdd:pfam03938   6 DMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDgalleeereeKEQELQKKEQE----LQQLQQKA 81
                          90
                  ....*....|....*....
gi 15233789   449 SSEaLRKKEAKERARQMKK 467
Cdd:pfam03938  82 QQE-LQKKQQELLQPIQDK 99
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
402-469 9.68e-03

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: 36.26  E-value: 9.68e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15233789 402 QARNKTDGARQKAAQ---EAYKELENVRQEALQRKKAEKKKILEEAQAklssEALRKKE-AKERARQMKKSM 469
Cdd:cd06503  44 KAKEEAEELLAEYEEklaEARAEAQEIIEEARKEAEKIKEEILAEAKE----EAERILEqAKAEIEQEKEKA 111
 
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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