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Conserved domains on  [gi|501075448|ref|WP_012126317|]
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MULTISPECIES: cellulose biosynthesis protein BcsQ [Cronobacter]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
1-237 1.60e-118

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member PRK10037:

Pssm-ID: 476819  Cd Length: 250  Bit Score: 338.00  E-value: 1.60e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448   1 MTVLALQGVRGGVGTTSLTAALGWALHQLGESVLVIDASPDNLLRLSFNIDFDHADGWARALLDDKPWQSTAWRYAPGLD 80
Cdd:PRK10037   1 MAILGLQGVRGGVGTTSITAALAWSLQMLGENVLVIDACPDNLLRLSFNVDFTHRQGWARALLDGQDWRDAGLRYTSQLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448  81 VLPYGALRQTERENDVT--PALGAFAQHLHLLKASGQWRWILLDLPCGFDAVTRSLLQVADRTLCVVQPDANCHARLHQQ 158
Cdd:PRK10037  81 LLPFGQLSIEEQENPQHwqTRLGDICSALQQLKASGRYQWILLDLPRGASPLTRQLLSLCDHSLAIVNVDANCHIRLHQQ 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501075448 159 ALPSGCDLLANFRLISSQIQNDIWQLWLQTQRNLVPVAVHRDEAMMESLAAKQPVGEYRPDSLVAEEIVTLANWCLLHY 237
Cdd:PRK10037 161 ALPAGAHILINDLRIGSQLQDDLYQLWLQSQRRLLPMLIHRDEAMAECLAAKQPLGEYRSDSLAAEEILTLANWCLLHY 239
 
Name Accession Description Interval E-value
PRK10037 PRK10037
cellulose biosynthesis protein BcsQ;
1-237 1.60e-118

cellulose biosynthesis protein BcsQ;


Pssm-ID: 182204  Cd Length: 250  Bit Score: 338.00  E-value: 1.60e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448   1 MTVLALQGVRGGVGTTSLTAALGWALHQLGESVLVIDASPDNLLRLSFNIDFDHADGWARALLDDKPWQSTAWRYAPGLD 80
Cdd:PRK10037   1 MAILGLQGVRGGVGTTSITAALAWSLQMLGENVLVIDACPDNLLRLSFNVDFTHRQGWARALLDGQDWRDAGLRYTSQLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448  81 VLPYGALRQTERENDVT--PALGAFAQHLHLLKASGQWRWILLDLPCGFDAVTRSLLQVADRTLCVVQPDANCHARLHQQ 158
Cdd:PRK10037  81 LLPFGQLSIEEQENPQHwqTRLGDICSALQQLKASGRYQWILLDLPRGASPLTRQLLSLCDHSLAIVNVDANCHIRLHQQ 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501075448 159 ALPSGCDLLANFRLISSQIQNDIWQLWLQTQRNLVPVAVHRDEAMMESLAAKQPVGEYRPDSLVAEEIVTLANWCLLHY 237
Cdd:PRK10037 161 ALPAGAHILINDLRIGSQLQDDLYQLWLQSQRRLLPMLIHRDEAMAECLAAKQPLGEYRSDSLAAEEILTLANWCLLHY 239
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
1-234 4.68e-111

Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in cellulose biosynthesis. (Roemling U. and Galperin M.Y. "Bacterial cellulose biosynthesis. Diversity of operons and subunits" (manuscript in preparation)). A second component of the extracellular matrix of the multicellular morphotype (rdar) of Salmonella typhimurium and Escherichia coli is cellulose. The family does contain a P-loop sequence motif suggesting a nucleotide binding function, but this has not been confirmed.


Pssm-ID: 429004 [Multi-domain]  Cd Length: 234  Bit Score: 318.55  E-value: 4.68e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448    1 MTVLALQGVRGGVGTTSLTAALGWALHQLGESVLVIDASPDNLLRLSFNIDFDHADGWARALLDDKPWQSTAWRYAPGLD 80
Cdd:pfam06564   1 MKILALQGVRGGVGTTSILAALAWALQRLGERVLLIDLSPDNLLRLHFNVPFEHRQGWARAELDGADWRDAALEYTPGLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448   81 VLPYGALRQTEREN--DVTPALGAFAQHLHLLKasGQWRWILLDLPCGFDAVTRSLLQVADRTLCVVQPDANCHARLHQQ 158
Cdd:pfam06564  81 LLPFGRLSVEEQENlqQLQPDPGAWCRRLQQLK--GRYDWVLFDLPAGPSPLTRQLLSLADLSLLVVNPDANCHVLLHQQ 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501075448  159 ALPSGCDLLANFRLISSQIQNDIWQLWLQTQRNLVPVAVHRDEAMMESLAAKQPVGEYRPDSLVAEEIVTLANWCL 234
Cdd:pfam06564 159 PLPDADHLLINDFRPASQLQQDLLQLWRQSQRRLLPLVIHRDEALAEALAAKQPLGEYRPDSLAAEEVLTLANWCL 234
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
1-238 2.28e-78

cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found immediately upsteam of bacterial cellulose synthase (bcs) genes in a broad range of bacteria, including both copies of the bcs locus in Klebsiella pneumoniae. In several species it is seen clearly as part of the bcs operon. It is identified as a probable component of the bacterial cellulose metabolic process not only by gene location, but also by partial phylogenetic profiling, or Haft-Selengut algorithm (), based on a bacterial cellulose biosynthesis genome property profile. Cellulose plays an important role in biofilm formation and structural integrity in some bacteria. Mutants in yhjQ in Escherichia coli, show altered morphology an growth, but the function of YhjQ has not yet been determined. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274549 [Multi-domain]  Cd Length: 246  Bit Score: 236.09  E-value: 2.28e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448    1 MTVLALQGVRGGVGTTSLTAALGWALHQLGESVLVIDASPDNLLRLSFNIDFDHADGWARALLDDKPWQSTAWRYAPGLD 80
Cdd:TIGR03371   1 MKVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLHFGMDWSVRDGWARALLNGADWAAAAYRSPDGVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448   81 VLPYGALRQTERENDVTPALGAFAQHLHLLKASGQwRWILLDLPCGFDAVTRSLLQVADRTLCVVQPDANCHARLHQQAL 160
Cdd:TIGR03371  81 FLPYGDLSADEREAYQAHDAGWLARLLQQLDLAAR-DWVLIDLPRGPSPITRQALAAADLVLVVVNADAACYATLHQLAL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448  161 --------PSGCDLLANFRLISSQIQNDIWQLWLQTQ-RNLVPVAVHRDEAMMESLAAKQPVGEYRPDSLVAEEIVTLAN 231
Cdd:TIGR03371 160 alfagsgpRDGPRFLINQFDPARQLSRDVRAVLRQTLgSRLLPFVIHRDEAVSEALARGTPVLNYAPHSQAAHDIRTLAG 239

                  ....*..
gi 501075448  232 WCLLHYR 238
Cdd:TIGR03371 240 WLLSKLS 246
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
1-232 6.39e-18

ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440805 [Multi-domain]  Cd Length: 253  Bit Score: 79.90  E-value: 6.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448   1 MTVLALQGVRGGVGTTSLTAALGWALHQLGESVLVIDASPDNLLRLSFNIDFDHAD-GWARALLDDKPWQSTAWR-YAPG 78
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDpTLYDLLLDDAPLEDAIVPtEIPG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448  79 LDVLP-YGALRQTERENDVTPALGAFAQHLhLLKASGQWRWILLDLPCGFDAVTRSLLQVADRTLCVVQPDAncharlhq 157
Cdd:COG1192   81 LDLIPaNIDLAGAEIELVSRPGRELRLKRA-LAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEY-------- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448 158 QALPSGCDLLANFRLISSQIQNDIWQL-------------------WLQTQ--RNLVPVAVHRDEAMMESLAAKQPVGEY 216
Cdd:COG1192  152 LSLEGLAQLLETIEEVREDLNPKLEILgilltmvdprtrlsrevleELREEfgDKVLDTVIPRSVALAEAPSAGKPVFEY 231
                        250
                 ....*....|....*.
gi 501075448 217 RPDSLVAEEIVTLANW 232
Cdd:COG1192  232 DPKSKGAKAYRALAEE 247
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
3-231 4.61e-14

pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.


Pssm-ID: 349765 [Multi-domain]  Cd Length: 235  Bit Score: 69.23  E-value: 4.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448   3 VLALQGVRGGVGTTSLTAALGWALHQL-GESVLVID---ASPDNLLRLSFNIDFDHADGwARAL--LDDKPWQSTAWRYA 76
Cdd:cd03111    2 VVAVVGAKGGVGASTLAVNLAQELAQRaKDKVLLIDldlPFGDLGLYLNLRPDYDLADV-IQNLdrLDRTLLDSAVTRHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448  77 PGLDVLPygaLRQTERENDvtpALGAfAQHLHLL-KASGQWRWILLDLPCGFDAVTRSLLQVADRTLCVVQPDANC--HA 153
Cdd:cd03111   81 SGLSLLP---APQELEDLE---ALGA-EQVDKLLqVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSlrNA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448 154 -RLHQ---QALPSG--CDLLANFRLISSQIQ-NDIWQLwlqTQRNLVPVAVHRDEAMMESLAAKQPVGEYRPDSLVAEEI 226
Cdd:cd03111  154 rRLLDslrELEGSSdrLRLVLNRYDKKSEISpKDIEEA---LGLEVFATLPNDYKAVSESANTGRPLVEVAPRSALVRAL 230

                 ....*
gi 501075448 227 VTLAN 231
Cdd:cd03111  231 QDLAA 235
 
Name Accession Description Interval E-value
PRK10037 PRK10037
cellulose biosynthesis protein BcsQ;
1-237 1.60e-118

cellulose biosynthesis protein BcsQ;


Pssm-ID: 182204  Cd Length: 250  Bit Score: 338.00  E-value: 1.60e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448   1 MTVLALQGVRGGVGTTSLTAALGWALHQLGESVLVIDASPDNLLRLSFNIDFDHADGWARALLDDKPWQSTAWRYAPGLD 80
Cdd:PRK10037   1 MAILGLQGVRGGVGTTSITAALAWSLQMLGENVLVIDACPDNLLRLSFNVDFTHRQGWARALLDGQDWRDAGLRYTSQLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448  81 VLPYGALRQTERENDVT--PALGAFAQHLHLLKASGQWRWILLDLPCGFDAVTRSLLQVADRTLCVVQPDANCHARLHQQ 158
Cdd:PRK10037  81 LLPFGQLSIEEQENPQHwqTRLGDICSALQQLKASGRYQWILLDLPRGASPLTRQLLSLCDHSLAIVNVDANCHIRLHQQ 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501075448 159 ALPSGCDLLANFRLISSQIQNDIWQLWLQTQRNLVPVAVHRDEAMMESLAAKQPVGEYRPDSLVAEEIVTLANWCLLHY 237
Cdd:PRK10037 161 ALPAGAHILINDLRIGSQLQDDLYQLWLQSQRRLLPMLIHRDEAMAECLAAKQPLGEYRSDSLAAEEILTLANWCLLHY 239
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
1-234 4.68e-111

Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in cellulose biosynthesis. (Roemling U. and Galperin M.Y. "Bacterial cellulose biosynthesis. Diversity of operons and subunits" (manuscript in preparation)). A second component of the extracellular matrix of the multicellular morphotype (rdar) of Salmonella typhimurium and Escherichia coli is cellulose. The family does contain a P-loop sequence motif suggesting a nucleotide binding function, but this has not been confirmed.


Pssm-ID: 429004 [Multi-domain]  Cd Length: 234  Bit Score: 318.55  E-value: 4.68e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448    1 MTVLALQGVRGGVGTTSLTAALGWALHQLGESVLVIDASPDNLLRLSFNIDFDHADGWARALLDDKPWQSTAWRYAPGLD 80
Cdd:pfam06564   1 MKILALQGVRGGVGTTSILAALAWALQRLGERVLLIDLSPDNLLRLHFNVPFEHRQGWARAELDGADWRDAALEYTPGLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448   81 VLPYGALRQTEREN--DVTPALGAFAQHLHLLKasGQWRWILLDLPCGFDAVTRSLLQVADRTLCVVQPDANCHARLHQQ 158
Cdd:pfam06564  81 LLPFGRLSVEEQENlqQLQPDPGAWCRRLQQLK--GRYDWVLFDLPAGPSPLTRQLLSLADLSLLVVNPDANCHVLLHQQ 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501075448  159 ALPSGCDLLANFRLISSQIQNDIWQLWLQTQRNLVPVAVHRDEAMMESLAAKQPVGEYRPDSLVAEEIVTLANWCL 234
Cdd:pfam06564 159 PLPDADHLLINDFRPASQLQQDLLQLWRQSQRRLLPLVIHRDEALAEALAAKQPLGEYRPDSLAAEEVLTLANWCL 234
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
1-238 2.28e-78

cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found immediately upsteam of bacterial cellulose synthase (bcs) genes in a broad range of bacteria, including both copies of the bcs locus in Klebsiella pneumoniae. In several species it is seen clearly as part of the bcs operon. It is identified as a probable component of the bacterial cellulose metabolic process not only by gene location, but also by partial phylogenetic profiling, or Haft-Selengut algorithm (), based on a bacterial cellulose biosynthesis genome property profile. Cellulose plays an important role in biofilm formation and structural integrity in some bacteria. Mutants in yhjQ in Escherichia coli, show altered morphology an growth, but the function of YhjQ has not yet been determined. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274549 [Multi-domain]  Cd Length: 246  Bit Score: 236.09  E-value: 2.28e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448    1 MTVLALQGVRGGVGTTSLTAALGWALHQLGESVLVIDASPDNLLRLSFNIDFDHADGWARALLDDKPWQSTAWRYAPGLD 80
Cdd:TIGR03371   1 MKVIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLHFGMDWSVRDGWARALLNGADWAAAAYRSPDGVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448   81 VLPYGALRQTERENDVTPALGAFAQHLHLLKASGQwRWILLDLPCGFDAVTRSLLQVADRTLCVVQPDANCHARLHQQAL 160
Cdd:TIGR03371  81 FLPYGDLSADEREAYQAHDAGWLARLLQQLDLAAR-DWVLIDLPRGPSPITRQALAAADLVLVVVNADAACYATLHQLAL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448  161 --------PSGCDLLANFRLISSQIQNDIWQLWLQTQ-RNLVPVAVHRDEAMMESLAAKQPVGEYRPDSLVAEEIVTLAN 231
Cdd:TIGR03371 160 alfagsgpRDGPRFLINQFDPARQLSRDVRAVLRQTLgSRLLPFVIHRDEAVSEALARGTPVLNYAPHSQAAHDIRTLAG 239

                  ....*..
gi 501075448  232 WCLLHYR 238
Cdd:TIGR03371 240 WLLSKLS 246
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
1-232 6.39e-18

ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440805 [Multi-domain]  Cd Length: 253  Bit Score: 79.90  E-value: 6.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448   1 MTVLALQGVRGGVGTTSLTAALGWALHQLGESVLVIDASPDNLLRLSFNIDFDHAD-GWARALLDDKPWQSTAWR-YAPG 78
Cdd:COG1192    1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDpTLYDLLLDDAPLEDAIVPtEIPG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448  79 LDVLP-YGALRQTERENDVTPALGAFAQHLhLLKASGQWRWILLDLPCGFDAVTRSLLQVADRTLCVVQPDAncharlhq 157
Cdd:COG1192   81 LDLIPaNIDLAGAEIELVSRPGRELRLKRA-LAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEY-------- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448 158 QALPSGCDLLANFRLISSQIQNDIWQL-------------------WLQTQ--RNLVPVAVHRDEAMMESLAAKQPVGEY 216
Cdd:COG1192  152 LSLEGLAQLLETIEEVREDLNPKLEILgilltmvdprtrlsrevleELREEfgDKVLDTVIPRSVALAEAPSAGKPVFEY 231
                        250
                 ....*....|....*.
gi 501075448 217 RPDSLVAEEIVTLANW 232
Cdd:COG1192  232 DPKSKGAKAYRALAEE 247
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
3-148 1.47e-16

Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443989 [Multi-domain]  Cd Length: 358  Bit Score: 77.46  E-value: 1.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448   3 VLALQGVRGGVGTTSLTAALGWAL-HQLGESVLVIDAspdNLLR--LSFNIDFDHADGWARAL-----LDDKPWQSTAWR 74
Cdd:COG4963  104 VIAVVGAKGGVGATTLAVNLAWALaRESGRRVLLVDL---DLQFgdVALYLDLEPRRGLADALrnpdrLDETLLDRALTR 180
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501075448  75 YAPGLDVLPygALRQTERENDVTPAlgAFAQHLHLLKAsgQWRWILLDLPCGFDAVTRSLLQVADRTLCVVQPD 148
Cdd:COG4963  181 HSSGLSVLA--APADLERAEEVSPE--AVERLLDLLRR--HFDYVVVDLPRGLNPWTLAALEAADEVVLVTEPD 248
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
3-231 4.61e-14

pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.


Pssm-ID: 349765 [Multi-domain]  Cd Length: 235  Bit Score: 69.23  E-value: 4.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448   3 VLALQGVRGGVGTTSLTAALGWALHQL-GESVLVID---ASPDNLLRLSFNIDFDHADGwARAL--LDDKPWQSTAWRYA 76
Cdd:cd03111    2 VVAVVGAKGGVGASTLAVNLAQELAQRaKDKVLLIDldlPFGDLGLYLNLRPDYDLADV-IQNLdrLDRTLLDSAVTRHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448  77 PGLDVLPygaLRQTERENDvtpALGAfAQHLHLL-KASGQWRWILLDLPCGFDAVTRSLLQVADRTLCVVQPDANC--HA 153
Cdd:cd03111   81 SGLSLLP---APQELEDLE---ALGA-EQVDKLLqVLRAFYDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLPSlrNA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448 154 -RLHQ---QALPSG--CDLLANFRLISSQIQ-NDIWQLwlqTQRNLVPVAVHRDEAMMESLAAKQPVGEYRPDSLVAEEI 226
Cdd:cd03111  154 rRLLDslrELEGSSdrLRLVLNRYDKKSEISpKDIEEA---LGLEVFATLPNDYKAVSESANTGRPLVEVAPRSALVRAL 230

                 ....*
gi 501075448 227 VTLAN 231
Cdd:cd03111  231 QDLAA 235
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
17-231 5.71e-13

MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440223 [Multi-domain]  Cd Length: 230  Bit Score: 66.07  E-value: 5.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448  17 SLTAALGWALHQLGESVLVIDASPD--NLLRLsFNIDFDHadGWARALLDDKPWQSTAWRYAPGLDVLPygALRQTEREN 94
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGlaNLDVL-LGLEPKA--TLADVLAGEADLEDAIVQGPGGLDVLP--GGSGPAELA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448  95 DVTPALgAFAQHLHLLkaSGQWRWILLDLPCGFDAVTRSLLQVADRTLCVVQPDANCHAR-------LHQQALPSGCDLL 167
Cdd:COG0455   76 ELDPEE-RLIRVLEEL--ERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDayallklLRRRLGVRRAGVV 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501075448 168 AN-------FRLISSQIQNDIWQLwLQTQRNLVpVAVHRDEAMMESLAAKQPVGEYRPDSLVAEEIVTLAN 231
Cdd:COG0455  153 VNrvrseaeARDVFERLEQVAERF-LGVRLRVL-GVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAA 221
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
10-148 1.02e-10

septum site-determining protein MinD; Septum site-determining protein MinD is part of the operon MinCDE that determines the site of the formation of a septum at mid-cell, an important part of bacterial cell division. MinC is a nonspecific inhibitor of the septum protein FtsZ. MinE is the supressor of MinC. MinD plays a pivotal role, selecting the mid-cell over other sites through the activation and regulation of MinC and MinE. MinD is a membrane-associated ATPase, related to nitrogenase iron protein.


Pssm-ID: 349756 [Multi-domain]  Cd Length: 236  Bit Score: 59.91  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448  10 RGGVGTTSLTAALGWALHQLGESVLVIDA-----SPDNLLRLSFNIDFDHAD---GWAR---ALLDDKPWqstawryaPG 78
Cdd:cd02036    9 KGGVGKTTTTANLGVALAKLGKKVLLIDAdiglrNLDLILGLENRIVYTLVDvleGECRleqALIKDKRW--------EN 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448  79 LDVLPYGalrQTERENDVTPAlgAFAQHLHLLKASGQwrWILLDLPCGFDAVTRSLLQVADRTLCVVQPD 148
Cdd:cd02036   81 LYLLPAS---QTRDKDALTPE--KLEELVKELKDSFD--FILIDSPAGIESGFINAIAPADEAIIVTNPE 143
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
3-148 3.89e-09

Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440255 [Multi-domain]  Cd Length: 289  Bit Score: 55.58  E-value: 3.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448   3 VLALQGVRGGVGTTSLTAALGWALHQLGESVLVIDAspdNLLRLSFNIDFDHAD--GWARALLDDKPWQSTAWRY-APGL 79
Cdd:COG0489   94 VIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDA---DLRGPSLHRMLGLENrpGLSDVLAGEASLEDVIQPTeVEGL 170
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448  80 DVLPYGALRQTERENDVTPALGAFAQHLHllkasGQWRWILLDL-PCGFDAVTRSLLQVADRTLCVVQPD 148
Cdd:COG0489  171 DVLPAGPLPPNPSELLASKRLKQLLEELR-----GRYDYVIIDTpPGLGVADATLLASLVDGVLLVVRPG 235
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
11-223 5.94e-08

MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) is a major determinant for a variety of flagellation patterns. It effects location and number of bacterial flagella during C-ring assembly.


Pssm-ID: 349758 [Multi-domain]  Cd Length: 230  Bit Score: 51.80  E-value: 5.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448  11 GGVGTTSLTAALGWALHQLGESVLVID-----ASPDNLLRLSFNIDFDHadgwarALLDDKPWQSTAWRYAPGLDVLPYG 85
Cdd:cd02038   10 GGVGKTNVSANLALALSKLGKRVLLLDadlglANLDILLGLAPKKTLGD------VLKGRVSLEDIIVEGPEGLDIIPGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448  86 ALrqterenDVTPALGAFAQHLHLLKA----SGQWRWILLDLPCGFDAVTRSLLQVADRTLCVVQP------DA-----N 150
Cdd:cd02038   84 SG-------MEELANLDPEQKAKLIEElsslESNYDYLLIDTGAGISRNVLDFLLAADEVIVVTTPeptsitDAyalikV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448 151 CHARLhqqalpsgcdLLANFRLISSQIQN-----DIWQLWLQTQRNLVPV------AVHRDEAMMESLAAKQPVGEYRPD 219
Cdd:cd02038  157 LSRRG----------GKKNFRLIVNMARSpkegrATFERLKKVAKRFLDInldfvgFIPYDQSVRRAVRSQKPFVLLFPN 226

                 ....
gi 501075448 220 SLVA 223
Cdd:cd02038  227 SKAS 230
CpaE_hom_Actino TIGR03815
helicase/secretion neighborhood CpaE-like protein; Members of this protein family belong to ...
2-148 3.91e-07

helicase/secretion neighborhood CpaE-like protein; Members of this protein family belong to the MinD/ParA family of P-loop NTPases, and in particular show homology to the CpaE family of pilus assembly proteins (see ). Nearly all members are found, not only in a gene context consistent with pilus biogenesis or a pilus-like secretion apparatus, but also near a DEAD/DEAH-box helicase, suggesting an involvement in DNA transfer activity. The model describes a clade restricted to the Actinobacteria.


Pssm-ID: 274798 [Multi-domain]  Cd Length: 322  Bit Score: 50.03  E-value: 3.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448    2 TVLALQGVRGGVGTTSLTAALGWALHQLGESVLVIDASPdnllrLSFNIDF----DHADGWARALLD--DKPWQSTAWRY 75
Cdd:TIGR03815  94 VVVAVIGGRGGAGASTLAAALALAAARHGLRTLLVDADP-----WGGGLDLllgaEDVPGLRWPDLSqaRGRLPAGALRD 168
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501075448   76 AP----GLDVLPYGALRQTErendVTPAlgAFAQHLHLLKASGQwrWILLDLPCGFDAVTRSLLQVADRTLCVVQPD 148
Cdd:TIGR03815 169 ALprrgGLSVLSWGRAVGAA----LPPA--AVRAVLDAARRGGD--LVVVDLPRRLTPAAETALESADLVLVVVPAD 237
minD CHL00175
septum-site determining protein; Validated
10-148 4.22e-07

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 49.77  E-value: 4.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448  10 RGGVGTTSLTAALGWALHQLGESVLVIDA-----SPDNLLRLSFNIDF---DHADGWAR---ALLDDKPWqstawryaPG 78
Cdd:CHL00175  24 KGGVGKTTTTANLGMSIARLGYRVALIDAdiglrNLDLLLGLENRVLYtamDVLEGECRldqALIRDKRW--------KN 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501075448  79 LDVLPYGALRQ---TERENdvtpalgafAQHLHLLKASGQWRWILLDLPCGFDAVTRSLLQVADRTLCVVQPD 148
Cdd:CHL00175  96 LSLLAISKNRQrynVTRKN---------MNMLVDSLKNRGYDYILIDCPAGIDVGFINAIAPAQEAIVVTTPE 159
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
4-148 8.16e-07

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 48.50  E-value: 8.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448    4 LALQGVRGGVGTTSLTAALGWALHQLGESVLVIDASPDNLLRLSFNIDFDHADGWA--------RALLDDkpwqstaWRY 75
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQalaeglkgRVNLDP-------ILL 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501075448   76 AP-----GLDVLPYGALRQT-ERENDVTPALGAFAQHLHLLKasGQWRWILLDLPCGFDAVTRSLLQVADRTLCVVQPD 148
Cdd:pfam01656  74 KEksdegGLDLIPGNIDLEKfEKELLGPRKEERLREALEALK--EDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPE 150
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
8-54 1.63e-05

Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell.


Pssm-ID: 396792  Cd Length: 302  Bit Score: 45.03  E-value: 1.63e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 501075448    8 GVRGGVGTTSLTAALGWALHQLGESVLVIDASPDNLLRLSFNIDFDH 54
Cdd:pfam02374   7 GGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQKFGH 53
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
3-40 2.25e-05

partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 42.91  E-value: 2.25e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 501075448   3 VLALQGVRGGVGTTSLTAALGWALHQLGESVLVIDASP 40
Cdd:cd02042    2 VIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDP 39
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
3-37 6.64e-05

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 40.88  E-value: 6.64e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 501075448   3 VLALQGVRGGVGTTSLTAALGWALHQLGESVLVID 37
Cdd:cd01983    2 VIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLID 36
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
10-43 5.29e-04

CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 40.15  E-value: 5.29e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 501075448  10 RGGVGTTSLTAALGWALHQLGESVLVIDASPD-NL 43
Cdd:COG3640    8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNaNL 42
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
3-150 1.40e-03

bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.


Pssm-ID: 349772 [Multi-domain]  Cd Length: 190  Bit Score: 38.32  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448   3 VLALQGVRGGVGTTSLTAALGWALHQLGESVLVIDAspdNLLR--LSFNIDFDHADGWARALLDDKPWQSTAWRY-APGL 79
Cdd:cd05387   21 VIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDA---DLRRpsLHRLLGLPNEPGLSEVLSGQASLEDVIQSTnIPNL 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501075448  80 DVLPYGALRQTERENDVTPALGAFAQHLhllkaSGQWRWILLDL-PCGFDAVTRSLLQVADRTLCVVQPDAN 150
Cdd:cd05387   98 DVLPAGTVPPNPSELLSSPRFAELLEEL-----KEQYDYVIIDTpPVLAVADALILAPLVDGVLLVVRAGKT 164
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
1-83 3.06e-03

AAA domain; This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.


Pssm-ID: 433350 [Multi-domain]  Cd Length: 177  Bit Score: 37.18  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501075448    1 MTVLALQGVRGGVGTTSLTAALGWALHQLGESVLVIDASPDNLLRLSFNIDFDHADG-WARALLDDKPWQSTAW-RYAPG 78
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKtIYELLIGECNIEEAIIkTVIEN 80

                  ....*
gi 501075448   79 LDVLP 83
Cdd:pfam13614  81 LDLIP 85
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
10-43 4.50e-03

accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenase (CODH). CODH from Rhodospirillum rubrum catalyzes the reversible oxidation of CO to CO2. CODH contains a nickel-iron-sulfur cluster (C-center) and an iron-sulfur cluster (B-center). CO oxidation occurs at the C-center. Three accessory proteins encoded by cooCTJ genes are involved in nickel incorporation into a nickel site. CooC functions as a nickel insertase that mobilizes nickel to apoCODH using energy released from ATP hydrolysis. CooC is a homodimer and has NTPase activities. Mutation at the P-loop abolishs its function.


Pssm-ID: 349754 [Multi-domain]  Cd Length: 249  Bit Score: 37.29  E-value: 4.50e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 501075448  10 RGGVGTTSLTAALGWALHQLGESVLVIDASPD-NL 43
Cdd:cd02034    8 KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNsNL 42
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
11-54 9.40e-03

Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence.


Pssm-ID: 349755 [Multi-domain]  Cd Length: 250  Bit Score: 36.33  E-value: 9.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 501075448  11 GGVGTTSLTAALGWALHQLGESVLVIDASPDNLLRLSFNIDFDH 54
Cdd:cd02035    9 GGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGQKLGG 52
 
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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