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Conserved domains on  [gi|490311972|ref|WP_004206667|]
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MULTISPECIES: arsenite efflux transporter ATPase subunit ArsA [Enterobacteriaceae]

Protein Classification

arsenical pump-driving ATPase( domain architecture ID 11500026)

arsenical pump-driving ATPase is an anion-transporting ATPase that catalyzes the extrusion of the oxyanions arsenite, antimonite, and arsenate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
6-571 0e+00

arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).


:

Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 1062.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972    6 NIPPYLFFTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNVGQVFDQAIGNTIRPLTAVPALSALEIDPQEAARQY 85
Cdd:TIGR04291   1 ELPPYLFFTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNVGQVFGQTIGNKITAIAGVPGLFALEIDPQAAAQAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972   86 RARIVDPIKGLLPDDVVNSISEQLSGACTTEIAAFDEFTGLLTDASLLTRFDHIIFDTAPTGHTIRLLQLPGAWSSFIES 165
Cdd:TIGR04291  81 RARIVDPVRGVLPDDVVSSIEEQLSGACTTEIAAFDEFTGLLTDAELTQDFDHIIFDTAPTGHTIRLLQLPGAWSDFLDT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  166 NPDGASCLGPMAGLEKQREQYAHAVEALSDPERTRLVLVARLQNSTLQEVARTHEELAEIGLKNQYLVINGVLPEAEAEH 245
Cdd:TIGR04291 161 NPNGASCLGPLAGLEKQRAQYAKAVEALSDPERTRLILVARPQKSTLLEVARTHQELAAIGLKNQYLVINGVLPETEASD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  246 DALAAAIWQREQEALANLPAGLSELPTDTLLLQPVNMVGVSALKGLLDTRSEALPLPVTNILyTPENLSLSGLVDDIARS 325
Cdd:TIGR04291 241 DPLAQAIYKREQKALQHMPAILANLPRYTLPLKPYNLVGLEALRQLLNDDQPQLSLDITTPQ-VPDLPSLSRLIDEIAKS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  326 EHGLIMLMGKGGVGKTTMAAAIAVRLADMGFDVHLTTSDPAAHLSTTLNGSLKNLQVSRINPHDETERYRQHVLETKGRD 405
Cdd:TIGR04291 320 EKGLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSLNNLQVSRIDPKQETERYRQEVLATKGKE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  406 LDEAGKRLLEEDLRSPCTEEIAVFQAFSRVIREAGKRFVVMDTAPTGHTLLLLDATGAYHREIAKKMGSKG-HFTTPMMQ 484
Cdd:TIGR04291 400 LDEDGKAYLEEDLRSPCTEEIAVFQAFSRIIREAGDRFVVMDTAPTGHTLLLLDATGAYHREVERKMGDTPeHVTTPMMQ 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  485 LQDPDRTKVLLVTLPETTPVLEAANLQADLKRAGIHPWGWIINNSLSIADTRSPLLCQRAHQELPQIEAVKDQHADRIAL 564
Cdd:TIGR04291 480 LQDPERTKVLLVTLPETTPVLEAARLQEDLRRAGIEPWWWVINNSLAATNTTSPLLSQRAQNELKWIEKVKRIHADRYAV 559

                  ....*..
gi 490311972  565 VPVLASE 571
Cdd:TIGR04291 560 IPLQAEE 566
 
Name Accession Description Interval E-value
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
6-571 0e+00

arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 1062.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972    6 NIPPYLFFTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNVGQVFDQAIGNTIRPLTAVPALSALEIDPQEAARQY 85
Cdd:TIGR04291   1 ELPPYLFFTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNVGQVFGQTIGNKITAIAGVPGLFALEIDPQAAAQAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972   86 RARIVDPIKGLLPDDVVNSISEQLSGACTTEIAAFDEFTGLLTDASLLTRFDHIIFDTAPTGHTIRLLQLPGAWSSFIES 165
Cdd:TIGR04291  81 RARIVDPVRGVLPDDVVSSIEEQLSGACTTEIAAFDEFTGLLTDAELTQDFDHIIFDTAPTGHTIRLLQLPGAWSDFLDT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  166 NPDGASCLGPMAGLEKQREQYAHAVEALSDPERTRLVLVARLQNSTLQEVARTHEELAEIGLKNQYLVINGVLPEAEAEH 245
Cdd:TIGR04291 161 NPNGASCLGPLAGLEKQRAQYAKAVEALSDPERTRLILVARPQKSTLLEVARTHQELAAIGLKNQYLVINGVLPETEASD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  246 DALAAAIWQREQEALANLPAGLSELPTDTLLLQPVNMVGVSALKGLLDTRSEALPLPVTNILyTPENLSLSGLVDDIARS 325
Cdd:TIGR04291 241 DPLAQAIYKREQKALQHMPAILANLPRYTLPLKPYNLVGLEALRQLLNDDQPQLSLDITTPQ-VPDLPSLSRLIDEIAKS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  326 EHGLIMLMGKGGVGKTTMAAAIAVRLADMGFDVHLTTSDPAAHLSTTLNGSLKNLQVSRINPHDETERYRQHVLETKGRD 405
Cdd:TIGR04291 320 EKGLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSLNNLQVSRIDPKQETERYRQEVLATKGKE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  406 LDEAGKRLLEEDLRSPCTEEIAVFQAFSRVIREAGKRFVVMDTAPTGHTLLLLDATGAYHREIAKKMGSKG-HFTTPMMQ 484
Cdd:TIGR04291 400 LDEDGKAYLEEDLRSPCTEEIAVFQAFSRIIREAGDRFVVMDTAPTGHTLLLLDATGAYHREVERKMGDTPeHVTTPMMQ 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  485 LQDPDRTKVLLVTLPETTPVLEAANLQADLKRAGIHPWGWIINNSLSIADTRSPLLCQRAHQELPQIEAVKDQHADRIAL 564
Cdd:TIGR04291 480 LQDPERTKVLLVTLPETTPVLEAARLQEDLRRAGIEPWWWVINNSLAATNTTSPLLSQRAQNELKWIEKVKRIHADRYAV 559

                  ....*..
gi 490311972  565 VPVLASE 571
Cdd:TIGR04291 560 IPLQAEE 566
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
10-583 2.71e-129

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 391.94  E-value: 2.71e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  10 YLFFTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNVGQVFDQAIGNTIRPLTAVPALSALEIDPQEAARQYRARI 89
Cdd:NF041417  14 FVFFSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFGQSIGHRVTSIDDVENLSAIEIDPDAAAEEYRQRT 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  90 VDPIKGLLPDDVVNSISEQLSGACTTEIAAFDEFTGLLTDAslltRFDHIIFDTAPTGHTIRLLQLPGAWSSFIESNpdG 169
Cdd:NF041417  94 IEPMRQLLDDEQLKTVEEQLDSPCIEEIAAFDKFVEFMDEP----EYDVVVFDTAPTGHTIRLMELPSGWSEELEKG--G 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 170 ASCLGPMAGLEKQREQYAHAVEALSDPERTRLVLVARLQNSTLQEVARTHEELAEIGLKNQYLVINGVLPEAEAEhDALA 249
Cdd:NF041417 168 ATCIGPAASLQEQKEDYEKAIDTLQDDAQTSFVFVGKPEDASIDEIERSSKELADLGIKTSLLVINGYLPESVCE-DPFF 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 250 AAIWQREQEALANLPAGLSELPTDTLLLQPVNMVGVSALKGLLDTRSEALPLPVTNILYTPENLSLS-------GLVDDI 322
Cdd:NF041417 247 EMKREDEQEILEEVEREFAMQPIATYPLQPGEITGIDLLADVGEVLYEGKEPTVDVAVITEEETEETspsetdkEAVMEL 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 323 ARSEHG--LIMLMGKGGVGKTTMAAAIAVRLADMGFDVHLTTSDPAAHLS-----------TTLNgsLKNLQVSRINPHD 389
Cdd:NF041417 327 LRPQKDtrYLFFTGKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQdifgtevghepTKVG--VENLYAARIDQER 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 390 ETERYRQHVLETKGRDLD------EAGKRLLEEDLRSPCTEEIAVFQAFSRVIREAGKRFVVMDTAPTGHTLLLLDAT-- 461
Cdd:NF041417 405 ALEEYKTRMLDQVEQSFDkdqidvEAAKAQVREELESPCAEEMAALEKFVSYFDVDGYDVVVFDTAPTGHTLRLLELPsd 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 462 -------GAYHREIAKKMGSKghFTTPMMQLQDPDRTKVLLVTLPETTPVLEAANLQADLK-RAGIHPWGWIINNSLSIA 533
Cdd:NF041417 485 wkgfmdlGSLTKEASDVTGDK--YDRVIETMRDPERSTFVFVMYPEYTPMMEAWRAAEDLRnQVGIETSLVAVNYLLPEE 562
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|
gi 490311972 534 DTRSPLLCQRAHQELPQIEAVKDQHADRIALVPVLASEPAGIEKLRELMS 583
Cdd:NF041417 563 YGNNAFFESRRKQQQKYLEEIRDRFDVPMLLAPLQRDEPTGIEELRRFGS 612
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
8-293 1.88e-111

Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];


Pssm-ID: 439774  Cd Length: 299  Bit Score: 334.87  E-value: 1.88e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972   8 PPYLFFTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNVGQVFDQAIGNTIRPLtAVPALSALEIDPQEAARQYRA 87
Cdd:COG0003    3 TRIIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGTELGNEPTEV-AVPNLYALEIDPEAELEEYWE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  88 RIVDPIKGLLPDDVVNSISEqlSGACTTEIAAFDEFTGLLTDAslltRFDHIIFDTAPTGHTIRLLQLP---GAWSSFIE 164
Cdd:COG0003   82 RVRAPLRGLLPSAGVDELAE--SLPGTEELAALDELLELLEEG----EYDVIVVDTAPTGHTLRLLSLPellGWWLDRLL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 165 SNPDGASCLGP-------------MAGLEKQREQYAHAVEALSDPERTRLVLVARLQNSTLQEVARTHEELAEIGLKNQY 231
Cdd:COG0003  156 KLRRKASGLGRplagilglpddpvLEGLEELRERLERLRELLRDPERTSFRLVTNPERLAIAETRRALEELALYGIPVDG 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490311972 232 LVINGVLPEaEAEHDALAAAIWQREQEALANLPAGLSELPTDTLLLQPVNMVGVSALKGLLD 293
Cdd:COG0003  236 LVVNRVLPE-EADDDAFLAARRERQQEYLAEIEEAFAPLPVVEVPLLAEEVVGLEALRALAE 296
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
10-289 1.88e-88

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: 274.00  E-value: 1.88e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  10 YLFFTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNVGQVFDQAIGNTiRPLTAVPALSALEIDPQEAARQYRARI 89
Cdd:cd02035    2 IIFFGGKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGQKLGGE-TPVKGAPNLWAMEIDPEEALEEYWEEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  90 VDPIKGL--LPDDVVNSISEQLSGACTTEIAAFDEFTGLLTDAslltRFDHIIFDTAPTGHTIRLLQLPgawssfiesnp 167
Cdd:cd02035   81 KELLAQYlrLPGLDEVYAEELLSLPGMDEAAAFDELREYVESG----EYDVIVFDTAPTGHTLRLLSLP----------- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 168 dgasclgpmaglekqreqYAHAVEALSDPERTRLVLVARLQNSTLQEVARTHEELAEIGLKNQYLVINGVLPEAEAEHDA 247
Cdd:cd02035  146 ------------------LEQVRELLRDPERTTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVNQVLPEEADDSFF 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 490311972 248 LAAaiWQREQEALANLPAGLSELPTDTLLLQPVNMVGVSALK 289
Cdd:cd02035  208 LRR--RRQQQKYLDEIEELFEPLPVVEVPLLPEEVRGLEALR 247
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
10-289 1.77e-66

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: 218.76  E-value: 1.77e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972   10 YLFFTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNVGQVFDQAIGNTIRPLTavPALSALEIDPQEAARQYRARI 89
Cdd:pfam02374   3 WIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQKFGHEPTKVK--ENLSAMEIDPNMELEEYWQEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972   90 VDPIKGLLPDDVVNSISEQLSGA--CTTEIAAFDEFTGLLTDASlltrFDHIIFDTAPTGHTIRLLQLPGAWSSFIE--- 164
Cdd:pfam02374  81 QKYMNALLGLRMLEGILAEELASlpGIDEAASFDEFKKYMDEGE----YDVVVFDTAPTGHTLRLLSLPTVLGWYLEkiv 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  165 ------------SNPDGASCLG-PMAGLEKQREQYAHAVEALSDPERTRLVLVARLQNSTLQEVARTHEELAEIGLKNQY 231
Cdd:pfam02374 157 klknqigplakpFLGMGGVSIPeALESLEETKERIERAREILTDPERTSFRLVCIPEKMSLYETERAIQYLAKYGIDVDA 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 490311972  232 LVINGVLPEAEAEHDALAAAIWQREQEALANLPAGLSELPTDTLLLQPVNMVGVSALK 289
Cdd:pfam02374 237 VIVNQVLPENVQENCPFCEARKKIQQKYLDEIEELFSDFPVAKLPLLPEEVVGLEKLE 294
ParA_partition NF041546
ParA family partition ATPase;
16-46 8.19e-06

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 46.78  E-value: 8.19e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 490311972  16 KGGVGKTSISCATAIRLAEQGKRVLLVSTDP 46
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADP 38
PHA02518 PHA02518
ParA-like protein; Provisional
16-121 1.21e-05

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 46.77  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  16 KGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNVGQVFDQAigNTIRPLTAVPALS-ALEIDPQEAARQYrarivdpik 94
Cdd:PHA02518   9 KGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAR--EEGEPLIPVVRMGkSIRADLPKVASGY--------- 77
                         90       100
                 ....*....|....*....|....*..
gi 490311972  95 gllpDDVVNSISEQLSGACTTEIAAFD 121
Cdd:PHA02518  78 ----DYVVVDGAPQDSELARAALRIAD 100
ParA_partition NF041546
ParA family partition ATPase;
335-365 3.29e-03

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 39.07  E-value: 3.29e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 490311972 335 KGGVGKTTMAAAIAVRLADMGFDVHLTTSDP 365
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADP 38
 
Name Accession Description Interval E-value
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
6-571 0e+00

arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 1062.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972    6 NIPPYLFFTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNVGQVFDQAIGNTIRPLTAVPALSALEIDPQEAARQY 85
Cdd:TIGR04291   1 ELPPYLFFTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNVGQVFGQTIGNKITAIAGVPGLFALEIDPQAAAQAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972   86 RARIVDPIKGLLPDDVVNSISEQLSGACTTEIAAFDEFTGLLTDASLLTRFDHIIFDTAPTGHTIRLLQLPGAWSSFIES 165
Cdd:TIGR04291  81 RARIVDPVRGVLPDDVVSSIEEQLSGACTTEIAAFDEFTGLLTDAELTQDFDHIIFDTAPTGHTIRLLQLPGAWSDFLDT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  166 NPDGASCLGPMAGLEKQREQYAHAVEALSDPERTRLVLVARLQNSTLQEVARTHEELAEIGLKNQYLVINGVLPEAEAEH 245
Cdd:TIGR04291 161 NPNGASCLGPLAGLEKQRAQYAKAVEALSDPERTRLILVARPQKSTLLEVARTHQELAAIGLKNQYLVINGVLPETEASD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  246 DALAAAIWQREQEALANLPAGLSELPTDTLLLQPVNMVGVSALKGLLDTRSEALPLPVTNILyTPENLSLSGLVDDIARS 325
Cdd:TIGR04291 241 DPLAQAIYKREQKALQHMPAILANLPRYTLPLKPYNLVGLEALRQLLNDDQPQLSLDITTPQ-VPDLPSLSRLIDEIAKS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  326 EHGLIMLMGKGGVGKTTMAAAIAVRLADMGFDVHLTTSDPAAHLSTTLNGSLKNLQVSRINPHDETERYRQHVLETKGRD 405
Cdd:TIGR04291 320 EKGLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSLNNLQVSRIDPKQETERYRQEVLATKGKE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  406 LDEAGKRLLEEDLRSPCTEEIAVFQAFSRVIREAGKRFVVMDTAPTGHTLLLLDATGAYHREIAKKMGSKG-HFTTPMMQ 484
Cdd:TIGR04291 400 LDEDGKAYLEEDLRSPCTEEIAVFQAFSRIIREAGDRFVVMDTAPTGHTLLLLDATGAYHREVERKMGDTPeHVTTPMMQ 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  485 LQDPDRTKVLLVTLPETTPVLEAANLQADLKRAGIHPWGWIINNSLSIADTRSPLLCQRAHQELPQIEAVKDQHADRIAL 564
Cdd:TIGR04291 480 LQDPERTKVLLVTLPETTPVLEAARLQEDLRRAGIEPWWWVINNSLAATNTTSPLLSQRAQNELKWIEKVKRIHADRYAV 559

                  ....*..
gi 490311972  565 VPVLASE 571
Cdd:TIGR04291 560 IPLQAEE 566
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
10-583 2.71e-129

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 391.94  E-value: 2.71e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  10 YLFFTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNVGQVFDQAIGNTIRPLTAVPALSALEIDPQEAARQYRARI 89
Cdd:NF041417  14 FVFFSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFGQSIGHRVTSIDDVENLSAIEIDPDAAAEEYRQRT 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  90 VDPIKGLLPDDVVNSISEQLSGACTTEIAAFDEFTGLLTDAslltRFDHIIFDTAPTGHTIRLLQLPGAWSSFIESNpdG 169
Cdd:NF041417  94 IEPMRQLLDDEQLKTVEEQLDSPCIEEIAAFDKFVEFMDEP----EYDVVVFDTAPTGHTIRLMELPSGWSEELEKG--G 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 170 ASCLGPMAGLEKQREQYAHAVEALSDPERTRLVLVARLQNSTLQEVARTHEELAEIGLKNQYLVINGVLPEAEAEhDALA 249
Cdd:NF041417 168 ATCIGPAASLQEQKEDYEKAIDTLQDDAQTSFVFVGKPEDASIDEIERSSKELADLGIKTSLLVINGYLPESVCE-DPFF 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 250 AAIWQREQEALANLPAGLSELPTDTLLLQPVNMVGVSALKGLLDTRSEALPLPVTNILYTPENLSLS-------GLVDDI 322
Cdd:NF041417 247 EMKREDEQEILEEVEREFAMQPIATYPLQPGEITGIDLLADVGEVLYEGKEPTVDVAVITEEETEETspsetdkEAVMEL 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 323 ARSEHG--LIMLMGKGGVGKTTMAAAIAVRLADMGFDVHLTTSDPAAHLS-----------TTLNgsLKNLQVSRINPHD 389
Cdd:NF041417 327 LRPQKDtrYLFFTGKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQdifgtevghepTKVG--VENLYAARIDQER 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 390 ETERYRQHVLETKGRDLD------EAGKRLLEEDLRSPCTEEIAVFQAFSRVIREAGKRFVVMDTAPTGHTLLLLDAT-- 461
Cdd:NF041417 405 ALEEYKTRMLDQVEQSFDkdqidvEAAKAQVREELESPCAEEMAALEKFVSYFDVDGYDVVVFDTAPTGHTLRLLELPsd 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 462 -------GAYHREIAKKMGSKghFTTPMMQLQDPDRTKVLLVTLPETTPVLEAANLQADLK-RAGIHPWGWIINNSLSIA 533
Cdd:NF041417 485 wkgfmdlGSLTKEASDVTGDK--YDRVIETMRDPERSTFVFVMYPEYTPMMEAWRAAEDLRnQVGIETSLVAVNYLLPEE 562
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|
gi 490311972 534 DTRSPLLCQRAHQELPQIEAVKDQHADRIALVPVLASEPAGIEKLRELMS 583
Cdd:NF041417 563 YGNNAFFESRRKQQQKYLEEIRDRFDVPMLLAPLQRDEPTGIEELRRFGS 612
GET3_arsA_TRC40 TIGR00345
transport-energizing ATPase, TRC40/GET3/ArsA family; Members of this family are ATPases that ...
24-294 1.62e-111

transport-energizing ATPase, TRC40/GET3/ArsA family; Members of this family are ATPases that energize transport, although with different partner proteins for different functions. Recent findings show that TRC40 (GET3 in yeast) in involved in the insertion of tail-anchored membrane proteins in eukaryotes. A similar function is expected for members of this family in archaea. However, the earliest discovery of a function for this protein family is ArsA, an arsenic resistance protein that partners with ArsB (see pfam02040) for As(III) efflux. [Hypothetical proteins, Conserved]


Pssm-ID: 273027 [Multi-domain]  Cd Length: 284  Bit Score: 334.45  E-value: 1.62e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972   24 ISCATAIRLAEQGKRVLLVSTDPASNVGQVFDQAIGNTIRPLTAVPALSALEIDPQEAARQYRARIVDPIKGLLPDDvvN 103
Cdd:TIGR00345   1 ISAATAIRLAEQGKKVLLVSTDPAHSLSDVFEQEIGHTPTKVTGVENLSAVEIDPQAALEEYRAKLVEQIKGNLPDG--D 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  104 SISEQLSGACTT----EIAAFDEFTGLLTDASLltRFDHIIFDTAPTGHTIRLLQLPGAWSSFIESNPDGASCLGPMAG- 178
Cdd:TIGR00345  79 MLGDQLEGAALSpgidEIAAFDEFLKHMTDAEN--EFDVVIFDTAPTGHTLRLLQLPEVLSSFLEKFIKIRSKLGPMAKl 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  179 -------------LEKQREQYAHAVEALSDPERTRLVLVARLQNSTLQEVARTHEELAEIGLKNQYLVINGVLPEAEAeh 245
Cdd:TIGR00345 157 fmgageddealekLEELKEQIEAAREILSDPERTSFVLVVIPEKMSLYESERAHKELAKYGIKVDAVIVNQVLPENAQ-- 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 490311972  246 DALAAAIWQREQEALANLPAGLSELPTDTLLLQPVNMVGVSALKGLLDT 294
Cdd:TIGR00345 235 DEFCQARWELQQKYLKQIPEKFADLPVAEVPLQKEEMVGLEALKRLSKT 283
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
8-293 1.88e-111

Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];


Pssm-ID: 439774  Cd Length: 299  Bit Score: 334.87  E-value: 1.88e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972   8 PPYLFFTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNVGQVFDQAIGNTIRPLtAVPALSALEIDPQEAARQYRA 87
Cdd:COG0003    3 TRIIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGTELGNEPTEV-AVPNLYALEIDPEAELEEYWE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  88 RIVDPIKGLLPDDVVNSISEqlSGACTTEIAAFDEFTGLLTDAslltRFDHIIFDTAPTGHTIRLLQLP---GAWSSFIE 164
Cdd:COG0003   82 RVRAPLRGLLPSAGVDELAE--SLPGTEELAALDELLELLEEG----EYDVIVVDTAPTGHTLRLLSLPellGWWLDRLL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 165 SNPDGASCLGP-------------MAGLEKQREQYAHAVEALSDPERTRLVLVARLQNSTLQEVARTHEELAEIGLKNQY 231
Cdd:COG0003  156 KLRRKASGLGRplagilglpddpvLEGLEELRERLERLRELLRDPERTSFRLVTNPERLAIAETRRALEELALYGIPVDG 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490311972 232 LVINGVLPEaEAEHDALAAAIWQREQEALANLPAGLSELPTDTLLLQPVNMVGVSALKGLLD 293
Cdd:COG0003  236 LVVNRVLPE-EADDDAFLAARRERQQEYLAEIEEAFAPLPVVEVPLLAEEVVGLEALRALAE 296
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
10-289 1.88e-88

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: 274.00  E-value: 1.88e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  10 YLFFTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNVGQVFDQAIGNTiRPLTAVPALSALEIDPQEAARQYRARI 89
Cdd:cd02035    2 IIFFGGKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGQKLGGE-TPVKGAPNLWAMEIDPEEALEEYWEEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  90 VDPIKGL--LPDDVVNSISEQLSGACTTEIAAFDEFTGLLTDAslltRFDHIIFDTAPTGHTIRLLQLPgawssfiesnp 167
Cdd:cd02035   81 KELLAQYlrLPGLDEVYAEELLSLPGMDEAAAFDELREYVESG----EYDVIVFDTAPTGHTLRLLSLP----------- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 168 dgasclgpmaglekqreqYAHAVEALSDPERTRLVLVARLQNSTLQEVARTHEELAEIGLKNQYLVINGVLPEAEAEHDA 247
Cdd:cd02035  146 ------------------LEQVRELLRDPERTTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVNQVLPEEADDSFF 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 490311972 248 LAAaiWQREQEALANLPAGLSELPTDTLLLQPVNMVGVSALK 289
Cdd:cd02035  208 LRR--RRQQQKYLDEIEELFEPLPVVEVPLLPEEVRGLEALR 247
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
329-581 1.10e-74

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: 238.18  E-value: 1.10e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 329 LIMLMGKGGVGKTTMAAAIAVRLADMGFDVHLTTSDPAAHLSTTLNGSL---------KNLQVSRINPHDETERYRQHVL 399
Cdd:cd02035    2 IIFFGGKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGQKLggetpvkgaPNLWAMEIDPEEALEEYWEEVK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 400 ETKGR--DLDEAGKRLLEEDLRSPCTEEIAVFQAFSRVIREAGKRFVVMDTAPTGHTLLLLDATgayhreiakkmgskgh 477
Cdd:cd02035   82 ELLAQylRLPGLDEVYAEELLSLPGMDEAAAFDELREYVESGEYDVIVFDTAPTGHTLRLLSLP---------------- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 478 FTTPMMQLQDPDRTKVLLVTLPETTPVLEAANLQADLKRAGIHPWGWIINNSLSIADTRSPLLCQRAHQELPQIEAVKDQ 557
Cdd:cd02035  146 LEQVRELLRDPERTTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVNQVLPEEADDSFFLRRRRQQQKYLDEIEELF 225
                        250       260
                 ....*....|....*....|....
gi 490311972 558 HADRIALVPVLASEPAGIEKLREL 581
Cdd:cd02035  226 EPLPVVEVPLLPEEVRGLEALRAL 249
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
10-289 1.77e-66

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: 218.76  E-value: 1.77e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972   10 YLFFTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNVGQVFDQAIGNTIRPLTavPALSALEIDPQEAARQYRARI 89
Cdd:pfam02374   3 WIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQKFGHEPTKVK--ENLSAMEIDPNMELEEYWQEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972   90 VDPIKGLLPDDVVNSISEQLSGA--CTTEIAAFDEFTGLLTDASlltrFDHIIFDTAPTGHTIRLLQLPGAWSSFIE--- 164
Cdd:pfam02374  81 QKYMNALLGLRMLEGILAEELASlpGIDEAASFDEFKKYMDEGE----YDVVVFDTAPTGHTLRLLSLPTVLGWYLEkiv 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  165 ------------SNPDGASCLG-PMAGLEKQREQYAHAVEALSDPERTRLVLVARLQNSTLQEVARTHEELAEIGLKNQY 231
Cdd:pfam02374 157 klknqigplakpFLGMGGVSIPeALESLEETKERIERAREILTDPERTSFRLVCIPEKMSLYETERAIQYLAKYGIDVDA 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 490311972  232 LVINGVLPEAEAEHDALAAAIWQREQEALANLPAGLSELPTDTLLLQPVNMVGVSALK 289
Cdd:pfam02374 237 VIVNQVLPENVQENCPFCEARKKIQQKYLDEIEELFSDFPVAKLPLLPEEVVGLEKLE 294
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
329-583 3.40e-50

Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];


Pssm-ID: 439774  Cd Length: 299  Bit Score: 175.39  E-value: 3.40e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 329 LIMLMGKGGVGKTTMAAAIAVRLADMGFDVHLTTSDPAAHLSTTLNGSL---------KNLQVSRINPHDETERYRQHVL 399
Cdd:COG0003    5 IIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGTELgneptevavPNLYALEIDPEAELEEYWERVR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 400 ETKGRDLDEAGKRLLEEDLrsPCTEEIAVFQAFSRVIREAGKRFVVMDTAPTGHTLLLLDA---TGAY-------HREIA 469
Cdd:COG0003   85 APLRGLLPSAGVDELAESL--PGTEELAALDELLELLEEGEYDVIVVDTAPTGHTLRLLSLpelLGWWldrllklRRKAS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 470 KKM----GSKGHFTTPMMQ---------------LQDPDRTKVLLVTLPETTPVLEAANLQADLKRAGIHPWGWIINNSL 530
Cdd:COG0003  163 GLGrplaGILGLPDDPVLEgleelrerlerlrelLRDPERTSFRLVTNPERLAIAETRRALEELALYGIPVDGLVVNRVL 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490311972 531 SIADTRSPLLCQRAHQELPQIEAVKDQHADR-IALVPVLASEPAGIEKLRELMS 583
Cdd:COG0003  243 PEEADDDAFLAARRERQQEYLAEIEEAFAPLpVVEVPLLAEEVVGLEALRALAE 296
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
330-581 1.07e-39

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: 146.73  E-value: 1.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  330 IMLMGKGGVGKTTMAAAIAVRLADMGFDVHLTTSDPAAHLSTTLNGSL--------KNLQVSRINPHDETERYRQHVLET 401
Cdd:pfam02374   4 IFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQKFgheptkvkENLSAMEIDPNMELEEYWQEVQKY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  402 KGRDL--DEAGKRLLEEDLRSPCTEEIAVFQAFSRVIREAGKRFVVMDTAPTGHTLLLL---DATGAYHREIAKKMGSKG 476
Cdd:pfam02374  84 MNALLglRMLEGILAEELASLPGIDEAASFDEFKKYMDEGEYDVVVFDTAPTGHTLRLLslpTVLGWYLEKIVKLKNQIG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  477 HFTTPMM--------------------------QLQDPDRTKVLLVTLPETTPVLEAANLQADLKRAGIHPWGWIINNSL 530
Cdd:pfam02374 164 PLAKPFLgmggvsipealesleetkerierareILTDPERTSFRLVCIPEKMSLYETERAIQYLAKYGIDVDAVIVNQVL 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 490311972  531 SIADTRSPLLCQ--RAHQE--LPQIEAV-KDQHadrIALVPVLASEPAGIEKLREL 581
Cdd:pfam02374 244 PENVQENCPFCEarKKIQQkyLDEIEELfSDFP---VAKLPLLPEEVVGLEKLEKF 296
GET3_arsA_TRC40 TIGR00345
transport-energizing ATPase, TRC40/GET3/ArsA family; Members of this family are ATPases that ...
343-583 7.60e-27

transport-energizing ATPase, TRC40/GET3/ArsA family; Members of this family are ATPases that energize transport, although with different partner proteins for different functions. Recent findings show that TRC40 (GET3 in yeast) in involved in the insertion of tail-anchored membrane proteins in eukaryotes. A similar function is expected for members of this family in archaea. However, the earliest discovery of a function for this protein family is ArsA, an arsenic resistance protein that partners with ArsB (see pfam02040) for As(III) efflux. [Hypothetical proteins, Conserved]


Pssm-ID: 273027 [Multi-domain]  Cd Length: 284  Bit Score: 110.26  E-value: 7.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  343 MAAAIAVRLADMGFDVHLTTSDPAAHLSTTLN----------GSLKNLQVSRINPHDETERYRQHVLE-TKG----RDLD 407
Cdd:TIGR00345   1 ISAATAIRLAEQGKKVLLVSTDPAHSLSDVFEqeightptkvTGVENLSAVEIDPQAALEEYRAKLVEqIKGnlpdGDML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  408 EAgkrLLEEDLRSPCTEEIAVFQAFSRVIREAGKRF--VVMDTAPTGHTLLLL---DATGAYHR---EIAKKMGS----- 474
Cdd:TIGR00345  81 GD---QLEGAALSPGIDEIAAFDEFLKHMTDAENEFdvVIFDTAPTGHTLRLLqlpEVLSSFLEkfiKIRSKLGPmaklf 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  475 ----------------KGHFTTPMMQLQDPDRTKVLLVTLPETTPVLEAANLQADLKRAGIHPWGWIINNSL--SIADTR 536
Cdd:TIGR00345 158 mgageddealekleelKEQIEAAREILSDPERTSFVLVVIPEKMSLYESERAHKELAKYGIKVDAVIVNQVLpeNAQDEF 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 490311972  537 spllCQ-RAHQELPQIEAVKDQHADR-IALVPVLASEPAGIEKLRELMS 583
Cdd:TIGR00345 238 ----CQaRWELQQKYLKQIPEKFADLpVAEVPLQKEEMVGLEALKRLSK 282
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
12-146 3.15e-09

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: 57.95  E-value: 3.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  12 FFTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNVGQVFDqaigntIRPLTAVPALSALEIDPQEAARqyrARIVD 91
Cdd:COG1192    6 VANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLG------LDPDDLDPTLYDLLLDDAPLED---AIVPT 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490311972  92 PIKGLlpdDVVNSiSEQLSGAcTTEIAAFDEFTGLLTDA--SLLTRFDHIIFDTAPT 146
Cdd:COG1192   77 EIPGL---DLIPA-NIDLAGA-EIELVSRPGRELRLKRAlaPLADDYDYILIDCPPS 128
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
329-527 4.23e-09

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: 54.36  E-value: 4.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 329 LIMLMG-KGGVGKTTMAAAIAVRLADMGFDVHLTTSDpaahlsttlngslknlqvsrinphdeteryrqhvletkgrdld 407
Cdd:cd01983    2 VIAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLD------------------------------------------- 38
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 408 eagkrlleedlrspcteeiavfqafsrvireagkRFVVMDTAPTGHTLLLLDatgayhreiakkmgskghftTPMMQLQD 487
Cdd:cd01983   39 ----------------------------------DYVLIDGGGGLETGLLLG--------------------TIVALLAL 64
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 490311972 488 PDRTKVLLVTLPETTPVLEAANL--QADLKRAGIHPWGWIIN 527
Cdd:cd01983   65 KKADEVIVVVDPELGSLLEAVKLllALLLLGIGIRPDGIVLN 106
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
15-244 5.13e-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: 57.89  E-value: 5.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  15 GKGGVGKTSISCATAIRLAEQGKRVLLVSTDP-ASNVGQVFDqaigntirpLTAVPALSAL---EIDPQEAARQYRARIV 90
Cdd:COG0489  100 GKGGEGKSTVAANLALALAQSGKRVLLIDADLrGPSLHRMLG---------LENRPGLSDVlagEASLEDVIQPTEVEGL 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  91 D--PIKGLLPDDvvnsiseqlsgactTEIAAFDEFTGLLTDasLLTRFDHIIFDTAP-TGHT-IRLLQlpgawssfiesn 166
Cdd:COG0489  171 DvlPAGPLPPNP--------------SELLASKRLKQLLEE--LRGRYDYVIIDTPPgLGVAdATLLA------------ 222
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490311972 167 pdgasclgpmaglekqreQYAHAVealsdpertrlVLVARLQNSTLQEVARTHEELAEIGLKNQYLVINGVLPEAEAE 244
Cdd:COG0489  223 ------------------SLVDGV-----------LLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNMVCPKGERY 271
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
10-54 7.40e-09

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: 54.08  E-value: 7.40e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 490311972  10 YLFFTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNVGQVF 54
Cdd:cd02042    3 IAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL 47
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
13-71 1.50e-08

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 55.94  E-value: 1.50e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490311972  13 FTGKGGVGKTSIScATAIR-LAEQGKRVLLVSTDPASNVGqvfdQAIG-----NTIRPLTAVPAL 71
Cdd:COG3640    5 VAGKGGVGKTTLS-ALLARyLAEKGKPVLAVDADPNANLA----EALGleveaDLIKPLGEMREL 64
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
9-45 1.02e-07

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: 50.51  E-value: 1.02e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 490311972   9 PYLFFTG-KGGVGKTSISCATAIRLAEQGKRVLLVSTD 45
Cdd:cd01983    1 RVIAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
16-146 1.11e-06

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: 49.12  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972   16 KGGVGKTSISCATAIRLAEQGKRVLLVSTDP---ASNVGQVFDQAIGNTIRPLTAVpalsalEIDPQEAARQYRARIVDp 92
Cdd:pfam13614  10 KGGVGKTTTSVNLAAALAKKGKKVLLIDLDPqgnATSGLGIDKNNVEKTIYELLIG------ECNIEEAIIKTVIENLD- 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 490311972   93 ikgLLPDDVvnsiseQLSGAcTTEIAAFDEFTGLLTDA--SLLTRFDHIIFDTAPT 146
Cdd:pfam13614  83 ---LIPSNI------DLAGA-EIELIGIENRENILKEAlePVKDNYDYIIIDCPPS 128
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
15-49 1.30e-06

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: 49.65  E-value: 1.30e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 490311972   15 GKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASN 49
Cdd:pfam01656   6 TKGGVGKTTLAANLARALARRGLRVLLIDLDPQSN 40
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
335-373 1.95e-06

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: 47.15  E-value: 1.95e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 490311972 335 KGGVGKTTMAAAIAVRLADMGFDVHLTTSDPAAHLSTTL 373
Cdd:cd02042    9 KGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL 47
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
13-54 3.19e-06

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: 48.85  E-value: 3.19e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 490311972  13 FTGKGGVGKTSIsCATAIR-LAEQGKRVLLVSTDPASNVGQVF 54
Cdd:cd02034    5 VAGKGGVGKTTI-AALLIRyLAKKGGKVLAVDADPNSNLAETL 46
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
13-49 6.99e-06

4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;


Pssm-ID: 395090  Cd Length: 271  Bit Score: 47.82  E-value: 6.99e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 490311972   13 FTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASN 49
Cdd:pfam00142   5 IYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKAD 41
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
330-373 7.18e-06

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 47.85  E-value: 7.18e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 490311972 330 IMLMGKGGVGKTTMAAAIAVRLADMGFDVHLTTSDPAAHLSTTL 373
Cdd:COG3640    3 IAVAGKGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEAL 46
ParA_partition NF041546
ParA family partition ATPase;
16-46 8.19e-06

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 46.78  E-value: 8.19e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 490311972  16 KGGVGKTSISCATAIRLAEQGKRVLLVSTDP 46
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADP 38
PHA02518 PHA02518
ParA-like protein; Provisional
16-121 1.21e-05

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 46.77  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  16 KGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNVGQVFDQAigNTIRPLTAVPALS-ALEIDPQEAARQYrarivdpik 94
Cdd:PHA02518   9 KGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAR--EEGEPLIPVVRMGkSIRADLPKVASGY--------- 77
                         90       100
                 ....*....|....*....|....*..
gi 490311972  95 gllpDDVVNSISEQLSGACTTEIAAFD 121
Cdd:PHA02518  78 ----DYVVVDGAPQDSELARAALRIAD 100
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
15-45 1.43e-05

Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 46.97  E-value: 1.43e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 490311972  15 GKGGVGKTSISCATAIRLAEQGKRVLLVSTD 45
Cdd:COG2894   10 GKGGVGKTTTTANLGTALALLGKKVVLIDAD 40
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
13-46 1.49e-05

nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia.


Pssm-ID: 349759  Cd Length: 265  Bit Score: 46.74  E-value: 1.49e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 490311972  13 FTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDP 46
Cdd:cd02040    5 IYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDP 38
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
15-45 2.50e-05

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: 46.02  E-value: 2.50e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 490311972  15 GKGGVGKTSISCATAIRLAEQGKRVLLVSTD 45
Cdd:cd02038    8 GKGGVGKTNVSANLALALSKLGKRVLLLDAD 38
chlL CHL00072
photochlorophyllide reductase subunit L
15-46 2.76e-05

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 46.27  E-value: 2.76e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 490311972  15 GKGGVGKTSISCATAIRLAEQGKRVLLVSTDP 46
Cdd:CHL00072   7 GKGGIGKSTTSCNISIALARRGKKVLQIGCDP 38
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
15-45 5.30e-05

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: 44.89  E-value: 5.30e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 490311972  15 GKGGVGKTSISCATAIRLAEQGKRVLLVSTD 45
Cdd:cd02036    8 GKGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
335-373 6.60e-05

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: 44.85  E-value: 6.60e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 490311972 335 KGGVGKTTMAAAIAVRLADMGFDVHLTTSDPAAHLSTTL 373
Cdd:COG1192   10 KGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGL 48
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
330-358 7.79e-05

NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits.


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 44.37  E-value: 7.79e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 490311972  330 IMLM-GKGGVGKTTMAAAIAVRLADMGFDV 358
Cdd:pfam10609   6 IAVAsGKGGVGKSTVAVNLALALARLGYKV 35
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
15-46 1.09e-04

L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. Protochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. Three genes, bchL, bchN and bchB, are involved in light-independent protochlorophyllide reduction in bacteriochlorophyll biosynthesis. In cyanobacteria, algae, and gymnosperms, three similar genes, chlL, chlN and chlB are involved in protochlorophyllide reduction during chlorophylls biosynthesis. BchL/chlL, bchN/chlN and bchB/chlB exhibit significant sequence similarity to the nifH, nifD and nifK subunits of nitrogenase, respectively. Nitrogenase catalyzes the reductive formation of ammonia from dinitrogen.


Pssm-ID: 349752  Cd Length: 267  Bit Score: 44.21  E-value: 1.09e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 490311972  15 GKGGVGKTSISCATAIRLAEQGKRVLLVSTDP 46
Cdd:cd02032    7 GKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDP 38
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
334-463 1.20e-04

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: 43.87  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  334 GKGGVGKTTMAAAIAVRLADMGFDVHLTTSDPAAHLSTTLNGslknlqVSRINPHDETE----RYRQHV------LETKG 403
Cdd:pfam01656   6 TKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGL------EGDIAPALQALaeglKGRVNLdpillkEKSDE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490311972  404 RDLDEAGKRLLEEDLRSpCTEEIAVFQAFSRVIREAGKRF--VVMDTAPtGHTLLLLDATGA 463
Cdd:pfam01656  80 GGLDLIPGNIDLEKFEK-ELLGPRKEERLREALEALKEDYdyVIIDGAP-GLGELLRNALIA 139
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
334-358 1.85e-04

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: 43.34  E-value: 1.85e-04
                         10        20
                 ....*....|....*....|....*
gi 490311972 334 GKGGVGKTTMAAAIAVRLADMGFDV 358
Cdd:cd02036    8 GKGGVGKTTTTANLGVALAKLGKKV 32
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
13-46 2.18e-04

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 43.22  E-value: 2.18e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 490311972  13 FTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDP 46
Cdd:PRK13230   6 FYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDP 39
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
334-358 2.57e-04

Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 42.49  E-value: 2.57e-04
                         10        20
                 ....*....|....*....|....*
gi 490311972 334 GKGGVGKTTMAAAIAVRLADMGFDV 358
Cdd:cd02037    8 GKGGVGKSTVAVNLALALAKKGYKV 32
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
14-45 3.38e-04

septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division]


Pssm-ID: 131023 [Multi-domain]  Cd Length: 261  Bit Score: 42.71  E-value: 3.38e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 490311972   14 TGKGGVGKTSISCATAIRLAEQGKRVLLVSTD 45
Cdd:TIGR01968   8 SGKGGVGKTTTTANLGTALARLGKKVVLIDAD 39
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
334-358 4.38e-04

Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 42.35  E-value: 4.38e-04
                         10        20
                 ....*....|....*....|....*
gi 490311972 334 GKGGVGKTTMAAAIAVRLADMGFDV 358
Cdd:COG2894   10 GKGGVGKTTTTANLGTALALLGKKV 34
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
334-527 5.36e-04

cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 42.03  E-value: 5.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  334 GKGGVGKTTMAAAIAVRLADMGFDVHLTTSDPA-AHLSTTLNgsLKNLQVSRINPHDETERYRQHVLETK--------GR 404
Cdd:TIGR01969   8 GKGGTGKTTITANLGVALAKLGKKVLALDADITmANLELILG--MEDKPVTLHDVLAGEADIKDAIYEGPfgvkvipaGV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  405 DLD---EAGKRLLEEdlrspcteeiavfqafsrVIREAGKRFvvmdtaptghTLLLLDATGAYHREIAKKMGSKghfttp 481
Cdd:TIGR01969  86 SLEglrKADPDKLED------------------VLKEIIDDT----------DFLLIDAPAGLERDAVTALAAA------ 131
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 490311972  482 mmqlqdpdrTKVLLVTLPETTPVLEAANLQADLKRAGIHPWGWIIN 527
Cdd:TIGR01969 132 ---------DELLLVVNPEISSITDALKTKIVAEKLGTAILGVVLN 168
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
15-45 6.65e-04

NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits.


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 41.67  E-value: 6.65e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 490311972   15 GKGGVGKTSISCATAIRLAEQGKRVLLVSTD 45
Cdd:pfam10609  11 GKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
332-392 6.73e-04

transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI superfamily which contains a ATP-binding domain. Proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion. The specific function of TraL protein is unknown.


Pssm-ID: 349771  Cd Length: 155  Bit Score: 40.40  E-value: 6.73e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490311972 332 LMGKGGVGKTTMAAAIAVRLADMGFDVHLTTSDPAahlsttlNGSL---KNLQVSRINPHDETE 392
Cdd:cd05386    6 LQGKGGVGKSVIASLLAQYLIDKGQPVSCIDTDPV-------NKTFagyKALNVQRINIIDNDE 62
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
13-46 7.03e-04

NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) of the protochlorophyllide reductase, and the BchX subunit of the Chlorophyllide reductase. Members of this family use energy from ATP hydrolysis and transfer electrons through a Fe4-S4 cluster to other subunit for substrate reduction


Pssm-ID: 349761  Cd Length: 266  Bit Score: 41.58  E-value: 7.03e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 490311972  13 FTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDP 46
Cdd:cd02117    5 VYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDP 38
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
335-386 7.14e-04

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: 40.65  E-value: 7.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 490311972  335 KGGVGKTTMAAAIAVRLADMGFDVHLTTSDPAAHLSTTLnGSLKNLQVSRIN 386
Cdd:pfam13614  10 KGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGL-GIDKNNVEKTIY 60
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
240-527 8.70e-04

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: 41.71  E-value: 8.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 240 EAEAEHDALAAAIWQREQEALANLPAGLSELPTDTLLLQPVNMVGVSALKGLLDTRSEALPLPVTNILYtpenlsLSGLV 319
Cdd:COG0489   11 LREEAQALLLLLLLLLLLLRLEEAAAAAALAAAAPAAAAPAPLPPAPALLLLLLLLLGLLLLLLLALAL------LLLLL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 320 DDIARSEHGLIMLM-GKGGVGKTTMAAAIAVRLADMGFDV-------------HLTTSDPAAHLSTTLNGSLKNLQVsrI 385
Cdd:COG0489   85 LLLLRLLLEVIAVTsGKGGEGKSTVAANLALALAQSGKRVllidadlrgpslhRMLGLENRPGLSDVLAGEASLEDV--I 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 386 NPhdeTERYRQHVLeTKGRDLDEAgkrlleedlrspctEEIAVFQAFSRVIREAGKRF--VVMDTAP-TGHTLLLLdatg 462
Cdd:COG0489  163 QP---TEVEGLDVL-PAGPLPPNP--------------SELLASKRLKQLLEELRGRYdyVIIDTPPgLGVADATL---- 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490311972 463 ayhreIAKKMGSkghfttpmmqlqdpdrtkVLLVTLPETTPVLEAANLQADLKRAGIHPWGWIIN 527
Cdd:COG0489  221 -----LASLVDG------------------VLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLN 262
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
14-54 1.35e-03

cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 40.87  E-value: 1.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 490311972   14 TGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPA-SNVGQVF 54
Cdd:TIGR01969   7 SGKGGTGKTTITANLGVALAKLGKKVLALDADITmANLELIL 48
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
11-45 1.59e-03

DNA replication protein DnaC [Replication, recombination and repair];


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 40.53  E-value: 1.59e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 490311972  11 LFFTGKGGVGKTSISCATAIRLAEQGKRVLLVSTD 45
Cdd:COG1484  102 LILLGPPGTGKTHLAIALGHEACRAGYRVRFTTAP 136
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
23-145 2.10e-03

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: 39.87  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  23 SISCATAIRLAEQGKRVLLVSTDP-ASNVGQVFDQAIGNTIRpltavpALSALEIDPQEAARQYRARIVdpikgLLPddv 101
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLgLANLDVLLGLEPKATLA------DVLAGEADLEDAIVQGPGGLD-----VLP--- 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 490311972 102 vnsiseqlSGACTTEIAAFDEFTGLLTDASLLTR-FDHIIFDTAP 145
Cdd:COG0455   67 --------GGSGPAELAELDPEERLIRVLEELERfYDVVLVDTGA 103
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
15-46 2.12e-03

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 40.33  E-value: 2.12e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 490311972  15 GKGGVGKTSISCATAIRLAEQGKRVLLVSTDP 46
Cdd:PRK13185   9 GKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDP 40
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
15-45 2.36e-03

Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 39.79  E-value: 2.36e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 490311972  15 GKGGVGKTSISCATAIRLAEQGKRVLLVSTD 45
Cdd:cd02037    8 GKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
330-406 2.86e-03

NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) of the protochlorophyllide reductase, and the BchX subunit of the Chlorophyllide reductase. Members of this family use energy from ATP hydrolysis and transfer electrons through a Fe4-S4 cluster to other subunit for substrate reduction


Pssm-ID: 349761  Cd Length: 266  Bit Score: 39.66  E-value: 2.86e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490311972 330 IMLMGKGGVGKTTMAAAIAVRLADMGFDVHLTTSDPAAHLSTTLNGSLknlqvsRINPHDETERYRQHVLETKGRDL 406
Cdd:cd02117    3 IVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGK------VPPTIDEMLTEDGTAEELRREDL 73
ParA_partition NF041546
ParA family partition ATPase;
335-365 3.29e-03

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 39.07  E-value: 3.29e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 490311972 335 KGGVGKTTMAAAIAVRLADMGFDVHLTTSDP 365
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADP 38
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
330-405 3.72e-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: 39.22  E-value: 3.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490311972 330 IMLMGKGGVGKTTMAAAIAVRLADMGFDVHLTTSDPAAHLSTTLngslkNLQVSRINPHDETERYRQHVLETKGRD 405
Cdd:cd02034    3 IAVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETL-----GVEVEKLPLIKTIGDIRERTGAKKGEP 73
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
334-364 6.93e-03

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: 38.32  E-value: 6.93e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 490311972 334 GKGGVGKTTMAAAIAVRLADMGFDVHLTTSD 364
Cdd:cd02038    8 GKGGVGKTNVSANLALALSKLGKRVLLLDAD 38
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
15-49 7.08e-03

X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls into bacteriochlorophylls by reducing the chlorin B-ring. This family contains the X subunit of this three-subunit enzyme. Sequence and structure similarity between bchX, protochlorophyllide reductase L subunit (bchL and chlL) and nitrogenase Fe protein (nifH gene) suggest their functional similarity. Members of the BchX family serve as the unique electron donors to their respective catalytic subunits (bchN-bchB, bchY-bchZ and nitrogenase component 1). Mechanistically, they hydrolyze ATP and transfer electrons through a Fe4-S4 cluster.


Pssm-ID: 349753  Cd Length: 329  Bit Score: 39.04  E-value: 7.08e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 490311972  15 GKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASN 49
Cdd:cd02033   38 GKGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKSD 72
PRK08939 PRK08939
primosomal protein DnaI; Reviewed
1-42 7.21e-03

primosomal protein DnaI; Reviewed


Pssm-ID: 236353 [Multi-domain]  Cd Length: 306  Bit Score: 38.70  E-value: 7.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 490311972   1 MKFLQNIPPY-----LFFTGKGGVGKTSISCATAIRLAEQGKRVLLV 42
Cdd:PRK08939 144 LDFLEAYPPGekvkgLYLYGDFGVGKSYLLAAIANELAKKGVSSTLL 190
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
12-264 8.41e-03

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: 38.56  E-value: 8.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  12 FFTGKGGVGKTSISCATAIRLAEQ-GKRVLLVSTD-PASNVGQVFDQAIGNTIRPLTAVPAlsalEIDPqEAARQYRARI 89
Cdd:COG4963  107 VVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDlQFGDVALYLDLEPRRGLADALRNPD----RLDE-TLLDRALTRH 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972  90 VDPIKgLLPDDVVNSISEQLSGactteiaafDEFTGLLTdaSLLTRFDHIIFDtaptghtirllqLPGAWSSFIEsnpdg 169
Cdd:COG4963  182 SSGLS-VLAAPADLERAEEVSP---------EAVERLLD--LLRRHFDYVVVD------------LPRGLNPWTL----- 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311972 170 asclgpmaglekqreqyahAVEALSDpertRLVLVARLQNSTLQEVARTHEELAEIGLKNQ--YLVINGVLPEAEAEHDA 247
Cdd:COG4963  233 -------------------AALEAAD----EVVLVTEPDLPSLRNAKRLLDLLRELGLPDDkvRLVLNRVPKRGEISAKD 289
                        250
                 ....*....|....*..
gi 490311972 248 LAAAIwqrEQEALANLP 264
Cdd:COG4963  290 IEEAL---GLPVAAVLP 303
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
334-364 9.34e-03

septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division]


Pssm-ID: 131023 [Multi-domain]  Cd Length: 261  Bit Score: 38.09  E-value: 9.34e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 490311972  334 GKGGVGKTTMAAAIAVRLADMGFDVHLTTSD 364
Cdd:TIGR01968   9 GKGGVGKTTTTANLGTALARLGKKVVLIDAD 39
 
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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