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Conserved domains on  [gi|496059301|ref|WP_008783808|]
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MULTISPECIES: arsenical pump-driving ATPase [Citrobacter]

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 ...
 8-573 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: 1050.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301    8 DIPPFIFFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPASNVGQVFSQTIGHRITDISTVENLAAMEVDPMAAAQAY 87
Cdd:TIGR04291   1 ELPPYLFFTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNVGQVFGQTIGNKITAIAGVPGLFALEIDPQAAAQAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301   88 RDRVLDPVRGLMPTEVVSSIEEQLSGSCTTEIAAFDEFTGLLTNHELREKYDHIVFDTAPTGHTIRMLELPGAWSGYLEA 167
Cdd:TIGR04291  81 RARIVDPVRGVLPDDVVSSIEEQLSGACTTEIAAFDEFTGLLTDAELTQDFDHIIFDTAPTGHTIRLLQLPGAWSDFLDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  168 NPDAAANLGPLVGLEKQQHQYSDAVKALSDAALTRLVLVARAQTSTLKEVSHTHDELYAIGLQHQHLAINGVLPPFAGEN 247
Cdd:TIGR04291 161 NPNGASCLGPLAGLEKQRAQYAKAVEALSDPERTRLILVARPQKSTLLEVARTHQELAAIGLKNQYLVINGVLPETEASD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  248 DPLAQSILAREEKALQAMPENLANLPRSQLYLKPFNLVGLEALRQLFTENKASLPLPATTLNTLDLPKLSSLVDELSQTG 327
Cdd:TIGR04291 241 DPLAQAIYKREQKALQHMPAILANLPRYTLPLKPYNLVGLEALRQLLNDDQPQLSLDITTPQVPDLPSLSRLIDEIAKSE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  328 KGLVMTMGKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTLDGSLPNLQVSRIDPKVETERYRRFVLENQGKGL 407
Cdd:TIGR04291 321 KGLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSLNNLQVSRIDPKQETERYRQEVLATKGKEL 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  408 DAEGLAVLEEDLRSPCTEEIAVFQAFSRIIKEADDHFVIMDTAPTGHTLLLLDATGAYHREMVRQMGQTHDHVMTPMMQL 487
Cdd:TIGR04291 401 DEDGKAYLEEDLRSPCTEEIAVFQAFSRIIREAGDRFVVMDTAPTGHTLLLLDATGAYHREVERKMGDTPEHVTTPMMQL 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  488 QDPEKTKVIIVTLAETTPVLEAANLQQDLRRAGIEPWAWVVNNSLAAAEPSSPFLKTRASRELPLISDVGEQYAKRIALT 567
Cdd:TIGR04291 481 QDPERTKVLLVTLPETTPVLEAARLQEDLRRAGIEPWWWVINNSLAATNTTSPLLSQRAQNELKWIEKVKRIHADRYAVI 560


                  ....*.
gi 496059301  568 ALQSQE 573
Cdd:TIGR04291 561 PLQAEE 566
 
Name Accession Description Interval E-value
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 8-573 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: 1050.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301    8 DIPPFIFFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPASNVGQVFSQTIGHRITDISTVENLAAMEVDPMAAAQAY 87
Cdd:TIGR04291   1 ELPPYLFFTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNVGQVFGQTIGNKITAIAGVPGLFALEIDPQAAAQAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301   88 RDRVLDPVRGLMPTEVVSSIEEQLSGSCTTEIAAFDEFTGLLTNHELREKYDHIVFDTAPTGHTIRMLELPGAWSGYLEA 167
Cdd:TIGR04291  81 RARIVDPVRGVLPDDVVSSIEEQLSGACTTEIAAFDEFTGLLTDAELTQDFDHIIFDTAPTGHTIRLLQLPGAWSDFLDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  168 NPDAAANLGPLVGLEKQQHQYSDAVKALSDAALTRLVLVARAQTSTLKEVSHTHDELYAIGLQHQHLAINGVLPPFAGEN 247
Cdd:TIGR04291 161 NPNGASCLGPLAGLEKQRAQYAKAVEALSDPERTRLILVARPQKSTLLEVARTHQELAAIGLKNQYLVINGVLPETEASD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  248 DPLAQSILAREEKALQAMPENLANLPRSQLYLKPFNLVGLEALRQLFTENKASLPLPATTLNTLDLPKLSSLVDELSQTG 327
Cdd:TIGR04291 241 DPLAQAIYKREQKALQHMPAILANLPRYTLPLKPYNLVGLEALRQLLNDDQPQLSLDITTPQVPDLPSLSRLIDEIAKSE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  328 KGLVMTMGKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTLDGSLPNLQVSRIDPKVETERYRRFVLENQGKGL 407
Cdd:TIGR04291 321 KGLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSLNNLQVSRIDPKQETERYRQEVLATKGKEL 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  408 DAEGLAVLEEDLRSPCTEEIAVFQAFSRIIKEADDHFVIMDTAPTGHTLLLLDATGAYHREMVRQMGQTHDHVMTPMMQL 487
Cdd:TIGR04291 401 DEDGKAYLEEDLRSPCTEEIAVFQAFSRIIREAGDRFVVMDTAPTGHTLLLLDATGAYHREVERKMGDTPEHVTTPMMQL 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  488 QDPEKTKVIIVTLAETTPVLEAANLQQDLRRAGIEPWAWVVNNSLAAAEPSSPFLKTRASRELPLISDVGEQYAKRIALT 567
Cdd:TIGR04291 481 QDPERTKVLLVTLPETTPVLEAARLQEDLRRAGIEPWWWVINNSLAATNTTSPLLSQRAQNELKWIEKVKRIHADRYAVI 560


                  ....*.
gi 496059301  568 ALQSQE 573
Cdd:TIGR04291 561 PLQAEE 566
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 12-583 9.95e-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: 390.78  E-value: 9.95e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  12 FIFFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPASNVGQVFSQTIGHRITDISTVENLAAMEVDPMAAAQAYRDRV 91
Cdd:NF041417  14 FVFFSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFGQSIGHRVTSIDDVENLSAIEIDPDAAAEEYRQRT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  92 LDPVRGLMPTEVVSSIEEQLSGSCTTEIAAFDEFTGLLTNHElrekYDHIVFDTAPTGHTIRMLELPGAWSGYLEANpdA 171
Cdd:NF041417  94 IEPMRQLLDDEQLKTVEEQLDSPCIEEIAAFDKFVEFMDEPE----YDVVVFDTAPTGHTIRLMELPSGWSEELEKG--G 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 172 AANLGPLVGLEKQQHQYSDAVKALSDAALTRLVLVARAQTSTLKEVSHTHDELYAIGLQHQHLAINGVLPPFAGEnDPLA 251
Cdd:NF041417 168 ATCIGPAASLQEQKEDYEKAIDTLQDDAQTSFVFVGKPEDASIDEIERSSKELADLGIKTSLLVINGYLPESVCE-DPFF 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 252 QSILAREEKALQAMPENLANLPRSQLYLKPFNLVGLEALRQ----LFTENKASLP----LPATTLNTLDLPKLSSLVDEL 323
Cdd:NF041417 247 EMKREDEQEILEEVEREFAMQPIATYPLQPGEITGIDLLADvgevLYEGKEPTVDvaviTEEETEETSPSETDKEAVMEL 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 324 SQTGKG---LVMTmGKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTL---------DGSLPNLQVSRIDPKVE 391
Cdd:NF041417 327 LRPQKDtryLFFT-GKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQDIFgtevgheptKVGVENLYAARIDQERA 405

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 392 TERYRRFVLENQGKGLDAEGLAV------LEEDLRSPCTEEIAVFQAFSRIIKEADDHFVIMDTAPTGHTLLLLDAT--- 462
Cdd:NF041417 406 LEEYKTRMLDQVEQSFDKDQIDVeaakaqVREELESPCAEEMAALEKFVSYFDVDGYDVVVFDTAPTGHTLRLLELPsdw 485

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 463 ------GAYHREMVRQMGQTHDHVMTPMmqlQDPEKTKVIIVTLAETTPVLEAANLQQDLR-RAGIEPWAWVVNNSLAAA 535
Cdd:NF041417 486 kgfmdlGSLTKEASDVTGDKYDRVIETM---RDPERSTFVFVMYPEYTPMMEAWRAAEDLRnQVGIETSLVAVNYLLPEE 562

                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*...
gi 496059301 536 EPSSPFLKTRASRELPLISDVGEQYAKRIALTALQSQEPVGINLLEEM 583
Cdd:NF041417 563 YGNNAFFESRRKQQQKYLEEIRDRFDVPMLLAPLQRDEPTGIEELRRF 610
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
8-296 1.09e-103

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 314.84  E-value: 1.09e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301   8 DIPPFIFFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPASNVGQVFSQTIGHRITDIStVENLAAMEVDPMAAAQAY 87
Cdd:COG0003    1 DMTRIIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGTELGNEPTEVA-VPNLYALEIDPEAELEEY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  88 RDRVLDPVRGLMPTEVVSSIEEqlSGSCTTEIAAFDEFTGLLTNhelrEKYDHIVFDTAPTGHTIRMLELP---GAWSGY 164
Cdd:COG0003   80 WERVRAPLRGLLPSAGVDELAE--SLPGTEELAALDELLELLEE----GEYDVIVVDTAPTGHTLRLLSLPellGWWLDR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 165 LEANPDAAANLGPLV-------------GLEKQQHQYSDAVKALSDAALTRLVLVARAQTSTLKEVSHTHDELYAIGLQH 231
Cdd:COG0003  154 LLKLRRKASGLGRPLagilglpddpvleGLEELRERLERLRELLRDPERTSFRLVTNPERLAIAETRRALEELALYGIPV 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059301 232 QHLAINGVLPPFAGEnDPLAQSILAREEKALQAMPENLANLPRSQLYLKPFNLVGLEALRQLFTE 296
Cdd:COG0003  234 DGLVVNRVLPEEADD-DAFLAARRERQQEYLAEIEEAFAPLPVVEVPLLAEEVVGLEALRALAEE 297
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 12-293 2.11e-85

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: 265.91  E-value: 2.11e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  12 FIFFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPASNVGQVFSQTIGHRiTDISTVENLAAMEVDPMAAAQAYRDRV 91
Cdd:cd02035    2 IIFFGGKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGQKLGGE-TPVKGAPNLWAMEIDPEEALEEYWEEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  92 LDPVRGL--MPTEVVSSIEEQLSGSCTTEIAAFDEFTGLLTNhelrEKYDHIVFDTAPTGHTIRMLELPgawsgyleanp 169
Cdd:cd02035   81 KELLAQYlrLPGLDEVYAEELLSLPGMDEAAAFDELREYVES----GEYDVIVFDTAPTGHTLRLLSLP----------- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 170 daaanlgplvglekqqhqYSDAVKALSDAALTRLVLVARAQTSTLKEVSHTHDELYAIGLQHQHLAINGVLPPfaGENDP 249
Cdd:cd02035  146 ------------------LEQVRELLRDPERTTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVNQVLPE--EADDS 205

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 496059301 250 LAQSILAREEKALQAMPENLANLPRSQLYLKPFNLVGLEALRQL 293
Cdd:cd02035  206 FFLRRRRQQQKYLDEIEELFEPLPVVEVPLLPEEVRGLEALRAL 249
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 12-293 1.35e-59

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: 200.65  E-value: 1.35e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301   12 FIFFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPASNVGQVFSQTIGHRITDIStvENLAAMEVDPMAAAQAYRDRV 91
Cdd:pfam02374   3 WIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQKFGHEPTKVK--ENLSAMEIDPNMELEEYWQEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301   92 LDPVRGLMPTEVVSSIEEQLSGS--CTTEIAAFDEFTGLLTNHElrekYDHIVFDTAPTGHTIRMLELPGAWSGYLEANP 169
Cdd:pfam02374  81 QKYMNALLGLRMLEGILAEELASlpGIDEAASFDEFKKYMDEGE----YDVVVFDTAPTGHTLRLLSLPTVLGWYLEKIV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  170 DAAANLGPLVG----------------LEKQQHQYSDAVKALSDAALTRLVLVARAQTSTLKEVSHTHDELYAIGLQHQH 233
Cdd:pfam02374 157 KLKNQIGPLAKpflgmggvsipealesLEETKERIERAREILTDPERTSFRLVCIPEKMSLYETERAIQYLAKYGIDVDA 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  234 LAINGVLPPFAGENDPLAQSILAREEKALQAMPENLANLPRSQLYLKPFNLVGLEALRQL 293
Cdd:pfam02374 237 VIVNQVLPENVQENCPFCEARKKIQQKYLDEIEELFSDFPVAKLPLLPEEVVGLEKLEKF 296
ParA_partition NF041546
ParA family partition ATPase;
336-366 1.67e-06

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 49.09  E-value: 1.67e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 496059301 336 KGGVGKTTVAASVAVSLAKRGHKVHLTTSDP 366
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADP 38
PHA02518 PHA02518
ParA-like protein; Provisional
 18-48 1.36e-05

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 46.38  E-value: 1.36e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 496059301  18 KGGVGKTSLACATAVWLADQGKRTLLVSTDP 48
Cdd:PHA02518   9 KGGAGKTTVATNLASWLHADGHKVLLVDLDP 39
ParA_partition NF041546
ParA family partition ATPase;
18-48 3.26e-05

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 45.24  E-value: 3.26e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 496059301  18 KGGVGKTSLACATAVWLADQGKRTLLVSTDP 48
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 ...
 8-573 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: 1050.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301    8 DIPPFIFFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPASNVGQVFSQTIGHRITDISTVENLAAMEVDPMAAAQAY 87
Cdd:TIGR04291   1 ELPPYLFFTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNVGQVFGQTIGNKITAIAGVPGLFALEIDPQAAAQAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301   88 RDRVLDPVRGLMPTEVVSSIEEQLSGSCTTEIAAFDEFTGLLTNHELREKYDHIVFDTAPTGHTIRMLELPGAWSGYLEA 167
Cdd:TIGR04291  81 RARIVDPVRGVLPDDVVSSIEEQLSGACTTEIAAFDEFTGLLTDAELTQDFDHIIFDTAPTGHTIRLLQLPGAWSDFLDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  168 NPDAAANLGPLVGLEKQQHQYSDAVKALSDAALTRLVLVARAQTSTLKEVSHTHDELYAIGLQHQHLAINGVLPPFAGEN 247
Cdd:TIGR04291 161 NPNGASCLGPLAGLEKQRAQYAKAVEALSDPERTRLILVARPQKSTLLEVARTHQELAAIGLKNQYLVINGVLPETEASD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  248 DPLAQSILAREEKALQAMPENLANLPRSQLYLKPFNLVGLEALRQLFTENKASLPLPATTLNTLDLPKLSSLVDELSQTG 327
Cdd:TIGR04291 241 DPLAQAIYKREQKALQHMPAILANLPRYTLPLKPYNLVGLEALRQLLNDDQPQLSLDITTPQVPDLPSLSRLIDEIAKSE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  328 KGLVMTMGKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTLDGSLPNLQVSRIDPKVETERYRRFVLENQGKGL 407
Cdd:TIGR04291 321 KGLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSLNNLQVSRIDPKQETERYRQEVLATKGKEL 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  408 DAEGLAVLEEDLRSPCTEEIAVFQAFSRIIKEADDHFVIMDTAPTGHTLLLLDATGAYHREMVRQMGQTHDHVMTPMMQL 487
Cdd:TIGR04291 401 DEDGKAYLEEDLRSPCTEEIAVFQAFSRIIREAGDRFVVMDTAPTGHTLLLLDATGAYHREVERKMGDTPEHVTTPMMQL 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  488 QDPEKTKVIIVTLAETTPVLEAANLQQDLRRAGIEPWAWVVNNSLAAAEPSSPFLKTRASRELPLISDVGEQYAKRIALT 567
Cdd:TIGR04291 481 QDPERTKVLLVTLPETTPVLEAARLQEDLRRAGIEPWWWVINNSLAATNTTSPLLSQRAQNELKWIEKVKRIHADRYAVI 560


                  ....*.
gi 496059301  568 ALQSQE 573
Cdd:TIGR04291 561 PLQAEE 566
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 12-583 9.95e-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: 390.78  E-value: 9.95e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  12 FIFFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPASNVGQVFSQTIGHRITDISTVENLAAMEVDPMAAAQAYRDRV 91
Cdd:NF041417  14 FVFFSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFGQSIGHRVTSIDDVENLSAIEIDPDAAAEEYRQRT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  92 LDPVRGLMPTEVVSSIEEQLSGSCTTEIAAFDEFTGLLTNHElrekYDHIVFDTAPTGHTIRMLELPGAWSGYLEANpdA 171
Cdd:NF041417  94 IEPMRQLLDDEQLKTVEEQLDSPCIEEIAAFDKFVEFMDEPE----YDVVVFDTAPTGHTIRLMELPSGWSEELEKG--G 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 172 AANLGPLVGLEKQQHQYSDAVKALSDAALTRLVLVARAQTSTLKEVSHTHDELYAIGLQHQHLAINGVLPPFAGEnDPLA 251
Cdd:NF041417 168 ATCIGPAASLQEQKEDYEKAIDTLQDDAQTSFVFVGKPEDASIDEIERSSKELADLGIKTSLLVINGYLPESVCE-DPFF 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 252 QSILAREEKALQAMPENLANLPRSQLYLKPFNLVGLEALRQ----LFTENKASLP----LPATTLNTLDLPKLSSLVDEL 323
Cdd:NF041417 247 EMKREDEQEILEEVEREFAMQPIATYPLQPGEITGIDLLADvgevLYEGKEPTVDvaviTEEETEETSPSETDKEAVMEL 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 324 SQTGKG---LVMTmGKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTL---------DGSLPNLQVSRIDPKVE 391
Cdd:NF041417 327 LRPQKDtryLFFT-GKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQDIFgtevgheptKVGVENLYAARIDQERA 405

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 392 TERYRRFVLENQGKGLDAEGLAV------LEEDLRSPCTEEIAVFQAFSRIIKEADDHFVIMDTAPTGHTLLLLDAT--- 462
Cdd:NF041417 406 LEEYKTRMLDQVEQSFDKDQIDVeaakaqVREELESPCAEEMAALEKFVSYFDVDGYDVVVFDTAPTGHTLRLLELPsdw 485

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 463 ------GAYHREMVRQMGQTHDHVMTPMmqlQDPEKTKVIIVTLAETTPVLEAANLQQDLR-RAGIEPWAWVVNNSLAAA 535
Cdd:NF041417 486 kgfmdlGSLTKEASDVTGDKYDRVIETM---RDPERSTFVFVMYPEYTPMMEAWRAAEDLRnQVGIETSLVAVNYLLPEE 562

                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*...
gi 496059301 536 EPSSPFLKTRASRELPLISDVGEQYAKRIALTALQSQEPVGINLLEEM 583
Cdd:NF041417 563 YGNNAFFESRRKQQQKYLEEIRDRFDVPMLLAPLQRDEPTGIEELRRF 610
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
8-296 1.09e-103

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 314.84  E-value: 1.09e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301   8 DIPPFIFFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPASNVGQVFSQTIGHRITDIStVENLAAMEVDPMAAAQAY 87
Cdd:COG0003    1 DMTRIIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGTELGNEPTEVA-VPNLYALEIDPEAELEEY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  88 RDRVLDPVRGLMPTEVVSSIEEqlSGSCTTEIAAFDEFTGLLTNhelrEKYDHIVFDTAPTGHTIRMLELP---GAWSGY 164
Cdd:COG0003   80 WERVRAPLRGLLPSAGVDELAE--SLPGTEELAALDELLELLEE----GEYDVIVVDTAPTGHTLRLLSLPellGWWLDR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 165 LEANPDAAANLGPLV-------------GLEKQQHQYSDAVKALSDAALTRLVLVARAQTSTLKEVSHTHDELYAIGLQH 231
Cdd:COG0003  154 LLKLRRKASGLGRPLagilglpddpvleGLEELRERLERLRELLRDPERTSFRLVTNPERLAIAETRRALEELALYGIPV 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059301 232 QHLAINGVLPPFAGEnDPLAQSILAREEKALQAMPENLANLPRSQLYLKPFNLVGLEALRQLFTE 296
Cdd:COG0003  234 DGLVVNRVLPEEADD-DAFLAARRERQQEYLAEIEEAFAPLPVVEVPLLAEEVVGLEALRALAEE 297
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 12-293 2.11e-85

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: 265.91  E-value: 2.11e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  12 FIFFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPASNVGQVFSQTIGHRiTDISTVENLAAMEVDPMAAAQAYRDRV 91
Cdd:cd02035    2 IIFFGGKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGQKLGGE-TPVKGAPNLWAMEIDPEEALEEYWEEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  92 LDPVRGL--MPTEVVSSIEEQLSGSCTTEIAAFDEFTGLLTNhelrEKYDHIVFDTAPTGHTIRMLELPgawsgyleanp 169
Cdd:cd02035   81 KELLAQYlrLPGLDEVYAEELLSLPGMDEAAAFDELREYVES----GEYDVIVFDTAPTGHTLRLLSLP----------- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 170 daaanlgplvglekqqhqYSDAVKALSDAALTRLVLVARAQTSTLKEVSHTHDELYAIGLQHQHLAINGVLPPfaGENDP 249
Cdd:cd02035  146 ------------------LEQVRELLRDPERTTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVNQVLPE--EADDS 205

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 496059301 250 LAQSILAREEKALQAMPENLANLPRSQLYLKPFNLVGLEALRQL 293
Cdd:cd02035  206 FFLRRRRQQQKYLDEIEELFEPLPVVEVPLLPEEVRGLEALRAL 249
GET3_arsA_TRC40 TIGR00345
transport-energizing ATPase, TRC40/GET3/ArsA family; Members of this family are ATPases that ...
 27-293 4.51e-81

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: 256.25  E-value: 4.51e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301   27 ACATAVWLADQGKRTLLVSTDPASNVGQVFSQTIGHRITDISTVENLAAMEVDPMAAAQAYRDRVLDPVRGLMPTEvvSS 106
Cdd:TIGR00345   2 SAATAIRLAEQGKKVLLVSTDPAHSLSDVFEQEIGHTPTKVTGVENLSAVEIDPQAALEEYRAKLVEQIKGNLPDG--DM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  107 IEEQLSGSCTT----EIAAFDEFTGLLTNHELreKYDHIVFDTAPTGHTIRMLELPGAWSGYLEANPDAAANLGPLVG-- 180
Cdd:TIGR00345  80 LGDQLEGAALSpgidEIAAFDEFLKHMTDAEN--EFDVVIFDTAPTGHTLRLLQLPEVLSSFLEKFIKIRSKLGPMAKlf 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  181 ------------LEKQQHQYSDAVKALSDAALTRLVLVARAQTSTLKEVSHTHDELYAIGLQHQHLAINGVLPpfagEN- 247
Cdd:TIGR00345 158 mgageddealekLEELKEQIEAAREILSDPERTSFVLVVIPEKMSLYESERAHKELAKYGIKVDAVIVNQVLP----ENa 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 496059301  248 -DPLAQSILAREEKALQAMPENLANLPRSQLYLKPFNLVGLEALRQL 293
Cdd:TIGR00345 234 qDEFCQARWELQQKYLKQIPEKFADLPVAEVPLQKEEMVGLEALKRL 280
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 330-584 3.68e-72

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: 231.63  E-value: 3.68e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 330 LVMTMGKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTLDGSL---------PNLQVSRIDPKVETERYRRFVL 400
Cdd:cd02035    2 IIFFGGKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGQKLggetpvkgaPNLWAMEIDPEEALEEYWEEVK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 401 EN--QGKGLDAEGLAVLEEDLRSPCTEEIAVFQAFSRIIKEADDHFVIMDTAPTGHTLLLLDATgayhremVRQMgqthd 478
Cdd:cd02035   82 ELlaQYLRLPGLDEVYAEELLSLPGMDEAAAFDELREYVESGEYDVIVFDTAPTGHTLRLLSLP-------LEQV----- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 479 hvmtpMMQLQDPEKTKVIIVTLAETTPVLEAANLQQDLRRAGIEPWAWVVNNSLAAAEPSSPFLKTRASRELPLISDVGE 558
Cdd:cd02035  150 -----RELLRDPERTTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVNQVLPEEADDSFFLRRRRQQQKYLDEIEEL 224

                        250       260
                 ....*....|....*....|....*.
gi 496059301 559 QYAKRIALTALQSQEPVGINLLEEMA 584
Cdd:cd02035  225 FEPLPVVEVPLLPEEVRGLEALRALA 250
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 12-293 1.35e-59

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: 200.65  E-value: 1.35e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301   12 FIFFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPASNVGQVFSQTIGHRITDIStvENLAAMEVDPMAAAQAYRDRV 91
Cdd:pfam02374   3 WIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQKFGHEPTKVK--ENLSAMEIDPNMELEEYWQEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301   92 LDPVRGLMPTEVVSSIEEQLSGS--CTTEIAAFDEFTGLLTNHElrekYDHIVFDTAPTGHTIRMLELPGAWSGYLEANP 169
Cdd:pfam02374  81 QKYMNALLGLRMLEGILAEELASlpGIDEAASFDEFKKYMDEGE----YDVVVFDTAPTGHTLRLLSLPTVLGWYLEKIV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  170 DAAANLGPLVG----------------LEKQQHQYSDAVKALSDAALTRLVLVARAQTSTLKEVSHTHDELYAIGLQHQH 233
Cdd:pfam02374 157 KLKNQIGPLAKpflgmggvsipealesLEETKERIERAREILTDPERTSFRLVCIPEKMSLYETERAIQYLAKYGIDVDA 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  234 LAINGVLPPFAGENDPLAQSILAREEKALQAMPENLANLPRSQLYLKPFNLVGLEALRQL 293
Cdd:pfam02374 237 VIVNQVLPENVQENCPFCEARKKIQQKYLDEIEELFSDFPVAKLPLLPEEVVGLEKLEKF 296
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
330-585 3.41e-50

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 175.39  E-value: 3.41e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 330 LVMTMGKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTLDGSL---------PNLQVSRIDPKVETERYRRFVL 400
Cdd:COG0003    5 IIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGTELgneptevavPNLYALEIDPEAELEEYWERVR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 401 ENQGKGLDAEGLAVLEEDLrsPCTEEIAVFQAFSRIIKEADDHFVIMDTAPTGHTLLLLDA---TGAY----------HR 467
Cdd:COG0003   85 APLRGLLPSAGVDELAESL--PGTEELAALDELLELLEEGEYDVIVVDTAPTGHTLRLLSLpelLGWWldrllklrrkAS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 468 EMVRQMGQTHDHVMTPMMQ---------------LQDPEKTKVIIVTLAETTPVLEAANLQQDLRRAGIEPWAWVVNNSL 532
Cdd:COG0003  163 GLGRPLAGILGLPDDPVLEgleelrerlerlrelLRDPERTSFRLVTNPERLAIAETRRALEELALYGIPVDGLVVNRVL 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 496059301 533 AAAEPSSPFLKTRASRELPLISDVGEQYAKR-IALTALQSQEPVGINLLEEMAK 585
Cdd:COG0003  243 PEEADDDAFLAARRERQQEYLAEIEEAFAPLpVVEVPLLAEEVVGLEALRALAE 296
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 335-585 2.21e-42

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: 154.43  E-value: 2.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  335 GKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTLD---GSLP-----NLQVSRIDPKVETERYRRFVLENQGKG 406
Cdd:pfam02374   8 GKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNqkfGHEPtkvkeNLSAMEIDPNMELEEYWQEVQKYMNAL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  407 LDAEGL-AVLEEDLRS-PCTEEIAVFQAFSRIIKEADDHFVIMDTAPTGHTLLLL------------------------- 459
Cdd:pfam02374  88 LGLRMLeGILAEELASlPGIDEAASFDEFKKYMDEGEYDVVVFDTAPTGHTLRLLslptvlgwylekivklknqigplak 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  460 ---DATGAYHREMVRQMGQTHDHVMTPMMQLQDPEKTKVIIVTLAETTPVLEAANLQQDLRRAGIEPWAWVVNNSLAAAE 536
Cdd:pfam02374 168 pflGMGGVSIPEALESLEETKERIERAREILTDPERTSFRLVCIPEKMSLYETERAIQYLAKYGIDVDAVIVNQVLPENV 247

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 496059301  537 PSS-PFLKTRASRELPLISDVGEQYA-KRIALTALQSQEPVGINLLEEMAK 585
Cdd:pfam02374 248 QENcPFCEARKKIQQKYLDEIEELFSdFPVAKLPLLPEEVVGLEKLEKFSK 298
GET3_arsA_TRC40 TIGR00345
transport-energizing ATPase, TRC40/GET3/ArsA family; Members of this family are ATPases that ...
 344-585 2.89e-30

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: 120.27  E-value: 2.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  344 VAASVAVSLAKRGHKVHLTTSDPAAHLSYTLD----------GSLPNLQVSRIDPKVETERYR----RFVLENQGKGLDA 409
Cdd:TIGR00345   1 ISAATAIRLAEQGKKVLLVSTDPAHSLSDVFEqeightptkvTGVENLSAVEIDPQAALEEYRaklvEQIKGNLPDGDML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  410 EGLavLEEDLRSPCTEEIAVFQAFSRIIKEADDHF--VIMDTAPTGHTLLLL---DATGAYHREMV---RQMG------- 474
Cdd:TIGR00345  81 GDQ--LEGAALSPGIDEIAAFDEFLKHMTDAENEFdvVIFDTAPTGHTLRLLqlpEVLSSFLEKFIkirSKLGpmaklfm 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  475 --QTHDHVMTPM-----------MQLQDPEKTKVIIVTLAETTPVLEAANLQQDLRRAGIEPWAWVVNNSLaAAEPSSPF 541
Cdd:TIGR00345 159 gaGEDDEALEKLeelkeqieaarEILSDPERTSFVLVVIPEKMSLYESERAHKELAKYGIKVDAVIVNQVL-PENAQDEF 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 496059301  542 LKTRASRELPLISDVGEQYA-KRIALTALQSQEPVGINLLEEMAK 585
Cdd:TIGR00345 238 CQARWELQQKYLKQIPEKFAdLPVAEVPLQKEEMVGLEALKRLSK 282
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 336-452 3.01e-11

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: 64.11  E-value: 3.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 336 KGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTLDGSLPNLQVSRIDPKVETERYRRFVLENQGKGLD----AEG 411
Cdd:COG1192   10 KGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIPGLDlipaNID 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 496059301 412 LAVLEEDLRSpcteEIAVFQAFSRIIKEADDHF--VIMDTAPT 452
Cdd:COG1192   90 LAGAEIELVS----RPGRELRLKRALAPLADDYdyILIDCPPS 128
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 14-148 5.81e-10

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: 60.26  E-value: 5.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  14 FFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPASNVgqvfsqTIGHRITDISTVENLAAMEVDPMAAAQAYRDRVLD 93
Cdd:COG1192    6 VANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNL------TSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEIP 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496059301  94 PVRgLMPtevvSSIEeqLSGsCTTEIAAFDEFTGLLTN--HELREKYDHIVFDTAPT 148
Cdd:COG1192   80 GLD-LIP----ANID--LAG-AEIELVSRPGRELRLKRalAPLADDYDYILIDCPPS 128
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 335-464 1.00e-09

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: 58.90  E-value: 1.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  335 GKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSyTLDGSLPNLQVS------------RIDPKVETERYRRFVLEN 402
Cdd:pfam01656   6 TKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNS-SVEGLEGDIAPAlqalaeglkgrvNLDPILLKEKSDEGGLDL 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059301  403 QGKGLDAEGLAVLEEDLRspctEEIAVFQAFSRIIKEADdhFVIMDTAPtGHTLLLLDATGA 464
Cdd:pfam01656  85 IPGNIDLEKFEKELLGPR----KEERLREALEALKEDYD--YVIIDGAP-GLGELLRNALIA 139
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 12-147 1.60e-09

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: 58.51  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301   12 FIFFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPASNVgqvfSQTIGHRITDISTVENLAA-----MEVDPMAAAQA 86
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNN----SSVEGLEGDIAPALQALAEglkgrVNLDPILLKEK 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059301   87 YRDRVLDpvrglmptEVVSSIEEQLSGSCTTEIAAFDEFTGLLtnHELREKYDHIVFDTAP 147
Cdd:pfam01656  77 SDEGGLD--------LIPGNIDLEKFEKELLGPRKEERLREAL--EALKEDYDYVIIDGAP 127
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 327-359 2.55e-09

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 58.14  E-value: 2.55e-09
                         10        20        30
                 ....*....|....*....|....*....|...
gi 496059301 327 GKGLVMTMGKGGVGKTTVAASVAVSLAKRGHKV 359
Cdd:COG2894    2 GKVIVVTSGKGGVGKTTTTANLGTALALLGKKV 34
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 14-56 2.99e-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: 55.24  E-value: 2.99e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 496059301  14 FFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPASNVGQVF 56
Cdd:cd02042    5 VANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL 47
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 336-452 1.01e-08

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: 54.90  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  336 KGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTLDGSLPNLQVSRIDPKVETERYRRFVLENQGKGLD----AEG 411
Cdd:pfam13614  10 KGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIENLDlipsNID 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 496059301  412 LAVLEEDLRSPCTEEIAVFQAFSRIIKEADdhFVIMDTAPT 452
Cdd:pfam13614  90 LAGAEIELIGIENRENILKEALEPVKDNYD--YIIIDCPPS 128
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 330-359 3.83e-08

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: 54.52  E-value: 3.83e-08
                         10        20        30
                 ....*....|....*....|....*....|
gi 496059301 330 LVMTMGKGGVGKTTVAASVAVSLAKRGHKV 359
Cdd:cd02036    3 IVITSGKGGVGKTTTTANLGVALAKLGKKV 32
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 18-148 8.48e-08

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: 52.20  E-value: 8.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301   18 KGGVGKTSLACATAVWLADQGKRTLLVSTDPASNVgqvfsqTIGHRITDISTVENLAAMEVDPMAAAQAYRDRVLDPVRg 97
Cdd:pfam13614  10 KGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNA------TSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVIENLD- 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 496059301   98 LMPtevvSSIEeqLSGsctteiaAFDEFTGLLTNH--------ELREKYDHIVFDTAPT 148
Cdd:pfam13614  83 LIP----SNID--LAG-------AEIELIGIENREnilkealePVKDNYDYIIIDCPPS 128
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 330-359 1.29e-07

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: 52.84  E-value: 1.29e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 496059301  330 LVMTmGKGGVGKTTVAASVAVSLAKRGHKV 359
Cdd:pfam10609   7 AVAS-GKGGVGKSTVAVNLALALARLGYKV 35
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 13-55 1.53e-07

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 52.86  E-value: 1.53e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 496059301  13 IFFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPASNVGQV 55
Cdd:COG3640    3 IAVAGKGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEA 45
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 336-371 3.48e-07

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: 49.46  E-value: 3.48e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 496059301 336 KGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLS 371
Cdd:cd02042    9 KGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLT 44
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 327-365 4.89e-07

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: 51.57  E-value: 4.89e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 496059301  327 GKGLVMTMGKGGVGKTTVAASVAVSLAKRGHKVHLTTSD 365
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD 39
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 335-374 6.65e-07

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 50.94  E-value: 6.65e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 496059301 335 GKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTL 374
Cdd:COG3640    7 GKGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEAL 46
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 330-359 1.17e-06

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: 49.42  E-value: 1.17e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 496059301 330 LVMTmGKGGVGKTTVAASVAVSLAKRGHKV 359
Cdd:cd02037    4 AVLS-GKGGVGKSTVAVNLALALAKKGYKV 32
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 13-47 1.57e-06

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: 47.04  E-value: 1.57e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 496059301  13 IFFTG-KGGVGKTSLACATAVWLADQGKRTLLVSTD 47
Cdd:cd01983    3 IAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
ParA_partition NF041546
ParA family partition ATPase;
336-366 1.67e-06

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 49.09  E-value: 1.67e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 496059301 336 KGGVGKTTVAASVAVSLAKRGHKVHLTTSDP 366
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADP 38
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 12-56 4.10e-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: 48.46  E-value: 4.10e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 496059301  12 FIFFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPASNVGQVF 56
Cdd:cd02034    2 KIAVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETL 46
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 330-529 1.03e-05

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: 47.49  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 330 LVMTMGKGGVGKTTVAASVAVSLAKRGHKVHL---TTSDPAAHLSYTLDGS--LPNLQVSRIDpkveteryrrfvLENQG 404
Cdd:COG0489   95 IAVTSGKGGEGKSTVAANLALALAQSGKRVLLidaDLRGPSLHRMLGLENRpgLSDVLAGEAS------------LEDVI 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 405 KGLDAEGLAVLEEDLRSPCTEEIAVFQAFSRIIKEADDHF--VIMDTAP-TGHTllllDATgayhremvrqmgqthdhVM 481
Cdd:COG0489  163 QPTEVEGLDVLPAGPLPPNPSELLASKRLKQLLEELRGRYdyVIIDTPPgLGVA----DAT-----------------LL 221

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 496059301 482 TPMMqlqdpekTKVIIVTLAETTPVLEAANLQQDLRRAGIEPWAWVVN 529
Cdd:COG0489  222 ASLV-------DGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLN 262
PHA02518 PHA02518
ParA-like protein; Provisional
 18-48 1.36e-05

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 46.38  E-value: 1.36e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 496059301  18 KGGVGKTSLACATAVWLADQGKRTLLVSTDP 48
Cdd:PHA02518   9 KGGAGKTTVATNLASWLHADGHKVLLVDLDP 39
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 14-157 1.50e-05

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: 47.42  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  14 FFTGKGGVGKTSLACATAVWLADQ-GKRTLLVSTD-PASNVGQVFSQTIGHRITDIstVENLAAMevDPMAAAQA---YR 88
Cdd:COG4963  107 VVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDlQFGDVALYLDLEPRRGLADA--LRNPDRL--DETLLDRAltrHS 182

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059301  89 DR--VLDPVRGLMPTEVVSSieeqlsgsctteiaafDEFTGLLtnHELREKYDHIVFDTAP--TGHTIRMLEL 157
Cdd:COG4963  183 SGlsVLAAPADLERAEEVSP----------------EAVERLL--DLLRRHFDYVVVDLPRglNPWTLAALEA 237
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 13-241 1.51e-05

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: 47.10  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  13 IFFT-GKGGVGKTSLACATAVWLADQGKRTLLVSTDpasnvgqVFSQTIgHRITDISTVENLAAMEVDPMAAAQAYRDRV 91
Cdd:COG0489   95 IAVTsGKGGEGKSTVAANLALALAQSGKRVLLIDAD-------LRGPSL-HRMLGLENRPGLSDVLAGEASLEDVIQPTE 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  92 LDPVR----GLMPTEvvssieeqlsgscTTEIAAFDEFTGLLTnhELREKYDHIVFDTAPtghtirmlelpgawsgyLEA 167
Cdd:COG0489  167 VEGLDvlpaGPLPPN-------------PSELLASKRLKQLLE--ELRGRYDYVIIDTPP-----------------GLG 214

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059301 168 NPDAAAnLGPLVglekqqhqysDAVkalsdaaltrlVLVARAQTSTLKEVSHTHDELYAIGLQHQHLAINGVLP 241
Cdd:COG0489  215 VADATL-LASLV----------DGV-----------LLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNMVCP 266
chlL CHL00072
photochlorophyllide reductase subunit L
 335-378 1.66e-05

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 47.04  E-value: 1.66e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 496059301 335 GKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTLDGSL 378
Cdd:CHL00072   7 GKGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTLTGFL 50
minD CHL00175
septum-site determining protein; Validated
 330-365 2.09e-05

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 46.69  E-value: 2.09e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 496059301 330 LVMTMGKGGVGKTTVAASVAVSLAKRGHKVHLTTSD 365
Cdd:CHL00175  18 IVITSGKGGVGKTTTTANLGMSIARLGYRVALIDAD 53
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 333-451 2.44e-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: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 333 TMGKGGVGKTTVAASVAVSLAKRGHKVHLTTSD-------------PAAHLSYTLDGSLPNLQVSridpkVETERYRRFV 399
Cdd:cd02038    6 TSGKGGVGKTNVSANLALALSKLGKRVLLLDADlglanldillglaPKKTLGDVLKGRVSLEDII-----VEGPEGLDII 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496059301 400 LENQGkgldAEGLAVLEEDLRSpcteeiAVFQAFSRIIKEADdhFVIMDTAP 451
Cdd:cd02038   81 PGGSG----MEELANLDPEQKA------KLIEELSSLESNYD--YLLIDTGA 120
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 330-374 2.98e-05

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: 45.88  E-value: 2.98e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 496059301  330 LVMTMGKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPA-AHLSYTL 374
Cdd:TIGR01969   3 ITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITmANLELIL 48
ParA_partition NF041546
ParA family partition ATPase;
18-48 3.26e-05

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 45.24  E-value: 3.26e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 496059301  18 KGGVGKTSLACATAVWLADQGKRTLLVSTDP 48
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADP 38
PHA02518 PHA02518
ParA-like protein; Provisional
 336-366 6.65e-05

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 44.46  E-value: 6.65e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 496059301 336 KGGVGKTTVAASVAVSLAKRGHKVHLTTSDP 366
Cdd:PHA02518   9 KGGAGKTTVATNLASWLHADGHKVLLVDLDP 39
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 335-374 7.53e-05

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: 44.61  E-value: 7.53e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 496059301 335 GKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTL 374
Cdd:cd02034    7 GKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETL 46
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 335-397 7.91e-05

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: 44.66  E-value: 7.91e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059301 335 GKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTLDGSL-PNLQVSRIDPKVETERYRR 397
Cdd:cd02117    7 GKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGKvPPTIDEMLTEDGTAEELRR 70
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 330-365 8.21e-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: 42.03  E-value: 8.21e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 496059301 330 LVMTMGKGGVGKTTVAASVAVSLAKRGHKVHLTTSD 365
Cdd:cd01983    3 IAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 335-378 8.48e-05

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: 44.60  E-value: 8.48e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 496059301 335 GKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTLDGSL 378
Cdd:cd02032    7 GKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPKHDSTFTLTGFL 50
PRK10818 PRK10818
septum site-determining protein MinD;
330-358 1.52e-04

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 43.77  E-value: 1.52e-04
                         10        20
                 ....*....|....*....|....*....
gi 496059301 330 LVMTMGKGGVGKTTVAASVAVSLAKRGHK 358
Cdd:PRK10818   5 IVVTSGKGGVGKTTSSAAIATGLAQKGKK 33
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 335-378 2.85e-04

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 43.03  E-value: 2.85e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 496059301 335 GKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTLDGSL 378
Cdd:PRK13185   9 GKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPKHDSTFTLTGKL 52
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 17-147 4.46e-04

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: 42.17  E-value: 4.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  17 GKGGVGKTSLACATAVWLADQGKRTLLVSTD-PASNV----GQVFSQTIGHRITDISTVEnlaamevdpmaaaqayrdrv 91
Cdd:cd02038    8 GKGGVGKTNVSANLALALSKLGKRVLLLDADlGLANLdillGLAPKKTLGDVLKGRVSLE-------------------- 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059301  92 ldpvrglmptEVVSSIEEQLS----GSCTTEIAAFDE--FTGLLTN-HELREKYDHIVFDTAP 147
Cdd:cd02038   68 ----------DIIVEGPEGLDiipgGSGMEELANLDPeqKAKLIEElSSLESNYDYLLIDTGA 120
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 17-47 4.68e-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: 42.19  E-value: 4.68e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 496059301  17 GKGGVGKTSLACATAVWLADQGKRTLLVSTD 47
Cdd:cd02036    8 GKGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 262-384 4.74e-04

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 42.74  E-value: 4.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 262 LQAMPENLANlPRSQLYLKPFNlvGLEALRQL----FTENKASL----PLPATTLNTLDLPKLSSLVD---ELSQTGKG- 329
Cdd:PRK13869  30 LQAMSEALFP-PTSHKSLRKFT--SGEAARLMkisdSTLRKMTLagegPQPELASNGRRFYTLGQINEirqMLAGSTRGr 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059301 330 -----------------LVMTMGKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTLdGSLPNLQVS 384
Cdd:PRK13869 107 esidfvphrrgsehlqvIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALL-GVLPETDVG 177
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 261-383 5.29e-04

plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 274585 [Multi-domain]  Cd Length: 387  Bit Score: 42.66  E-value: 5.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  261 ALQAMPENLANlPRSQLYLKPFN------LVGLEA--LRQLFTENKAslPLPATTLN-----TL-DLPKLSSLVDELSQT 326
Cdd:TIGR03453  14 QLQALRERLFP-PNARKTLRKFTsgevakLLGVSDsyLRQLSLEGKG--PEPETLSNgrrsyTLeQINELRRHLAQRGRE 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  327 GKGLV-------------MTMGKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSyTLDGSLPNLQV 383
Cdd:TIGR03453  91 ARRYLphrrggehlqviaVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLS-ALFGYQPEFDV 159
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 13-70 7.85e-04

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 41.68  E-value: 7.85e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 496059301  13 IFFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPASNVgqvfSQTIGHRitDISTV 70
Cdd:PRK13230   4 FCFYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADC----TRNLVGE--KIPTV 55
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 13-48 8.14e-04

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: 41.34  E-value: 8.14e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 496059301  13 IFFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDP 48
Cdd:cd02040    3 IAIYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDP 38
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 25-275 1.08e-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: 41.03  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301  25 SLACATAVWLADQGKRTLLVSTDP-ASNVGQVFSQTIGHritdisTVENLAAMEVDPMAAAQAYRDRVldpvrglmptEV 103
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLgLANLDVLLGLEPKA------TLADVLAGEADLEDAIVQGPGGL----------DV 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 104 VSsieeqlSGSCTTEIAAFDEFTGLLTNH-ELREKYDHIVFDTAPtghtirmlelpgawsgyleanpdaaanlgplvGLe 182
Cdd:COG0455   65 LP------GGSGPAELAELDPEERLIRVLeELERFYDVVLVDTGA--------------------------------GI- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 183 kqqhqySDAVKALSDAAlTRLVLVARAQTSTLKEVSHTHDELY-AIGLQHQHLAINGVLPPFAGENdpLAQSILAREEKA 261
Cdd:COG0455  106 ------SDSVLLFLAAA-DEVVVVTTPEPTSITDAYALLKLLRrRLGVRRAGVVVNRVRSEAEARD--VFERLEQVAERF 176

                        250
                 ....*....|....
gi 496059301 262 LQAMPENLANLPRS 275
Cdd:COG0455  177 LGVRLRVLGVIPED 190
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
13-51 1.08e-03

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 41.28  E-value: 1.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 496059301   13 IFFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPASN 51
Cdd:pfam00142   3 IAIYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKAD 41
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 17-47 1.21e-03

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 40.81  E-value: 1.21e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 496059301  17 GKGGVGKT----SLACAtavwLADQGKRTLLVSTD 47
Cdd:COG2894   10 GKGGVGKTtttaNLGTA----LALLGKKVVLIDAD 40
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 335-376 1.73e-03

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 40.52  E-value: 1.73e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 496059301 335 GKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTLDG 376
Cdd:PRK13230   8 GKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVG 49
PRK13768 PRK13768
GTPase; Provisional
 12-50 1.97e-03

GTPase; Provisional


Pssm-ID: 237498 [Multi-domain]  Cd Length: 253  Bit Score: 40.24  E-value: 1.97e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 496059301  12 FIFFTGKGGVGKTSLACATAVWLADQGKRTLLVSTDPAS 50
Cdd:PRK13768   4 IVFFLGTAGSGKTTLTKALSDWLEEQGYDVAIVNLDPAV 42
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 17-47 2.01e-03

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: 40.13  E-value: 2.01e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 496059301   17 GKGGVGKTSLACATAVWLADQGKRTLLVSTD 47
Cdd:pfam10609  11 GKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 335-379 2.14e-03

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: 40.19  E-value: 2.14e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 496059301 335 GKGGVGKTTVAASVAVSLAKRGHKVHLTTSDPAAHLSYTLDGSLP 379
Cdd:cd02040    7 GKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKADSTRLLLGGKA 51
PRK14974 PRK14974
signal recognition particle-docking protein FtsY;
308-365 4.02e-03

signal recognition particle-docking protein FtsY;


Pssm-ID: 237875 [Multi-domain]  Cd Length: 336  Bit Score: 39.57  E-value: 4.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 496059301 308 LNTLDLPKLSSLVDELSQTGKGLV-MTMGKGGVGKTTVAASVAVSLAKRGHKVHLTTSD 365
Cdd:PRK14974 119 LEVLSVGDLFDLIEEIKSKGKPVViVFVGVNGTGKTTTIAKLAYYLKKNGFSVVIAAGD 177
chlL CHL00072
photochlorophyllide reductase subunit L
 17-48 4.29e-03

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 39.33  E-value: 4.29e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 496059301  17 GKGGVGKTSLACATAVWLADQGKRTLLVSTDP 48
Cdd:CHL00072   7 GKGGIGKSTTSCNISIALARRGKKVLQIGCDP 38
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 18-48 4.39e-03

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 39.61  E-value: 4.39e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 496059301  18 KGGVGKTSLACATAVWLADQGKRTLLV-STDP 48
Cdd:PHA02519 115 KGGVYKTSSAVHTAQWLALQGHRVLLIeGNDP 146
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
 330-366 4.65e-03

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: 38.09  E-value: 4.65e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 496059301 330 LVMtMGKGGVGKTTVAASVAVSLAKRGHKVHLTTSDP 366
Cdd:cd05386    4 FVL-QGKGGVGKSVIASLLAQYLIDKGQPVSCIDTDP 39
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
298-363 4.85e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 38.99  E-value: 4.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059301 298 KASLPLPATtLNTLD---LPKLS-SLVDELSQT-----GKGLVMTmGKGGVGKTTVAASVAVSLAKRGHKVHLTT 363
Cdd:COG1484   62 AARFPAAKT-LEDFDfdaQPGLDrRQILELATLdfierGENLILL-GPPGTGKTHLAIALGHEACRAGYRVRFTT 134
SRP_G cd18539
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ...
 331-368 6.35e-03

GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349786  Cd Length: 193  Bit Score: 38.35  E-value: 6.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 496059301 331 VMTMGKGGVGKTTVAASVAVSLAKRGHKVHLTTSD---PAA 368
Cdd:cd18539    3 ILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADvyrPAA 43
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 229-461 6.79e-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: 38.94  E-value: 6.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 229 LQHQHLAINGVLPPFAGENDPLAQSILAREEKALQAMPENLANLPRSQLYLKPFNLVGLEALRQLFTENKASLPLPATTL 308
Cdd:COG4963    2 LVALRPLPRISIQAFCESAALAALIEAAAEDRRLALAAVAVASGGAAAAAAAYLSAPTPNLILLEALSESAALLADVLPL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 309 NTLDLPKLSSLVDELSQTGKGLVMTM--GKGGVGKTTVAASVAVSLAKR-GHKV-----HLTTSDPAAHL----SYTLDG 376
Cdd:COG4963   82 SPDELRAALARLLDPGAARRGRVIAVvgAKGGVGATTLAVNLAWALAREsGRRVllvdlDLQFGDVALYLdlepRRGLAD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059301 377 SLPNLqvSRIDPkvetERYRRFVLEnqgkglDAEGLAVL--EEDLRSPctEEIAVfQAFSRIIKEADDHF--VIMDTAP- 451
Cdd:COG4963  162 ALRNP--DRLDE----TLLDRALTR------HSSGLSVLaaPADLERA--EEVSP-EAVERLLDLLRRHFdyVVVDLPRg 226

                        250
                 ....*....|.
gi 496059301 452 -TGHTLLLLDA 461
Cdd:COG4963  227 lNPWTLAALEA 237
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 336-366 7.04e-03

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: 38.48  E-value: 7.04e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 496059301  336 KGGVGKTTVAASVAVSLAKRGHKVHLTTSDP 366
Cdd:TIGR03371  10 RGGVGKTTLTANLASALKLLGEPVLAIDLDP 40
 
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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