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Conserved domains on  [gi|553308510|ref|WP_023053584|]
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arsenical pump-driving ATPase [Megasphaera vaginalis (ex Srinivasan et al. 2021)]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
arsen_driv_ArsA super family cl37414
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 11-566 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).


The actual alignment was detected with superfamily member TIGR04291:

Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 792.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510   11 LTKYLFFTGKGGVGKTSAACATAVVLADEGKKVLLISTDPASNLQDVFETELDGKAKPIKGVDNLEVINLDPLEAAHNYK 90
Cdd:TIGR04291   2 LPPYLFFTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNVGQVFGQTIGNKITAIAGVPGLFALEIDPQAAAQAYR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510   91 ESVVAPFRGKLPDSVIENMEEQLSGSCTVEIAAFNEFSNFITNPKLNTEYDNIIFDTAPTGHTLRMLQLPSAWTGFISES 170
Cdd:TIGR04291  82 ARIVDPVRGVLPDDVVSSIEEQLSGACTTEIAAFDEFTGLLTDAELTQDFDHIIFDTAPTGHTIRLLQLPGAWSDFLDTN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  171 THGASCLGQLSGLEAKKEIYKQAVQNLSDESVTTLVLVTRPDKTPLNEVARASKELSEIGIKNQILVINGLL---EHYDD 247
Cdd:TIGR04291 162 PNGASCLGPLAGLEKQRAQYAKAVEALSDPERTRLILVARPQKSTLLEVARTHQELAAIGLKNQYLVINGVLpetEASDD 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  248 DLSESIFNKQKLALENMPDMLTEFDTYTIALRSYNITGIDAIRNLLKKDQISE---QKVEVKGKLFNLDDVVSDLVKNNR 324
Cdd:TIGR04291 242 PLAQAIYKREQKALQHMPAILANLPRYTLPLKPYNLVGLEALRQLLNDDQPQLsldITTPQVPDLPSLSRLIDEIAKSEK 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLSTTDPADHIKFMIDSS-SGISMSHIDEKEELKKYQDEVLENARKTMS 403
Cdd:TIGR04291 322 GLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSlNNLQVSRIDPKQETERYRQEVLATKGKELD 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  404 EDDVAYIEEDLRSPCTQEIAVFRAFAELVEKADDEIVVIDTAPTGHTLLLLDSTLSYHKEVQRTQGQIPESVKNLLPRLR 483
Cdd:TIGR04291 402 EDGKAYLEEDLRSPCTEEIAVFQAFSRIIREAGDRFVVMDTAPTGHTLLLLDATGAYHREVERKMGDTPEHVTTPMMQLQ 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  484 G-EETEVLIVSLAEATPFYEAYRLEEDLKRASIHTNWWIVNSSLYKANPSNKLLSAKANEEVKWINKILDHTSGKLAVIE 562
Cdd:TIGR04291 482 DpERTKVLLVTLPETTPVLEAARLQEDLRRAGIEPWWWVINNSLAATNTTSPLLSQRAQNELKWIEKVKRIHADRYAVIP 561


                  ....
gi 553308510  563 WTKE 566
Cdd:TIGR04291 562 LQAE 565
 
Name Accession Description Interval E-value
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 11-566 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: 792.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510   11 LTKYLFFTGKGGVGKTSAACATAVVLADEGKKVLLISTDPASNLQDVFETELDGKAKPIKGVDNLEVINLDPLEAAHNYK 90
Cdd:TIGR04291   2 LPPYLFFTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNVGQVFGQTIGNKITAIAGVPGLFALEIDPQAAAQAYR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510   91 ESVVAPFRGKLPDSVIENMEEQLSGSCTVEIAAFNEFSNFITNPKLNTEYDNIIFDTAPTGHTLRMLQLPSAWTGFISES 170
Cdd:TIGR04291  82 ARIVDPVRGVLPDDVVSSIEEQLSGACTTEIAAFDEFTGLLTDAELTQDFDHIIFDTAPTGHTIRLLQLPGAWSDFLDTN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  171 THGASCLGQLSGLEAKKEIYKQAVQNLSDESVTTLVLVTRPDKTPLNEVARASKELSEIGIKNQILVINGLL---EHYDD 247
Cdd:TIGR04291 162 PNGASCLGPLAGLEKQRAQYAKAVEALSDPERTRLILVARPQKSTLLEVARTHQELAAIGLKNQYLVINGVLpetEASDD 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  248 DLSESIFNKQKLALENMPDMLTEFDTYTIALRSYNITGIDAIRNLLKKDQISE---QKVEVKGKLFNLDDVVSDLVKNNR 324
Cdd:TIGR04291 242 PLAQAIYKREQKALQHMPAILANLPRYTLPLKPYNLVGLEALRQLLNDDQPQLsldITTPQVPDLPSLSRLIDEIAKSEK 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLSTTDPADHIKFMIDSS-SGISMSHIDEKEELKKYQDEVLENARKTMS 403
Cdd:TIGR04291 322 GLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSlNNLQVSRIDPKQETERYRQEVLATKGKELD 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  404 EDDVAYIEEDLRSPCTQEIAVFRAFAELVEKADDEIVVIDTAPTGHTLLLLDSTLSYHKEVQRTQGQIPESVKNLLPRLR 483
Cdd:TIGR04291 402 EDGKAYLEEDLRSPCTEEIAVFQAFSRIIREAGDRFVVMDTAPTGHTLLLLDATGAYHREVERKMGDTPEHVTTPMMQLQ 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  484 G-EETEVLIVSLAEATPFYEAYRLEEDLKRASIHTNWWIVNSSLYKANPSNKLLSAKANEEVKWINKILDHTSGKLAVIE 562
Cdd:TIGR04291 482 DpERTKVLLVTLPETTPVLEAARLQEDLRRAGIEPWWWVINNSLAATNTTSPLLSQRAQNELKWIEKVKRIHADRYAVIP 561


                  ....
gi 553308510  563 WTKE 566
Cdd:TIGR04291 562 LQAE 565
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
12-295 1.02e-105

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 319.84  E-value: 1.02e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  12 TKYLFFTGKGGVGKTSAACATAVVLADEGKKVLLISTDPASNLQDVFETELDGKAKPIKgVDNLEVINLDPLEAAHNYKE 91
Cdd:COG0003    3 TRIIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGTELGNEPTEVA-VPNLYALEIDPEAELEEYWE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  92 SVVAPFRGKLPDSVIENMEEqlSGSCTVEIAAFNEFSNFITNPklntEYDNIIFDTAPTGHTLRMLQLP---SAWTGFIS 168
Cdd:COG0003   82 RVRAPLRGLLPSAGVDELAE--SLPGTEELAALDELLELLEEG----EYDVIVVDTAPTGHTLRLLSLPellGWWLDRLL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 169 ESTHGASCLGQ-------------LSGLEAKKEIYKQAVQNLSDESVTTLVLVTRPDKTPLNEVARASKELSEIGIKNQI 235
Cdd:COG0003  156 KLRRKASGLGRplagilglpddpvLEGLEELRERLERLRELLRDPERTSFRLVTNPERLAIAETRRALEELALYGIPVDG 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553308510 236 LVINGLLEHYDDDLS--ESIFNKQKLALENMPDMLTEFDTYTIALRSYNITGIDAIRNLLKK 295
Cdd:COG0003  236 LVVNRVLPEEADDDAflAARRERQQEYLAEIEEAFAPLPVVEVPLLAEEVVGLEALRALAEE 297
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 12-552 8.17e-103

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: 323.37  E-value: 8.17e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  12 TKYLFFTGKGGVGKTSAACATAVVLADEGKKVLLISTDPASNLQDVFETELDGKAKPIKGVDNLEVINLDPLEAAHNYKE 91
Cdd:NF041417  12 TEFVFFSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFGQSIGHRVTSIDDVENLSAIEIDPDAAAEEYRQ 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  92 SVVAPFRGKLPDSVIENMEEQLSGSCTVEIAAFNEFSNFITNPklntEYDNIIFDTAPTGHTLRMLQLPSAWTGFISESt 171
Cdd:NF041417  92 RTIEPMRQLLDDEQLKTVEEQLDSPCIEEIAAFDKFVEFMDEP----EYDVVVFDTAPTGHTIRLMELPSGWSEELEKG- 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 172 hGASCLGQLSGLEAKKEIYKQAVQNLSDESVTTLVLVTRPDKTPLNEVARASKELSEIGIKNQILVINGLLEhydDDLSE 251
Cdd:NF041417 167 -GATCIGPAASLQEQKEDYEKAIDTLQDDAQTSFVFVGKPEDASIDEIERSSKELADLGIKTSLLVINGYLP---ESVCE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 252 SIFNKQKLALEN--MPDMLTEFDTYTIA---LRSYNITGIDAIRNL-----------LKKDQISEQKVEVKGKLFNLDDV 315
Cdd:NF041417 243 DPFFEMKREDEQeiLEEVEREFAMQPIAtypLQPGEITGIDLLADVgevlyegkeptVDVAVITEEETEETSPSETDKEA 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 316 VSDLV--KNNRKVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLSTTDPADHIKFMIDSS----------SGISMSHIDE 383
Cdd:NF041417 323 VMELLrpQKDTRYLFFTGKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQDIFGTEvgheptkvgvENLYAARIDQ 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 384 KEELKKYQDEVLENARKTMSEDDV------AYIEEDLRSPCTQEIAVFRAFAELVEKADDEIVVIDTAPTGHTLLLLDST 457
Cdd:NF041417 403 ERALEEYKTRMLDQVEQSFDKDQIdveaakAQVREELESPCAEEMAALEKFVSYFDVDGYDVVVFDTAPTGHTLRLLELP 482

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 458 LSYHKEV---QRTQGQIPES---VKNLLPRLRGEETEVLI-VSLAEATPFYEAYRLEEDLK-RASIHTNWWIVNSSLYKA 529
Cdd:NF041417 483 SDWKGFMdlgSLTKEASDVTgdkYDRVIETMRDPERSTFVfVMYPEYTPMMEAWRAAEDLRnQVGIETSLVAVNYLLPEE 562

                        570       580
                 ....*....|....*....|...
gi 553308510 530 NPSNKLLSAKANEEVKWINKILD 552
Cdd:NF041417 563 YGNNAFFESRRKQQQKYLEEIRD 585
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 13-292 1.11e-93

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: 287.10  E-value: 1.11e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  13 KYLFFTGKGGVGKTSAACATAVVLADEGKKVLLISTDPASNLQDVFETELdGKAKPIKGVDNLEVINLDPLEAAHNYKES 92
Cdd:cd02035    1 RIIFFGGKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGQKL-GGETPVKGAPNLWAMEIDPEEALEEYWEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  93 VVAPFR--GKLPDSVIENMEEQLSGSCTVEIAAFNEFSNFITNPklntEYDNIIFDTAPTGHTLRMLQLPsawtgfises 170
Cdd:cd02035   80 VKELLAqyLRLPGLDEVYAEELLSLPGMDEAAAFDELREYVESG----EYDVIVFDTAPTGHTLRLLSLP---------- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 171 thgasclgqlsgleakkeiYKQAVQNLSDESVTTLVLVTRPDKTPLNEVARASKELSEIGIKNQILVINGLL-EHYDDDL 249
Cdd:cd02035  146 -------------------LEQVRELLRDPERTTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVNQVLpEEADDSF 206

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 553308510 250 SESIFNKQKLALENMPDMLTEFDTYTIALRSYNITGIDAIRNL 292
Cdd:cd02035  207 FLRRRRQQQKYLDEIEELFEPLPVVEVPLLPEEVRGLEALRAL 249
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 12-289 2.87e-60

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: 202.19  E-value: 2.87e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510   12 TKYLFFTGKGGVGKTSAACATAVVLADEGKKVLLISTDPASNLQDVFETELdgKAKPIKGVDNLEVINLDPLEAAHNYKE 91
Cdd:pfam02374   1 MRWIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQKF--GHEPTKVKENLSAMEIDPNMELEEYWQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510   92 SVVAPFRGKL-PDSVIENMEEQL-SGSCTVEIAAFNEFSNFITNPklntEYDNIIFDTAPTGHTLRMLQLPSAWTGFISE 169
Cdd:pfam02374  79 EVQKYMNALLgLRMLEGILAEELaSLPGIDEAASFDEFKKYMDEG----EYDVVVFDTAPTGHTLRLLSLPTVLGWYLEK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  170 ---------------STHGASCLGQ-LSGLEAKKEIYKQAVQNLSDESVTTLVLVTRPDKTPLNEVARASKELSEIGIKN 233
Cdd:pfam02374 155 ivklknqigplakpfLGMGGVSIPEaLESLEETKERIERAREILTDPERTSFRLVCIPEKMSLYETERAIQYLAKYGIDV 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 553308510  234 QILVINGLLEHYDDDLS---ESIFNKQKLALENMPDMLTEFDTYTIALRSYNITGIDAI 289
Cdd:pfam02374 235 DAVIVNQVLPENVQENCpfcEARKKIQQKYLDEIEELFSDFPVAKLPLLPEEVVGLEKL 293
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 17-77 3.93e-06

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 48.61  E-value: 3.93e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553308510  17 FTGKGGVGKTSAACATAVVLADEGKKVLLISTDP----ASNLQDV-FETELDGKAKpiKGVDNLEV 77
Cdd:PRK13230   6 FYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPkadcTRNLVGEkIPTVLDVLRE--KGIDNLGL 69
ParA_partition NF041546
ParA family partition ATPase;
20-73 1.25e-05

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 46.39  E-value: 1.25e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 553308510  20 KGGVGKTSAACATAVVLADEGKKVLLISTDPASNLQDVFETELDGKAKPIKGVD 73
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPVVGLA 61
ParA_partition NF041546
ParA family partition ATPase;
332-362 4.20e-04

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 41.77  E-value: 4.20e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 553308510 332 KGGVGKTTIASSVALKLSKLGKKVHLSTTDP 362
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 ...
 11-566 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: 792.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510   11 LTKYLFFTGKGGVGKTSAACATAVVLADEGKKVLLISTDPASNLQDVFETELDGKAKPIKGVDNLEVINLDPLEAAHNYK 90
Cdd:TIGR04291   2 LPPYLFFTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNVGQVFGQTIGNKITAIAGVPGLFALEIDPQAAAQAYR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510   91 ESVVAPFRGKLPDSVIENMEEQLSGSCTVEIAAFNEFSNFITNPKLNTEYDNIIFDTAPTGHTLRMLQLPSAWTGFISES 170
Cdd:TIGR04291  82 ARIVDPVRGVLPDDVVSSIEEQLSGACTTEIAAFDEFTGLLTDAELTQDFDHIIFDTAPTGHTIRLLQLPGAWSDFLDTN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  171 THGASCLGQLSGLEAKKEIYKQAVQNLSDESVTTLVLVTRPDKTPLNEVARASKELSEIGIKNQILVINGLL---EHYDD 247
Cdd:TIGR04291 162 PNGASCLGPLAGLEKQRAQYAKAVEALSDPERTRLILVARPQKSTLLEVARTHQELAAIGLKNQYLVINGVLpetEASDD 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  248 DLSESIFNKQKLALENMPDMLTEFDTYTIALRSYNITGIDAIRNLLKKDQISE---QKVEVKGKLFNLDDVVSDLVKNNR 324
Cdd:TIGR04291 242 PLAQAIYKREQKALQHMPAILANLPRYTLPLKPYNLVGLEALRQLLNDDQPQLsldITTPQVPDLPSLSRLIDEIAKSEK 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLSTTDPADHIKFMIDSS-SGISMSHIDEKEELKKYQDEVLENARKTMS 403
Cdd:TIGR04291 322 GLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSlNNLQVSRIDPKQETERYRQEVLATKGKELD 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  404 EDDVAYIEEDLRSPCTQEIAVFRAFAELVEKADDEIVVIDTAPTGHTLLLLDSTLSYHKEVQRTQGQIPESVKNLLPRLR 483
Cdd:TIGR04291 402 EDGKAYLEEDLRSPCTEEIAVFQAFSRIIREAGDRFVVMDTAPTGHTLLLLDATGAYHREVERKMGDTPEHVTTPMMQLQ 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  484 G-EETEVLIVSLAEATPFYEAYRLEEDLKRASIHTNWWIVNSSLYKANPSNKLLSAKANEEVKWINKILDHTSGKLAVIE 562
Cdd:TIGR04291 482 DpERTKVLLVTLPETTPVLEAARLQEDLRRAGIEPWWWVINNSLAATNTTSPLLSQRAQNELKWIEKVKRIHADRYAVIP 561


                  ....
gi 553308510  563 WTKE 566
Cdd:TIGR04291 562 LQAE 565
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
12-295 1.02e-105

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 319.84  E-value: 1.02e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  12 TKYLFFTGKGGVGKTSAACATAVVLADEGKKVLLISTDPASNLQDVFETELDGKAKPIKgVDNLEVINLDPLEAAHNYKE 91
Cdd:COG0003    3 TRIIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGTELGNEPTEVA-VPNLYALEIDPEAELEEYWE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  92 SVVAPFRGKLPDSVIENMEEqlSGSCTVEIAAFNEFSNFITNPklntEYDNIIFDTAPTGHTLRMLQLP---SAWTGFIS 168
Cdd:COG0003   82 RVRAPLRGLLPSAGVDELAE--SLPGTEELAALDELLELLEEG----EYDVIVVDTAPTGHTLRLLSLPellGWWLDRLL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 169 ESTHGASCLGQ-------------LSGLEAKKEIYKQAVQNLSDESVTTLVLVTRPDKTPLNEVARASKELSEIGIKNQI 235
Cdd:COG0003  156 KLRRKASGLGRplagilglpddpvLEGLEELRERLERLRELLRDPERTSFRLVTNPERLAIAETRRALEELALYGIPVDG 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553308510 236 LVINGLLEHYDDDLS--ESIFNKQKLALENMPDMLTEFDTYTIALRSYNITGIDAIRNLLKK 295
Cdd:COG0003  236 LVVNRVLPEEADDDAflAARRERQQEYLAEIEEAFAPLPVVEVPLLAEEVVGLEALRALAEE 297
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 12-552 8.17e-103

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: 323.37  E-value: 8.17e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  12 TKYLFFTGKGGVGKTSAACATAVVLADEGKKVLLISTDPASNLQDVFETELDGKAKPIKGVDNLEVINLDPLEAAHNYKE 91
Cdd:NF041417  12 TEFVFFSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFGQSIGHRVTSIDDVENLSAIEIDPDAAAEEYRQ 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  92 SVVAPFRGKLPDSVIENMEEQLSGSCTVEIAAFNEFSNFITNPklntEYDNIIFDTAPTGHTLRMLQLPSAWTGFISESt 171
Cdd:NF041417  92 RTIEPMRQLLDDEQLKTVEEQLDSPCIEEIAAFDKFVEFMDEP----EYDVVVFDTAPTGHTIRLMELPSGWSEELEKG- 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 172 hGASCLGQLSGLEAKKEIYKQAVQNLSDESVTTLVLVTRPDKTPLNEVARASKELSEIGIKNQILVINGLLEhydDDLSE 251
Cdd:NF041417 167 -GATCIGPAASLQEQKEDYEKAIDTLQDDAQTSFVFVGKPEDASIDEIERSSKELADLGIKTSLLVINGYLP---ESVCE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 252 SIFNKQKLALEN--MPDMLTEFDTYTIA---LRSYNITGIDAIRNL-----------LKKDQISEQKVEVKGKLFNLDDV 315
Cdd:NF041417 243 DPFFEMKREDEQeiLEEVEREFAMQPIAtypLQPGEITGIDLLADVgevlyegkeptVDVAVITEEETEETSPSETDKEA 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 316 VSDLV--KNNRKVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLSTTDPADHIKFMIDSS----------SGISMSHIDE 383
Cdd:NF041417 323 VMELLrpQKDTRYLFFTGKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQDIFGTEvgheptkvgvENLYAARIDQ 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 384 KEELKKYQDEVLENARKTMSEDDV------AYIEEDLRSPCTQEIAVFRAFAELVEKADDEIVVIDTAPTGHTLLLLDST 457
Cdd:NF041417 403 ERALEEYKTRMLDQVEQSFDKDQIdveaakAQVREELESPCAEEMAALEKFVSYFDVDGYDVVVFDTAPTGHTLRLLELP 482

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 458 LSYHKEV---QRTQGQIPES---VKNLLPRLRGEETEVLI-VSLAEATPFYEAYRLEEDLK-RASIHTNWWIVNSSLYKA 529
Cdd:NF041417 483 SDWKGFMdlgSLTKEASDVTgdkYDRVIETMRDPERSTFVfVMYPEYTPMMEAWRAAEDLRnQVGIETSLVAVNYLLPEE 562

                        570       580
                 ....*....|....*....|...
gi 553308510 530 NPSNKLLSAKANEEVKWINKILD 552
Cdd:NF041417 563 YGNNAFFESRRKQQQKYLEEIRD 585
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 13-292 1.11e-93

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: 287.10  E-value: 1.11e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  13 KYLFFTGKGGVGKTSAACATAVVLADEGKKVLLISTDPASNLQDVFETELdGKAKPIKGVDNLEVINLDPLEAAHNYKES 92
Cdd:cd02035    1 RIIFFGGKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGQKL-GGETPVKGAPNLWAMEIDPEEALEEYWEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  93 VVAPFR--GKLPDSVIENMEEQLSGSCTVEIAAFNEFSNFITNPklntEYDNIIFDTAPTGHTLRMLQLPsawtgfises 170
Cdd:cd02035   80 VKELLAqyLRLPGLDEVYAEELLSLPGMDEAAAFDELREYVESG----EYDVIVFDTAPTGHTLRLLSLP---------- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 171 thgasclgqlsgleakkeiYKQAVQNLSDESVTTLVLVTRPDKTPLNEVARASKELSEIGIKNQILVINGLL-EHYDDDL 249
Cdd:cd02035  146 -------------------LEQVRELLRDPERTTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVNQVLpEEADDSF 206

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 553308510 250 SESIFNKQKLALENMPDMLTEFDTYTIALRSYNITGIDAIRNL 292
Cdd:cd02035  207 FLRRRRQQQKYLDEIEELFEPLPVVEVPLLPEEVRGLEALRAL 249
GET3_arsA_TRC40 TIGR00345
transport-energizing ATPase, TRC40/GET3/ArsA family; Members of this family are ATPases that ...
 28-294 2.87e-70

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: 227.75  E-value: 2.87e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510   28 AACATAVVLADEGKKVLLISTDPASNLQDVFETELDGKAKPIKGVDNLEVINLDPLEAAHNYKESVVAPFRGKLPDSviE 107
Cdd:TIGR00345   1 ISAATAIRLAEQGKKVLLVSTDPAHSLSDVFEQEIGHTPTKVTGVENLSAVEIDPQAALEEYRAKLVEQIKGNLPDG--D 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  108 NMEEQLSGSCTV----EIAAFNEFSNFITNPKLntEYDNIIFDTAPTGHTLRMLQLPSAWTGFISESTHGASCLGQLSG- 182
Cdd:TIGR00345  79 MLGDQLEGAALSpgidEIAAFDEFLKHMTDAEN--EFDVVIFDTAPTGHTLRLLQLPEVLSSFLEKFIKIRSKLGPMAKl 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  183 -------------LEAKKEIYKQAVQNLSDESVTTLVLVTRPDKTPLNEVARASKELSEIGIKNQILVINGLL-EHYDDD 248
Cdd:TIGR00345 157 fmgageddealekLEELKEQIEAAREILSDPERTSFVLVVIPEKMSLYESERAHKELAKYGIKVDAVIVNQVLpENAQDE 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 553308510  249 LSESIFNKQKLALENMPDMLTEFDTYTIALRSYNITGIDAIRNLLK 294
Cdd:TIGR00345 237 FCQARWELQQKYLKQIPEKFADLPVAEVPLQKEEMVGLEALKRLSK 282
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 12-289 2.87e-60

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: 202.19  E-value: 2.87e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510   12 TKYLFFTGKGGVGKTSAACATAVVLADEGKKVLLISTDPASNLQDVFETELdgKAKPIKGVDNLEVINLDPLEAAHNYKE 91
Cdd:pfam02374   1 MRWIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQKF--GHEPTKVKENLSAMEIDPNMELEEYWQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510   92 SVVAPFRGKL-PDSVIENMEEQL-SGSCTVEIAAFNEFSNFITNPklntEYDNIIFDTAPTGHTLRMLQLPSAWTGFISE 169
Cdd:pfam02374  79 EVQKYMNALLgLRMLEGILAEELaSLPGIDEAASFDEFKKYMDEG----EYDVVVFDTAPTGHTLRLLSLPTVLGWYLEK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  170 ---------------STHGASCLGQ-LSGLEAKKEIYKQAVQNLSDESVTTLVLVTRPDKTPLNEVARASKELSEIGIKN 233
Cdd:pfam02374 155 ivklknqigplakpfLGMGGVSIPEaLESLEETKERIERAREILTDPERTSFRLVCIPEKMSLYETERAIQYLAKYGIDV 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 553308510  234 QILVINGLLEHYDDDLS---ESIFNKQKLALENMPDMLTEFDTYTIALRSYNITGIDAI 289
Cdd:pfam02374 235 DAVIVNQVLPENVQENCpfcEARKKIQQKYLDEIEELFSDFPVAKLPLLPEEVVGLEKL 293
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 325-569 6.57e-51

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: 175.39  E-value: 6.57e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLSTTDPADHI----------KFMIDSSSGISMSHIDEKEELKKYQDEV 394
Cdd:cd02035    1 RIIFFGGKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLsdafgqklggETPVKGAPNLWAMEIDPEEALEEYWEEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 395 LENARK--TMSEDDVAYIEEDLRSPCTQEIAVFRAFAELVEKADDEIVVIDTAPTGHtlllldstlsyhkevqrTQG--Q 470
Cdd:cd02035   81 KELLAQylRLPGLDEVYAEELLSLPGMDEAAAFDELREYVESGEYDVIVFDTAPTGH-----------------TLRllS 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 471 IPesVKNLLPRLR-GEETEVLIVSLAEATPFYEAYRLEEDLKRASIHTNWWIVNSSLYKANPSNKLLSAKANEEVKWINK 549
Cdd:cd02035  144 LP--LEQVRELLRdPERTTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVNQVLPEEADDSFFLRRRRQQQKYLDEI 221

                        250       260
                 ....*....|....*....|
gi 553308510 550 ILDHTSGKLAVIEWTKEDLR 569
Cdd:cd02035  222 EELFEPLPVVEVPLLPEEVR 241
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
322-550 1.53e-33

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 129.55  E-value: 1.53e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 322 NNRKVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLSTTDPADHIK--FMIDSSSG---ISMSH-----IDEKEELKKYQ 391
Cdd:COG0003    1 DMTRIIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGdvLGTELGNEpteVAVPNlyaleIDPEAELEEYW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 392 DEVLENARKTMSEDDVAYIEEDLrsPCTQEIAVFRAFAELVEKADDEIVVIDTAPTGH-----------------TLLLL 454
Cdd:COG0003   81 ERVRAPLRGLLPSAGVDELAESL--PGTEELAALDELLELLEEGEYDVIVVDTAPTGHtlrllslpellgwwldrLLKLR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 455 DSTLSYHKEVQRTQGQIPESVKNLLPRLR------------GEETEVLIVSLAEATPFYEAYRLEEDLKRASIHTNWWIV 522
Cdd:COG0003  159 RKASGLGRPLAGILGLPDDPVLEGLEELRerlerlrellrdPERTSFRLVTNPERLAIAETRRALEELALYGIPVDGLVV 238

                        250       260
                 ....*....|....*....|....*...
gi 553308510 523 NSSLYKANPSNKLLSAKANEEVKWINKI 550
Cdd:COG0003  239 NRVLPEEADDDAFLAARRERQQEYLAEI 266
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 325-523 2.02e-26

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: 109.36  E-value: 2.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLSTTDPADHIKFMIDSSSG---------ISMSHIDEKEELKKYQDEVL 395
Cdd:pfam02374   2 RWIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQKFGheptkvkenLSAMEIDPNMELEEYWQEVQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  396 ENARKTMSEDDVAYIEEDLRS--PCTQEIAVFRAFAELVEKADDEIVVIDTAPTGHT---LLLLDSTLSYHKEVQRTQGQ 470
Cdd:pfam02374  82 KYMNALLGLRMLEGILAEELAslPGIDEAASFDEFKKYMDEGEYDVVVFDTAPTGHTlrlLSLPTVLGWYLEKIVKLKNQ 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553308510  471 IPESVKNLLP------------------RLRG--------EETEVLIVSLAEATPFYEAYRLEEDLKRASIHTNWWIVN 523
Cdd:pfam02374 162 IGPLAKPFLGmggvsipealesleetkeRIERareiltdpERTSFRLVCIPEKMSLYETERAIQYLAKYGIDVDAVIVN 240
GET3_arsA_TRC40 TIGR00345
transport-energizing ATPase, TRC40/GET3/ArsA family; Members of this family are ATPases that ...
 340-557 7.41e-15

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: 75.21  E-value: 7.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  340 IASSVALKLSKLGKKVHLSTTDPA-----------DHIKFMIDSSSGISMSHIDEKEELKKYQDEVLENARK--TMSEDD 406
Cdd:TIGR00345   1 ISAATAIRLAEQGKKVLLVSTDPAhslsdvfeqeiGHTPTKVTGVENLSAVEIDPQAALEEYRAKLVEQIKGnlPDGDML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  407 VAYIEEDLRSPCTQEIAVFRAFAELVEKADDE--IVVIDTAPTGH----------------------TLLLLDSTLSYHK 462
Cdd:TIGR00345  81 GDQLEGAALSPGIDEIAAFDEFLKHMTDAENEfdVVIFDTAPTGHtlrllqlpevlssflekfikirSKLGPMAKLFMGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  463 EVQRTQGQIPESVKNLLPRLR-----GEETEVLIVSLAEATPFYEAYRLEEDLKRASIHTNWWIVNSSLYKaNPSNKLLS 537
Cdd:TIGR00345 161 GEDDEALEKLEELKEQIEAAReilsdPERTSFVLVVIPEKMSLYESERAHKELAKYGIKVDAVIVNQVLPE-NAQDEFCQ 239

                         250       260
                  ....*....|....*....|
gi 553308510  538 AKANEEVKWINKILDHTSGK 557
Cdd:TIGR00345 240 ARWELQQKYLKQIPEKFADL 259
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 19-240 7.98e-11

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: 63.28  E-value: 7.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  19 GKGGVGKTSAACATAVVLADEGKKVLLISTD-------------PASNLQDVF--ETELDGKAKPIkGVDNLEVInldpl 83
Cdd:COG0489  100 GKGGEGKSTVAANLALALAQSGKRVLLIDADlrgpslhrmlgleNRPGLSDVLagEASLEDVIQPT-EVEGLDVL----- 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  84 eaahnykesvvapFRGKLPDSvienmeeqlsgscTVEIAAFNEFSNFITNpkLNTEYDNIIFDTAP-TGHT-LRMLQlps 161
Cdd:COG0489  174 -------------PAGPLPPN-------------PSELLASKRLKQLLEE--LRGRYDYVIIDTPPgLGVAdATLLA--- 222

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553308510 162 awtgfisesthgasclgqlsgleakkeiykqavqnlsdESVTTLVLVTRPDKTPLNEVARASKELSEIGIKNQILVING 240
Cdd:COG0489  223 --------------------------------------SLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM 263
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 14-58 5.62e-09

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


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 54.47  E-value: 5.62e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 553308510  14 YLFFTGKGGVGKTSAACATAVVLADEGKKVLLISTDPASNLQDVF 58
Cdd:cd02042    3 IAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL 47
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 19-155 1.34e-07

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


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 52.73  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510   19 GKGGVGKTSAACATAVVLADEGKKVLLISTDPASNLqdvfeTELDGKAKPIKGVDNL------EVINLDPLEAAHNYKES 92
Cdd:pfam01656   6 TKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNN-----SSVEGLEGDIAPALQAlaeglkGRVNLDPILLKEKSDEG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553308510   93 VVAPFRGKLPDSVIENMEEQLSGSCTVEiAAFNEfsnfitnpkLNTEYDNIIFDTAPT-GHTLR 155
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKELLGPRKEERLR-EALEA---------LKEDYDYVIIDGAPGlGELLR 134
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 16-54 2.81e-07

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: 52.17  E-value: 2.81e-07
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 553308510  16 FFTGKGGVGKTSAACATAVVLADEGKKVLLISTDPASNL 54
Cdd:COG1192    6 VANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNL 44
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 17-54 2.96e-07

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 51.71  E-value: 2.96e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 553308510  17 FTGKGGVGKTSAACATAVVLADEGKKVLLISTDPASNL 54
Cdd:COG3640    5 VAGKGGVGKTTLSALLARYLAEKGKPVLAVDADPNANL 42
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 326-446 3.18e-07

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


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 51.58  E-value: 3.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  326 VIFTMGKGGVGKTTIASSVALKLSKLGKKVhlsttdpadhikFMIDSSSGISMSHIDEKEElkkYQDEVLENA----RKT 401
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRV------------LLIDLDPQSNNSSVEGLEG---DIAPALQALaeglKGR 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553308510  402 MSEDDVAYIEEDLRS-----PCTQEIAVF--------------RAFAELVEKADdeIVVIDTAP 446
Cdd:pfam01656  66 VNLDPILLKEKSDEGgldliPGNIDLEKFekellgprkeerlrEALEALKEDYD--YVIIDGAP 127
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 13-49 3.52e-07

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


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 48.97  E-value: 3.52e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 553308510  13 KYLFFTG-KGGVGKTSAACATAVVLADEGKKVLLISTD 49
Cdd:cd01983    1 RVIAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 320-355 1.16e-06

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: 50.14  E-value: 1.16e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 553308510  320 VKNnrkVIFTM-GKGGVGKTTIASSVALKLSKLGKKV 355
Cdd:pfam10609   2 VKH---VIAVAsGKGGVGKSTVAVNLALALARLGYKV 35
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 17-77 3.93e-06

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 48.61  E-value: 3.93e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553308510  17 FTGKGGVGKTSAACATAVVLADEGKKVLLISTDP----ASNLQDV-FETELDGKAKpiKGVDNLEV 77
Cdd:PRK13230   6 FYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPkadcTRNLVGEkIPTVLDVLRE--KGIDNLGL 69
PRK12724 PRK12724
flagellar biosynthesis regulator FlhF; Provisional
 257-409 6.88e-06

flagellar biosynthesis regulator FlhF; Provisional


Pssm-ID: 183703 [Multi-domain]  Cd Length: 432  Bit Score: 48.81  E-value: 6.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 257 QKLALENMPDMLTEFDTYTIALRsynITGIDAIRN---LLKKDQISEQKVEVKGKLFnlddvvSDLVKNNRKVIFTMGKG 333
Cdd:PRK12724 162 ERLVREGMSQSYVEEMASKLEER---LSPVDQGRNhnvTERAVTYLEERVSVDSDLF------SGTGKNQRKVVFFVGPT 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 334 GVGKTTIASSVALKLS-KLGKKVHLSTTD-----PADHIKFMIDSssgISMSHIDEKeELKKYQDEVLENARKTMSEDDV 407
Cdd:PRK12724 233 GSGKTTSIAKLAAKYFlHMGKSVSLYTTDnyriaAIEQLKRYADT---MGMPFYPVK-DIKKFKETLARDGSELILIDTA 308


                 ..
gi 553308510 408 AY 409
Cdd:PRK12724 309 GY 310
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 22-240 7.82e-06

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


Pssm-ID: 349772 [Multi-domain]  Cd Length: 190  Bit Score: 46.79  E-value: 7.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  22 GVGKTSAACATAVVLADEGKKVLLISTDP-ASNLQDVFETE--------LDGKAKPIKGVDNLEVINLDPLEAAHnykes 92
Cdd:cd05387   30 GEGKSTVAANLAVALAQSGKRVLLIDADLrRPSLHRLLGLPnepglsevLSGQASLEDVIQSTNIPNLDVLPAGT----- 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  93 vVAPFRGKLPDSviENMEEQLSgsctveiaafnefsnfitnpKLNTEYDNIIFDTAPTGHtlrmlqlpsawtgfiseSTH 172
Cdd:cd05387  105 -VPPNPSELLSS--PRFAELLE--------------------ELKEQYDYVIIDTPPVLA-----------------VAD 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553308510 173 GAScLGQLSGleakkeiykqavqnlsdesvtTLVLVTRPDKTPLNEVARASKELSEIGIKNQILVING 240
Cdd:cd05387  145 ALI-LAPLVD---------------------GVLLVVRAGKTRRREVKEALERLEQAGAKVLGVVLNK 190
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 20-150 8.27e-06

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


Pssm-ID: 433350 [Multi-domain]  Cd Length: 177  Bit Score: 46.42  E-value: 8.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510   20 KGGVGKTSAACATAVVLADEGKKVLLISTDPASNLQDVFETELDGKAKPIkgvdnLEVINLDpleaaHNYKESVVAPFRG 99
Cdd:pfam13614  10 KGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTI-----YELLIGE-----CNIEEAIIKTVIE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 553308510  100 KLpDSVIENMEeqLSGsctVEIAAFN-EFSNFITNPKLNT---EYDNIIFDTAPT 150
Cdd:pfam13614  80 NL-DLIPSNID--LAG---AEIELIGiENRENILKEALEPvkdNYDYIIIDCPPS 128
ParA_partition NF041546
ParA family partition ATPase;
20-73 1.25e-05

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 46.39  E-value: 1.25e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 553308510  20 KGGVGKTSAACATAVVLADEGKKVLLISTDPASNLQDVFETELDGKAKPIKGVD 73
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPVVGLA 61
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 17-76 1.44e-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: 46.92  E-value: 1.44e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  17 FTGKGGVGKTSAACATAVVLADEGKKVLLISTDPASNLQDVFETELDgKAKPIKGVDNLE 76
Cdd:cd02034    5 VAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVE-KLPLIKTIGDIR 63
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 325-355 1.76e-05

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 46.59  E-value: 1.76e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 553308510 325 KVI-FTMGKGGVGKTTIASSVALKLSKLGKKV 355
Cdd:COG2894    3 KVIvVTSGKGGVGKTTTTANLGTALALLGKKV 34
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 325-378 1.85e-05

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


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 44.45  E-value: 1.85e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553308510 325 KVI-FTMGKGGVGKTTIASSVALKLSKLGKKVHLSTTDP--------ADHIkfMIDSSSGISM 378
Cdd:cd02042    1 KVIaVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPqgsltswlYDYI--LIDTPPSLGL 61
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 329-355 2.25e-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: 2.25e-05
                         10        20
                 ....*....|....*....|....*..
gi 553308510 329 TMGKGGVGKTTIASSVALKLSKLGKKV 355
Cdd:cd02038    6 TSGKGGVGKTNVSANLALALSKLGKRV 32
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 325-355 2.72e-05

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: 45.57  E-value: 2.72e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 553308510 325 KVIFTM-GKGGVGKTTIASSVALKLSKLGKKV 355
Cdd:cd02037    1 HIIAVLsGKGGVGKSTVAVNLALALAKKGYKV 32
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 19-49 2.77e-05

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 45.82  E-value: 2.77e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 553308510  19 GKGGVGKT--SAACATAvvLADEGKKVLLISTD 49
Cdd:COG2894   10 GKGGVGKTttTANLGTA--LALLGKKVVLIDAD 40
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
17-68 2.78e-05

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 45.90  E-value: 2.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 553308510   17 FTGKGGVGKTSAACATAVVLADEGKKVLLISTDPASnlqDVFETELDGKAKP 68
Cdd:pfam00142   5 IYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKA---DSTRLLLGGKLQP 53
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 17-50 3.19e-05

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


Pssm-ID: 349759  Cd Length: 265  Bit Score: 45.97  E-value: 3.19e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 553308510  17 FTGKGGVGKTSAACATAVVLADEGKKVLLISTDP 50
Cdd:cd02040    5 IYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDP 38
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 324-361 4.11e-05

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


Pssm-ID: 349756 [Multi-domain]  Cd Length: 236  Bit Score: 45.27  E-value: 4.11e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 553308510 324 RKVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLSTTD 361
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 19-78 4.23e-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: 45.25  E-value: 4.23e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553308510  19 GKGGVGKTSAACATAVVLADEGKKVLLISTD-------------PASNLQDVFETELDGKAKPIKGVDNLEVI 78
Cdd:cd02038    8 GKGGVGKTNVSANLALALSKLGKRVLLLDADlglanldillglaPKKTLGDVLKGRVSLEDIIVEGPEGLDII 80
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 309-446 6.14e-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: 45.18  E-value: 6.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 309 LFNLDDVVSDLVKNNRKVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLSTTD---PADHIKFMIDSSSGISMSHIDEKE 385
Cdd:COG0489   78 ALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADlrgPSLHRMLGLENRPGLSDVLAGEAS 157

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553308510 386 elkkyqdevLENARKTMSEDDVAYIEEDLRSPCTQEIAVFRAFAELVEKADDE--IVVIDTAP 446
Cdd:COG0489  158 ---------LEDVIQPTEVEGLDVLPAGPLPPNPSELLASKRLKQLLEELRGRydYVIIDTPP 211
chlL CHL00072
photochlorophyllide reductase subunit L
 19-50 8.97e-05

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 44.73  E-value: 8.97e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 553308510  19 GKGGVGKTSAACATAVVLADEGKKVLLISTDP 50
Cdd:CHL00072   7 GKGGIGKSTTSCNISIALARRGKKVLQIGCDP 38
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 324-366 1.14e-04

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: 41.65  E-value: 1.14e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 553308510 324 RKVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLstTDPADHI 366
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLL--IDLDDYV 41
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 19-109 1.15e-04

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


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 43.64  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  19 GKGGVGKTSAACATAVVLADEGKKVLLISTDPAS-------NLQDVFETELDGKAKPIKgVDNLEVINLDPLeaaHNYKE 91
Cdd:cd02037    8 GKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGpsiprllGVEGKPLHQSEEGIVPVE-VGGIKVMSIGFL---LPEDD 83

                         90
                 ....*....|....*...
gi 553308510  92 SVVapFRGKLPDSVIENM 109
Cdd:cd02037   84 AVI--WRGPMKSGAIKQF 99
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 323-361 1.59e-04

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


Pssm-ID: 131023 [Multi-domain]  Cd Length: 261  Bit Score: 43.48  E-value: 1.59e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 553308510  323 NRKVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLSTTD 361
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD 39
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 325-447 1.81e-04

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: 43.31  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510 325 KVI-FTMGKGGVGKTTIASSVALKLSKLGKKVHLsttdpadhikfmID------SSSGISMSHIDEKEELKK--YQDEVL 395
Cdd:COG1192    2 KVIaVANQKGGVGKTTTAVNLAAALARRGKRVLL------------IDldpqgnLTSGLGLDPDDLDPTLYDllLDDAPL 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553308510 396 ENA-RKTMSE--------DDVAYIEEDLRSPCTQEIAVFRAFAELVEKADdeIVVIDTAPT 447
Cdd:COG1192   70 EDAiVPTEIPgldlipanIDLAGAEIELVSRPGRELRLKRALAPLADDYD--YILIDCPPS 128
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 325-362 1.92e-04

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


Pssm-ID: 349761  Cd Length: 266  Bit Score: 43.51  E-value: 1.92e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 553308510 325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLSTTDP 362
Cdd:cd02117    1 ESIVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDP 38
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 19-50 2.72e-04

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


Pssm-ID: 349752  Cd Length: 267  Bit Score: 43.06  E-value: 2.72e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 553308510  19 GKGGVGKTSAACATAVVLADEGKKVLLISTDP 50
Cdd:cd02032    7 GKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDP 38
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 325-355 2.79e-04

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 42.85  E-value: 2.79e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 553308510 325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKV 355
Cdd:COG3640    1 MKIAVAGKGGVGKTTLSALLARYLAEKGKPV 31
ParA_partition NF041546
ParA family partition ATPase;
332-362 4.20e-04

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 41.77  E-value: 4.20e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 553308510 332 KGGVGKTTIASSVALKLSKLGKKVHLSTTDP 362
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADP 38
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 324-355 4.25e-04

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


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 42.41  E-value: 4.25e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 553308510  324 RKVIFTMGKGGVGKTTIASSVALKLSKLGKKV 355
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKV 32
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 19-49 4.76e-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: 41.80  E-value: 4.76e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 553308510  19 GKGGVGKTSAACATAVVLADEGKKVLLISTD 49
Cdd:cd02036    8 GKGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 325-355 7.69e-04

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


Pssm-ID: 349752  Cd Length: 267  Bit Score: 41.51  E-value: 7.69e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 553308510 325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKV 355
Cdd:cd02032    1 LVIAVYGKGGIGKSTTSSNLSAAFAKRGKKV 31
NB-ARC pfam00931
NB-ARC domain;
304-418 7.74e-04

NB-ARC domain;


Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 41.60  E-value: 7.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553308510  304 EVKGKLFNlddvvsdlvKNNRKVIFTMGKGGVGKTTIASSVALKLSKLGKK------VHLSTTDPADHIKFMIDSSSGIS 377
Cdd:pfam00931   7 KVIGKLSE---------KDEPGIVGIHGMGGVGKTTLAAQIFNDFDEVEGHfdsvawVVVSKTFTISTLQQTILQNLGLS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 553308510  378 MSHIDEKEELKKYQD--EVLENARKTMSEDDVaYIEEDLRSPC 418
Cdd:pfam00931  78 EDDWDNKEEGELARKirRALLTKRFLLVLDDV-WDEEDWDKIG 119
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 325-362 9.50e-04

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


Pssm-ID: 433350 [Multi-domain]  Cd Length: 177  Bit Score: 40.26  E-value: 9.50e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 553308510  325 KVI-FTMGKGGVGKTTIASSVALKLSKLGKKVHLSTTDP 362
Cdd:pfam13614   2 KVIaIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDP 40
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 17-50 1.04e-03

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


Pssm-ID: 349761  Cd Length: 266  Bit Score: 41.20  E-value: 1.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 553308510  17 FTGKGGVGKTSAACATAVVLADEGKKVLLISTDP 50
Cdd:cd02117    5 VYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDP 38
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 19-50 1.19e-03

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 41.10  E-value: 1.19e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 553308510  19 GKGGVGKTSAACATAVVLADEGKKVLLISTDP 50
Cdd:PRK13185   9 GKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDP 40
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 325-355 1.24e-03

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 41.10  E-value: 1.24e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 553308510 325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKV 355
Cdd:PRK13185   3 LVLAVYGKGGIGKSTTSSNLSAAFAKLGKKV 33
minD CHL00175
septum-site determining protein; Validated
 324-361 1.35e-03

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 40.91  E-value: 1.35e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 553308510 324 RKVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLSTTD 361
Cdd:CHL00175  16 RIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDAD 53
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 19-49 1.66e-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: 40.51  E-value: 1.66e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 553308510   19 GKGGVGKTSAACATAVVLADEGKKVLLISTD 49
Cdd:pfam10609  11 GKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
PHA02518 PHA02518
ParA-like protein; Provisional
 20-50 1.73e-03

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 40.22  E-value: 1.73e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 553308510  20 KGGVGKTSAACATAVVLADEGKKVLLISTDP 50
Cdd:PHA02518   9 KGGAGKTTVATNLASWLHADGHKVLLVDLDP 39
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
 325-362 1.99e-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: 39.24  E-value: 1.99e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 553308510 325 KVIFTM-GKGGVGKTTIASSVALKLSKLGKKVHLSTTDP 362
Cdd:cd05386    1 KIHFVLqGKGGVGKSVIASLLAQYLIDKGQPVSCIDTDP 39
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 10-68 2.41e-03

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


Pssm-ID: 349753  Cd Length: 329  Bit Score: 40.20  E-value: 2.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 553308510  10 KLTKYLFFTGKGGVGKTSAACATAVVLADEGKKVLLISTDPASnlqDVFETELDGKAKP 68
Cdd:cd02033   29 KETQIIAIYGKGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKS---DTTSLLFGGKACP 84
PHA02518 PHA02518
ParA-like protein; Provisional
 332-362 2.50e-03

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 39.45  E-value: 2.50e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 553308510 332 KGGVGKTTIASSVALKLSKLGKKVHLSTTDP 362
Cdd:PHA02518   9 KGGAGKTTVATNLASWLHADGHKVLLVDLDP 39
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 331-364 3.52e-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: 39.42  E-value: 3.52e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 553308510 331 GKGGVGKTTIASSVALKLSKLGKKVHLSTTDP-AD 364
Cdd:cd02040    7 GKGGIGKSTTASNLSAALAEMGKKVLHVGCDPkAD 41
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 18-61 5.03e-03

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


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 38.94  E-value: 5.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 553308510   18 TGKGGVGKTSAACATAVVLADEGKKVLLISTDPA-SNLQDVFETE 61
Cdd:TIGR01969   7 SGKGGTGKTTITANLGVALAKLGKKVLALDADITmANLELILGME 51
PRK10818 PRK10818
septum site-determining protein MinD;
18-49 6.34e-03

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 38.77  E-value: 6.34e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 553308510  18 TGKGGVGKTSAACATAVVLADEGKKVLLISTD 49
Cdd:PRK10818   9 SGKGGVGKTTSSAAIATGLAQKGKKTVVIDFD 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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