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Conserved domains on  [gi|696223624|ref|WP_032804094|]
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MULTISPECIES: arsenical pump-driving ATPase [Haemophilus]

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: 791.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624   11 LTKYLFFTGKGGVGKTSTACATAVALADEGKKVLLISTDPASNLQDVFETELDGKAKPIKGVDNLEVINLDPLEAAHNYK 90
Cdd:TIGR04291   2 LPPYLFFTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNVGQVFGQTIGNKITAIAGVPGLFALEIDPQAAAQAYR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624   91 ESVVGPFRGKLPDSVIENMEEQLSGSCTVEIAAFNEFSNFITNSKLNTDYNHIIFDTAPTGHTLRMLQLPSAWTDFISES 170
Cdd:TIGR04291  82 ARIVDPVRGVLPDDVVSSIEEQLSGACTTEIAAFDEFTGLLTDAELTQDFDHIIFDTAPTGHTIRLLQLPGAWSDFLDTN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  171 THGASCLGQLSGLDTKKETYKKAVENLSDKSLTTLVLVTRSDKTPLNEVARASKELSEIGIKNQILVINGVL---ENYDD 247
Cdd:TIGR04291 162 PNGASCLGPLAGLEKQRAQYAKAVEALSDPERTRLILVARPQKSTLLEVARTHQELAAIGLKNQYLVINGVLpetEASDD 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  248 DLSENIFNKQKLALENMPEMLTEFDTYTIALRSYNITGIDSIRNLLKKDQINE---QKVEVKGKLFNLDDVVSDLVKNNR 324
Cdd:TIGR04291 242 PLAQAIYKREQKALQHMPAILANLPRYTLPLKPYNLVGLEALRQLLNDDQPQLsldITTPQVPDLPSLSRLIDEIAKSEK 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLATTDPADHIKFMIDSS-SGISMSHIDEKEELKKYQDEVLGNARKTMS 403
Cdd:TIGR04291 322 GLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSlNNLQVSRIDPKQETERYRQEVLATKGKELD 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  404 EDDVAYIEEDLRSPCTQEIAVFRAFAELVEKADDEIVVIDTAPTGHTLLLLDSTLSYHQEVQRTQGQVPESVKNLLPRLR 483
Cdd:TIGR04291 402 EDGKAYLEEDLRSPCTEEIAVFQAFSRIIREAGDRFVVMDTAPTGHTLLLLDATGAYHREVERKMGDTPEHVTTPMMQLQ 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  484 G-EETEVLIVSLAEATPFYEAYRLEEDLTRASIHTNWWIVNSSLYKANPSNKMLSAKVNEEVKWINKILDHTSGKLAVIE 562
Cdd:TIGR04291 482 DpERTKVLLVTLPETTPVLEAARLQEDLRRAGIEPWWWVINNSLAATNTTSPLLSQRAQNELKWIEKVKRIHADRYAVIP 561


                  ....
gi 696223624  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: 791.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624   11 LTKYLFFTGKGGVGKTSTACATAVALADEGKKVLLISTDPASNLQDVFETELDGKAKPIKGVDNLEVINLDPLEAAHNYK 90
Cdd:TIGR04291   2 LPPYLFFTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNVGQVFGQTIGNKITAIAGVPGLFALEIDPQAAAQAYR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624   91 ESVVGPFRGKLPDSVIENMEEQLSGSCTVEIAAFNEFSNFITNSKLNTDYNHIIFDTAPTGHTLRMLQLPSAWTDFISES 170
Cdd:TIGR04291  82 ARIVDPVRGVLPDDVVSSIEEQLSGACTTEIAAFDEFTGLLTDAELTQDFDHIIFDTAPTGHTIRLLQLPGAWSDFLDTN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  171 THGASCLGQLSGLDTKKETYKKAVENLSDKSLTTLVLVTRSDKTPLNEVARASKELSEIGIKNQILVINGVL---ENYDD 247
Cdd:TIGR04291 162 PNGASCLGPLAGLEKQRAQYAKAVEALSDPERTRLILVARPQKSTLLEVARTHQELAAIGLKNQYLVINGVLpetEASDD 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  248 DLSENIFNKQKLALENMPEMLTEFDTYTIALRSYNITGIDSIRNLLKKDQINE---QKVEVKGKLFNLDDVVSDLVKNNR 324
Cdd:TIGR04291 242 PLAQAIYKREQKALQHMPAILANLPRYTLPLKPYNLVGLEALRQLLNDDQPQLsldITTPQVPDLPSLSRLIDEIAKSEK 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLATTDPADHIKFMIDSS-SGISMSHIDEKEELKKYQDEVLGNARKTMS 403
Cdd:TIGR04291 322 GLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSlNNLQVSRIDPKQETERYRQEVLATKGKELD 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  404 EDDVAYIEEDLRSPCTQEIAVFRAFAELVEKADDEIVVIDTAPTGHTLLLLDSTLSYHQEVQRTQGQVPESVKNLLPRLR 483
Cdd:TIGR04291 402 EDGKAYLEEDLRSPCTEEIAVFQAFSRIIREAGDRFVVMDTAPTGHTLLLLDATGAYHREVERKMGDTPEHVTTPMMQLQ 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  484 G-EETEVLIVSLAEATPFYEAYRLEEDLTRASIHTNWWIVNSSLYKANPSNKMLSAKVNEEVKWINKILDHTSGKLAVIE 562
Cdd:TIGR04291 482 DpERTKVLLVTLPETTPVLEAARLQEDLRRAGIEPWWWVINNSLAATNTTSPLLSQRAQNELKWIEKVKRIHADRYAVIP 561


                  ....
gi 696223624  563 WTKE 566
Cdd:TIGR04291 562 LQAE 565
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
12-295 1.00e-106

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 322.54  E-value: 1.00e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  12 TKYLFFTGKGGVGKTSTACATAVALADEGKKVLLISTDPASNLQDVFETELDGKAKPIKgVDNLEVINLDPLEAAHNYKE 91
Cdd:COG0003    3 TRIIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGTELGNEPTEVA-VPNLYALEIDPEAELEEYWE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  92 SVVGPFRGKLPDSVIENMEEqlSGSCTVEIAAFNEFSNFITNSklntDYNHIIFDTAPTGHTLRMLQLP---SAWTDFIS 168
Cdd:COG0003   82 RVRAPLRGLLPSAGVDELAE--SLPGTEELAALDELLELLEEG----EYDVIVVDTAPTGHTLRLLSLPellGWWLDRLL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 169 ESTHGASCLGQ-------------LSGLDTKKETYKKAVENLSDKSLTTLVLVTRSDKTPLNEVARASKELSEIGIKNQI 235
Cdd:COG0003  156 KLRRKASGLGRplagilglpddpvLEGLEELRERLERLRELLRDPERTSFRLVTNPERLAIAETRRALEELALYGIPVDG 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 696223624 236 LVINGVLENYDDDLS--ENIFNKQKLALENMPEMLTEFDTYTIALRSYNITGIDSIRNLLKK 295
Cdd:COG0003  236 LVVNRVLPEEADDDAflAARRERQQEYLAEIEEAFAPLPVVEVPLLAEEVVGLEALRALAEE 297
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 12-552 8.44e-97

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: 307.58  E-value: 8.44e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  12 TKYLFFTGKGGVGKTSTACATAVALADEGKKVLLISTDPASNLQDVFETELDGKAKPIKGVDNLEVINLDPLEAAHNYKE 91
Cdd:NF041417  12 TEFVFFSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFGQSIGHRVTSIDDVENLSAIEIDPDAAAEEYRQ 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  92 SVVGPFRGKLPDSVIENMEEQLSGSCTVEIAAFNEFSNFITNSklntDYNHIIFDTAPTGHTLRMLQLPSAWTDFISESt 171
Cdd:NF041417  92 RTIEPMRQLLDDEQLKTVEEQLDSPCIEEIAAFDKFVEFMDEP----EYDVVVFDTAPTGHTIRLMELPSGWSEELEKG- 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 172 hGASCLGQLSGLDTKKETYKKAVENLSDKSLTTLVLVTRSDKTPLNEVARASKELSEIGIKNQILVINGVLEnydDDLSE 251
Cdd:NF041417 167 -GATCIGPAASLQEQKEDYEKAIDTLQDDAQTSFVFVGKPEDASIDEIERSSKELADLGIKTSLLVINGYLP---ESVCE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 252 NIFNKQKLALEN--MPEMLTEFDTYTIA---LRSYNITGIDSIRNL-----------LKKDQINEQKVEVKGKLFNLDDV 315
Cdd:NF041417 243 DPFFEMKREDEQeiLEEVEREFAMQPIAtypLQPGEITGIDLLADVgevlyegkeptVDVAVITEEETEETSPSETDKEA 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 316 VSDLV--KNNRKVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLATTDPADHIKFMIDSS----------SGISMSHIDE 383
Cdd:NF041417 323 VMELLrpQKDTRYLFFTGKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQDIFGTEvgheptkvgvENLYAARIDQ 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 384 KEELKKYQDEVL------GNARKTMSEDDVAYIEEDLRSPCTQEIAVFRAFAELVEKADDEIVVIDTAPTGHTLLLLDST 457
Cdd:NF041417 403 ERALEEYKTRMLdqveqsFDKDQIDVEAAKAQVREELESPCAEEMAALEKFVSYFDVDGYDVVVFDTAPTGHTLRLLELP 482

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 458 LSYHQEV---QRTQGQVPES---VKNLLPRLRGEETEVLI-VSLAEATPFYEAYRLEEDL-TRASIHTNWWIVNSSLYKA 529
Cdd:NF041417 483 SDWKGFMdlgSLTKEASDVTgdkYDRVIETMRDPERSTFVfVMYPEYTPMMEAWRAAEDLrNQVGIETSLVAVNYLLPEE 562

                        570       580
                 ....*....|....*....|...
gi 696223624 530 NPSNKMLSAKVNEEVKWINKILD 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 1.90e-94

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: 289.02  E-value: 1.90e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  13 KYLFFTGKGGVGKTSTACATAVALADEGKKVLLISTDPASNLQDVFETELdGKAKPIKGVDNLEVINLDPLEAAHNYKES 92
Cdd:cd02035    1 RIIFFGGKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGQKL-GGETPVKGAPNLWAMEIDPEEALEEYWEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  93 VVGPFR--GKLPDSVIENMEEQLSGSCTVEIAAFNEFSNFITNSklntDYNHIIFDTAPTGHTLRMLQLPsawtdfises 170
Cdd:cd02035   80 VKELLAqyLRLPGLDEVYAEELLSLPGMDEAAAFDELREYVESG----EYDVIVFDTAPTGHTLRLLSLP---------- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 171 thgasclgqlsgldtkketYKKAVENLSDKSLTTLVLVTRSDKTPLNEVARASKELSEIGIKNQILVINGVL-ENYDDDL 249
Cdd:cd02035  146 -------------------LEQVRELLRDPERTTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVNQVLpEEADDSF 206

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 696223624 250 SENIFNKQKLALENMPEMLTEFDTYTIALRSYNITGIDSIRNL 292
Cdd:cd02035  207 FLRRRRQQQKYLDEIEELFEPLPVVEVPLLPEEVRGLEALRAL 249
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 12-289 1.69e-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: 199.88  E-value: 1.69e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624   12 TKYLFFTGKGGVGKTSTACATAVALADEGKKVLLISTDPASNLQDVFETELdgKAKPIKGVDNLEVINLDPLEAAHNYKE 91
Cdd:pfam02374   1 MRWIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQKF--GHEPTKVKENLSAMEIDPNMELEEYWQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624   92 SVVGPFRGKL-PDSVIENMEEQL-SGSCTVEIAAFNEFSNFITNSklntDYNHIIFDTAPTGHTLRMLQLPSAWTDFISE 169
Cdd:pfam02374  79 EVQKYMNALLgLRMLEGILAEELaSLPGIDEAASFDEFKKYMDEG----EYDVVVFDTAPTGHTLRLLSLPTVLGWYLEK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  170 ---------------STHGASCLGQ-LSGLDTKKETYKKAVENLSDKSLTTLVLVTRSDKTPLNEVARASKELSEIGIKN 233
Cdd:pfam02374 155 ivklknqigplakpfLGMGGVSIPEaLESLEETKERIERAREILTDPERTSFRLVCIPEKMSLYETERAIQYLAKYGIDV 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 696223624  234 QILVINGVL-ENYDDDLS--ENIFNKQKLALENMPEMLTEFDTYTIALRSYNITGIDSI 289
Cdd:pfam02374 235 DAVIVNQVLpENVQENCPfcEARKKIQQKYLDEIEELFSDFPVAKLPLLPEEVVGLEKL 293
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 17-77 1.04e-07

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 53.62  E-value: 1.04e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 696223624  17 FTGKGGVGKTSTACATAVALADEGKKVLLISTDP----ASNLQDV-FETELDGKAKpiKGVDNLEV 77
Cdd:PRK13230   6 FYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPkadcTRNLVGEkIPTVLDVLRE--KGIDNLGL 69
ParA_partition NF041546
ParA family partition ATPase;
20-73 5.64e-07

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 50.24  E-value: 5.64e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 696223624  20 KGGVGKTSTACATAVALADEGKKVLLISTDPASNLQDVFETELDGKAKPIKGVD 73
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPVVGLA 61
ParA_partition NF041546
ParA family partition ATPase;
332-362 1.26e-04

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 43.31  E-value: 1.26e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 696223624 332 KGGVGKTTIASSVALKLSKLGKKVHLATTDP 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: 791.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624   11 LTKYLFFTGKGGVGKTSTACATAVALADEGKKVLLISTDPASNLQDVFETELDGKAKPIKGVDNLEVINLDPLEAAHNYK 90
Cdd:TIGR04291   2 LPPYLFFTGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNVGQVFGQTIGNKITAIAGVPGLFALEIDPQAAAQAYR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624   91 ESVVGPFRGKLPDSVIENMEEQLSGSCTVEIAAFNEFSNFITNSKLNTDYNHIIFDTAPTGHTLRMLQLPSAWTDFISES 170
Cdd:TIGR04291  82 ARIVDPVRGVLPDDVVSSIEEQLSGACTTEIAAFDEFTGLLTDAELTQDFDHIIFDTAPTGHTIRLLQLPGAWSDFLDTN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  171 THGASCLGQLSGLDTKKETYKKAVENLSDKSLTTLVLVTRSDKTPLNEVARASKELSEIGIKNQILVINGVL---ENYDD 247
Cdd:TIGR04291 162 PNGASCLGPLAGLEKQRAQYAKAVEALSDPERTRLILVARPQKSTLLEVARTHQELAAIGLKNQYLVINGVLpetEASDD 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  248 DLSENIFNKQKLALENMPEMLTEFDTYTIALRSYNITGIDSIRNLLKKDQINE---QKVEVKGKLFNLDDVVSDLVKNNR 324
Cdd:TIGR04291 242 PLAQAIYKREQKALQHMPAILANLPRYTLPLKPYNLVGLEALRQLLNDDQPQLsldITTPQVPDLPSLSRLIDEIAKSEK 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLATTDPADHIKFMIDSS-SGISMSHIDEKEELKKYQDEVLGNARKTMS 403
Cdd:TIGR04291 322 GLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSlNNLQVSRIDPKQETERYRQEVLATKGKELD 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  404 EDDVAYIEEDLRSPCTQEIAVFRAFAELVEKADDEIVVIDTAPTGHTLLLLDSTLSYHQEVQRTQGQVPESVKNLLPRLR 483
Cdd:TIGR04291 402 EDGKAYLEEDLRSPCTEEIAVFQAFSRIIREAGDRFVVMDTAPTGHTLLLLDATGAYHREVERKMGDTPEHVTTPMMQLQ 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  484 G-EETEVLIVSLAEATPFYEAYRLEEDLTRASIHTNWWIVNSSLYKANPSNKMLSAKVNEEVKWINKILDHTSGKLAVIE 562
Cdd:TIGR04291 482 DpERTKVLLVTLPETTPVLEAARLQEDLRRAGIEPWWWVINNSLAATNTTSPLLSQRAQNELKWIEKVKRIHADRYAVIP 561


                  ....
gi 696223624  563 WTKE 566
Cdd:TIGR04291 562 LQAE 565
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
12-295 1.00e-106

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 322.54  E-value: 1.00e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  12 TKYLFFTGKGGVGKTSTACATAVALADEGKKVLLISTDPASNLQDVFETELDGKAKPIKgVDNLEVINLDPLEAAHNYKE 91
Cdd:COG0003    3 TRIIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGTELGNEPTEVA-VPNLYALEIDPEAELEEYWE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  92 SVVGPFRGKLPDSVIENMEEqlSGSCTVEIAAFNEFSNFITNSklntDYNHIIFDTAPTGHTLRMLQLP---SAWTDFIS 168
Cdd:COG0003   82 RVRAPLRGLLPSAGVDELAE--SLPGTEELAALDELLELLEEG----EYDVIVVDTAPTGHTLRLLSLPellGWWLDRLL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 169 ESTHGASCLGQ-------------LSGLDTKKETYKKAVENLSDKSLTTLVLVTRSDKTPLNEVARASKELSEIGIKNQI 235
Cdd:COG0003  156 KLRRKASGLGRplagilglpddpvLEGLEELRERLERLRELLRDPERTSFRLVTNPERLAIAETRRALEELALYGIPVDG 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 696223624 236 LVINGVLENYDDDLS--ENIFNKQKLALENMPEMLTEFDTYTIALRSYNITGIDSIRNLLKK 295
Cdd:COG0003  236 LVVNRVLPEEADDDAflAARRERQQEYLAEIEEAFAPLPVVEVPLLAEEVVGLEALRALAEE 297
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 12-552 8.44e-97

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: 307.58  E-value: 8.44e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  12 TKYLFFTGKGGVGKTSTACATAVALADEGKKVLLISTDPASNLQDVFETELDGKAKPIKGVDNLEVINLDPLEAAHNYKE 91
Cdd:NF041417  12 TEFVFFSGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFGQSIGHRVTSIDDVENLSAIEIDPDAAAEEYRQ 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  92 SVVGPFRGKLPDSVIENMEEQLSGSCTVEIAAFNEFSNFITNSklntDYNHIIFDTAPTGHTLRMLQLPSAWTDFISESt 171
Cdd:NF041417  92 RTIEPMRQLLDDEQLKTVEEQLDSPCIEEIAAFDKFVEFMDEP----EYDVVVFDTAPTGHTIRLMELPSGWSEELEKG- 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 172 hGASCLGQLSGLDTKKETYKKAVENLSDKSLTTLVLVTRSDKTPLNEVARASKELSEIGIKNQILVINGVLEnydDDLSE 251
Cdd:NF041417 167 -GATCIGPAASLQEQKEDYEKAIDTLQDDAQTSFVFVGKPEDASIDEIERSSKELADLGIKTSLLVINGYLP---ESVCE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 252 NIFNKQKLALEN--MPEMLTEFDTYTIA---LRSYNITGIDSIRNL-----------LKKDQINEQKVEVKGKLFNLDDV 315
Cdd:NF041417 243 DPFFEMKREDEQeiLEEVEREFAMQPIAtypLQPGEITGIDLLADVgevlyegkeptVDVAVITEEETEETSPSETDKEA 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 316 VSDLV--KNNRKVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLATTDPADHIKFMIDSS----------SGISMSHIDE 383
Cdd:NF041417 323 VMELLrpQKDTRYLFFTGKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQDIFGTEvgheptkvgvENLYAARIDQ 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 384 KEELKKYQDEVL------GNARKTMSEDDVAYIEEDLRSPCTQEIAVFRAFAELVEKADDEIVVIDTAPTGHTLLLLDST 457
Cdd:NF041417 403 ERALEEYKTRMLdqveqsFDKDQIDVEAAKAQVREELESPCAEEMAALEKFVSYFDVDGYDVVVFDTAPTGHTLRLLELP 482

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 458 LSYHQEV---QRTQGQVPES---VKNLLPRLRGEETEVLI-VSLAEATPFYEAYRLEEDL-TRASIHTNWWIVNSSLYKA 529
Cdd:NF041417 483 SDWKGFMdlgSLTKEASDVTgdkYDRVIETMRDPERSTFVfVMYPEYTPMMEAWRAAEDLrNQVGIETSLVAVNYLLPEE 562

                        570       580
                 ....*....|....*....|...
gi 696223624 530 NPSNKMLSAKVNEEVKWINKILD 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 1.90e-94

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: 289.02  E-value: 1.90e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  13 KYLFFTGKGGVGKTSTACATAVALADEGKKVLLISTDPASNLQDVFETELdGKAKPIKGVDNLEVINLDPLEAAHNYKES 92
Cdd:cd02035    1 RIIFFGGKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGQKL-GGETPVKGAPNLWAMEIDPEEALEEYWEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  93 VVGPFR--GKLPDSVIENMEEQLSGSCTVEIAAFNEFSNFITNSklntDYNHIIFDTAPTGHTLRMLQLPsawtdfises 170
Cdd:cd02035   80 VKELLAqyLRLPGLDEVYAEELLSLPGMDEAAAFDELREYVESG----EYDVIVFDTAPTGHTLRLLSLP---------- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 171 thgasclgqlsgldtkketYKKAVENLSDKSLTTLVLVTRSDKTPLNEVARASKELSEIGIKNQILVINGVL-ENYDDDL 249
Cdd:cd02035  146 -------------------LEQVRELLRDPERTTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVNQVLpEEADDSF 206

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 696223624 250 SENIFNKQKLALENMPEMLTEFDTYTIALRSYNITGIDSIRNL 292
Cdd:cd02035  207 FLRRRRQQQKYLDEIEELFEPLPVVEVPLLPEEVRGLEALRAL 249
GET3_arsA_TRC40 TIGR00345
transport-energizing ATPase, TRC40/GET3/ArsA family; Members of this family are ATPases that ...
 29-294 2.32e-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: 228.13  E-value: 2.32e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624   29 ACATAVALADEGKKVLLISTDPASNLQDVFETELDGKAKPIKGVDNLEVINLDPLEAAHNYKESVVGPFRGKLPDSviEN 108
Cdd:TIGR00345   2 SAATAIRLAEQGKKVLLVSTDPAHSLSDVFEQEIGHTPTKVTGVENLSAVEIDPQAALEEYRAKLVEQIKGNLPDG--DM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  109 MEEQLSGSCTV----EIAAFNEFSNFITNSKLntDYNHIIFDTAPTGHTLRMLQLPSAWTDFISESTHGASCLGQLSG-- 182
Cdd:TIGR00345  80 LGDQLEGAALSpgidEIAAFDEFLKHMTDAEN--EFDVVIFDTAPTGHTLRLLQLPEVLSSFLEKFIKIRSKLGPMAKlf 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  183 ------------LDTKKETYKKAVENLSDKSLTTLVLVTRSDKTPLNEVARASKELSEIGIKNQILVINGVL-ENYDDDL 249
Cdd:TIGR00345 158 mgageddealekLEELKEQIEAAREILSDPERTSFVLVVIPEKMSLYESERAHKELAKYGIKVDAVIVNQVLpENAQDEF 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 696223624  250 SENIFNKQKLALENMPEMLTEFDTYTIALRSYNITGIDSIRNLLK 294
Cdd:TIGR00345 238 CQARWELQQKYLKQIPEKFADLPVAEVPLQKEEMVGLEALKRLSK 282
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 12-289 1.69e-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: 199.88  E-value: 1.69e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624   12 TKYLFFTGKGGVGKTSTACATAVALADEGKKVLLISTDPASNLQDVFETELdgKAKPIKGVDNLEVINLDPLEAAHNYKE 91
Cdd:pfam02374   1 MRWIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQKF--GHEPTKVKENLSAMEIDPNMELEEYWQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624   92 SVVGPFRGKL-PDSVIENMEEQL-SGSCTVEIAAFNEFSNFITNSklntDYNHIIFDTAPTGHTLRMLQLPSAWTDFISE 169
Cdd:pfam02374  79 EVQKYMNALLgLRMLEGILAEELaSLPGIDEAASFDEFKKYMDEG----EYDVVVFDTAPTGHTLRLLSLPTVLGWYLEK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  170 ---------------STHGASCLGQ-LSGLDTKKETYKKAVENLSDKSLTTLVLVTRSDKTPLNEVARASKELSEIGIKN 233
Cdd:pfam02374 155 ivklknqigplakpfLGMGGVSIPEaLESLEETKERIERAREILTDPERTSFRLVCIPEKMSLYETERAIQYLAKYGIDV 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 696223624  234 QILVINGVL-ENYDDDLS--ENIFNKQKLALENMPEMLTEFDTYTIALRSYNITGIDSI 289
Cdd:pfam02374 235 DAVIVNQVLpENVQENCPfcEARKKIQQKYLDEIEELFSDFPVAKLPLLPEEVVGLEKL 293
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 325-570 2.10e-50

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: 174.23  E-value: 2.10e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLATTDPADHI----------KFMIDSSSGISMSHIDEKEELKKYQDEV 394
Cdd:cd02035    1 RIIFFGGKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLsdafgqklggETPVKGAPNLWAMEIDPEEALEEYWEEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 395 LGNARK--TMSEDDVAYIEEDLRSPCTQEIAVFRAFAELVEKADDEIVVIDTAPTGHtlllldstlsyhqevqrTQG--Q 470
Cdd:cd02035   81 KELLAQylRLPGLDEVYAEELLSLPGMDEAAAFDELREYVESGEYDVIVFDTAPTGH-----------------TLRllS 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 471 VPesVKNLLPRLR-GEETEVLIVSLAEATPFYEAYRLEEDLTRASIHTNWWIVNSSLYKANPSNKMLSAKVNEEVKWINK 549
Cdd:cd02035  144 LP--LEQVRELLRdPERTTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVNQVLPEEADDSFFLRRRRQQQKYLDEI 221

                        250       260
                 ....*....|....*....|.
gi 696223624 550 ILDHTSGKLAVIEWTKEDLCG 570
Cdd:cd02035  222 EELFEPLPVVEVPLLPEEVRG 242
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
322-550 1.37e-33

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 129.94  E-value: 1.37e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 322 NNRKVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLATTDPADHIK--FMIDSSSG---ISMSH-----IDEKEELKKYQ 391
Cdd:COG0003    1 DMTRIIFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGdvLGTELGNEpteVAVPNlyaleIDPEAELEEYW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 392 DEVLGNARKTMSEDDVAYIEEDLrsPCTQEIAVFRAFAELVEKADDEIVVIDTAPTGH-----------------TLLLL 454
Cdd:COG0003   81 ERVRAPLRGLLPSAGVDELAESL--PGTEELAALDELLELLEEGEYDVIVVDTAPTGHtlrllslpellgwwldrLLKLR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 455 DSTLSYHQEVQRTQGQVPESVKNLLPRLR------------GEETEVLIVSLAEATPFYEAYRLEEDLTRASIHTNWWIV 522
Cdd:COG0003  159 RKASGLGRPLAGILGLPDDPVLEGLEELRerlerlrellrdPERTSFRLVTNPERLAIAETRRALEELALYGIPVDGLVV 238

                        250       260
                 ....*....|....*....|....*...
gi 696223624 523 NSSLYKANPSNKMLSAKVNEEVKWINKI 550
Cdd:COG0003  239 NRVLPEEADDDAFLAARRERQQEYLAEI 266
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 325-550 4.19e-25

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: 105.51  E-value: 4.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLATTDPADHIKFMIDSSSG---------ISMSHIDEKEELKKYQDEVL 395
Cdd:pfam02374   2 RWIFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQKFGheptkvkenLSAMEIDPNMELEEYWQEVQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  396 GNARKTMSEDDVAYIEEDLRS--PCTQEIAVFRAFAELVEKADDEIVVIDTAPTGHT---LLLLDSTLSYHQEVQRTQGQ 470
Cdd:pfam02374  82 KYMNALLGLRMLEGILAEELAslPGIDEAASFDEFKKYMDEGEYDVVVFDTAPTGHTlrlLSLPTVLGWYLEKIVKLKNQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  471 VPESVKNLLP------------------RLRG--------EETEVLIVSLAEATPFYEAYRLEEDLTRASIHTNWWIVNs 524
Cdd:pfam02374 162 IGPLAKPFLGmggvsipealesleetkeRIERareiltdpERTSFRLVCIPEKMSLYETERAIQYLAKYGIDVDAVIVN- 240

                         250       260
                  ....*....|....*....|....*...
gi 696223624  525 SLYKANPSN--KMLSAKVNEEVKWINKI 550
Cdd:pfam02374 241 QVLPENVQEncPFCEARKKIQQKYLDEI 268
GET3_arsA_TRC40 TIGR00345
transport-energizing ATPase, TRC40/GET3/ArsA family; Members of this family are ATPases that ...
 340-570 1.50e-13

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: 71.35  E-value: 1.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  340 IASSVALKLSKLGKKVHLATTDPA-----------DHIKFMIDSSSGISMSHIDEKEELKKYQDEVLGNARK--TMSEDD 406
Cdd:TIGR00345   1 ISAATAIRLAEQGKKVLLVSTDPAhslsdvfeqeiGHTPTKVTGVENLSAVEIDPQAALEEYRAKLVEQIKGnlPDGDML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  407 VAYIEEDLRSPCTQEIAVFRAFAELVEKADDE--IVVIDTAPTGH----------------------TLLLLDSTLSYHQ 462
Cdd:TIGR00345  81 GDQLEGAALSPGIDEIAAFDEFLKHMTDAENEfdVVIFDTAPTGHtlrllqlpevlssflekfikirSKLGPMAKLFMGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  463 EVQRTQGQVPESVKNLLPRLR-----GEETEVLIVSLAEATPFYEAYRLEEDLTRASIHTNWWIVNSSLYKaNPSNKMLS 537
Cdd:TIGR00345 161 GEDDEALEKLEELKEQIEAAReilsdPERTSFVLVVIPEKMSLYESERAHKELAKYGIKVDAVIVNQVLPE-NAQDEFCQ 239

                         250       260       270
                  ....*....|....*....|....*....|....
gi 696223624  538 AKVNEEVKWINKILDHTSGK-LAVIEWTKEDLCG 570
Cdd:TIGR00345 240 ARWELQQKYLKQIPEKFADLpVAEVPLQKEEMVG 273
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 19-241 7.13e-12

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: 66.36  E-value: 7.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  19 GKGGVGKTSTACATAVALADEGKKVLLISTD-------------PASNLQDVF--ETELDGKAKPIkGVDNLEVInldpl 83
Cdd:COG0489  100 GKGGEGKSTVAANLALALAQSGKRVLLIDADlrgpslhrmlgleNRPGLSDVLagEASLEDVIQPT-EVEGLDVL----- 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  84 eaahnykesvvgpFRGKLPDSvienmeeqlsgscTVEIAAFNEFSNFITNskLNTDYNHIIFDTAP-TGHT-LRMLQlps 161
Cdd:COG0489  174 -------------PAGPLPPN-------------PSELLASKRLKQLLEE--LRGRYDYVIIDTPPgLGVAdATLLA--- 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 162 awtdfisesthgasclgqlsgldtkketykkavenlsdKSLTTLVLVTRSDKTPLNEVARASKELSEIGIKNQILVINGV 241
Cdd:COG0489  223 --------------------------------------SLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNMV 264
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 14-58 1.70e-10

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: 58.71  E-value: 1.70e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 696223624  14 YLFFTGKGGVGKTSTACATAVALADEGKKVLLISTDPASNLQDVF 58
Cdd:cd02042    3 IAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL 47
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 16-54 2.00e-09

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


Pssm-ID: 440805 [Multi-domain]  Cd Length: 253  Bit Score: 58.33  E-value: 2.00e-09
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 696223624  16 FFTGKGGVGKTSTACATAVALADEGKKVLLISTDPASNL 54
Cdd:COG1192    6 VANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNL 44
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 19-155 2.13e-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: 58.13  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624   19 GKGGVGKTSTACATAVALADEGKKVLLISTDPASNLqdvfeTELDGKAKPIKGVDNLEV------INLDPLEAAHNYKES 92
Cdd:pfam01656   6 TKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNN-----SSVEGLEGDIAPALQALAeglkgrVNLDPILLKEKSDEG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 696223624   93 VVgpfrgklpDSVIENMEEQLSGSCTVEIAAFNEFSNFITNSKLNTDYnhIIFDTAPT-GHTLR 155
Cdd:pfam01656  81 GL--------DLIPGNIDLEKFEKELLGPRKEERLREALEALKEDYDY--VIIDGAPGlGELLR 134
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 13-49 3.45e-08

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: 51.66  E-value: 3.45e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 696223624  13 KYLFFTG-KGGVGKTSTACATAVALADEGKKVLLISTD 49
Cdd:cd01983    1 RVIAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 17-54 6.04e-08

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 54.02  E-value: 6.04e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 696223624  17 FTGKGGVGKTSTACATAVALADEGKKVLLISTDPASNL 54
Cdd:COG3640    5 VAGKGGVGKTTLSALLARYLAEKGKPVLAVDADPNANL 42
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 20-150 6.44e-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: 52.59  E-value: 6.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624   20 KGGVGKTSTACATAVALADEGKKVLLISTDPASNLQDVFETELDGKAKPIkgvdnLEVINLDpleaaHNYKESVVGPFRG 99
Cdd:pfam13614  10 KGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTI-----YELLIGE-----CNIEEAIIKTVIE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 696223624  100 KLpDSVIENMEeqLSGsctVEIAAFN-EFSNFITNSKLNT---DYNHIIFDTAPT 150
Cdd:pfam13614  80 NL-DLIPSNID--LAG---AEIELIGiENRENILKEALEPvkdNYDYIIIDCPPS 128
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 17-77 1.04e-07

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 53.62  E-value: 1.04e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 696223624  17 FTGKGGVGKTSTACATAVALADEGKKVLLISTDP----ASNLQDV-FETELDGKAKpiKGVDNLEV 77
Cdd:PRK13230   6 FYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPkadcTRNLVGEkIPTVLDVLRE--KGIDNLGL 69
ParA_partition NF041546
ParA family partition ATPase;
20-73 5.64e-07

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 50.24  E-value: 5.64e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 696223624  20 KGGVGKTSTACATAVALADEGKKVLLISTDPASNLQDVFETELDGKAKPIKGVD 73
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPVVGLA 61
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 326-446 6.41e-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: 50.42  E-value: 6.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  326 VIFTMGKGGVGKTTIASSVALKLSKLGKKVhlattdpadhikFMIDSSSGISMSHIDEKE-ELKKYQDEVLGNARKTMSE 404
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRV------------LLIDLDPQSNNSSVEGLEgDIAPALQALAEGLKGRVNL 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 696223624  405 DDVAYIEEDLRS-----PCTQEIAVF--------------RAFAELVEKADdeIVVIDTAP 446
Cdd:pfam01656  69 DPILLKEKSDEGgldliPGNIDLEKFekellgprkeerlrEALEALKEDYD--YVIIDGAP 127
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 17-50 6.43e-07

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: 50.97  E-value: 6.43e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 696223624  17 FTGKGGVGKTSTACATAVALADEGKKVLLISTDP 50
Cdd:cd02040    5 IYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDP 38
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
17-68 6.79e-07

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 50.91  E-value: 6.79e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 696223624   17 FTGKGGVGKTSTACATAVALADEGKKVLLISTDPASnlqDVFETELDGKAKP 68
Cdd:pfam00142   5 IYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKA---DSTRLLLGGKLQP 53
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 696223624  320 VKNnrkVIFTM-GKGGVGKTTIASSVALKLSKLGKKV 355
Cdd:pfam10609   2 VKH---VIAVAsGKGGVGKSTVAVNLALALARLGYKV 35
chlL CHL00072
photochlorophyllide reductase subunit L
 19-50 1.95e-06

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 49.74  E-value: 1.95e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 696223624  19 GKGGVGKTSTACATAVALADEGKKVLLISTDP 50
Cdd:CHL00072   7 GKGGIGKSTTSCNISIALARRGKKVLQIGCDP 38
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 325-378 2.26e-06

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


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 47.15  E-value: 2.26e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 696223624 325 KVI-FTMGKGGVGKTTIASSVALKLSKLGKKVHLATTDP--------ADHIkfMIDSSSGISM 378
Cdd:cd02042    1 KVIaVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPqgsltswlYDYI--LIDTPPSLGL 61
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 19-49 2.44e-06

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 49.29  E-value: 2.44e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 696223624  19 GKGGVGKTSTACATAVALADEGKKVLLISTD 49
Cdd:COG2894   10 GKGGVGKTTTTANLGTALALLGKKVVLIDAD 40
PRK12724 PRK12724
flagellar biosynthesis regulator FlhF; Provisional
 257-449 2.46e-06

flagellar biosynthesis regulator FlhF; Provisional


Pssm-ID: 183703 [Multi-domain]  Cd Length: 432  Bit Score: 49.96  E-value: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 257 QKLALENMPEMLTEFDTYTIALRsynITGIDSIRN---LLKKDQINEQKVEVKGKLFnlddvvSDLVKNNRKVIFTMGKG 333
Cdd:PRK12724 162 ERLVREGMSQSYVEEMASKLEER---LSPVDQGRNhnvTERAVTYLEERVSVDSDLF------SGTGKNQRKVVFFVGPT 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 334 GVGKTTIASSVALKLS-KLGKKVHLATTDPadhikfmidsssgismSHIDEKEELKKYQDevlgnarkTMSEDdvAYIEE 412
Cdd:PRK12724 233 GSGKTTSIAKLAAKYFlHMGKSVSLYTTDN----------------YRIAAIEQLKRYAD--------TMGMP--FYPVK 286

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 696223624 413 DLRSpctqeiavfraFAELVEKADDEIVVIDTAPTGH 449
Cdd:PRK12724 287 DIKK-----------FKETLARDGSELILIDTAGYSH 312
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 19-50 3.08e-06

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: 48.83  E-value: 3.08e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 696223624  19 GKGGVGKTSTACATAVALADEGKKVLLISTDP 50
Cdd:cd02032    7 GKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDP 38
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 19-109 4.86e-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: 47.88  E-value: 4.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  19 GKGGVGKTSTACATAVALADEGKKVLLISTDPAS-------NLQDVFETELDGKAKPIKgVDNLEVINLDPLeaaHNYKE 91
Cdd:cd02037    8 GKGGVGKSTVAVNLALALAKKGYKVGLLDADIYGpsiprllGVEGKPLHQSEEGIVPVE-VGGIKVMSIGFL---LPEDD 83

                         90
                 ....*....|....*...
gi 696223624  92 SVVgpFRGKLPDSVIENM 109
Cdd:cd02037   84 AVI--WRGPMKSGAIKQF 99
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 17-76 5.38e-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: 48.08  E-value: 5.38e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624  17 FTGKGGVGKTSTACATAVALADEGKKVLLISTDPASNLQDVFETELDgKAKPIKGVDNLE 76
Cdd:cd02034    5 VAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVE-KLPLIKTIGDIR 63
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 19-49 6.02e-06

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: 47.58  E-value: 6.02e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 696223624  19 GKGGVGKTSTACATAVALADEGKKVLLISTD 49
Cdd:cd02036    8 GKGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 19-78 6.94e-06

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: 47.56  E-value: 6.94e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 696223624  19 GKGGVGKTSTACATAVALADEGKKVLLISTD-------------PASNLQDVFETELDGKAKPIKGVDNLEVI 78
Cdd:cd02038    8 GKGGVGKTNVSANLALALSKLGKRVLLLDADlglanldillglaPKKTLGDVLKGRVSLEDIIVEGPEGLDII 80
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 325-361 1.16e-05

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 46.97  E-value: 1.16e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 696223624 325 KVI-FTMGKGGVGKTTIASSVALKLSKLGKKVHLATTD 361
Cdd:COG2894    3 KVIvVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD 40
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 19-50 1.17e-05

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 47.26  E-value: 1.17e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 696223624  19 GKGGVGKTSTACATAVALADEGKKVLLISTDP 50
Cdd:PRK13185   9 GKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDP 40
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 19-49 1.89e-05

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


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 46.29  E-value: 1.89e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 696223624   19 GKGGVGKTSTACATAVALADEGKKVLLISTD 49
Cdd:pfam10609  11 GKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 329-355 2.19e-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: 2.19e-05
                         10        20
                 ....*....|....*....|....*..
gi 696223624 329 TMGKGGVGKTTIASSVALKLSKLGKKV 355
Cdd:cd02038    6 TSGKGGVGKTNVSANLALALSKLGKRV 32
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 325-444 2.25e-05

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 46.31  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKVhLAT-TDPADH----IKFMIDSSSGISMSHIdeKEELKKYqdevLGNAR 399
Cdd:COG3640    1 MKIAVAGKGGVGKTTLSALLARYLAEKGKPV-LAVdADPNANlaeaLGLEVEADLIKPLGEM--RELIKER----TGAPG 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 400 KTMSED--DVAYIEEDlrspCTQEI-----------------------AVFRAFAELVEKADDEIVVIDT 444
Cdd:COG3640   74 GGMFKLnpKVDDIPEE----YLVEGdgvdllvmgtieeggsgcycpenALLRALLNHLVLGNYEYVVVDM 139
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 309-446 2.56e-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: 46.33  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 309 LFNLDDVVSDLVKNNRKVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLATTD---PADHIKFMIDSSSGISmSHIDEKE 385
Cdd:COG0489   78 ALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADlrgPSLHRMLGLENRPGLS-DVLAGEA 156

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 696223624 386 ELkkyqDEVLgnarKTMSEDDVAYIEEDLRSPCTQEIAVFRAFAELVEKADDE--IVVIDTAP 446
Cdd:COG0489  157 SL----EDVI----QPTEVEGLDVLPAGPLPPNPSELLASKRLKQLLEELRGRydYVIIDTPP 211
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 324-361 2.56e-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: 46.04  E-value: 2.56e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 696223624 324 RKVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLATTD 361
Cdd:cd02036    1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDAD 38
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 325-355 2.82e-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: 2.82e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 696223624 325 KVIFTM-GKGGVGKTTIASSVALKLSKLGKKV 355
Cdd:cd02037    1 HIIAVLsGKGGVGKSTVAVNLALALAKKGYKV 32
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 324-366 2.88e-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: 43.19  E-value: 2.88e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 696223624 324 RKVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLATTDpaDHI 366
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD--DYV 41
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 17-50 4.56e-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: 45.43  E-value: 4.56e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 696223624  17 FTGKGGVGKTSTACATAVALADEGKKVLLISTDP 50
Cdd:cd02117    5 VYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDP 38
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 323-361 9.78e-05

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: 44.25  E-value: 9.78e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 696223624  323 NRKVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLATTD 361
Cdd:TIGR01968   1 ARVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD 39
ParA_partition NF041546
ParA family partition ATPase;
332-362 1.26e-04

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 43.31  E-value: 1.26e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 696223624 332 KGGVGKTTIASSVALKLSKLGKKVHLATTDP 362
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADP 38
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 325-362 1.28e-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: 43.89  E-value: 1.28e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 696223624 325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLATTDP 362
Cdd:cd02117    1 ESIVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDP 38
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 18-61 1.55e-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: 43.57  E-value: 1.55e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 696223624   18 TGKGGVGKTSTACATAVALADEGKKVLLISTDPA-SNLQDVFETE 61
Cdd:TIGR01969   7 SGKGGTGKTTITANLGVALAKLGKKVLALDADITmANLELILGME 51
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 325-447 1.86e-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: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696223624 325 KVI-FTMGKGGVGKTTIASSVALKLSKLGKKVHLATTDP-AdhikfmiDSSSGISMSHIDEKEELKK--YQDEVLGNA-R 399
Cdd:COG1192    2 KVIaVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPqG-------NLTSGLGLDPDDLDPTLYDllLDDAPLEDAiV 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 696223624 400 KTMSE--------DDVAYIEEDLRSPCTQEIAVFRAFAELVEKADdeIVVIDTAPT 447
Cdd:COG1192   75 PTEIPgldlipanIDLAGAEIELVSRPGRELRLKRALAPLADDYD--YILIDCPPS 128
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 18-49 1.87e-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: 1.87e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 696223624   18 TGKGGVGKTSTACATAVALADEGKKVLLISTD 49
Cdd:TIGR01968   8 SGKGGVGKTTTTANLGTALARLGKKVVLIDAD 39
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 7-68 2.58e-04

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: 43.28  E-value: 2.58e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 696223624   7 PDIKLTKYLFFTGKGGVGKTSTACATAVALADEGKKVLLISTDPASnlqDVFETELDGKAKP 68
Cdd:cd02033   26 PPTKETQIIAIYGKGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKS---DTTSLLFGGKACP 84
PHA02518 PHA02518
ParA-like protein; Provisional
 20-50 2.98e-04

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 42.53  E-value: 2.98e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 696223624  20 KGGVGKTSTACATAVALADEGKKVLLISTDP 50
Cdd:PHA02518   9 KGGAGKTTVATNLASWLHADGHKVLLVDLDP 39
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 324-361 3.10e-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: 42.80  E-value: 3.10e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 696223624  324 RKVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLATTD 361
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDAD 38
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
18-49 4.88e-04

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 42.72  E-value: 4.88e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 696223624  18 TGKGGVGKTSTACATAVALADEGKKVLLISTD 49
Cdd:PRK11670 114 SGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 325-362 6.47e-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: 41.03  E-value: 6.47e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 696223624  325 KVI-FTMGKGGVGKTTIASSVALKLSKLGKKVHLATTDP 362
Cdd:pfam13614   2 KVIaIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDP 40
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 325-362 6.90e-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: 41.90  E-value: 6.90e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 696223624 325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLATTDP 362
Cdd:cd02032    1 LVIAVYGKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDP 38
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 16-46 8.67e-04

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: 41.64  E-value: 8.67e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 696223624  16 FFTGKGGVGKTSTACATAVALADE-GKKVLLI 46
Cdd:COG4963  107 VVGAKGGVGATTLAVNLAWALAREsGRRVLLV 138
minD CHL00175
septum-site determining protein; Validated
 324-361 9.36e-04

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 41.29  E-value: 9.36e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 696223624 324 RKVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLATTD 361
Cdd:CHL00175  16 RIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDAD 53
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 325-355 1.23e-03

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 41.10  E-value: 1.23e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 696223624 325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKV 355
Cdd:PRK13185   3 LVLAVYGKGGIGKSTTSSNLSAAFAKLGKKV 33
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
 325-362 1.46e-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: 39.63  E-value: 1.46e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 696223624 325 KVIFTM-GKGGVGKTTIASSVALKLSKLGKKVHLATTDP 362
Cdd:cd05386    1 KIHFVLqGKGGVGKSVIASLLAQYLIDKGQPVSCIDTDP 39
PHA02518 PHA02518
ParA-like protein; Provisional
 332-362 1.54e-03

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 40.22  E-value: 1.54e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 696223624 332 KGGVGKTTIASSVALKLSKLGKKVHLATTDP 362
Cdd:PHA02518   9 KGGAGKTTVATNLASWLHADGHKVLLVDLDP 39
PRK10818 PRK10818
septum site-determining protein MinD;
18-49 1.99e-03

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 40.31  E-value: 1.99e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 696223624  18 TGKGGVGKTSTACATAVALADEGKKVLLISTD 49
Cdd:PRK10818   9 SGKGGVGKTTSSAAIATGLAQKGKKTVVIDFD 40
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 331-364 2.33e-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: 2.33e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 696223624 331 GKGGVGKTTIASSVALKLSKLGKKVHLATTDP-AD 364
Cdd:cd02040    7 GKGGIGKSTTASNLSAALAEMGKKVLHVGCDPkAD 41
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 20-55 4.21e-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: 39.25  E-value: 4.21e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 696223624   20 KGGVGKTSTACATAVALADEGKKVLLISTDPASNLQ 55
Cdd:TIGR03371  10 RGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLR 45
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
 325-361 8.14e-03

GTPase domain similar to the signal recognition particle subunit 54; 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 cognate 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: 349769 [Multi-domain]  Cd Length: 193  Bit Score: 37.74  E-value: 8.14e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 696223624 325 KVIFTMGKGGVGKTTIASSVALKLSKLGKKVHLATTD 361
Cdd:cd03115    1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAAD 37
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 324-362 8.40e-03

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 38.60  E-value: 8.40e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 696223624 324 RKVIFtMGKGGVGKTTIASSVALKLSKLGKKVHLATTDP 362
Cdd:PRK13230   2 RKFCF-YGKGGIGKSTTVCNIAAALAESGKKVLVVGCDP 39
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
 13-49 8.85e-03

GTPase domain similar to the signal recognition particle subunit 54; 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 cognate 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: 349769 [Multi-domain]  Cd Length: 193  Bit Score: 37.74  E-value: 8.85e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 696223624  13 KYLFFTGKGGVGKTSTACATAVALADEGKKVLLISTD 49
Cdd:cd03115    1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAAD 37
 
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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