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Conserved domains on  [gi|146387067|pdb|2OXR|A]
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Chain A, ATP(GTP)binding protein

Protein Classification

PRK13768 family protein( domain architecture ID 10014406)

PRK13768 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13768 PRK13768
GTPase; Provisional
15-262 2.81e-128

GTPase; Provisional


:

Pssm-ID: 237498 [Multi-domain]  Cd Length: 253  Bit Score: 363.81  E-value: 2.81e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A        15 MIVVFVGTAGSGKTTLTGEFGRYLEDN-YKVAYVNLDTGVKELPYEPSIDVREFVTVEEIMRE-GYGPNGAIVESYDRLM 92
Cdd:PRK13768   3 YIVFFLGTAGSGKTTLTKALSDWLEEQgYDVAIVNLDPAVEYLPYTPDFDVRDYVTAREIMKKyGLGPNGALIASVDLLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A        93 EKFNEYLNKILRLEKenDYVLIDTPGQMETFLFHEFGVRLMENLP---YPLVVYISDPEILKKPNDYCFVRFFALLIDLR 169
Cdd:PRK13768  83 TKADEIKEEIESLDA--DYVLVDTPGQMELFAFRESGRKLVERLSgssKSVVVFLIDAVLAKTPSDFVSLLLLALSVQLR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       170 LGATTIPALNKVDLLSEEEKERHRKYFEDIDYLTARLKLDPSMQGLMAYKMCSMMTEVLPPVRVLYLSAKTREGFEDLET 249
Cdd:PRK13768 161 LGLPQIPVLNKADLLSEEELERILKWLEDPEYLLEELKLEKGLQGLLSLELLRALEETGLPVRVIPVSAKTGEGFDELYA 240
                        250
                 ....*....|...
2OXR_A       250 LAYEHYCTCGDLT 262
Cdd:PRK13768 241 AIQEVFCGGEDLT 253
 
Name Accession Description Interval E-value
PRK13768 PRK13768
GTPase; Provisional
15-262 2.81e-128

GTPase; Provisional


Pssm-ID: 237498 [Multi-domain]  Cd Length: 253  Bit Score: 363.81  E-value: 2.81e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A        15 MIVVFVGTAGSGKTTLTGEFGRYLEDN-YKVAYVNLDTGVKELPYEPSIDVREFVTVEEIMRE-GYGPNGAIVESYDRLM 92
Cdd:PRK13768   3 YIVFFLGTAGSGKTTLTKALSDWLEEQgYDVAIVNLDPAVEYLPYTPDFDVRDYVTAREIMKKyGLGPNGALIASVDLLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A        93 EKFNEYLNKILRLEKenDYVLIDTPGQMETFLFHEFGVRLMENLP---YPLVVYISDPEILKKPNDYCFVRFFALLIDLR 169
Cdd:PRK13768  83 TKADEIKEEIESLDA--DYVLVDTPGQMELFAFRESGRKLVERLSgssKSVVVFLIDAVLAKTPSDFVSLLLLALSVQLR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       170 LGATTIPALNKVDLLSEEEKERHRKYFEDIDYLTARLKLDPSMQGLMAYKMCSMMTEVLPPVRVLYLSAKTREGFEDLET 249
Cdd:PRK13768 161 LGLPQIPVLNKADLLSEEELERILKWLEDPEYLLEELKLEKGLQGLLSLELLRALEETGLPVRVIPVSAKTGEGFDELYA 240
                        250
                 ....*....|...
2OXR_A       250 LAYEHYCTCGDLT 262
Cdd:PRK13768 241 AIQEVFCGGEDLT 253
GPN1 cd17870
GPN-loop GTPase 1; GPN-loop GTPase 1 (GPN1, also kown as MBD2-interacting protein or MBDin, ...
15-253 5.90e-103

GPN-loop GTPase 1; GPN-loop GTPase 1 (GPN1, also kown as MBD2-interacting protein or MBDin, RNAPII-associated protein 4, and XPA-binding protein 1) is a GTPase is required for nuclear targeting of RNA polymerase II. It forms heterodimers with GPN3.


Pssm-ID: 349779 [Multi-domain]  Cd Length: 241  Bit Score: 299.10  E-value: 5.90e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       15 MIVVFVGTAGSGKTTLTGEFGRYLEDN-YKVAYVNLDTGVKELPYEPSIDVREFVTVEEIMRE-GYGPNGAIVESYDRLM 92
Cdd:cd17870   1 VVIIVVGMAGSGKTTFVQRLNAYLHDNkKPPYVINLDPAVKSLPYPPNIDIRDTVNYKEVMKQyGLGPNGAIVTSLNLFA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       93 EKFNEYLNKILRLEKENDYVLIDTPGQMETFLFHEFGVRLMENLPY---PLVVYISDPEILKKPNDYCFVRFFALLIDLR 169
Cdd:cd17870  81 TKFDQVINLIEKRASELDYVIIDTPGQIEVFTWSASGSIITEALASsfpTVVVYVVDTPRCTSPITFMSNMLYACSILYK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A      170 LGATTIPALNKVDLLSEeekERHRKYFEDIDYLTARLKLDPSMQGLMAYKMCSMMTEVLPPVRVLYLSAKTREGFEDLET 249
Cdd:cd17870 161 TKLPFILVFNKTDVVSH---DFAIEWMEDFESFQDALKEDSSYMSSLSRSMSLVLDEFYNNLRVVGVSAKTGEGFEELLE 237

                ....
2OXR_A      250 LAYE 253
Cdd:cd17870 238 AIDE 241
ATP_bind_1 pfam03029
Conserved hypothetical ATP binding protein; Members of this family are found in a range of ...
19-257 3.66e-72

Conserved hypothetical ATP binding protein; Members of this family are found in a range of archaea and eukaryotes and have hypothesized ATP binding activity.


Pssm-ID: 397252 [Multi-domain]  Cd Length: 238  Bit Score: 220.71  E-value: 3.66e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A         19 FVGTAGSGKTTLTGEFGRYLED-NYKVAYVNLDTGVKELPYEPSIDVREFVTVEEIMRE-GYGPNGAIVESYDRLMEKFN 96
Cdd:pfam03029   1 VVGPAGSGKTTFVGALSEILPLrGRPVYVVNLDPAAENLPYPADIDIRELITVADVMEDyGLGPNGALTVAMDFGRITLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A         97 EYLNkilRLEKENDYVLIDTPGQMETFLFHEFGVRLMENLPY---PLVVYISDPEILKKPNDYCFVRFFALLIDLRLGAT 173
Cdd:pfam03029  81 WLDE---ELKREDDYYLFDTPGQIELFTHWDSLAIIVEALESrgaLGAVYLVDTRRLTDPTDFFSGLLYALSIMLRLGLP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A        174 TIPALNKVDLLSEeekERHRKYFEDIDYLTARLKLDPSMQGLMAYKMCSMMTEVLPPVRVLYLSAKTREGFEDLETLAYE 253
Cdd:pfam03029 158 FVVALNKFDLLSL---EFALKWFTDPEDLQLLLELDDGKYRKLNEAIREALDLFYLVPVFLPDARERGESMEDLLTLIDE 234

                  ....
2OXR_A        254 HYCT 257
Cdd:pfam03029 235 ALQY 238
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
12-262 1.62e-23

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 93.51  E-value: 1.62e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       12 MASMIVVFVGTAGSGKTTLTGEFgrylednykvayvnldtgvkelpyepsidVREFVTVEEImregYGPNGAIVEsydrl 91
Cdd:COG1100   1 MGEKKIVVVGTGGVGKTSLVNRL-----------------------------VGDIFSLEKY----LSTNGVTID----- 42
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       92 mekfneylNKILRLEKEN-DYVLIDTPGQMEtflFHEFGVRLMENLPYP-LVVYISDPEIlkkPNDYCFVRFFALLI-DL 168
Cdd:COG1100  43 --------KKELKLDGLDvDLVIWDTPGQDE---FRETRQFYARQLTGAsLYLFVVDGTR---EETLQSLYELLESLrRL 108
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A      169 RLGATTIPALNKVDLLSEEEKerhrkyfEDIDYLTARLKLDpsmqglmaykmcsmmtevlPPVRVLYLSAKTREGFEDLE 248
Cdd:COG1100 109 GKKSPIILVLNKIDLYDEEEI-------EDEERLKEALSED-------------------NIVEVVATSAKTGEGVEELF 162
                       250
                ....*....|....
2OXR_A      249 TLAYEHYCTCGDLT 262
Cdd:COG1100 163 AALAEILRGEGDSL 176
SRP54 smart00962
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ...
16-118 6.85e-05

SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.


Pssm-ID: 214940  Cd Length: 197  Bit Score: 42.78  E-value: 6.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A          16 IVVFVGTAGSGKTTLTGEFGRYL--EDNYKVAYVNLDT----GVKELpyepsidvREFVTVEEIMREGYGPNGAIVESYD 89
Cdd:smart00962   3 VILLVGPNGVGKTTTIAKLAARLklKGGKKVLLVAADTfraaAVEQL--------KTYAEILGVVPVAGGEGADPVAVAK 74
                           90       100
                   ....*....|....*....|....*....
2OXR_A          90 RLMEKFNeylnkilrlEKENDYVLIDTPG 118
Cdd:smart00962  75 DAVELAK---------ARGYDVVLIDTAG 94
 
Name Accession Description Interval E-value
PRK13768 PRK13768
GTPase; Provisional
15-262 2.81e-128

GTPase; Provisional


Pssm-ID: 237498 [Multi-domain]  Cd Length: 253  Bit Score: 363.81  E-value: 2.81e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A        15 MIVVFVGTAGSGKTTLTGEFGRYLEDN-YKVAYVNLDTGVKELPYEPSIDVREFVTVEEIMRE-GYGPNGAIVESYDRLM 92
Cdd:PRK13768   3 YIVFFLGTAGSGKTTLTKALSDWLEEQgYDVAIVNLDPAVEYLPYTPDFDVRDYVTAREIMKKyGLGPNGALIASVDLLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A        93 EKFNEYLNKILRLEKenDYVLIDTPGQMETFLFHEFGVRLMENLP---YPLVVYISDPEILKKPNDYCFVRFFALLIDLR 169
Cdd:PRK13768  83 TKADEIKEEIESLDA--DYVLVDTPGQMELFAFRESGRKLVERLSgssKSVVVFLIDAVLAKTPSDFVSLLLLALSVQLR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       170 LGATTIPALNKVDLLSEEEKERHRKYFEDIDYLTARLKLDPSMQGLMAYKMCSMMTEVLPPVRVLYLSAKTREGFEDLET 249
Cdd:PRK13768 161 LGLPQIPVLNKADLLSEEELERILKWLEDPEYLLEELKLEKGLQGLLSLELLRALEETGLPVRVIPVSAKTGEGFDELYA 240
                        250
                 ....*....|...
2OXR_A       250 LAYEHYCTCGDLT 262
Cdd:PRK13768 241 AIQEVFCGGEDLT 253
GPN1 cd17870
GPN-loop GTPase 1; GPN-loop GTPase 1 (GPN1, also kown as MBD2-interacting protein or MBDin, ...
15-253 5.90e-103

GPN-loop GTPase 1; GPN-loop GTPase 1 (GPN1, also kown as MBD2-interacting protein or MBDin, RNAPII-associated protein 4, and XPA-binding protein 1) is a GTPase is required for nuclear targeting of RNA polymerase II. It forms heterodimers with GPN3.


Pssm-ID: 349779 [Multi-domain]  Cd Length: 241  Bit Score: 299.10  E-value: 5.90e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       15 MIVVFVGTAGSGKTTLTGEFGRYLEDN-YKVAYVNLDTGVKELPYEPSIDVREFVTVEEIMRE-GYGPNGAIVESYDRLM 92
Cdd:cd17870   1 VVIIVVGMAGSGKTTFVQRLNAYLHDNkKPPYVINLDPAVKSLPYPPNIDIRDTVNYKEVMKQyGLGPNGAIVTSLNLFA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       93 EKFNEYLNKILRLEKENDYVLIDTPGQMETFLFHEFGVRLMENLPY---PLVVYISDPEILKKPNDYCFVRFFALLIDLR 169
Cdd:cd17870  81 TKFDQVINLIEKRASELDYVIIDTPGQIEVFTWSASGSIITEALASsfpTVVVYVVDTPRCTSPITFMSNMLYACSILYK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A      170 LGATTIPALNKVDLLSEeekERHRKYFEDIDYLTARLKLDPSMQGLMAYKMCSMMTEVLPPVRVLYLSAKTREGFEDLET 249
Cdd:cd17870 161 TKLPFILVFNKTDVVSH---DFAIEWMEDFESFQDALKEDSSYMSSLSRSMSLVLDEFYNNLRVVGVSAKTGEGFEELLE 237

                ....
2OXR_A      250 LAYE 253
Cdd:cd17870 238 AIDE 241
ATP_bind_1 pfam03029
Conserved hypothetical ATP binding protein; Members of this family are found in a range of ...
19-257 3.66e-72

Conserved hypothetical ATP binding protein; Members of this family are found in a range of archaea and eukaryotes and have hypothesized ATP binding activity.


Pssm-ID: 397252 [Multi-domain]  Cd Length: 238  Bit Score: 220.71  E-value: 3.66e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A         19 FVGTAGSGKTTLTGEFGRYLED-NYKVAYVNLDTGVKELPYEPSIDVREFVTVEEIMRE-GYGPNGAIVESYDRLMEKFN 96
Cdd:pfam03029   1 VVGPAGSGKTTFVGALSEILPLrGRPVYVVNLDPAAENLPYPADIDIRELITVADVMEDyGLGPNGALTVAMDFGRITLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A         97 EYLNkilRLEKENDYVLIDTPGQMETFLFHEFGVRLMENLPY---PLVVYISDPEILKKPNDYCFVRFFALLIDLRLGAT 173
Cdd:pfam03029  81 WLDE---ELKREDDYYLFDTPGQIELFTHWDSLAIIVEALESrgaLGAVYLVDTRRLTDPTDFFSGLLYALSIMLRLGLP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A        174 TIPALNKVDLLSEeekERHRKYFEDIDYLTARLKLDPSMQGLMAYKMCSMMTEVLPPVRVLYLSAKTREGFEDLETLAYE 253
Cdd:pfam03029 158 FVVALNKFDLLSL---EFALKWFTDPEDLQLLLELDDGKYRKLNEAIREALDLFYLVPVFLPDARERGESMEDLLTLIDE 234

                  ....
2OXR_A        254 HYCT 257
Cdd:pfam03029 235 ALQY 238
GPN cd17868
GPN-loop GTPase; GPN-loop GTPases are deeply evolutionarily conserved family of three small ...
16-185 9.70e-32

GPN-loop GTPase; GPN-loop GTPases are deeply evolutionarily conserved family of three small GTPases, Gpn1, 2, and 3. They form heterodimers, interact with RNA polymerase II and may function in nuclear import of RNA polymerase II.


Pssm-ID: 349777 [Multi-domain]  Cd Length: 198  Bit Score: 115.88  E-value: 9.70e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       16 IVVFvGTAGSGKTTLT---GEFGRYLEDNYKVayVNLDTGVKELPYEPSIDVREFVTVEEIMRE-GYGPNGAIVESYDRL 91
Cdd:cd17868   3 ILVI-GPAGSGKTTFCknmKEHLRARKRNPYV--INLDPGNINEPLDYDIDIRDLIKYDDIMEElDLGPNGSIVYSLEYF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       92 MEKFNEYLNKILRLEKENDYVLIDTPGQMETFLFHEFGVRLMENLP---YPLV-VYISDPEILKKPNDYCFVRFFALLID 167
Cdd:cd17868  80 EKNFDWFEKKLENEDKNPHYILFDCPGQIELFTHSDSLPKIIERFAswfISVViVNLIDSQFLSDKSKFLSNLLIALSSM 159
                       170
                ....*....|....*...
2OXR_A      168 LRLGATTIPALNKVDLLS 185
Cdd:cd17868 160 FRLELPQINVISKMDLLD 177
GPN2 cd17871
GPN-loop GTPase 2; GPN-loop GTPase 2 (GPN2) is a small GTPase required for proper localization ...
18-185 4.34e-24

GPN-loop GTPase 2; GPN-loop GTPase 2 (GPN2) is a small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). It forms heterodimers with GPN1 or GPN3.


Pssm-ID: 349780  Cd Length: 196  Bit Score: 95.68  E-value: 4.34e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       18 VFVGTAGSGKTTLTGEFGRYLED-NYKVAYVNLDTGVKELPYEPSIDVREFVTVEEIM-REGYGPNGAIVESYDRLMEKF 95
Cdd:cd17871   4 VVIGPPGSGKTTYCKGMQQFLSAlGRKVAVVNLDPANEFLPYPCDVDIRELITVEDVMeELKLGPNGGLLYCMEYLEKNI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       96 NEYLNKILRLEKEndYVLIDTPGQMETFLFHEFG---VRLMENLPYPLV-VYISDPEILKKPNDYCFVRFFALLIDLRLG 171
Cdd:cd17871  84 DWLIDKLKKLKDS--YLIFDCPGQVELYTHHNSLrniLDKLQKWLYRLVaVHLVDSHYCSDPSKFISALLLSLSTMLRLE 161
                       170
                ....*....|....
2OXR_A      172 ATTIPALNKVDLLS 185
Cdd:cd17871 162 LPHVNVLSKIDLVS 175
GPN3 cd17872
GPN-loop GTPase 3; GPN-loop GTPase 3 (GPN3) is a small GTPase that is required for nuclear ...
20-185 9.38e-24

GPN-loop GTPase 3; GPN-loop GTPase 3 (GPN3) is a small GTPase that is required for nuclear targeting of RNA polymerase II. It forms heterodimers with GPN1.


Pssm-ID: 349781 [Multi-domain]  Cd Length: 196  Bit Score: 94.90  E-value: 9.38e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       20 VGTAGSGKTTLTGEFGRYLEDNYK-VAYVNLDTGVKELPYEPSIDVREFVTVEEIMRE-GYGPNGAIV-------ESYDR 90
Cdd:cd17872   6 MGPAGSGKSTYCSTLQEHCETLGRsVHVVNLDPAAEEFEYPVSIDIRDLISLEDVMEElGLGPNGGLVycmeyllENLDW 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       91 LMEKFNEYlnkilrlekENDYVLIDTPGQMETF----LFHEFgVRLMENLPY-PLVVYISDPEILKKPNDYCFVRFFALL 165
Cdd:cd17872  86 LEEQLGDY---------EDDYLIFDCPGQIELYthlpVMKRL-VDALQRWGFrLCAVYLLDSQFISDASKFISGVLSALS 155
                       170       180
                ....*....|....*....|
2OXR_A      166 IDLRLGATTIPALNKVDLLS 185
Cdd:cd17872 156 AMIQLELPHVNVLTKMDLVS 175
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
12-262 1.62e-23

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 93.51  E-value: 1.62e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       12 MASMIVVFVGTAGSGKTTLTGEFgrylednykvayvnldtgvkelpyepsidVREFVTVEEImregYGPNGAIVEsydrl 91
Cdd:COG1100   1 MGEKKIVVVGTGGVGKTSLVNRL-----------------------------VGDIFSLEKY----LSTNGVTID----- 42
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       92 mekfneylNKILRLEKEN-DYVLIDTPGQMEtflFHEFGVRLMENLPYP-LVVYISDPEIlkkPNDYCFVRFFALLI-DL 168
Cdd:COG1100  43 --------KKELKLDGLDvDLVIWDTPGQDE---FRETRQFYARQLTGAsLYLFVVDGTR---EETLQSLYELLESLrRL 108
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A      169 RLGATTIPALNKVDLLSEEEKerhrkyfEDIDYLTARLKLDpsmqglmaykmcsmmtevlPPVRVLYLSAKTREGFEDLE 248
Cdd:COG1100 109 GKKSPIILVLNKIDLYDEEEI-------EDEERLKEALSED-------------------NIVEVVATSAKTGEGVEELF 162
                       250
                ....*....|....
2OXR_A      249 TLAYEHYCTCGDLT 262
Cdd:COG1100 163 AALAEILRGEGDSL 176
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
15-180 3.42e-15

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: 69.38  E-value: 3.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       15 MIVVFVGT-AGSGKTTLTGEFGRYL-EDNYKVAYVNLDtgvkelpyepsidvrefvtveeimregygpngaivesydrlm 92
Cdd:cd01983   1 RVIAVTGGkGGVGKTTLAAALAVALaAKGYKVLLIDLD------------------------------------------ 38
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       93 ekfneylnkilrlekenDYVLIDTPGQMETFLFHEFGVRLMENLPYPLVVYISDPEILKKPNDYCFvrFFALLIDLRLGA 172
Cdd:cd01983  39 -----------------DYVLIDGGGGLETGLLLGTIVALLALKKADEVIVVVDPELGSLLEAVKL--LLALLLLGIGIR 99

                ....*...
2OXR_A      173 TTIPALNK 180
Cdd:cd01983 100 PDGIVLNK 107
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
16-124 2.92e-05

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


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 43.87  E-value: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A         16 IVVFVGTAGSGKTTLTGEFGRYL-EDNYKVAYVNLDTGVKELPYEPSI--DVREFVTVEEIMREGYGPNGAIVE------ 86
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALaRRGLRVLLIDLDPQSNNSSVEGLEgdIAPALQALAEGLKGRVNLDPILLKeksdeg 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
2OXR_A         87 ------SYDRLMEKFNEYLNKIL---------RLEKENDYVLIDTPGQMETFL 124
Cdd:pfam01656  81 gldlipGNIDLEKFEKELLGPRKeerlrealeALKEDYDYVIIDGAPGLGELL 133
SRP54 pfam00448
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ...
16-122 6.81e-05

SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.


Pssm-ID: 459814 [Multi-domain]  Cd Length: 193  Bit Score: 42.53  E-value: 6.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A         16 IVVFVGTAGSGKTTLTGEFGRYL-EDNYKVAYVNLDT----GVKELpyepsidvREFVTVEEIMREGYGPNGAIVESYDR 90
Cdd:pfam00448   2 VILLVGLQGSGKTTTIAKLAAYLkKKGKKVLLVAADTfraaAIEQL--------KQLAEKLGVPVFGSKTGADPAAVAFD 73
                          90       100       110
                  ....*....|....*....|....*....|..
2OXR_A         91 LMEKFneylnkilrLEKENDYVLIDTPGQMET 122
Cdd:pfam00448  74 AVEKA---------KAENYDVVLVDTAGRLQN 96
SRP54 smart00962
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ...
16-118 6.85e-05

SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.


Pssm-ID: 214940  Cd Length: 197  Bit Score: 42.78  E-value: 6.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A          16 IVVFVGTAGSGKTTLTGEFGRYL--EDNYKVAYVNLDT----GVKELpyepsidvREFVTVEEIMREGYGPNGAIVESYD 89
Cdd:smart00962   3 VILLVGPNGVGKTTTIAKLAARLklKGGKKVLLVAADTfraaAVEQL--------KTYAEILGVVPVAGGEGADPVAVAK 74
                           90       100
                   ....*....|....*....|....*....
2OXR_A          90 RLMEKFNeylnkilrlEKENDYVLIDTPG 118
Cdd:smart00962  75 DAVELAK---------ARGYDVVLIDTAG 94
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
24-118 1.93e-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: 41.77  E-value: 1.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       24 GSGKTTLTGEFGRYL-EDNYKVAYVNLDT--------GVKELPYEPSI-DV-REFVTVEEIMREGYGPNGAIVESYDRLM 92
Cdd:COG1192  12 GVGKTTTAVNLAAALaRRGKRVLLIDLDPqgnltsglGLDPDDLDPTLyDLlLDDAPLEDAIVPTEIPGLDLIPANIDLA 91
                        90       100       110
                ....*....|....*....|....*....|....*.
2OXR_A       93 E--------KFNEY-LNKILR-LEKENDYVLIDTPG 118
Cdd:COG1192  92 GaeielvsrPGRELrLKRALApLADDYDYILIDCPP 127
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
16-118 3.38e-04

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 41.39  E-value: 3.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       16 IVVFVGTAGSGKTTLTGEF-GRY-LEDNYKVAYVNLDT----GVKELpyepsidvREF-----VTVEEIMREgygpngai 84
Cdd:COG1419 166 VIALVGPTGVGKTTTIAKLaARFvLRGKKKVALITTDTyrigAVEQL--------KTYarilgVPVEVAYDP-------- 229
                        90       100       110
                ....*....|....*....|....*....|....
2OXR_A       85 vESYDRLMEKFNEYlnkilrlekenDYVLIDTPG 118
Cdd:COG1419 230 -EELKEALERLRDK-----------DLVLIDTAG 251
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
16-207 4.78e-04

CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase expression / formation protein, and UreG a urease accessory protein. Both these proteins contain a P-loop nucleotide binding motif. HypB has GTPase activity and is a guanine nucleotide binding protein. It is not known whether UreG binds GTP or some other nucleotide. Both enzymes are involved in nickel binding. HypB can store nickel and is required for nickel dependent hydrogenase expression. UreG is required for functional incorporation of the urease nickel metallocenter. GTP hydrolysis may required by these proteins for nickel incorporation into other nickel proteins. This family of domains also contains P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression, and the cobW gene product, which may be involved in cobalamin biosynthesis in Pseudomonas denitrificans.


Pssm-ID: 396860  Cd Length: 179  Bit Score: 39.93  E-value: 4.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A         16 IVVFVGTAGSGKTTLTGEFGRYLEDNYKVAYVnldtgVKELpYEPSIDVREFVTVEEIMREgyGPNGAIVESydrLMEKF 95
Cdd:pfam02492   2 VTVITGFLGSGKTTLLNHLLKQNRAGLRIAVI-----VNEF-GETGIDAELLSETGVLIVE--LSNGCICCT---IREDL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A         96 NEYLNKILRLEKENDYVLIDTPGQ------METFLFHEFGVRLMenlpYPLVVYISDPEILKKPNDycfvrFFALLIDlR 169
Cdd:pfam02492  71 SMALEALLEREGRLDVIFIETTGLaepapvAQTFLSPELRSPVL----LDGVITVVDAANEADGEK-----IPRKAGD-Q 140
                         170       180       190
                  ....*....|....*....|....*....|....*...
2OXR_A        170 LGATTIPALNKVDLLSEEEKERHRKyfEDIDYLTARLK 207
Cdd:pfam02492 141 IAFADLIVLNKTDLAPEVALLEVLE--EDLRRLNPGAP 176
FlhF cd17873
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ...
16-130 4.88e-04

signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP)-type GTPase that is essential for the placement and assembly of polar flagella. It is similar to the 54 kd subunit (SRP54) of the signal recognition particle (SRP) that mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR).


Pssm-ID: 349782 [Multi-domain]  Cd Length: 189  Bit Score: 39.84  E-value: 4.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       16 IVVFVGTAGSGKTTLTGEFG-RY-LEDNYKVAYVNLDT----GVKELpyepsidvREFVtveEIMregyGPNGAIVESYD 89
Cdd:cd17873   2 VIALVGPTGVGKTTTLAKLAaRYvLKKGKKVALITTDTyrigAVEQL--------KTYA---EIM----GIPVEVAEDPE 66
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
2OXR_A       90 RlmekfneyLNKILRLEKENDYVLIDTPG----------QMETFLFHEFGV 130
Cdd:cd17873  67 D--------LADALERLSDRDLILIDTAGrsprdkeqleELKELLGAGEDI 109
SRP54_G cd17875
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ...
16-51 5.74e-04

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


Pssm-ID: 349784  Cd Length: 193  Bit Score: 39.87  E-value: 5.74e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
2OXR_A       16 IVVFVGTAGSGKTTLTGEFGRYLED-NYKVAYVNLDT 51
Cdd:cd17875   2 VIMFVGLQGSGKTTTAAKLAYYYQKkGYKVGLVCADT 38
AAA_28 pfam13521
AAA domain;
17-149 1.11e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 38.78  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A         17 VVFVGTAGSGKTTLTgefgRYLEDNYKVAYvnldtgvkelpyepsidVREFVTveEIMREGYGPNGAIVESYDRLM---E 93
Cdd:pfam13521   2 IVITGGPSTGKTTLA----EALAARFGYPV-----------------VPEAAR--EILEELGADGGDALPWVEDLLafaR 58
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
2OXR_A         94 KFNEYLNKILRLEKENDYVLIDTpGQMETFLFHEFG--------VRLMENLPYPLVVYIS-DPEI 149
Cdd:pfam13521  59 GVLEAQLEDEAAAAANDLLFFDR-GPLDTLAYSRAYggpcppelEAAARASRYDLVFLLPpDPEI 122
PRK14974 PRK14974
signal recognition particle-docking protein FtsY;
16-122 1.23e-03

signal recognition particle-docking protein FtsY;


Pssm-ID: 237875 [Multi-domain]  Cd Length: 336  Bit Score: 39.57  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A        16 IVVFVGTAGSGKTTLTGEFGRYLEDN-YKVAYVNLDT---GVKElpyepSIDVR-EFVTVEEIMREgYGPNGAIVeSYDR 90
Cdd:PRK14974 142 VIVFVGVNGTGKTTTIAKLAYYLKKNgFSVVIAAGDTfraGAIE-----QLEEHaERLGVKVIKHK-YGADPAAV-AYDA 214
                         90       100       110
                 ....*....|....*....|....*....|....
2OXR_A        91 LmekfnEYL--NKIlrlekenDYVLIDTPGQMET 122
Cdd:PRK14974 215 I-----EHAkaRGI-------DVVLIDTAGRMHT 236
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
15-147 2.12e-03

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 38.61  E-value: 2.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       15 MIVVFVGTAGSGKTTLTGEFGRYL-EDNYKVAYVNLDT--------GVKE--LPYEPSIDVREFVTvEEIMREGYG---- 79
Cdd:COG3640   1 MKIAVAGKGGVGKTTLSALLARYLaEKGKPVLAVDADPnanlaealGLEVeaDLIKPLGEMRELIK-ERTGAPGGGmfkl 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       80 -------PNGAIVESYD-RLM-----EKFNE----YLNKILR------LEKENDYVLIDTPGQMEtflfHeFGVRLMENL 136
Cdd:COG3640  80 npkvddiPEEYLVEGDGvDLLvmgtiEEGGSgcycPENALLRallnhlVLGNYEYVVVDMEAGIE----H-LGRGTAEGV 154
                       170
                ....*....|.
2OXR_A      137 PYPLVVyiSDP 147
Cdd:COG3640 155 DLLLVV--SEP 163
minD CHL00175
septum-site determining protein; Validated
11-122 4.62e-03

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 37.83  E-value: 4.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A        11 GMASMIVVFVGTAGSGKTTLTGEFGRYLED-NYKVAYVNLDTGVKELPYEPSIDVREFVTVEEIM-----------REGY 78
Cdd:CHL00175  13 TMSRIIVITSGKGGVGKTTTTANLGMSIARlGYRVALIDADIGLRNLDLLLGLENRVLYTAMDVLegecrldqaliRDKR 92
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
2OXR_A        79 GPNGAIVE-SYDR----LMEKFNEYLNKILRlEKENDYVLIDTPGQMET 122
Cdd:CHL00175  93 WKNLSLLAiSKNRqrynVTRKNMNMLVDSLK-NRGYDYILIDCPAGIDV 140
CLP1_P pfam16575
mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of ...
21-118 4.70e-03

mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of Clp1 mRNA cleavage and polyadenylation factor, Clp1, proteins in eukaryotes. Clp1 is essential for 3'-end processing of mRNAs. This region carries the P-loop suggesting it is the region that binds adenine or guanine nucleotide.


Pssm-ID: 406878  Cd Length: 187  Bit Score: 37.23  E-value: 4.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A         21 GTAGSGKTTLTgefgRYL-----EDNYKVAYVNLDTGVKEL--PY--------EPSIDVREFVTVEEIMREgYG---PNG 82
Cdd:pfam16575   1 GPKDSGKSTLC----RILlnyavRKGRKPVYVDLDVGQSEIgpPGtislalveRPIDVPEGFSLDAPLVYF-FGhtsPSG 75
                          90       100       110
                  ....*....|....*....|....*....|....*...
2OXR_A         83 AIvESYDRLMEK-FNEYLNKILRLEKENDY-VLIDTPG 118
Cdd:pfam16575  76 NP-DLYLALVKElARVIESRLEANKKAKASgVIINTPG 112
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
16-51 7.13e-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: 36.58  E-value: 7.13e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
2OXR_A       16 IVVFVGTAGSGKTTLTGEFGRYLEDN-YKVAYVNLDT 51
Cdd:cd03115   2 VILLVGLQGSGKTTTLAKLARYYQEKgKKVLLIAADT 38
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
16-120 7.19e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.20  E-value: 7.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A          16 IVVFVGTAGSGKTTLTGEFGRYL-EDNYKVAYVNLDTgvkelPYEPSIDVREFVTVEEIMREGYGpnGAIVESYDRLMEK 94
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELgPPGGGVIYIDGED-----ILEEVLDQLLLIIVGGKKASGSG--ELRLRLALALARK 76
                           90       100
                   ....*....|....*....|....*.
2OXR_A          95 FNeylnkilrlekeNDYVLIDTPGQM 120
Cdd:smart00382  77 LK------------PDVLILDEITSL 90
Fap7 COG1936
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
15-152 7.84e-03

Broad-specificity NMP kinase [Nucleotide transport and metabolism];


Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 36.33  E-value: 7.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       15 MIVVFVGTAGSGKTTLTGEFGRYLedNYKVayvnldtgvkelpyepsIDVREFVTVEEImregYGPNGAIVESYDRLMEK 94
Cdd:COG1936   1 MRIAITGTPGTGKTTVAKLLAERL--GLEV-----------------IHLNDLVKEEGL----YTEVDEERDSLVVDEDA 57
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
2OXR_A       95 FNEYLNKIlrleKENDYVLidtpgqmETFLFHEFgvrlmenlPYPLVVYI-SDPEILKK 152
Cdd:COG1936  58 LAEELEEL----KEGDVII-------EGHLAHLV--------DVDRVIVLrCNPEVLEE 97
flhF PRK05703
flagellar biosynthesis protein FlhF;
16-118 7.91e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 235570 [Multi-domain]  Cd Length: 424  Bit Score: 37.18  E-value: 7.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A        16 IVVFVGTAGSGKTT----LTGEFGrYLEDNYKVAYVNLDT---GVKE----------LPYEPSIDVREFvtveeimregy 78
Cdd:PRK05703 223 VVALVGPTGVGKTTtlakLAARYA-LLYGKKKVALITLDTyriGAVEqlktyakimgIPVEVVYDPKEL----------- 290
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
2OXR_A        79 gpngaivesyDRLMEKFNEYlnkilrlekenDYVLIDTPG 118
Cdd:PRK05703 291 ----------AKALEQLRDC-----------DVILIDTAG 309
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
15-123 9.66e-03

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


Pssm-ID: 349754 [Multi-domain]  Cd Length: 249  Bit Score: 36.52  E-value: 9.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OXR_A       15 MIVVFVGTAGSGKTTLTGEFGRYL-EDNYKVAYVNLDT--------GVkELPYEPSIDVREFVTVEEIMREGYGPNGAIV 85
Cdd:cd02034   1 MKIAVAGKGGVGKTTIAALLIRYLaKKGGKVLAVDADPnsnlaetlGV-EVEKLPLIKTIGDIRERTGAKKGEPPEGMSL 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
2OXR_A       86 ESYDR----------------LM---EKFNE----YLNKILR------LEKENDYVLIDTPGQMETF 123
Cdd:cd02034  80 NPYVDdiikeiivepdgidllVMgrpEGGGSgcycPVNALLRellrhlALKNYEYVVIDMEAGIEHL 146
 
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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