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Conserved domains on  [gi|2465735423|dbj|BDZ46318|]
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hypothetical protein GCM10025866_22270 [Naasia aerilata]

Protein Classification

TroA family protein( domain architecture ID 513)

TroA family protein; most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TroA-like super family cl00262
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 75-344 2.23e-150

Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.


The actual alignment was detected with superfamily member TIGR03868:

Pssm-ID: 469696 [Multi-domain]  Cd Length: 287  Bit Score: 426.56  E-value: 2.23e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  75 AVTVDNCGTSVTFDAAPQRVVTIKSTSTEMLLALGLGDRIVATAFQDGPLPDDLAKAGASLTSIADQVPSEETVLGLEPD 154
Cdd:TIGR03868   1 PVTVDNCGTDVTFDSAPQRVVTIKSSTTELLLALGLGDRIVGTAFPDGPVPAEWATDAAAVPPLSERVPSPEAVLETEPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 155 LVYAGWESNLTAEGAGARDELASLGIASYVSPAACKEPEYQPKKLSWDDVYAEITEVGDIFRVPDAAAALVRDQQAEVKA 234
Cdd:TIGR03868  81 LVYAGWESNLTAEGAGERADLASLGVNTYVAPSACKEDGYQPDPLTFDDVFAEITEVGTIFDVPDAAASLVAEQRAQLAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 235 ITPDDRGLTALWYSSGSATPYVGAGIGNPELLLDTIGLTNIAGDVQDTWTPYSWESVVAADPDVIVLVDASWNSAQKKMD 314
Cdd:TIGR03868 161 IEPDDRGLTALWYSSGSDTPFVGAGIGAPQMVMDTAGLTNIAADVHDTWTPMSWEAVVDADPDVIVLVDSAWNSAEKKIE 240

                         250       260       270
                  ....*....|....*....|....*....|
gi 2465735423 315 QLAGDPVTANLTAVKNKSYLVVPFAASEAG 344
Cdd:TIGR03868 241 VLESNPATSNLTAVQEQRYVVVPFAATEAG 270
 
Name Accession Description Interval E-value
F420-O_ABCperi TIGR03868
proposed F420-0 ABC transporter, periplasmic F420-0 binding protein; This small clade of ...
 75-344 2.23e-150

proposed F420-0 ABC transporter, periplasmic F420-0 binding protein; This small clade of ABC-type transporter periplasmic binding protein components is found as a three gene cassette along with a permease (TIGR03869) and an ATPase (TIGR03873). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this periplasmic binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.


Pssm-ID: 274826 [Multi-domain]  Cd Length: 287  Bit Score: 426.56  E-value: 2.23e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  75 AVTVDNCGTSVTFDAAPQRVVTIKSTSTEMLLALGLGDRIVATAFQDGPLPDDLAKAGASLTSIADQVPSEETVLGLEPD 154
Cdd:TIGR03868   1 PVTVDNCGTDVTFDSAPQRVVTIKSSTTELLLALGLGDRIVGTAFPDGPVPAEWATDAAAVPPLSERVPSPEAVLETEPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 155 LVYAGWESNLTAEGAGARDELASLGIASYVSPAACKEPEYQPKKLSWDDVYAEITEVGDIFRVPDAAAALVRDQQAEVKA 234
Cdd:TIGR03868  81 LVYAGWESNLTAEGAGERADLASLGVNTYVAPSACKEDGYQPDPLTFDDVFAEITEVGTIFDVPDAAASLVAEQRAQLAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 235 ITPDDRGLTALWYSSGSATPYVGAGIGNPELLLDTIGLTNIAGDVQDTWTPYSWESVVAADPDVIVLVDASWNSAQKKMD 314
Cdd:TIGR03868 161 IEPDDRGLTALWYSSGSDTPFVGAGIGAPQMVMDTAGLTNIAADVHDTWTPMSWEAVVDADPDVIVLVDSAWNSAEKKIE 240

                         250       260       270
                  ....*....|....*....|....*....|
gi 2465735423 315 QLAGDPVTANLTAVKNKSYLVVPFAASEAG 344
Cdd:TIGR03868 241 VLESNPATSNLTAVQEQRYVVVPFAATEAG 270
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 76-349 9.29e-76

Metal binding protein TroA_a. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.


Pssm-ID: 238568 [Multi-domain]  Cd Length: 284  Bit Score: 236.47  E-value: 9.29e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  76 VTVDNCGTSVTFDAAPQRVVTIKSTSTEMLLALGLGDRIVATAFQDGPLPDDLAKAGASLTSIADQVPSEETVLGLEPDL 155
Cdd:cd01148     3 LTVENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAGIDNKDLPELKAKYDKVPELAKKYPSKETVLAARPDL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 156 VYAGWESNLTAEGAGARDELASLGIASYVSPAACKEPeyqPKKLSWDDVYAEITEVGDIFRVPDAAAALVRDQQAEV--- 232
Cdd:cd01148    83 VFGGWSYGFDKGGLGTPDSLAELGIKTYILPESCGQR---RGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLaei 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 233 -KAITPDDRGLTALWYSSGSATPYVGAGIGNPELLLDTIGLTNIAGDVQDTWTPYSWESVVAADPDVIVLVD-ASWNSAQ 310
Cdd:cd01148   160 sAKVKGDGKKVAVFVYDSGEDKPFTSGRGGIPNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIVIIDyGDQNAAE 239

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2465735423 311 KKMDQLAGDPVTANLTAVKNKSYLVVPFAASEAGSAAPT 349
Cdd:cd01148   240 QKIKFLKENPALKNVPAVKNNRFIVLPLAEATPGIRNVD 278
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 93-337 3.15e-47

ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 162.09  E-value: 3.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  93 RVVTIKSTSTEMLLALGLGDRIVATAfqDGPLPDDLAKAGASLTSIAD-QVPSEETVLGLEPDLVYAGWESNltaeGAGA 171
Cdd:COG0614     2 RIVSLSPSATELLLALGAGDRLVGVS--DWGYCDYPELELKDLPVVGGtGEPNLEAILALKPDLVLASSSGN----DEED 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 172 RDELASLGIASYVSPAAckepeyqpkklSWDDVYAEITEVGDIFRVPDAAAALVRDQQAEVKAIT----PDDRGLTALWY 247
Cdd:COG0614    76 YEQLEKIGIPVVVLDPR-----------SLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRarlaGAEERPTVLYE 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 248 SSGSATPYVGAGIGNPELLLDTIGLTNIAGDVQDTWTPYSWESVVAADPDVIVLVDASWN--SAQKKMDQLAGDPVTANL 325
Cdd:COG0614   145 IWSGDPLYTAGGGSFIGELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDaeTAEEALEALLADPGWQSL 224

                         250
                  ....*....|..
gi 2465735423 326 TAVKNKSYLVVP 337
Cdd:COG0614   225 PAVKNGRVYVVP 236
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 95-331 2.82e-20

Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 426291 [Multi-domain]  Cd Length: 233  Bit Score: 88.58  E-value: 2.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  95 VTIKSTSTEMLLALGLGDRIVATAFQDGPLPDdlAKAGASLTSI-ADQVPSEETVLGLEPDLVYAGwesnlTAEGAGARD 173
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGVDAYTRDPLK--ADAVAAIVKVgAYGEINVERLAALKPDLVILS-----TGYLTDEAE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 174 ELASLGIASYVSpaackepEYQPKKLSWDDvyaEITEVGDIFRVPDAAAALVRDQQ---AEVKAITP-DDRGLTALWYSS 249
Cdd:pfam01497  74 ELLSLIIPTVIF-------ESSSTGESLKE---QIKQLGELLGLEDEAEELVAEIDsalAAAKKAVPsLTRKPVLVFGGA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 250 GSATPYVGAGIGNPELLLDTIGLTNIAGD-VQDTWTPYSWESVVAADPDVIvLVDASWNSAQKKMDQLAGDPVTANLTAV 328
Cdd:pfam01497 144 DGGGYVVAGSNTYIGDLLRILGIENIAAElSGSEYAPISFEAILSSNPDVI-IVSGRDSFTKTGPEFVAANPLWAGLPAV 222


                  ...
gi 2465735423 329 KNK 331
Cdd:pfam01497 223 KNG 225
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
 79-377 5.33e-10

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 60.31  E-value: 5.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  79 DNCGTSVTFDAAPQRVVTIKSTSTEMLLALGLGDRIVA----TAFQDGplpddlAKAGASLTSIADQVPSEETVLGLEPD 154
Cdd:PRK09534   48 DATGTEITLDERPERVVTLNPSAAQTMWELGARDRVVGvtqyASYLDG------AEERTNVSGGQPFGVNVEAVVGLDPD 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 155 LVYAgweSNLTAEGAGARdeLASLGIASYVSPAACkepeyqpkklSWDDVYAEITEVGDIFRVPDAAAALVRDQQAEVKA 234
Cdd:PRK09534  122 LVLA---PNAVAGDTVTR--LREAGITVFHFPAAT----------SIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDA 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 235 I---TPDDRGLTALWYSSGSAtpYVGAGIGNPELLLDTIGLTNIAGDVQ-DTWTPYSWESVVAADPDVIVLVDASwnsaq 310
Cdd:PRK09534  187 VedrTADVDDRPRVLYPLGDG--YTAGGNTFIGALIEAAGGHNVAADATtDGYPQLSEEVIVQQDPDVIVVATAS----- 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 311 kkmDQLAGDPVTANLTAVKNKSY--------------LVVPFAASEAGSAAPTRRSISPTSSPPSPRRLTPAPRQDHGDS 376
Cdd:PRK09534  260 ---ALVAETEPYASTTAGETGNVvtvnvnhinqpaprIVESMATMATAFHNTTTNDTLDAQPSATTTATSTAPPTDATDG 336


                  .
gi 2465735423 377 D 377
Cdd:PRK09534  337 T 337
 
Name Accession Description Interval E-value
F420-O_ABCperi TIGR03868
proposed F420-0 ABC transporter, periplasmic F420-0 binding protein; This small clade of ...
 75-344 2.23e-150

proposed F420-0 ABC transporter, periplasmic F420-0 binding protein; This small clade of ABC-type transporter periplasmic binding protein components is found as a three gene cassette along with a permease (TIGR03869) and an ATPase (TIGR03873). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this periplasmic binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.


Pssm-ID: 274826 [Multi-domain]  Cd Length: 287  Bit Score: 426.56  E-value: 2.23e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  75 AVTVDNCGTSVTFDAAPQRVVTIKSTSTEMLLALGLGDRIVATAFQDGPLPDDLAKAGASLTSIADQVPSEETVLGLEPD 154
Cdd:TIGR03868   1 PVTVDNCGTDVTFDSAPQRVVTIKSSTTELLLALGLGDRIVGTAFPDGPVPAEWATDAAAVPPLSERVPSPEAVLETEPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 155 LVYAGWESNLTAEGAGARDELASLGIASYVSPAACKEPEYQPKKLSWDDVYAEITEVGDIFRVPDAAAALVRDQQAEVKA 234
Cdd:TIGR03868  81 LVYAGWESNLTAEGAGERADLASLGVNTYVAPSACKEDGYQPDPLTFDDVFAEITEVGTIFDVPDAAASLVAEQRAQLAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 235 ITPDDRGLTALWYSSGSATPYVGAGIGNPELLLDTIGLTNIAGDVQDTWTPYSWESVVAADPDVIVLVDASWNSAQKKMD 314
Cdd:TIGR03868 161 IEPDDRGLTALWYSSGSDTPFVGAGIGAPQMVMDTAGLTNIAADVHDTWTPMSWEAVVDADPDVIVLVDSAWNSAEKKIE 240

                         250       260       270
                  ....*....|....*....|....*....|
gi 2465735423 315 QLAGDPVTANLTAVKNKSYLVVPFAASEAG 344
Cdd:TIGR03868 241 VLESNPATSNLTAVQEQRYVVVPFAATEAG 270
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 76-349 9.29e-76

Metal binding protein TroA_a. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.


Pssm-ID: 238568 [Multi-domain]  Cd Length: 284  Bit Score: 236.47  E-value: 9.29e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  76 VTVDNCGTSVTFDAAPQRVVTIKSTSTEMLLALGLGDRIVATAFQDGPLPDDLAKAGASLTSIADQVPSEETVLGLEPDL 155
Cdd:cd01148     3 LTVENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAGIDNKDLPELKAKYDKVPELAKKYPSKETVLAARPDL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 156 VYAGWESNLTAEGAGARDELASLGIASYVSPAACKEPeyqPKKLSWDDVYAEITEVGDIFRVPDAAAALVRDQQAEV--- 232
Cdd:cd01148    83 VFGGWSYGFDKGGLGTPDSLAELGIKTYILPESCGQR---RGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLaei 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 233 -KAITPDDRGLTALWYSSGSATPYVGAGIGNPELLLDTIGLTNIAGDVQDTWTPYSWESVVAADPDVIVLVD-ASWNSAQ 310
Cdd:cd01148   160 sAKVKGDGKKVAVFVYDSGEDKPFTSGRGGIPNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIVIIDyGDQNAAE 239

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2465735423 311 KKMDQLAGDPVTANLTAVKNKSYLVVPFAASEAGSAAPT 349
Cdd:cd01148   240 QKIKFLKENPALKNVPAVKNNRFIVLPLAEATPGIRNVD 278
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 93-337 3.15e-47

ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 162.09  E-value: 3.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  93 RVVTIKSTSTEMLLALGLGDRIVATAfqDGPLPDDLAKAGASLTSIAD-QVPSEETVLGLEPDLVYAGWESNltaeGAGA 171
Cdd:COG0614     2 RIVSLSPSATELLLALGAGDRLVGVS--DWGYCDYPELELKDLPVVGGtGEPNLEAILALKPDLVLASSSGN----DEED 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 172 RDELASLGIASYVSPAAckepeyqpkklSWDDVYAEITEVGDIFRVPDAAAALVRDQQAEVKAIT----PDDRGLTALWY 247
Cdd:COG0614    76 YEQLEKIGIPVVVLDPR-----------SLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRarlaGAEERPTVLYE 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 248 SSGSATPYVGAGIGNPELLLDTIGLTNIAGDVQDTWTPYSWESVVAADPDVIVLVDASWN--SAQKKMDQLAGDPVTANL 325
Cdd:COG0614   145 IWSGDPLYTAGGGSFIGELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDaeTAEEALEALLADPGWQSL 224

                         250
                  ....*....|..
gi 2465735423 326 TAVKNKSYLVVP 337
Cdd:COG0614   225 PAVKNGRVYVVP 236
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 81-337 3.22e-26

ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 106.43  E-value: 3.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  81 CGTSVTFdAAPQRVVTIKSTSTEMLLALGLGDRIVATafqdgplpD---DLAKAGASLTSIADQ-VPSEETVLGLEPDLV 156
Cdd:COG4558    18 AGASVAA-AAAERIVSLGGSVTEIVYALGAGDRLVGV--------DttsTYPAAAKALPDVGYMrQLSAEGILSLKPTLV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 157 yagwesnLTAEGAG---ARDELASLGIASYVSPAAckepeyqpkkLSWDDVYAEITEVGDIFRVPDAAAALVRDQQAEVK 233
Cdd:COG4558    89 -------LASEGAGppeVLDQLRAAGVPVVVVPAA----------PSLEGVLAKIRAVAAALGVPEAGEALAARLEADLA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 234 AITPDDRGLT-----ALWYSSGSATPYV-GAGIGnPELLLDTIGLTNIAGDVQDtWTPYSWESVVAADPDVIVLVDASWN 307
Cdd:COG4558   152 ALAARVAAIGkpprvLFLLSRGGGRPMVaGRGTA-ADALIRLAGGVNAAAGFEG-YKPLSAEALIAAAPDVILVMTRGLE 229

                         250       260       270
                  ....*....|....*....|....*....|
gi 2465735423 308 SAqKKMDQLAGDPVTANLTAVKNKSYLVVP 337
Cdd:COG4558   230 SL-GGVDGLLALPGLAQTPAGKNKRIVAMD 258
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 90-301 9.25e-24

Periplasmic binding protein YvrC. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria and archaea. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.


Pssm-ID: 238563 [Multi-domain]  Cd Length: 195  Bit Score: 97.35  E-value: 9.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  90 APQRVVTIKSTSTEMLLALGLGDRIVA-TAFQDgpLPDDLAKAgaslTSIAD-QVPSEETVLGLEPDLVYAgwesnltAE 167
Cdd:cd01143     2 EPERIVSLSPSITEILFALGAGDKIVGvDTYSN--YPKEVRKK----PKVGSySNPNVEKIVALKPDLVIV-------SS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 168 GAGAR--DELASLGIASYVSPAAckepeyqpkkLSWDDVYAEITEVGDIFRVPDAAAALV---RDQQAEVKAITPDDRGL 242
Cdd:cd01143    69 SSLAEllEKLKDAGIPVVVLPAA----------SSLDEIYDQIELIGKITGAEEEAEKLVkemKQKIDKVKDKGKTIKKS 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2465735423 243 TAlWYSSGSATPY-VGAG--IGNpelLLDTIGLTNIAGDVQDtWTPYSWESVVAADPDVIVL 301
Cdd:cd01143   139 KV-YIEVSLGGPYtAGKNtfINE---LIRLAGAKNIAADSGG-WPQVSPEEILKANPDVIIL 195
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 91-336 1.15e-22

Hemin binding protein HutB. These proteins have been shown to function as initial receptors in ABC transport of hemin and hemoproteins in many eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.


Pssm-ID: 238569 [Multi-domain]  Cd Length: 235  Bit Score: 95.41  E-value: 1.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  91 PQRVVTIKSTSTEMLLALGLGDRIVATafqdgplpDDLAKAGASLTSIAD-----QVPSeETVLGLEPDLVyagwesnLT 165
Cdd:cd01149     1 PERIVSLGGSVTEIVYALGAGDRLVGV--------DSTSTYPEAAAKLPDvgymrQLSA-EGVLSLKPTLV-------IA 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 166 AEGAG---ARDELASLGIASYVSPAAckepeyqpkkLSWDDVYAEITEVGDIFRVPDAAAALVRDQQAEVKAITPD---- 238
Cdd:cd01149    65 SDEAGppeALDQLRAAGVPVVTVPST----------PTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTvaah 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 239 -DRGLTALWYSSGSATPYVGAGIGNPELLLDTIGLTNIAGDVQDTwTPYSWESVVAADPDVIVLVDASWNSAqKKMDQLA 317
Cdd:cd01149   135 kKPPRVLFLLSHGGGAAMAAGRNTAADAIIALAGAVNAAAGFRGY-KPLSAEALIAAQPDVILVMSRGLDAV-GGVDGLL 212

                         250
                  ....*....|....*....
gi 2465735423 318 GDPVTANLTAVKNKSYLVV 336
Cdd:cd01149   213 KLPGLAQTPAGRNKRILAM 231
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 95-331 2.82e-20

Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 426291 [Multi-domain]  Cd Length: 233  Bit Score: 88.58  E-value: 2.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  95 VTIKSTSTEMLLALGLGDRIVATAFQDGPLPDdlAKAGASLTSI-ADQVPSEETVLGLEPDLVYAGwesnlTAEGAGARD 173
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGVDAYTRDPLK--ADAVAAIVKVgAYGEINVERLAALKPDLVILS-----TGYLTDEAE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 174 ELASLGIASYVSpaackepEYQPKKLSWDDvyaEITEVGDIFRVPDAAAALVRDQQ---AEVKAITP-DDRGLTALWYSS 249
Cdd:pfam01497  74 ELLSLIIPTVIF-------ESSSTGESLKE---QIKQLGELLGLEDEAEELVAEIDsalAAAKKAVPsLTRKPVLVFGGA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 250 GSATPYVGAGIGNPELLLDTIGLTNIAGD-VQDTWTPYSWESVVAADPDVIvLVDASWNSAQKKMDQLAGDPVTANLTAV 328
Cdd:pfam01497 144 DGGGYVVAGSNTYIGDLLRILGIENIAAElSGSEYAPISFEAILSSNPDVI-IVSGRDSFTKTGPEFVAANPLWAGLPAV 222


                  ...
gi 2465735423 329 KNK 331
Cdd:pfam01497 223 KNG 225
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 92-331 3.67e-18

Cobalamin binding protein BtuF. These proteins have been shown to function as initial receptors in ABC transport of vitamin B12 (cobalamin) in eubacterial and some archaeal species. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238564 [Multi-domain]  Cd Length: 245  Bit Score: 83.12  E-value: 3.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  92 QRVVTIKSTSTEMLLALGLGDRIV-ATAFQDGPlpdDLAKAGASLTSIADqvPSEETVLGLEPDLVYAgwesNLTAEGAG 170
Cdd:cd01144     1 MRIVSLAPSATELLYALGLGDQLVgVTDYCDYP---PEAKKLPRVGGFYQ--LDLERVLALKPDLVIA----WDDCNVCA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 171 ARDELASLGIASYVSPaackepeyqPKKLswDDVYAEITEVGDIFRVPDAAAALV---RDQQAEVKAITPDDRGLTALwY 247
Cdd:cd01144    72 VVDQLRAAGIPVLVSE---------PQTL--DDILADIRRLGTLAGRPARAEELAealRRRLAALRKQYASKPPPRVF-Y 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 248 SSGSATPYVGAGIGNPELLLdTIGLTNIAGDVQDTWTPYSWESVVAADPDVIVLvdaSWNSAQKKMDQLAGDPVTANLTA 327
Cdd:cd01144   140 QEWIDPLMTAGGDWVPELIA-LAGGVNVFADAGERSPQVSWEDVLAANPDVIVL---SPCGFGFTPAILRKEPAWQALPA 215


                  ....
gi 2465735423 328 VKNK 331
Cdd:cd01144   216 VRNG 219
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 74-340 6.64e-17

Periplasmic binding protein TroA_e. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238562 [Multi-domain]  Cd Length: 289  Bit Score: 80.48  E-value: 6.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  74 EAVTV-DNCGTSVTFDAAPQRVVTIKSTSTEMLLALGLGDRIVATAFQDGPLPdDLAKAGASLTSIADQV----PSEETV 148
Cdd:cd01142     6 ATRTItDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTSTVQQEP-WLYRLAPSLENVATGGtgndVNIEEL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 149 LGLEPDLVyagwesnLTAEGAGARDELASLGIASYVSpaackepeyqPKKLSWDDVYAEITEVGDIFRVPDAAAALVRDQ 228
Cdd:cd01142    85 LALKPDVV-------IVWSTDGKEAGKAVLRLLNALS----------LRDAELEEVKLTIALLGELLGRQEKAEALVAYF 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 229 QAEVKAITPDDRGLTA-----LWYSSGSATPYVGAGIGNpELLLDTIGLTNIAGDVQD-TWTPYSWESVVAADPDVIVLV 302
Cdd:cd01142   148 DDNLAYVAARTKKLPDserprVYYAGPDPLTTDGTGSIT-NSWIDLAGGINVASEATKkGSGEVSLEQLLKWNPDVIIVG 226

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2465735423 303 DAswnsaqKKMDQLAGDPVTANLTAVKNKSYLVVPFAA 340
Cdd:cd01142   227 NA------DTKAAILADPRWQNLRAVKNGRVYVNPEGA 258
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 92-236 1.00e-12

Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.


Pssm-ID: 238347 [Multi-domain]  Cd Length: 148  Bit Score: 65.27  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  92 QRVVTIKSTSTEMLLALGLGDRIVATAFQDGPLPDDLAKAGASLTSIADQVPSEETVLGLEPDLVYAGWESnltaeGAGA 171
Cdd:cd00636     1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSG-----LEAW 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2465735423 172 RDELASLGIASYVSPAACkepeyqpkKLSWDDVYAEITEVGDIFRVPDAAAALVRDQQAEVKAIT 236
Cdd:cd00636    76 LDKLSKIAIPVVVVDEAS--------ELSLENIKESIRLIGKALGKEENAEELIAELDARLAELR 132
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 92-337 1.36e-12

Metal binding protein HemV-2. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238567 [Multi-domain]  Cd Length: 262  Bit Score: 67.36  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  92 QRVVTIKSTSTEMLLALGLGDRIVA-----TAFQDGP---LPDDLAKAGASLTSIADQVPSEETVLGLEPDLVYAgweSN 163
Cdd:cd01147     6 ERVVAAGPGALRLLYALAAPDKIVGvddaeKSDEGRPyflASPELKDLPVIGRGGRGNTPNYEKIAALKPDVVID---VG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 164 LTAEGAGARDELASLGIASYVSpaackepeYQPKKLswDDVYAEITEVGDIFRVPDAAAALVRDQQAEVKAIT------P 237
Cdd:cd01147    83 SDDPTSIADDLQKKTGIPVVVL--------DGGDSL--EDTPEQIRLLGKVLGKEERAEELISFIESILADVEertkdiP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 238 DDRGLTALWYSSGSATP--YVGAGIGNPELLlDTIGLTNIA-GDVQDTWTPYSWESVVAADPDVIVLVDASWnsAQKKMD 314
Cdd:cd01147   153 DEEKPTVYFGRIGTKGAagLESGLAGSIEVF-ELAGGINVAdGLGGGGLKEVSPEQILLWNPDVIFLDTGSF--YLSLEG 229

                         250       260
                  ....*....|....*....|...
gi 2465735423 315 QLAGDPVTANLTAVKNKSYLVVP 337
Cdd:cd01147   230 YAKNRPFWQSLKAVKNGRVYLLP 252
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 84-331 3.48e-12

Siderophore binding protein FatB. These proteins have been shown to function as ABC-type initial receptors in the siderophore-mediated iron uptake in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238560 [Multi-domain]  Cd Length: 270  Bit Score: 66.13  E-value: 3.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  84 SVTFDAAPQRVVTIKSTSTEMLLALGLgdRIVATAfQDGPLPDDLAKA-GASLTSIADQV-PSEETVLGLEPDLVYAGwe 161
Cdd:cd01140     5 ETKVPKNPEKVVVFDVGALDTLDALGV--KVVGVP-KSSTLPEYLKKYkDDKYANVGTLFePDLEAIAALKPDLIIIG-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 162 sNLTAEgagARDELASLgiasyvspaACKEPEYQPKKLSWDDVYAEITEVGDIFRVPDAAAALVRD---QQAEVKAITPD 238
Cdd:cd01140    80 -GRLAE---KYDELKKI---------APTIDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEidaSIAEAKSAAKG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 239 DRGLTALWYSSGS---ATPyvGAGIGNpelLLDTIGLTNIAGDVQDT--WTPYSWESVVAADPDVIVLVDASWNSAQKKM 313
Cdd:cd01140   147 KKKALVVLVNGGKlsaFGP--GSRFGW---LHDLLGFEPADENIKASshGQPVSFEYILEANPDWLFVIDRGAAIGAEGS 221

                         250       260
                  ....*....|....*....|
gi 2465735423 314 --DQLAGDPVTANLTAVKNK 331
Cdd:cd01140   222 saKEVLDNDLVKNTTAWKNG 241
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 74-331 4.15e-12

ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 66.48  E-value: 4.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  74 EAVTV-DNCGTsVTFDAAPQRVVTIKSTSTEMLLALGL---GdriVATAFQDGPLPDDLAKAGASLTSI-ADQVPSEETV 148
Cdd:COG4594    35 GARTVkHAMGE-TTIPGTPKRVVVLEWSFADALLALGVtpvG---IADDNDYDRWVPYLRDLIKGVTSVgTRSQPNLEAI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 149 LGLEPDLVYAGwesnlTAEGAGARDELASlgIASYVspaackepEYQPKKLSWDDVYAEITEVGDIFRVPDAAAALVRDQ 228
Cdd:COG4594   111 AALKPDLIIAD-----KSRHEAIYDQLSK--IAPTV--------LFKSRNGDYQENLESFKTIAKALGKEEEAEAVLADH 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 229 Q---AEVKA-ITPDDRGLTALW----------YSSGSatpYVGAgignpelLLDTIGLTNIAGDVQDTWTPY---SWESV 291
Cdd:COG4594   176 DqriAEAKAkLAAADKGKKVAVgqfradglrlYTPNS---FAGS-------VLAALGFENPPKQSKDNGYGYsevSLEQL 245

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2465735423 292 VAADPDVIVLVDASWNSAQKkmdQLAGDPVTANLTAVKNK 331
Cdd:COG4594   246 PALDPDVLFIATYDDPSILK---EWKNNPLWKNLKAVKNG 282
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 89-337 1.65e-10

Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial receptors in ABC transport of Fe3+-siderophores in many eubacterial species. They belong to the TroA-like superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA-like protein is comprised of two globular subdomains connected by a long alpha helix and binds its specific ligands in the cleft between these domains.


Pssm-ID: 238566 [Multi-domain]  Cd Length: 256  Bit Score: 61.15  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  89 AAPQRVVTIKSTSTEMLLALGLgdRIVATAFQDGPLPDDLAKAgASLTSIAD----QVPSEETVLGLEPDLVYAgwesnL 164
Cdd:cd01146     1 AKPQRIVALDWGALETLLALGV--KPVGVADTAGYKPWIPEPA-LPLEGVVDvgtrGQPNLEAIAALKPDLILG-----S 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 165 TAEGAGARDELASlgIAsyvspaackeP----EYQPKKLSWDDVyaeITEVGDIFRVPDAAAALVRDQQ---AEVKAITP 237
Cdd:cd01146    73 ASRHDEIYDQLSQ--IA----------PtvllDSSPWLAEWKEN---LRLIAKALGKEEEAEKLLAEYDqrlAELRQKLP 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 238 DDRGLTAL---WYSSGSATPYVG---AGIgnpelLLDTIGLTNIAGDVQDTWTPY---SWESVVAADPDVIVLvdaSWNS 308
Cdd:cd01146   138 DKGPKPVSvvrFSDAGSIRLYGPnsfAGS-----VLEDLGLQNPWAQETTNDSGFatiSLERLAKADADVLFV---FTYE 209

                         250       260
                  ....*....|....*....|....*....
gi 2465735423 309 AQKKMDQLAGDPVTANLTAVKNKSYLVVP 337
Cdd:cd01146   210 DEELAQALQANPLWQNLPAVKNGRVYVVD 238
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
 79-377 5.33e-10

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 60.31  E-value: 5.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  79 DNCGTSVTFDAAPQRVVTIKSTSTEMLLALGLGDRIVA----TAFQDGplpddlAKAGASLTSIADQVPSEETVLGLEPD 154
Cdd:PRK09534   48 DATGTEITLDERPERVVTLNPSAAQTMWELGARDRVVGvtqyASYLDG------AEERTNVSGGQPFGVNVEAVVGLDPD 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 155 LVYAgweSNLTAEGAGARdeLASLGIASYVSPAACkepeyqpkklSWDDVYAEITEVGDIFRVPDAAAALVRDQQAEVKA 234
Cdd:PRK09534  122 LVLA---PNAVAGDTVTR--LREAGITVFHFPAAT----------SIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDA 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 235 I---TPDDRGLTALWYSSGSAtpYVGAGIGNPELLLDTIGLTNIAGDVQ-DTWTPYSWESVVAADPDVIVLVDASwnsaq 310
Cdd:PRK09534  187 VedrTADVDDRPRVLYPLGDG--YTAGGNTFIGALIEAAGGHNVAADATtDGYPQLSEEVIVQQDPDVIVVATAS----- 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 311 kkmDQLAGDPVTANLTAVKNKSY--------------LVVPFAASEAGSAAPTRRSISPTSSPPSPRRLTPAPRQDHGDS 376
Cdd:PRK09534  260 ---ALVAETEPYASTTAGETGNVvtvnvnhinqpaprIVESMATMATAFHNTTTNDTLDAQPSATTTATSTAPPTDATDG 336


                  .
gi 2465735423 377 D 377
Cdd:PRK09534  337 T 337
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 74-331 6.23e-10

ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 59.81  E-value: 6.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  74 EAVTVDNCGTSVTFDAAPQRVVTIKSTSTEMLLALGLGdrIVATAfqDGPLPDDLAKAGASltSIADqV-----PSEETV 148
Cdd:COG4607    34 ETVTVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVE--VAGVP--KGLLPDYLSKYADD--KYAN-VgtlfePDLEAI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 149 LGLEPDLVYAGWESnltaegAGARDELASlgIASYVSPAAckepeyQPKKLsWDDVYAEITEVGDIFRVPDAAAALVRD- 227
Cdd:COG4607   107 AALKPDLIIIGGRS------AKKYDELSK--IAPTIDLTV------DGEDY-LESLKRNTETLGEIFGKEDEAEELVADl 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 228 --QQAEVKAITP-DDRGLTALwYSSGSATPYvGAG--IGnpeLLLDTIGLTNiAGDVQDTWT---PYSWESVVAADPDVI 299
Cdd:COG4607   172 daKIAALKAAAAgKGTALIVL-TNGGKISAY-GPGsrFG---PIHDVLGFKP-ADEDIEASThgqAISFEFIAEANPDWL 245

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2465735423 300 VLVD--ASWNSAQKKMDQLAGDPVTANLTAVKNK 331
Cdd:COG4607   246 FVIDrdAAIGGEGPAAKQVLDNELVKQTTAWKNG 279
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 76-331 8.61e-09

Periplasmic binding protein TroA_f. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238559 [Multi-domain]  Cd Length: 342  Bit Score: 56.55  E-value: 8.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  76 VTV-DNCGTSVTFDAAPQRVVTikSTSTEM-LLALGLGDRIVAT-AFQDGPL----PDDLAKAGASLTSIADqVP----- 143
Cdd:cd01139     1 ITVtDVAGRKVTLDAPVERVLL--GEGRQLyALALLEGENPFARiVGWGGDLkkgdPDTYAKYKEKFPEIAD-IPligst 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 144 -----SEETVLGLEPDLVYAGWESNLTAEGAGARDELASLGIaSYVSPAACKEPEyqpkklswDDVYAEITEVGDIFRVP 218
Cdd:cd01139    78 yngdfSVEKVLTLKPDLVILNIWAKTTAEESGILEKLEQAGI-PVVFVDFRQKPL--------KNTTPSMRLLGKALGRE 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 219 DAAAALVRDQQAEVKAITpdDRGLTA--------LWYSSGSATPYVG-AGIGNPELLLDTIGLTNIAGDVQD-TWTPYSW 288
Cdd:cd01139   149 ERAEEFIEFYQERIDRIR--DRLAKInepkpkvfIELGAGGPEECCStYGNGNWGELVDAAGGDNIADGLIPgTSGELNA 226

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2465735423 289 ESVVAADPDVIVLVDASWNS-------------AQKK---MDQLAGDPVTANLTAVKNK 331
Cdd:cd01139   227 EYVIAANPEIIIATGGNWAKdpsgvslgpdgttADAKeslLRALLKRPGWSSLQAVKNG 285
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 85-331 6.22e-08

Periplasmic binding protein FeuA. These proteins have predicted to function as initial receptors in ABC transport of metal ions in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238558 [Multi-domain]  Cd Length: 248  Bit Score: 53.11  E-value: 6.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  85 VTFDAAPQRVVTIkSTSTEMLLALGLgdRIVATAFQDGPLPDDLAKAGASLTSIADQvPSEETVLGLEPDLVYAGWESNL 164
Cdd:cd01138     3 VEIPAKPKRIVAL-SGETEGLALLGI--KPVGAASIGGKNPYYKKKTLAKVVGIVDE-PNLEKVLELKPDLIIVSSKQEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 165 TAegagarDELASlgIASYVSpaackepeYQPKKLSWDDVYAEItevGDIFRVPDAAAALVRD--QQAE-----VKAITP 237
Cdd:cd01138    79 NY------EKLSK--IAPTVP--------VSYNSSDWEEQLKEI---GKLLNKEDEAEKWLADykQKAKeakekIKKKLG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 238 DDRGLTALWySSGSATPYVGAGIGNPELLLDTIGL--TNIAGDVQDT--WTPYSWESVVAADPDVIVLVDASWNSAQKKM 313
Cdd:cd01138   140 NDKSVAVLR-GRKQIYVFGEDGRGGGPILYADLGLkaPEKVKEIEDKpgYAAISLEVLPEFDADYIFLLFFTGPEAKADF 218

                         250
                  ....*....|....*...
gi 2465735423 314 DQLagdPVTANLTAVKNK 331
Cdd:cd01138   219 ESL---PIWKNLPAVKNN 233
PRK03379 PRK03379
vitamin B12-transporter protein BtuF; Provisional
 89-301 3.50e-05

vitamin B12-transporter protein BtuF; Provisional


Pssm-ID: 179575 [Multi-domain]  Cd Length: 260  Bit Score: 45.06  E-value: 3.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423  89 AAPqRVVTIKSTSTEMLLALGLGDrIVATAFQDGPlpddlaKAGASLTSIAD-QVPSEETVLGLEPDLVYAgWEsnltaE 167
Cdd:PRK03379   16 AAP-RVITLSPANTELAFAAGITP-VGVSSYSDYP------PQAKKIEQVATwQGMNLERIVALKPDLVLA-WR-----G 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2465735423 168 GAGAR--DELASLGIASYVSpaackepeyQPKKLswDDVYAEITEVGDIFRVPD---AAAALVRDQQAEVK---AITPDD 239
Cdd:PRK03379   82 GNAERqvDQLASLGIKVMWV---------DATSI--EQIANALRQLAPWSPQPEkaeQAAQSLLQQYAALKaqyADKPKK 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2465735423 240 R-----GLTALWYSSgsatpyvGAGIGNPelLLDTIGLTNIAGDVQDTWTPYSWESVVAADPDVIVL 301
Cdd:PRK03379  151 RvflqfGTNPLFTSG-------KHSIQSQ--VLSLCGGENIFADSRVPWPQVSREQVLARKPQAIVI 208
 
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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