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Conserved domains on  [gi|493865043|ref|WP_006811748|]
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MULTISPECIES: ABC transporter substrate-binding protein [Enterobacter cloacae complex]

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 ...
 23-321 1.37e-73

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 cd01148:

Pssm-ID: 469696 [Multi-domain]  Cd Length: 284  Bit Score: 228.76  E-value: 1.37e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  23 YPLTIENCGYKETFTKAPERVVALGQNTVEILLLLGLEDKVKASAFWPTKVLPQLAEQNAKIKTLTVEIPTLESILAQNP 102
Cdd:cd01148    1 YPLTVENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAGIDNKDLPELKAKYDKVPELAKKYPSKETVLAARP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 103 DFVPAQLPLLLGPEsKVAKREDLATVGVNSYLSPGMCATKKAAgdmygsrqALWDMtyLYKEIEDFAKIFNVEARGQAVI 182
Cdd:cd01148   81 DLVFGGWSYGFDKG-GLGTPDSLAELGIKTYILPESCGQRRGE--------ATLDD--VYNDIRNLGKIFDVEDRADKLV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 183 ADFKKREADLRQefgKNKKDLSFVFWFSSSSPSADAYVGGKNSASGFIANVLGGHNAITSESE-WPTVGWESIIAANPDV 261
Cdd:cd01148  150 ADLKARLAEISA---KVKGDGKKVAVFVYDSGEDKPFTSGRGGIPNAIITAAGGRNVFADVDEsWTTVSWETVIARNPDV 226

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493865043 262 IVV-SSLDRNRwaldnAEEKIKFLKSDPAVSQLDAVKKGHIVVMDGQAMNPTIRTLYGAEQ 321
Cdd:cd01148  227 IVIiDYGDQNA-----AEQKIKFLKENPALKNVPAVKNNRFIVLPLAEATPGIRNVDAIEK 282
 
Name Accession Description Interval E-value
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 23-321 1.37e-73

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: 228.76  E-value: 1.37e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  23 YPLTIENCGYKETFTKAPERVVALGQNTVEILLLLGLEDKVKASAFWPTKVLPQLAEQNAKIKTLTVEIPTLESILAQNP 102
Cdd:cd01148    1 YPLTVENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAGIDNKDLPELKAKYDKVPELAKKYPSKETVLAARP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 103 DFVPAQLPLLLGPEsKVAKREDLATVGVNSYLSPGMCATKKAAgdmygsrqALWDMtyLYKEIEDFAKIFNVEARGQAVI 182
Cdd:cd01148   81 DLVFGGWSYGFDKG-GLGTPDSLAELGIKTYILPESCGQRRGE--------ATLDD--VYNDIRNLGKIFDVEDRADKLV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 183 ADFKKREADLRQefgKNKKDLSFVFWFSSSSPSADAYVGGKNSASGFIANVLGGHNAITSESE-WPTVGWESIIAANPDV 261
Cdd:cd01148  150 ADLKARLAEISA---KVKGDGKKVAVFVYDSGEDKPFTSGRGGIPNAIITAAGGRNVFADVDEsWTTVSWETVIARNPDV 226

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493865043 262 IVV-SSLDRNRwaldnAEEKIKFLKSDPAVSQLDAVKKGHIVVMDGQAMNPTIRTLYGAEQ 321
Cdd:cd01148  227 IVIiDYGDQNA-----AEQKIKFLKENPALKNVPAVKNNRFIVLPLAEATPGIRNVDAIEK 282
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 42-326 2.92e-41

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 144.76  E-value: 2.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  42 RVVALGQNTVEILLLLGLEDKVKASAFWPTKVLPQLaeQNAKIKTL-TVEIPTLESILAQNPDFVpaqlpLLLGPESKVA 120
Cdd:COG0614    2 RIVSLSPSATELLLALGAGDRLVGVSDWGYCDYPEL--ELKDLPVVgGTGEPNLEAILALKPDLV-----LASSSGNDEE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 121 KREDLATVGVNSYLSPgmcatkkaagdmygsrqaLWDMTYLYKEIEDFAKIFNVEARGQAVIADFKKREADLRQEFGKNK 200
Cdd:COG0614   75 DYEQLEKIGIPVVVLD------------------PRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAE 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 201 KDLsfvFWFSSSSPSADAYVGGKNSASGFIANVLGGHNAIT-SESEWPTVGWESIIAANPDVIVVSSldrNRWALDNAEE 279
Cdd:COG0614  137 ERP---TVLYEIWSGDPLYTAGGGSFIGELLELAGGRNVAAdLGGGYPEVSLEQVLALDPDVIILSG---GGYDAETAEE 210

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 493865043 280 KIKFLKSDPAVSQLDAVKKGHIVVMDGQAMN-PTIRTLYGAEQVGEQL 326
Cdd:COG0614  211 ALEALLADPGWQSLPAVKNGRVYVVPGDLLSrPGPRLLLALEDLAKAL 258
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 44-307 9.46e-23

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: 94.74  E-value: 9.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043   44 VALGQNTVEILLLLGLEDKVkaSAFWPTKVLPQLAEQN-AKIKTLTVEIPTLESILAQNPDFVPAQLPLLLGPESKVAKr 122
Cdd:pfam01497   1 AALSPAYTEILYALGATDSI--VGVDAYTRDPLKADAVaAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEELLS- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  123 EDLATVGVNSylspgmcatkkaagdmygsrqalWDMTYLYKE-IEDFAKIFNVEARGQAVIADFKKREADLRQefgKNKK 201
Cdd:pfam01497  78 LIIPTVIFES-----------------------SSTGESLKEqIKQLGELLGLEDEAEELVAEIDSALAAAKK---AVPS 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  202 DLSFVFWFSSSSPSADAYVGGKNSASGFIANVLGGHNAI--TSESEWPTVGWESIIAANPDVIVVSSLDrnrwalDNAEE 279
Cdd:pfam01497 132 LTRKPVLVFGGADGGGYVVAGSNTYIGDLLRILGIENIAaeLSGSEYAPISFEAILSSNPDVIIVSGRD------SFTKT 205

                         250       260
                  ....*....|....*....|....*...
gi 493865043  280 KIKFLKSDPAVSQLDAVKKGHIVVMDGQ 307
Cdd:pfam01497 206 GPEFVAANPLWAGLPAVKNGRVYTLPSD 233
 
Name Accession Description Interval E-value
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 23-321 1.37e-73

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: 228.76  E-value: 1.37e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  23 YPLTIENCGYKETFTKAPERVVALGQNTVEILLLLGLEDKVKASAFWPTKVLPQLAEQNAKIKTLTVEIPTLESILAQNP 102
Cdd:cd01148    1 YPLTVENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAGIDNKDLPELKAKYDKVPELAKKYPSKETVLAARP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 103 DFVPAQLPLLLGPEsKVAKREDLATVGVNSYLSPGMCATKKAAgdmygsrqALWDMtyLYKEIEDFAKIFNVEARGQAVI 182
Cdd:cd01148   81 DLVFGGWSYGFDKG-GLGTPDSLAELGIKTYILPESCGQRRGE--------ATLDD--VYNDIRNLGKIFDVEDRADKLV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 183 ADFKKREADLRQefgKNKKDLSFVFWFSSSSPSADAYVGGKNSASGFIANVLGGHNAITSESE-WPTVGWESIIAANPDV 261
Cdd:cd01148  150 ADLKARLAEISA---KVKGDGKKVAVFVYDSGEDKPFTSGRGGIPNAIITAAGGRNVFADVDEsWTTVSWETVIARNPDV 226

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493865043 262 IVV-SSLDRNRwaldnAEEKIKFLKSDPAVSQLDAVKKGHIVVMDGQAMNPTIRTLYGAEQ 321
Cdd:cd01148  227 IVIiDYGDQNA-----AEQKIKFLKENPALKNVPAVKNNRFIVLPLAEATPGIRNVDAIEK 282
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 42-326 2.92e-41

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 144.76  E-value: 2.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  42 RVVALGQNTVEILLLLGLEDKVKASAFWPTKVLPQLaeQNAKIKTL-TVEIPTLESILAQNPDFVpaqlpLLLGPESKVA 120
Cdd:COG0614    2 RIVSLSPSATELLLALGAGDRLVGVSDWGYCDYPEL--ELKDLPVVgGTGEPNLEAILALKPDLV-----LASSSGNDEE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 121 KREDLATVGVNSYLSPgmcatkkaagdmygsrqaLWDMTYLYKEIEDFAKIFNVEARGQAVIADFKKREADLRQEFGKNK 200
Cdd:COG0614   75 DYEQLEKIGIPVVVLD------------------PRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAE 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 201 KDLsfvFWFSSSSPSADAYVGGKNSASGFIANVLGGHNAIT-SESEWPTVGWESIIAANPDVIVVSSldrNRWALDNAEE 279
Cdd:COG0614  137 ERP---TVLYEIWSGDPLYTAGGGSFIGELLELAGGRNVAAdLGGGYPEVSLEQVLALDPDVIILSG---GGYDAETAEE 210

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 493865043 280 KIKFLKSDPAVSQLDAVKKGHIVVMDGQAMN-PTIRTLYGAEQVGEQL 326
Cdd:COG0614  211 ALEALLADPGWQSLPAVKNGRVYVVPGDLLSrPGPRLLLALEDLAKAL 258
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 44-307 9.46e-23

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: 94.74  E-value: 9.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043   44 VALGQNTVEILLLLGLEDKVkaSAFWPTKVLPQLAEQN-AKIKTLTVEIPTLESILAQNPDFVPAQLPLLLGPESKVAKr 122
Cdd:pfam01497   1 AALSPAYTEILYALGATDSI--VGVDAYTRDPLKADAVaAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEELLS- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  123 EDLATVGVNSylspgmcatkkaagdmygsrqalWDMTYLYKE-IEDFAKIFNVEARGQAVIADFKKREADLRQefgKNKK 201
Cdd:pfam01497  78 LIIPTVIFES-----------------------SSTGESLKEqIKQLGELLGLEDEAEELVAEIDSALAAAKK---AVPS 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  202 DLSFVFWFSSSSPSADAYVGGKNSASGFIANVLGGHNAI--TSESEWPTVGWESIIAANPDVIVVSSLDrnrwalDNAEE 279
Cdd:pfam01497 132 LTRKPVLVFGGADGGGYVVAGSNTYIGDLLRILGIENIAaeLSGSEYAPISFEAILSSNPDVIIVSGRD------SFTKT 205

                         250       260
                  ....*....|....*....|....*...
gi 493865043  280 KIKFLKSDPAVSQLDAVKKGHIVVMDGQ 307
Cdd:pfam01497 206 GPEFVAANPLWAGLPAVKNGRVYTLPSD 233
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 1-327 7.87e-22

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 93.33  E-value: 7.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043   1 MKKVLCALGL-AVASMSTALATTypltiencgyketfTKAPERVVALGQNTVEILLLLGLEDKVKA---SAFWP--TKVL 74
Cdd:COG4558    1 MKRLALALLLlALAALAAGASVA--------------AAAAERIVSLGGSVTEIVYALGAGDRLVGvdtTSTYPaaAKAL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  75 PQLAEQnakiKTLTVEiptleSILAQNPDfvpaqlpLLL-----GPESKVAKredLATVGVNSYLSPgmcATKKAAGdmy 149
Cdd:COG4558   67 PDVGYM----RQLSAE-----GILSLKPT-------LVLasegaGPPEVLDQ---LRAAGVPVVVVP---AAPSLEG--- 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 150 gsrqalwdmtyLYKEIEDFAKIFNVEARGQAVIADFKKREADLRQE---FGKNKKDLSFVFWFSSSspsadAYVGGKNSA 226
Cdd:COG4558  122 -----------VLAKIRAVAAALGVPEAGEALAARLEADLAALAARvaaIGKPPRVLFLLSRGGGR-----PMVAGRGTA 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 227 SGFIANVLGGHNAITSESEWPTVGWESIIAANPDVIVVSslDRNRWALDNAEEkikfLKSDPAVSQLDAVKKGHIVVMDG 306
Cdd:COG4558  186 ADALIRLAGGVNAAAGFEGYKPLSAEALIAAAPDVILVM--TRGLESLGGVDG----LLALPGLAQTPAGKNKRIVAMDD 259

                        330       340
                 ....*....|....*....|..
gi 493865043 307 QA-MNPTIRTLYGAEQVGEQLR 327
Cdd:COG4558  260 LLlLGFGPRTPQAALALAQALY 281
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 40-308 1.12e-21

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: 91.56  E-value: 1.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  40 PERVVALGQNTVEILLLLGLEDK---VKASAFWP--TKVLPQLAEQnakiKTLTVEiptleSILAQNPDFVPAQLplLLG 114
Cdd:cd01149    1 PERIVSLGGSVTEIVYALGAGDRlvgVDSTSTYPeaAAKLPDVGYM----RQLSAE-----GVLSLKPTLVIASD--EAG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 115 PESKVAKredLATVGVNSYLSPgmcatkkaagdmygsrqALWDMTYLYKEIEDFAKIFNVEARGQAVIADFKKREADLRQ 194
Cdd:cd01149   70 PPEALDQ---LRAAGVPVVTVP-----------------STPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRK 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 195 ---EFGKNKKDLSFVFWFSssspsADAYVGGKNSASGFIANVLGGHNAITSESEWPTVGWESIIAANPDVIVVSSldRNR 271
Cdd:cd01149  130 tvaAHKKPPRVLFLLSHGG-----GAAMAAGRNTAADAIIALAGAVNAAAGFRGYKPLSAEALIAAQPDVILVMS--RGL 202

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 493865043 272 WALDNAEekikFLKSDPAVSQLDAVKKGHIVVMDGQA 308
Cdd:cd01149  203 DAVGGVD----GLLKLPGLAQTPAGRNKRILAMDDLL 235
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 41-322 4.49e-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: 81.96  E-value: 4.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  41 ERVVALGQNTVEILLLLGLEDK-VKASAF--WP--TKVLPQLAeqnakiKTLTVEIptlESILAQNPDFVPAQlplllGP 115
Cdd:cd01144    1 MRIVSLAPSATELLYALGLGDQlVGVTDYcdYPpeAKKLPRVG------GFYQLDL---ERVLALKPDLVIAW-----DD 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 116 ESKVAKREDLATVGVNSYLSPGmcatkkaagdmygsrQALWDMtylYKEIEDFAKIFNVEARGQAVIADFKKREADLRQE 195
Cdd:cd01144   67 CNVCAVVDQLRAAGIPVLVSEP---------------QTLDDI---LADIRRLGTLAGRPARAEELAEALRRRLAALRKQ 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 196 FGKNKKdlsfvfWFSSSSPSADA-YVGGKNSASGFIAnVLGGHNAI-TSESEWPTVGWESIIAANPDVIVVSsldrnrWA 273
Cdd:cd01144  129 YASKPP------PRVFYQEWIDPlMTAGGDWVPELIA-LAGGVNVFaDAGERSPQVSWEDVLAANPDVIVLS------PC 195

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 493865043 274 LDNAEEKIkfLKSDPAVSQLDAVKKGHIVVMDGQAMN-PTIRTLYGAEQV 322
Cdd:cd01144  196 GFGFTPAI--LRKEPAWQALPAVRNGRVYAVDGNWYFrPSPRLVDGLEQL 243
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 38-306 6.74e-17

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: 78.87  E-value: 6.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  38 KAPERVVALGQNTVEILLLLGledkVKASAFWPTKVLPQLAEQNAKIKTLTVEI-----PTLESILAQNPDfvpaqlpLL 112
Cdd:cd01146    1 AKPQRIVALDWGALETLLALG----VKPVGVADTAGYKPWIPEPALPLEGVVDVgtrgqPNLEAIAALKPD-------LI 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 113 LGPESKVAKREDLA-----TVGVNSYlspgmcatkkaagDMYGSRQALwdmtylykeIEDFAKIFNVEARGQAVIADFKK 187
Cdd:cd01146   70 LGSASRHDEIYDQLsqiapTVLLDSS-------------PWLAEWKEN---------LRLIAKALGKEEEAEKLLAEYDQ 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 188 READLRQEFGKNKKdlsFVFWFSSSSPSADAYVGGKNSASGFIANVLGGHNAITSESE----WPTVGWESIIAANPDVIV 263
Cdd:cd01146  128 RLAELRQKLPDKGP---KPVSVVRFSDAGSIRLYGPNSFAGSVLEDLGLQNPWAQETTndsgFATISLERLAKADADVLF 204

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 493865043 264 VSSldrnrwalDNAEEKIKFLKSDPAVSQLDAVKKGHIVVMDG 306
Cdd:cd01146  205 VFT--------YEDEELAQALQANPLWQNLPAVKNGRVYVVDD 239
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 38-264 1.58e-16

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: 76.55  E-value: 1.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  38 KAPERVVALGQNTVEILLLLGLEDKVKASAfwPTKVLPQLAEQNAKIKTLTVeiPTLESILAQNPDFVpaqlplLLGPES 117
Cdd:cd01143    1 KEPERIVSLSPSITEILFALGAGDKIVGVD--TYSNYPKEVRKKPKVGSYSN--PNVEKIVALKPDLV------IVSSSS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 118 KVAKREDLATVGVNSYLSPgmcATKKAAGdmygsrqalwdmtyLYKEIEDFAKIFNVEARGQAVIADFKKREADLRQEfG 197
Cdd:cd01143   71 LAELLEKLKDAGIPVVVLP---AASSLDE--------------IYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDK-G 132

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493865043 198 KNKKDLSFVFWFSSSSPsadaYVGGKNSASGFIANVLGGHNAITSESEWPTVGWESIIAANPDVIVV 264
Cdd:cd01143  133 KTIKKSKVYIEVSLGGP----YTAGKNTFINELIRLAGAKNIAADSGGWPQVSPEEILKANPDVIIL 195
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 33-308 1.27e-14

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: 72.68  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  33 KETFTKAPERVVALGQNTVEILLLLGLedKVKASAfwPTKVLPQLAE--QNAKIKTL-TVEIPTLESILAQNPDFVpaql 109
Cdd:cd01140    5 ETKVPKNPEKVVVFDVGALDTLDALGV--KVVGVP--KSSTLPEYLKkyKDDKYANVgTLFEPDLEAIAALKPDLI---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 110 plLLGPESKvAKREDLatvgvnsylspgmcatKKAAGDMYGSRQALWDMTYLYKEIEDFAKIFNVEARGQAVIADFKKRE 189
Cdd:cd01140   77 --IIGGRLA-EKYDEL----------------KKIAPTIDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASI 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 190 ADLRQEFGKNKKDLSFVFWfsssspsadayvGGK------NSASGFIANVLGGHNAITS---ESEWPTVGWESIIAANPD 260
Cdd:cd01140  138 AEAKSAAKGKKKALVVLVN------------GGKlsafgpGSRFGWLHDLLGFEPADENikaSSHGQPVSFEYILEANPD 205

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 493865043 261 VIVVssLDRNrwALDNAEEK-IKFLKSDPAVSQLDAVKKGHIVVMDGQA 308
Cdd:cd01140  206 WLFV--IDRG--AAIGAEGSsAKEVLDNDLVKNTTAWKNGKVIYLDPDL 250
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 41-202 4.32e-13

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: 66.04  E-value: 4.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  41 ERVVALGQNTVEILLLLGLEDKVKASAFWPTKVLPQLAEQNAKIKTLTVEIPTLESILAQNPDFVpaqlplLLGPESKVA 120
Cdd:cd00636    1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKALLEKVPDVGHGYEPNLEKIAALKPDLI------IANGSGLEA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 121 KREDLAtvgvnsylspgmcatKKAAGDMYGSRQALWDMTYLYKEIEDFAKIFNVEARGQAVIADFKKREADLRQEFGKNK 200
Cdd:cd00636   75 WLDKLS---------------KIAIPVVVVDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIP 139


                 ..
gi 493865043 201 KD 202
Cdd:cd00636  140 KK 141
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 41-304 1.83e-09

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: 57.34  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  41 ERVVALGQNTVEILLLLGLEDKV----------KASAFWPtkVLPQLAEQNAKIKTLTVEIPTLESILAQNPDFVpaqlp 110
Cdd:cd01147    6 ERVVAAGPGALRLLYALAAPDKIvgvddaeksdEGRPYFL--ASPELKDLPVIGRGGRGNTPNYEKIAALKPDVV----- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 111 LLLGPESKVAKREDL-ATVGVNSYLSPGMCATKKaagdmygsrqalwdmtyLYKEIEDFAKIFNVEARGQAVIADFKKRE 189
Cdd:cd01147   79 IDVGSDDPTSIADDLqKKTGIPVVVLDGGDSLED-----------------TPEQIRLLGKVLGKEERAEELISFIESIL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 190 ADLRqEFGKNKKDLSFVF--WFSSSSPSADAYVGGKNSaSGFIANVLGGHN--AITSESEWPTVGWESIIAANPDVIVVs 265
Cdd:cd01147  142 ADVE-ERTKDIPDEEKPTvyFGRIGTKGAAGLESGLAG-SIEVFELAGGINvaDGLGGGGLKEVSPEQILLWNPDVIFL- 218

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 493865043 266 sldRNRWALDNAEEKikfLKSDPAVSQLDAVKKGHIVVM 304
Cdd:cd01147  219 ---DTGSFYLSLEGY---AKNRPFWQSLKAVKNGRVYLL 251
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 31-304 1.47e-08

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: 55.05  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  31 GYKETFTKAPERVVALGQNTVEILLLLGLEDKVKASAFWPT--KVLPQLAEQNAKIKT-LTVEIPTLESILAQNPDFVPA 107
Cdd:cd01142   15 GRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTSTVQqePWLYRLAPSLENVATgGTGNDVNIEELLALKPDVVIV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 108 qlplllgpESKVAKREDLATVGVNSYLSPGmcatkkaagdmygsrqalWDMTYLYKE-IEDFAKIFNVEARGQAVIADFK 186
Cdd:cd01142   95 --------WSTDGKEAGKAVLRLLNALSLR------------------DAELEEVKLtIALLGELLGRQEKAEALVAYFD 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 187 KREADLRQEFgknkKDLSFVFWFSSSSPSADAY-VGGKNSASGFIANVLGGHNAI--TSESEWPTVGWESIIAANPDVIV 263
Cdd:cd01142  149 DNLAYVAART----KKLPDSERPRVYYAGPDPLtTDGTGSITNSWIDLAGGINVAseATKKGSGEVSLEQLLKWNPDVII 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 493865043 264 VSslDRNRWALdnaeekikfLKSDPAVSQLDAVKKGHIVVM 304
Cdd:cd01142  225 VG--NADTKAA---------ILADPRWQNLRAVKNGRVYVN 254
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 35-305 6.45e-07

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: 49.64  E-value: 6.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043  35 TFTKAPERVVALGqNTVEILLLLGLedKVKASAFWPTKVLPQLAEQNAKIKTLTVEiPTLESILAQNPDFvpaqlpLLLG 114
Cdd:cd01138    4 EIPAKPKRIVALS-GETEGLALLGI--KPVGAASIGGKNPYYKKKTLAKVVGIVDE-PNLEKVLELKPDL------IIVS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 115 P--ESKVAKREDLATVGVNSYLSPGmcatkkaagdmygsrqalWDmtylyKEIEDFAKIFNVEARGQAVIADFKKREADL 192
Cdd:cd01138   74 SkqEENYEKLSKIAPTVPVSYNSSD------------------WE-----EQLKEIGKLLNKEDEAEKWLADYKQKAKEA 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865043 193 RQEFgknKKDLSFVFWFSSSSPSADAYVGGKNSA-SGFIANVLGGHNA------ITSESEWPTVGWESIIAANPDVIVVS 265
Cdd:cd01138  131 KEKI---KKKLGNDKSVAVLRGRKQIYVFGEDGRgGGPILYADLGLKApekvkeIEDKPGYAAISLEVLPEFDADYIFLL 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 493865043 266 sldrnrwaLDNAEEKIKFLKSDPAVSQLDAVKKGHIVVMD 305
Cdd:cd01138  208 --------FFTGPEAKADFESLPIWKNLPAVKNNHVYIVD 239
 
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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