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Conserved domains on  [gi|15830953|ref|NP_309726|]
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ABC transporter ATP-binding protein [Escherichia coli O157:H7 str. Sakai]

Protein Classification

iron ABC transporter substrate-binding protein( domain architecture ID 10100159)

iron ABC transporter substrate-binding protein functions as the initial receptor in ABC transport of metal ions, most likely Fe(3+)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 38-289 7.09e-75

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: 231.46  E-value: 7.09e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953  38 EAQNITRIVSAGAPADLLLLAVA-PEKMVGFSSF---DFARQaLIPLSEHIRQLPRLGRLaGRASTLSLEGLMALHPDLV 113
Cdd:cd01147   1 VPKPVERVVAAGPGALRLLYALAaPDKIVGVDDAeksDEGRP-YFLASPELKDLPVIGRG-GRGNTPNYEKIAALKPDVV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 114 VDCGNTDETWISQARQvsEQTQIPWLLLNGK--LAQSAEQLTTLGKTLGEEHRAAEQANLASRFVGEAQAFAAS--PAAN 189
Cdd:cd01147  79 IDVGSDDPTSIADDLQ--KKTGIPVVVLDGGdsLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDipDEEK 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 190 LRFYAAR----GPRGLETGLKGSLhtEAAELLGLHNVAQIADRQGLTQVSMENLLRWQPDIILVQEAVTADFIRR----D 261
Cdd:cd01147 157 PTVYFGRigtkGAAGLESGLAGSI--EVFELAGGINVADGLGGGGLKEVSPEQILLWNPDVIFLDTGSFYLSLEGyaknR 234

                       250       260
                ....*....|....*....|....*...
gi 15830953 262 PLWHGVKAVAEQRILFLSGLPFGWLDAP 289
Cdd:cd01147 235 PFWQSLKAVKNGRVYLLPALPFNWYDTP 262
 
Name Accession Description Interval E-value
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 38-289 7.09e-75

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: 231.46  E-value: 7.09e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953  38 EAQNITRIVSAGAPADLLLLAVA-PEKMVGFSSF---DFARQaLIPLSEHIRQLPRLGRLaGRASTLSLEGLMALHPDLV 113
Cdd:cd01147   1 VPKPVERVVAAGPGALRLLYALAaPDKIVGVDDAeksDEGRP-YFLASPELKDLPVIGRG-GRGNTPNYEKIAALKPDVV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 114 VDCGNTDETWISQARQvsEQTQIPWLLLNGK--LAQSAEQLTTLGKTLGEEHRAAEQANLASRFVGEAQAFAAS--PAAN 189
Cdd:cd01147  79 IDVGSDDPTSIADDLQ--KKTGIPVVVLDGGdsLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDipDEEK 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 190 LRFYAAR----GPRGLETGLKGSLhtEAAELLGLHNVAQIADRQGLTQVSMENLLRWQPDIILVQEAVTADFIRR----D 261
Cdd:cd01147 157 PTVYFGRigtkGAAGLESGLAGSI--EVFELAGGINVADGLGGGGLKEVSPEQILLWNPDVIFLDTGSFYLSLEGyaknR 234

                       250       260
                ....*....|....*....|....*...
gi 15830953 262 PLWHGVKAVAEQRILFLSGLPFGWLDAP 289
Cdd:cd01147 235 PFWQSLKAVKNGRVYLLPALPFNWYDTP 262
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 44-308 3.45e-31

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 118.18  E-value: 3.45e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953  44 RIVSAGAPADLLLLAV-APEKMVGFSSFDFARqaliPLSEHIRQLPRLGRlagrASTLSLEGLMALHPDLVVdcGNTDET 122
Cdd:COG0614   2 RIVSLSPSATELLLALgAGDRLVGVSDWGYCD----YPELELKDLPVVGG----TGEPNLEAILALKPDLVL--ASSSGN 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 123 WISQARQVsEQTQIPWLLLNGK-LAQSAEQLTTLGKTLGEEHRAAEQANLASRFVGEAQAFAASPAANLR-FYAARGPRG 200
Cdd:COG0614  72 DEEDYEQL-EKIGIPVVVLDPRsLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTvLYEIWSGDP 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 201 LETGLKGSLHTEAAELLGLHNVAQiADRQGLTQVSMENLLRWQPDIILV--------QEAVTADFIRRDPLWHGVKAVAE 272
Cdd:COG0614 151 LYTAGGGSFIGELLELAGGRNVAA-DLGGGYPEVSLEQVLALDPDVIILsgggydaeTAEEALEALLADPGWQSLPAVKN 229

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15830953 273 QRILFLSGLPFGWldapPGINRLLGLRRLHAWLDPA 308
Cdd:COG0614 230 GRVYVVPGDLLSR----PGPRLLLALEDLAKALHPE 261
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 48-278 1.65e-14

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: 72.02  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953    48 AGAPADLLLLAVAPEKMVGFSSFDFarqaLIPLSEHIRQLPRlgrlAGRASTLSLEGLMALHPDLVVDCGNTDETWISQA 127
Cdd:pfam01497   4 SPAYTEILYALGATDSIVGVDAYTR----DPLKADAVAAIVK----VGAYGEINVERLAALKPDLVILSTGYLTDEAEEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953   128 RQVSEQTQIpwLLLNGKLAQSAEQLTTLGKTLGEEHRAAEQANLASRFVGEAQAFAASPAAN--LRFYAARGPRGLETGL 205
Cdd:pfam01497  76 LSLIIPTVI--FESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKpvLVFGGADGGGYVVAGS 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830953   206 kGSLHTEAAELLGLHNVAQIADRQGLTQVSMENLLRWQPDIILV--QEAVT---ADFIRRDPLWHGVKAVAEQRILFL 278
Cdd:pfam01497 154 -NTYIGDLLRILGIENIAAELSGSEYAPISFEAILSSNPDVIIVsgRDSFTktgPEFVAANPLWAGLPAVKNGRVYTL 230
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
 73-252 1.24e-03

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 40.28  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953   73 ARQALIPLSEHIRQLPRLGR----LAGRASTLSLEGLMALHPDLVVDCGNTDETWISQARQVSEQT-QIPwllLNGKLAQ 147
Cdd:PRK09534  79 ARDRVVGVTQYASYLDGAEErtnvSGGQPFGVNVEAVVGLDPDLVLAPNAVAGDTVTRLREAGITVfHFP---AATSIED 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953  148 SAEQLTTLGKTLGEEHRAAEQANLASRFVGEAQAFAASPAANLRFYAARGprGLETGLKGSLHTEAAELLGLHNVAQIAD 227
Cdd:PRK09534 156 VAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADVDDRPRVLYPLG--DGYTAGGNTFIGALIEAAGGHNVAADAT 233

                        170       180
                 ....*....|....*....|....*
gi 15830953  228 RQGLTQVSMENLLRWQPDIILVQEA 252
Cdd:PRK09534 234 TDGYPQLSEEVIVQQDPDVIVVATA 258
 
Name Accession Description Interval E-value
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 38-289 7.09e-75

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: 231.46  E-value: 7.09e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953  38 EAQNITRIVSAGAPADLLLLAVA-PEKMVGFSSF---DFARQaLIPLSEHIRQLPRLGRLaGRASTLSLEGLMALHPDLV 113
Cdd:cd01147   1 VPKPVERVVAAGPGALRLLYALAaPDKIVGVDDAeksDEGRP-YFLASPELKDLPVIGRG-GRGNTPNYEKIAALKPDVV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 114 VDCGNTDETWISQARQvsEQTQIPWLLLNGK--LAQSAEQLTTLGKTLGEEHRAAEQANLASRFVGEAQAFAAS--PAAN 189
Cdd:cd01147  79 IDVGSDDPTSIADDLQ--KKTGIPVVVLDGGdsLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDipDEEK 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 190 LRFYAAR----GPRGLETGLKGSLhtEAAELLGLHNVAQIADRQGLTQVSMENLLRWQPDIILVQEAVTADFIRR----D 261
Cdd:cd01147 157 PTVYFGRigtkGAAGLESGLAGSI--EVFELAGGINVADGLGGGGLKEVSPEQILLWNPDVIFLDTGSFYLSLEGyaknR 234

                       250       260
                ....*....|....*....|....*...
gi 15830953 262 PLWHGVKAVAEQRILFLSGLPFGWLDAP 289
Cdd:cd01147 235 PFWQSLKAVKNGRVYLLPALPFNWYDTP 262
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 44-308 3.45e-31

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 118.18  E-value: 3.45e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953  44 RIVSAGAPADLLLLAV-APEKMVGFSSFDFARqaliPLSEHIRQLPRLGRlagrASTLSLEGLMALHPDLVVdcGNTDET 122
Cdd:COG0614   2 RIVSLSPSATELLLALgAGDRLVGVSDWGYCD----YPELELKDLPVVGG----TGEPNLEAILALKPDLVL--ASSSGN 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 123 WISQARQVsEQTQIPWLLLNGK-LAQSAEQLTTLGKTLGEEHRAAEQANLASRFVGEAQAFAASPAANLR-FYAARGPRG 200
Cdd:COG0614  72 DEEDYEQL-EKIGIPVVVLDPRsLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTvLYEIWSGDP 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 201 LETGLKGSLHTEAAELLGLHNVAQiADRQGLTQVSMENLLRWQPDIILV--------QEAVTADFIRRDPLWHGVKAVAE 272
Cdd:COG0614 151 LYTAGGGSFIGELLELAGGRNVAA-DLGGGYPEVSLEQVLALDPDVIILsgggydaeTAEEALEALLADPGWQSLPAVKN 229

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15830953 273 QRILFLSGLPFGWldapPGINRLLGLRRLHAWLDPA 308
Cdd:COG0614 230 GRVYVVPGDLLSR----PGPRLLLALEDLAKALHPE 261
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 34-302 1.08e-29

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: 114.76  E-value: 1.08e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953  34 LTLPEaqNITRIVSAGAPADLLLLAVAPEKMVgfSSFDFARQALIPLSEHIRQLPRLgRLAGRASTLSLEGLMALHPDLV 113
Cdd:cd01142  18 VTIPD--EVKRIAALWGAGNAVVAALGGGKLI--VATTSTVQQEPWLYRLAPSLENV-ATGGTGNDVNIEELLALKPDVV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 114 VdCGNTDETwisQARQVSEQTqIPWLLL-NGKLAQSAEQLTTLGKTLGEEHRAAE--------QANLASRFvgeaqaFAA 184
Cdd:cd01142  93 I-VWSTDGK---EAGKAVLRL-LNALSLrDAELEEVKLTIALLGELLGRQEKAEAlvayfddnLAYVAART------KKL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 185 SPAANLRFYAaRGPRGLETGLKGSLHTEAAELLGLHNVAQIADRQGLTQVSMENLLRWQPDIILVQEAVTADFIRRDPLW 264
Cdd:cd01142 162 PDSERPRVYY-AGPDPLTTDGTGSITNSWIDLAGGINVASEATKKGSGEVSLEQLLKWNPDVIIVGNADTKAAILADPRW 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15830953 265 HGVKAVAEQRILFLSGLPFgWLDAPPGINRLLGL---RRLH 302
Cdd:cd01142 241 QNLRAVKNGRVYVNPEGAF-WWDRPSAEEALLGLwlaKTLY 280
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 48-278 1.65e-14

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: 72.02  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953    48 AGAPADLLLLAVAPEKMVGFSSFDFarqaLIPLSEHIRQLPRlgrlAGRASTLSLEGLMALHPDLVVDCGNTDETWISQA 127
Cdd:pfam01497   4 SPAYTEILYALGATDSIVGVDAYTR----DPLKADAVAAIVK----VGAYGEINVERLAALKPDLVILSTGYLTDEAEEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953   128 RQVSEQTQIpwLLLNGKLAQSAEQLTTLGKTLGEEHRAAEQANLASRFVGEAQAFAASPAAN--LRFYAARGPRGLETGL 205
Cdd:pfam01497  76 LSLIIPTVI--FESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKpvLVFGGADGGGYVVAGS 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830953   206 kGSLHTEAAELLGLHNVAQIADRQGLTQVSMENLLRWQPDIILV--QEAVT---ADFIRRDPLWHGVKAVAEQRILFL 278
Cdd:pfam01497 154 -NTYIGDLLRILGIENIAAELSGSEYAPISFEAILSSNPDVIIVsgRDSFTktgPEFVAANPLWAGLPAVKNGRVYTL 230
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 43-167 5.30e-11

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: 59.88  E-value: 5.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953  43 TRIVSAGAPADLLLLAVAPE-KMVGFSSFDFARQALiplsehiRQLPRLGRLAGRASTLSLEGLMALHPDLVVDCGNTDE 121
Cdd:cd00636   1 KRVVALDPGATELLLALGGDdKPVGVADPSGYPPEA-------KALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLE 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15830953 122 TWISQARQVSEQTQIPWLLLNGKLAQSAEQLTTLGKTLGEEHRAAE 167
Cdd:cd00636  74 AWLDKLSKIAIPVVVVDEASELSLENIKESIRLIGKALGKEENAEE 119
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 44-280 4.73e-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: 59.22  E-value: 4.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953  44 RIVSAGAPA--DLLLLAVAPekmVGFSSFDFARQALIPLSEHIRQLPRLGRlagrASTLSLEGLMALHPDLVVdcGNTde 121
Cdd:cd01146   5 RIVALDWGAleTLLALGVKP---VGVADTAGYKPWIPEPALPLEGVVDVGT----RGQPNLEAIAALKPDLIL--GSA-- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 122 twiSQARQVSEQ-TQI-PWLLLN--GKLAQSAEQLTTLGKTLGEEHRAAEQ-ANLASRFvgEAQAFAASPAANLRFYAAR 196
Cdd:cd01146  74 ---SRHDEIYDQlSQIaPTVLLDssPWLAEWKENLRLIAKALGKEEEAEKLlAEYDQRL--AELRQKLPDKGPKPVSVVR 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 197 --GPRGLETGLKGSLHTEAAELLGLHNVA--QIADRQGLTQVSMENLLRWQPDIILV---QEAVTADFIRRDPLWHGVKA 269
Cdd:cd01146 149 fsDAGSIRLYGPNSFAGSVLEDLGLQNPWaqETTNDSGFATISLERLAKADADVLFVftyEDEELAQALQANPLWQNLPA 228

                       250
                ....*....|.
gi 15830953 270 VAEQRILFLSG 280
Cdd:cd01146 229 VKNGRVYVVDD 239
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 43-249 2.10e-09

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: 56.89  E-value: 2.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953  43 TRIVSAGAPADLLLLAV-APEKMVGF-SSFDFARQALiplsehirQLPRLGRLAgrasTLSLEGLMALHPDLVVdcgNTD 120
Cdd:cd01149   2 ERIVSLGGSVTEIVYALgAGDRLVGVdSTSTYPEAAA--------KLPDVGYMR----QLSAEGVLSLKPTLVI---ASD 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 121 ETWISQARQVSEQTQIPWLLLNGK--LAQSAEQLTTLGKTLGEEHRAAEQANLASRFVGEAQAFAASPAANLR--FYAAR 196
Cdd:cd01149  67 EAGPPEALDQLRAAGVPVVTVPSTptLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRvlFLLSH 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15830953 197 GPRGLETGLKGSLHTEAAELLGLHNVAqiADRQGLTQVSMENLLRWQPDIILV 249
Cdd:cd01149 147 GGGAAMAAGRNTAADAIIALAGAVNAA--AGFRGYKPLSAEALIAAQPDVILV 197
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 82-308 1.07e-08

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 55.58  E-value: 1.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953  82 EHIRQLPRLGRlaGRAstLSLEGLMALHPDLVV---DCGNTDEtwISQARQVSeqtqIPWLLLNGK--LAQSAEQLTTLG 156
Cdd:COG4558  61 AAAKALPDVGY--MRQ--LSAEGILSLKPTLVLaseGAGPPEV--LDQLRAAG----VPVVVVPAApsLEGVLAKIRAVA 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 157 KTLGEEHRAAEqanLASRF---VGEAQAFAASPAANLR--FYAARGPRGLETGLKGSLHTEAAELLGLHNVAqiADRQGL 231
Cdd:COG4558 131 AALGVPEAGEA---LAARLeadLAALAARVAAIGKPPRvlFLLSRGGGRPMVAGRGTAADALIRLAGGVNAA--AGFEGY 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 232 TQVSMENLLRWQPDIILVQEAVTADFIRRDPLWH--GVK---AVAEQRILFLSGLPFGWLdappGINRLLGLRRLHAWLD 306
Cdd:COG4558 206 KPLSAEALIAAAPDVILVMTRGLESLGGVDGLLAlpGLAqtpAGKNKRIVAMDDLLLLGF----GPRTPQAALALAQALY 281


                ..
gi 15830953 307 PA 308
Cdd:COG4558 282 PA 283
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 44-301 1.85e-07

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: 51.53  E-value: 1.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953  44 RIVSAgAPA--DLLLLAVAPEKMVGFSSFdfarqaliplSEH---IRQLPRLGRLAgrasTLSLEGLMALHPDLVVdcgn 118
Cdd:cd01144   2 RIVSL-APSatELLYALGLGDQLVGVTDY----------CDYppeAKKLPRVGGFY----QLDLERVLALKPDLVI---- 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 119 tdeTWIS-QARQVSEQTQ---IPWLLLNGK-LAQSAEQLTTLGKTLGEEhRAAEQANLASRFVGEAQAFAASPAANLRFY 193
Cdd:cd01144  63 ---AWDDcNVCAVVDQLRaagIPVLVSEPQtLDDILADIRRLGTLAGRP-ARAEELAEALRRRLAALRKQYASKPPPRVF 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 194 AARGPRGLETGLKGSLhTEAAELLGLHNV-AQIADRQGltQVSMENLLRWQPDIILVQE---AVTADFIRRDPLWHGVKA 269
Cdd:cd01144 139 YQEWIDPLMTAGGDWV-PELIALAGGVNVfADAGERSP--QVSWEDVLAANPDVIVLSPcgfGFTPAILRKEPAWQALPA 215

                       250       260       270
                ....*....|....*....|....*....|..
gi 15830953 270 VAEQRILFLSGLPFGwldaPPGINRLLGLRRL 301
Cdd:cd01144 216 VRNGRVYAVDGNWYF----RPSPRLVDGLEQL 243
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 101-280 5.23e-07

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 50.69  E-value: 5.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 101 SLEGLMALHPDLVVdcgntdetwISQARQ--VSEQ-TQI-PWLLL---NGKLAQSAEQLTTLGKTLGEEHRAAE-QANLA 172
Cdd:COG4594 106 NLEAIAALKPDLII---------ADKSRHeaIYDQlSKIaPTVLFksrNGDYQENLESFKTIAKALGKEEEAEAvLADHD 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 173 SRFVgEAQAFAASPAANLRFYAARGprgLETGLkgSLHTE---AAELL---GLHNVAQI--ADRQGLTQVSMENLLRWQP 244
Cdd:COG4594 177 QRIA-EAKAKLAAADKGKKVAVGQF---RADGL--RLYTPnsfAGSVLaalGFENPPKQskDNGYGYSEVSLEQLPALDP 250

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15830953 245 DIILV----QEAVTADfIRRDPLWHGVKAVAEQRILFLSG 280
Cdd:COG4594 251 DVLFIatydDPSILKE-WKNNPLWKNLKAVKNGRVYEVDG 289
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 41-249 4.38e-06

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: 46.50  E-value: 4.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953  41 NITRIVSAgAPADL-LLLAV-APEKMVGFSSFD-FARQALIPLSEhirqlprlgrlaGRASTLSLEGLMALHPDLVVdcg 117
Cdd:cd01143   2 EPERIVSL-SPSITeILFALgAGDKIVGVDTYSnYPKEVRKKPKV------------GSYSNPNVEKIVALKPDLVI--- 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 118 nTDETWISQARQVSEQTQIPWLLLNGK--LAQSAEQLTTLGKTLGEEHRAAE---QANLASRFVGEAQAFAASpaanLRF 192
Cdd:cd01143  66 -VSSSSLAELLEKLKDAGIPVVVLPAAssLDEIYDQIELIGKITGAEEEAEKlvkEMKQKIDKVKDKGKTIKK----SKV 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15830953 193 YAARGPRGLETGLKGSLHTEAAELLGLHNVAqiADRQGLTQVSMENLLRWQPDIILV 249
Cdd:cd01143 141 YIEVSLGGPYTAGKNTFINELIRLAGAKNIA--ADSGGWPQVSPEEILKANPDVIIL 195
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 84-249 9.06e-06

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: 46.92  E-value: 9.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953  84 IRQLPRLGRLAGRasTLSLEGLMALHPDLVVdCGNTDETWISQARQVS--EQTQIPWLLL---NGKLAQSAEQLTTLGKT 158
Cdd:cd01139  68 IADIPLIGSTYNG--DFSVEKVLTLKPDLVI-LNIWAKTTAEESGILEklEQAGIPVVFVdfrQKPLKNTTPSMRLLGKA 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 159 LGEEHRAAEQANL-ASRFVGEAQAFAASPAANLRFYAARGPRGLE----TGLKGSLhTEAAELLGLHNvaqIADRQGLT- 232
Cdd:cd01139 145 LGREERAEEFIEFyQERIDRIRDRLAKINEPKPKVFIELGAGGPEeccsTYGNGNW-GELVDAAGGDN---IADGLIPGt 220

                       170
                ....*....|....*....
gi 15830953 233 --QVSMENLLRWQPDIILV 249
Cdd:cd01139 221 sgELNAEYVIAANPEIIIA 239
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 44-275 1.66e-05

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: 45.40  E-value: 1.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953  44 RIV-SAGAPADLLLLAVAPekmVGFSSFDFARQALIPLSEHIrqlprlgrLAGRASTLSLEGLMALHPDLVVdCGNTDET 122
Cdd:cd01138  11 RIVaLSGETEGLALLGIKP---VGAASIGGKNPYYKKKTLAK--------VVGIVDEPNLEKVLELKPDLII-VSSKQEE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 123 WISQARQVSEQTQIPWLLLNGKlaqsaEQLTTLGKTLGEEHRA----------AEQAN--LASRFVGEAQAFAASPAANL 190
Cdd:cd01138  79 NYEKLSKIAPTVPVSYNSSDWE-----EQLKEIGKLLNKEDEAekwladykqkAKEAKekIKKKLGNDKSVAVLRGRKQI 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 191 RFYAARGpRGLETGLKGSLHTEAAELlglhnVAQIADRQGLTQVSMENLLRWQPDIILVQ----EAVTADFIrRDPLWHG 266
Cdd:cd01138 154 YVFGEDG-RGGGPILYADLGLKAPEK-----VKEIEDKPGYAAISLEVLPEFDADYIFLLfftgPEAKADFE-SLPIWKN 226


                ....*....
gi 15830953 267 VKAVAEQRI 275
Cdd:cd01138 227 LPAVKNNHV 235
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 43-279 2.97e-04

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: 41.94  E-value: 2.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953  43 TRIVSAG-APADLLLLAVAPEKMVGFSSFDfarqaliplsehIRQLPRLGRLAGRASTL-----SLEGLMALHPDLVV-- 114
Cdd:cd01148  19 QRVVSNDqNTTEMMLALGLQDRMVGTAGID------------NKDLPELKAKYDKVPELakkypSKETVLAARPDLVFgg 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 115 -DCGN------TDETWISQARQVSEQTQI-PWLLLNGKLAQSAEQLTTLGKTLGEEHRAAEQ-ANLASRFVGEAQAFAAS 185
Cdd:cd01148  87 wSYGFdkgglgTPDSLAELGIKTYILPEScGQRRGEATLDDVYNDIRNLGKIFDVEDRADKLvADLKARLAEISAKVKGD 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953 186 PAANLRFYAARGPRGLETGLKGSLHTEAAELLGLHNVAQIADRQgLTQVSMENLLRWQPDIILVQE-------AVTADFI 258
Cdd:cd01148 167 GKKVAVFVYDSGEDKPFTSGRGGIPNAIITAAGGRNVFADVDES-WTTVSWETVIARNPDVIVIIDygdqnaaEQKIKFL 245

                       250       260
                ....*....|....*....|.
gi 15830953 259 RRDPLWHGVKAVAEQRILFLS 279
Cdd:cd01148 246 KENPALKNVPAVKNNRFIVLP 266
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
 73-252 1.24e-03

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 40.28  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953   73 ARQALIPLSEHIRQLPRLGR----LAGRASTLSLEGLMALHPDLVVDCGNTDETWISQARQVSEQT-QIPwllLNGKLAQ 147
Cdd:PRK09534  79 ARDRVVGVTQYASYLDGAEErtnvSGGQPFGVNVEAVVGLDPDLVLAPNAVAGDTVTRLREAGITVfHFP---AATSIED 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830953  148 SAEQLTTLGKTLGEEHRAAEQANLASRFVGEAQAFAASPAANLRFYAARGprGLETGLKGSLHTEAAELLGLHNVAQIAD 227
Cdd:PRK09534 156 VAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADVDDRPRVLYPLG--DGYTAGGNTFIGALIEAAGGHNVAADAT 233

                        170       180
                 ....*....|....*....|....*
gi 15830953  228 RQGLTQVSMENLLRWQPDIILVQEA 252
Cdd:PRK09534 234 TDGYPQLSEEVIVQQDPDVIVVATA 258
 
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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