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Conserved domains on  [gi|1175509954|ref|WP_082052602|]
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iron-siderophore ABC transporter substrate-binding protein [Shewanella algae]

Protein Classification

iron-siderophore ABC transporter substrate-binding protein( domain architecture ID 10100157)

iron-siderophore ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of iron-hydroxamate siderophores such as achromobactin and petrobactin

Gene Ontology:  GO:0015891

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 53-304 3.47e-56

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: 184.41  E-value: 3.47e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  53 SPPKRVVTLGAGAEDWTLSLGVVPIAIephywgGDAQGYLPWFRQAleAQELPLPAIISSYPELDVERLLALKPDLILAP 132
Cdd:cd01146     1 AKPQRIVALDWGALETLLALGVKPVGV------ADTAGYKPWIPEP--ALPLEGVVDVGTRGQPNLEAIAALKPDLILGS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 133 QSGITrESFLQLSALAPVIAYPDKPWLTPVKQQVELIAKALGKEAQAEALLRQQQAYIAQVAAENPEFNGVRLAYINAAS 212
Cdd:cd01146    73 ASRHD-EIYDQLSQIAPTVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 213 rVGNLSVYVTGDPRVDLLLALGFVLPPQlsgLNASRGHFAAHIGLERADMLDDAELLLSWYSSDKARAEVEAMAVIRRLP 292
Cdd:cd01146   152 -AGSIRLYGPNSFAGSVLEDLGLQNPWA---QETTNDSGFATISLERLAKADADVLFVFTYEDEELAQALQANPLWQNLP 227

                         250
                  ....*....|..
gi 1175509954 293 AMRRGRYLAITD 304
Cdd:cd01146   228 AVKNGRVYVVDD 239
 
Name Accession Description Interval E-value
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 53-304 3.47e-56

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: 184.41  E-value: 3.47e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  53 SPPKRVVTLGAGAEDWTLSLGVVPIAIephywgGDAQGYLPWFRQAleAQELPLPAIISSYPELDVERLLALKPDLILAP 132
Cdd:cd01146     1 AKPQRIVALDWGALETLLALGVKPVGV------ADTAGYKPWIPEP--ALPLEGVVDVGTRGQPNLEAIAALKPDLILGS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 133 QSGITrESFLQLSALAPVIAYPDKPWLTPVKQQVELIAKALGKEAQAEALLRQQQAYIAQVAAENPEFNGVRLAYINAAS 212
Cdd:cd01146    73 ASRHD-EIYDQLSQIAPTVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 213 rVGNLSVYVTGDPRVDLLLALGFVLPPQlsgLNASRGHFAAHIGLERADMLDDAELLLSWYSSDKARAEVEAMAVIRRLP 292
Cdd:cd01146   152 -AGSIRLYGPNSFAGSVLEDLGLQNPWA---QETTNDSGFATISLERLAKADADVLFVFTYEDEELAQALQANPLWQNLP 227

                         250
                  ....*....|..
gi 1175509954 293 AMRRGRYLAITD 304
Cdd:cd01146   228 AVKNGRVYVVDD 239
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 6-298 2.25e-33

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 126.19  E-value: 2.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954   6 RRLLALVVFLSLGLTGCYDPQQTKAQTPPQDGyPVCITTAHGTSCIESPPKRVVTLGAGAEDWTLSLGVVPIAIephywg 85
Cdd:COG4594     4 LLLLLILLLALLLLAACGSSSSDSSSSEAAAG-ARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPVGI------ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  86 GDAQGYLPWfrQALEAQELPLPAIISSYPELDVERLLALKPDLILAPQS---GItresFLQLSALAPVIAYP--DKPWLT 160
Cdd:COG4594    77 ADDNDYDRW--VPYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIADKSrheAI----YDQLSKIAPTVLFKsrNGDYQE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 161 PVKqQVELIAKALGKEAQAEALLRQQQAYIAQVAAENPEFN-GVRLAYINAasRVGNLSVYVTGDPRVDLLLALGFVLPP 239
Cdd:COG4594   151 NLE-SFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADkGKKVAVGQF--RADGLRLYTPNSFAGSVLAALGFENPP 227

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1175509954 240 QLSGLNASrghFAAHIGLERADMLDDAELLLSWYSSDKARAEVEAMAVIRRLPAMRRGR 298
Cdd:COG4594   228 KQSKDNGY---GYSEVSLEQLPALDPDVLFIATYDDPSILKEWKNNPLWKNLKAVKNGR 283
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
 6-298 9.02e-16

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 77.32  E-value: 9.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954   6 RRLLALVVFLSLGLTGCYDPQQTkaqtppQDGYPVCITTAHGTSCIESPPKRVVTLgagaedwTLSLGVVPIAIE----- 80
Cdd:PRK10957    1 PLYRLALLLLGLLLSGIAAAQAS------AAGWPRTVTDSRGSVTLESKPQRIVST-------SVTLTGTLLAIDapvia 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  81 -----PHYWGGDAQGYlpwFRQ-ALEAQE---LPLPAIissypELDVERLLALKPDLILAPQSG--ITRESFLQLSALAP 149
Cdd:PRK10957   68 sgattPNTRVADDQGF---FRQwSDVAKErgvEVLYIG-----EPDAEAVAAQMPDLIVISATGgdSALALYDQLSAIAP 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 150 --VIAYPDKPWltpvkQQVEL-IAKALGKEAQAEALLRQQQAYIAQVAAE-NPEFNGVR-LAYiNAASRVGNLsvYVTGD 224
Cdd:PRK10957  140 tlVIDYDDKSW-----QELATqLGEATGLEKQAAAVIAQFDAQLAEVKAKiTLPPQPVSaLVY-NGAGHSANL--WTPES 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1175509954 225 PRVDLLLALGFVLPPQLSGLNASRGHFAAH----IGLER-ADMLDDAELLLSwYSSDKARAEVEAMAVIRRLPAMRRGR 298
Cdd:PRK10957  212 AQGQLLEQLGFTLAELPAGLQASTSQGKRHdiiqLGGENlAAGLNGETLFLF-AGDDKDADAFLADPLLANLPAVQNKQ 289
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 99-298 1.88e-15

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: 74.71  E-value: 1.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  99 LEAQELPLPAIISSYPELDVERLLALKPDLILAPQSGITRESFLQLSALAPVIAYPDKPWLTPVKQQVELIAKALGKEAQ 178
Cdd:pfam01497  31 LKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEELLSLIIPTVIFESSSTGESLKEQIKQLGELLGLEDE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 179 AEALLRQQQAYIAQVAAENPEFNGVRLA-YINAASRVGnlsVYVTGDPRV-DLLLALGFVlppqlSGLNASRGHFAAHIG 256
Cdd:pfam01497 111 AEELVAEIDSALAAAKKAVPSLTRKPVLvFGGADGGGY---VVAGSNTYIgDLLRILGIE-----NIAAELSGSEYAPIS 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1175509954 257 LERADMLDDAELLLSWYSSDKAR--AEVEAMAVIRRLPAMRRGR 298
Cdd:pfam01497 183 FEAILSSNPDVIIVSGRDSFTKTgpEFVAANPLWAGLPAVKNGR 226
 
Name Accession Description Interval E-value
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 53-304 3.47e-56

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: 184.41  E-value: 3.47e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  53 SPPKRVVTLGAGAEDWTLSLGVVPIAIephywgGDAQGYLPWFRQAleAQELPLPAIISSYPELDVERLLALKPDLILAP 132
Cdd:cd01146     1 AKPQRIVALDWGALETLLALGVKPVGV------ADTAGYKPWIPEP--ALPLEGVVDVGTRGQPNLEAIAALKPDLILGS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 133 QSGITrESFLQLSALAPVIAYPDKPWLTPVKQQVELIAKALGKEAQAEALLRQQQAYIAQVAAENPEFNGVRLAYINAAS 212
Cdd:cd01146    73 ASRHD-EIYDQLSQIAPTVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 213 rVGNLSVYVTGDPRVDLLLALGFVLPPQlsgLNASRGHFAAHIGLERADMLDDAELLLSWYSSDKARAEVEAMAVIRRLP 292
Cdd:cd01146   152 -AGSIRLYGPNSFAGSVLEDLGLQNPWA---QETTNDSGFATISLERLAKADADVLFVFTYEDEELAQALQANPLWQNLP 227

                         250
                  ....*....|..
gi 1175509954 293 AMRRGRYLAITD 304
Cdd:cd01146   228 AVKNGRVYVVDD 239
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 6-298 2.25e-33

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 126.19  E-value: 2.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954   6 RRLLALVVFLSLGLTGCYDPQQTKAQTPPQDGyPVCITTAHGTSCIESPPKRVVTLGAGAEDWTLSLGVVPIAIephywg 85
Cdd:COG4594     4 LLLLLILLLALLLLAACGSSSSDSSSSEAAAG-ARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPVGI------ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  86 GDAQGYLPWfrQALEAQELPLPAIISSYPELDVERLLALKPDLILAPQS---GItresFLQLSALAPVIAYP--DKPWLT 160
Cdd:COG4594    77 ADDNDYDRW--VPYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIADKSrheAI----YDQLSKIAPTVLFKsrNGDYQE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 161 PVKqQVELIAKALGKEAQAEALLRQQQAYIAQVAAENPEFN-GVRLAYINAasRVGNLSVYVTGDPRVDLLLALGFVLPP 239
Cdd:COG4594   151 NLE-SFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADkGKKVAVGQF--RADGLRLYTPNSFAGSVLAALGFENPP 227

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1175509954 240 QLSGLNASrghFAAHIGLERADMLDDAELLLSWYSSDKARAEVEAMAVIRRLPAMRRGR 298
Cdd:COG4594   228 KQSKDNGY---GYSEVSLEQLPALDPDVLFIATYDDPSILKEWKNNPLWKNLKAVKNGR 283
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 57-330 4.78e-31

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 118.56  E-value: 4.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  57 RVVTLGAGAEDWTLSLGVVPIAIephywGGDAQGYLPWfrQALEAQELPlpaIISSYPELDVERLLALKPDLILAPQSGI 136
Cdd:COG0614     2 RIVSLSPSATELLLALGAGDRLV-----GVSDWGYCDY--PELELKDLP---VVGGTGEPNLEAILALKPDLVLASSSGN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 137 TRESFLQLSAL-APVIAYPDKpWLTPVKQQVELIAKALGKEAQAEALLRQQQAYIAQVAAENPEFNGVRLAYInAASRVG 215
Cdd:COG0614    72 DEEDYEQLEKIgIPVVVLDPR-SLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLY-EIWSGD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 216 NLSVYVTGDPRVDLLLALGFVlpPQLSGLNAsrghFAAHIGLERADMLD-DAeLLLSWYSSD-----KARAEVEAMAVIR 289
Cdd:COG0614   150 PLYTAGGGSFIGELLELAGGR--NVAADLGG----GYPEVSLEQVLALDpDV-IILSGGGYDaetaeEALEALLADPGWQ 222

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1175509954 290 RLPAMRRGRYLAITDPALVMASSYgSLLSVKWAIPKLVPQL 330
Cdd:COG0614   223 SLPAVKNGRVYVVPGDLLSRPGPR-LLLALEDLAKALHPEL 262
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 56-208 8.40e-18

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: 79.53  E-value: 8.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  56 KRVVTLGAGAEDWTLSLG--VVPIAIePHYWGGDAQGYLPwfrqaleaqeLPLPAIISSYPELDVERLLALKPDLILAPQ 133
Cdd:cd00636     1 KRVVALDPGATELLLALGgdDKPVGV-ADPSGYPPEAKAL----------LEKVPDVGHGYEPNLEKIAALKPDLIIANG 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1175509954 134 SGI--TRESFLQLSALAPVIAYPDKPWLTPVKQQVELIAKALGKEAQAEALLRQQQAYIAQVAAENPEFNGVRLAYI 208
Cdd:cd00636    70 SGLeaWLDKLSKIAIPVVVVDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLV 146
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
 6-298 9.02e-16

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 77.32  E-value: 9.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954   6 RRLLALVVFLSLGLTGCYDPQQTkaqtppQDGYPVCITTAHGTSCIESPPKRVVTLgagaedwTLSLGVVPIAIE----- 80
Cdd:PRK10957    1 PLYRLALLLLGLLLSGIAAAQAS------AAGWPRTVTDSRGSVTLESKPQRIVST-------SVTLTGTLLAIDapvia 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  81 -----PHYWGGDAQGYlpwFRQ-ALEAQE---LPLPAIissypELDVERLLALKPDLILAPQSG--ITRESFLQLSALAP 149
Cdd:PRK10957   68 sgattPNTRVADDQGF---FRQwSDVAKErgvEVLYIG-----EPDAEAVAAQMPDLIVISATGgdSALALYDQLSAIAP 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 150 --VIAYPDKPWltpvkQQVEL-IAKALGKEAQAEALLRQQQAYIAQVAAE-NPEFNGVR-LAYiNAASRVGNLsvYVTGD 224
Cdd:PRK10957  140 tlVIDYDDKSW-----QELATqLGEATGLEKQAAAVIAQFDAQLAEVKAKiTLPPQPVSaLVY-NGAGHSANL--WTPES 211

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1175509954 225 PRVDLLLALGFVLPPQLSGLNASRGHFAAH----IGLER-ADMLDDAELLLSwYSSDKARAEVEAMAVIRRLPAMRRGR 298
Cdd:PRK10957  212 AQGQLLEQLGFTLAELPAGLQASTSQGKRHdiiqLGGENlAAGLNGETLFLF-AGDDKDADAFLADPLLANLPAVQNKQ 289
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 99-298 1.88e-15

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: 74.71  E-value: 1.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  99 LEAQELPLPAIISSYPELDVERLLALKPDLILAPQSGITRESFLQLSALAPVIAYPDKPWLTPVKQQVELIAKALGKEAQ 178
Cdd:pfam01497  31 LKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEELLSLIIPTVIFESSSTGESLKEQIKQLGELLGLEDE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 179 AEALLRQQQAYIAQVAAENPEFNGVRLA-YINAASRVGnlsVYVTGDPRV-DLLLALGFVlppqlSGLNASRGHFAAHIG 256
Cdd:pfam01497 111 AEELVAEIDSALAAAKKAVPSLTRKPVLvFGGADGGGY---VVAGSNTYIgDLLRILGIE-----NIAAELSGSEYAPIS 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1175509954 257 LERADMLDDAELLLSWYSSDKAR--AEVEAMAVIRRLPAMRRGR 298
Cdd:pfam01497 183 FEAILSSNPDVIIVSGRDSFTKTgpEFVAANPLWAGLPAVKNGR 226
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 44-217 9.33e-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: 70.75  E-value: 9.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  44 TAHGTSCIESPPKRVVTLGAGAEDwTLS-LGVVPIAIephywggdaqgylpwfrqaleAQELPLPAIISSYP-------- 114
Cdd:cd01140     1 HALGETKVPKNPEKVVVFDVGALD-TLDaLGVKVVGV---------------------PKSSTLPEYLKKYKddkyanvg 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 115 ---ELDVERLLALKPDLILApqSGITRESFLQLSALAPVIAY---PDKPWlTPVKQQVELIAKALGKEAQAEALLRQQQA 188
Cdd:cd01140    59 tlfEPDLEAIAALKPDLIII--GGRLAEKYDELKKIAPTIDLgadLKNYL-ESVKQNIETLGKIFGKEEEAKELVAEIDA 135

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1175509954 189 YIAQV--AAENPE------FNGVRLAYINAASRVGNL 217
Cdd:cd01140   136 SIAEAksAAKGKKkalvvlVNGGKLSAFGPGSRFGWL 172
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 103-207 7.30e-13

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: 66.53  E-value: 7.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 103 ELPLPAIISSYPELDVERLLALKPDLILAPQSGItRESFLQLSALA-PVIAYPDKPWLTPVKQQVELIAKALGKEAQAEA 181
Cdd:cd01143    38 EVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSL-AELLEKLKDAGiPVVVLPAASSLDEIYDQIELIGKITGAEEEAEK 116

                          90       100
                  ....*....|....*....|....*.
gi 1175509954 182 LLRQQQAYIAQVAAENPEFNGVRLAY 207
Cdd:cd01143   117 LVKEMKQKIDKVKDKGKTIKKSKVYI 142
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 51-298 3.36e-12

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: 65.82  E-value: 3.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  51 IESPPKRVVTLGAGAEDWTLsLGVVPIAIEPHywggdaqgylPWFRQALEAQELPLPAIISSYPelDVERLLALKPDLIL 130
Cdd:cd01138     5 IPAKPKRIVALSGETEGLAL-LGIKPVGAASI----------GGKNPYYKKKTLAKVVGIVDEP--NLEKVLELKPDLII 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 131 ApqSGITRESFLQLSALAPVIAYP-DKPWltpVKQQVELIAKALGKEAQAEALLrqqQAYIAQVAAENPEFNGVRLAYIN 209
Cdd:cd01138    72 V--SSKQEENYEKLSKIAPTVPVSyNSSD---WEEQLKEIGKLLNKEDEAEKWL---ADYKQKAKEAKEKIKKKLGNDKS 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 210 AASRVGNLSVYVTGDP--RVDLLL--ALGFVLPPQLSGLNASRGHfaAHIGLER-ADMLDDAeLLLSWYSSDKARAEVEA 284
Cdd:cd01138   144 VAVLRGRKQIYVFGEDgrGGGPILyaDLGLKAPEKVKEIEDKPGY--AAISLEVlPEFDADY-IFLLFFTGPEAKADFES 220

                         250
                  ....*....|....
gi 1175509954 285 MAVIRRLPAMRRGR 298
Cdd:cd01138   221 LPIWKNLPAVKNNH 234
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 39-274 1.22e-10

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 61.61  E-value: 1.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  39 PVCITTAHGTSCIESPPKRVVTLGAGAEDWTLSLGVVPIAIEPHywgGDAQGYLPWFRQALEaqelPLPAI-ISSYPELd 117
Cdd:PRK11411   23 AVTVQDEQGTFTLEKTPQRIVVLELSFVDALAAVGVSPVGVADD---NDAKRILPEVRAHLK----PWQSVgTRSQPSL- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 118 vERLLALKPDLILAP---QSGITREsflqLSALAPVIAYPDK-----PWLtpvkQQVELIAKALGKEAQAEALLRQQQAY 189
Cdd:PRK11411   95 -EAIAALKPDLIIADssrHAGVYIA----LQKIAPTLLLKSRnetyqENL----QSAAIIGEVLGKKREMQARIEQHKER 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 190 IAQVAAENPEfnGVRLAYinAASRVGNLSVYVTGDPRVDLLLALGFVLPPqlsgLNASRGHFAAhIGLERADMLDDAELL 269
Cdd:PRK11411  166 MAQFASQLPK--GTRVAF--GTSREQQFNLHSPESYTGSVLAALGLNVPK----APMNGAAMPS-ISLEQLLALNPDWLL 236


                  ....*
gi 1175509954 270 LSWYS 274
Cdd:PRK11411  237 VAHYR 241
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 55-199 5.74e-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: 56.12  E-value: 5.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  55 PKRVVTLGAGAEDWTLSLG----VVpiaiephywGGDAQGYLPwfrqaLEAQELPlpaIISSYPELDVERLLALKPDLIL 130
Cdd:cd01149     1 PERIVSLGGSVTEIVYALGagdrLV---------GVDSTSTYP-----EAAAKLP---DVGYMRQLSAEGVLSLKPTLVI 63

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 131 APQSGITRESFLQLSALA-PVIAYPDKPWLTPVKQQVELIAKALGKEAQAEALLRQQQAYIAQVAAENPE 199
Cdd:cd01149    64 ASDEAGPPEALDQLRAAGvPVVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAA 133
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 100-198 8.13e-09

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 55.97  E-value: 8.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 100 EAQELPlpaIISSYPELDVERLLALKPDLILAPQSGITRESFLQLSALA-PVIAYPDKPWLTPVKQQVELIAKALGKEAQ 178
Cdd:COG4558    62 AAKALP---DVGYMRQLSAEGILSLKPTLVLASEGAGPPEVLDQLRAAGvPVVVVPAAPSLEGVLAKIRAVAAALGVPEA 138

                          90       100
                  ....*....|....*....|
gi 1175509954 179 AEALLRQQQAYIAQVAAENP 198
Cdd:COG4558   139 GEALAARLEADLAALAARVA 158
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 51-195 8.33e-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: 8.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  51 IESPPKRVVtLGAGAEDWTLslgvvpIAIEPHY-------WGGDAQGYLPWFRQALEAQeLP----LPAIISSY-PELDV 118
Cdd:cd01139    13 LDAPVERVL-LGEGRQLYAL------ALLEGENpfarivgWGGDLKKGDPDTYAKYKEK-FPeiadIPLIGSTYnGDFSV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 119 ERLLALKPDLILAPQSGITRESFL----QLSALA-PVIA--YPDKPwLTPVKQQVELIAKALGKEAQAEALLRQQQAYIA 191
Cdd:cd01139    85 EKVLTLKPDLVILNIWAKTTAEESgileKLEQAGiPVVFvdFRQKP-LKNTTPSMRLLGKALGREERAEEFIEFYQERID 163


                  ....
gi 1175509954 192 QVAA 195
Cdd:cd01139   164 RIRD 167
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 57-193 3.50e-07

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: 50.80  E-value: 3.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  57 RVVTLGAGAEDWTLSLGVVPIAIephywGGDAQGYLPWFRQALEA----QELPLPAIISSYPELDVERLLALKPDLILAP 132
Cdd:cd01147     7 RVVAAGPGALRLLYALAAPDKIV-----GVDDAEKSDEGRPYFLAspelKDLPVIGRGGRGNTPNYEKIAALKPDVVIDV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1175509954 133 --QSGITRESFLQLSALAPVIAYPDKPWLTPVKQQVELIAKALGKEAQAEALLRQQQAYIAQV 193
Cdd:cd01147    82 gsDDPTSIADDLQKKTGIPVVVLDGGDSLEDTPEQIRLLGKVLGKEERAEELISFIESILADV 144
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 100-208 1.46e-06

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: 48.84  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 100 EAQELPlpaIISSYPELDVERLLALKPDLILAPQSGITRESFLQLSALAPVIAYPDKPWLTPVKQQVELIAKALGKEAQA 179
Cdd:cd01144    35 EAKKLP---RVGGFYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAGIPVLVSEPQTLDDILADIRRLGTLAGRPARA 111

                          90       100
                  ....*....|....*....|....*....
gi 1175509954 180 EALLRQQQAYIAQVAAENPEFNGVRLAYI 208
Cdd:cd01144   112 EELAEALRRRLAALRKQYASKPPPRVFYQ 140
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 115-210 5.62e-06

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: 47.35  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 115 ELDVERLLALKPDLILAPqSGITRESFLQLSALAPVIAYPDKPWLTpVKQQVELIAKALGKEAQAEAL---LRQQQAYIA 191
Cdd:cd01142    78 DVNIEELLALKPDVVIVW-STDGKEAGKAVLRLLNALSLRDAELEE-VKLTIALLGELLGRQEKAEALvayFDDNLAYVA 155

                          90
                  ....*....|....*....
gi 1175509954 192 QVAAENPEFNGVRLAYINA 210
Cdd:cd01142   156 ARTKKLPDSERPRVYYAGP 174
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 38-228 4.55e-05

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: 44.64  E-value: 4.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  38 YPVCITTAHGTSCIESPPKRVVTLGAGAEDWTLSLGVvpiaiephywGGDAQGYLPWFRQA---LEAQELPLPAIISSYP 114
Cdd:cd01148     1 YPLTVENCGRSVTFDKAPQRVVSNDQNTTEMMLALGL----------QDRMVGTAGIDNKDlpeLKAKYDKVPELAKKYP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 115 ELdvERLLALKPDLILA-------PQSGITRESF----LQLSALAPVIAYPDKPW-LTPVKQQVELIAKALGKEAQAEAL 182
Cdd:cd01148    71 SK--ETVLAARPDLVFGgwsygfdKGGLGTPDSLaelgIKTYILPESCGQRRGEAtLDDVYNDIRNLGKIFDVEDRADKL 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1175509954 183 LRQQQAYIAQVAAenpefngvRLAYINAASRVgnlSVYVTGDPRVD 228
Cdd:cd01148   149 VADLKARLAEISA--------KVKGDGKKVAV---FVYDSGEDKPF 183
PRK10576 PRK10576
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
55-299 3.16e-04

Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;


Pssm-ID: 236719  Cd Length: 292  Bit Score: 41.92  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  55 PKRVVTLgagaeDW-----TLSLGVVPIAIephywgGDAQGYLPWFRQAleaqELPLPAI-ISSYPELDVERLLALKPDL 128
Cdd:PRK10576   32 PNRIVAL-----EWlpvelLLALGVTPYGV------ADTHNYRLWVSEP----ALPDSVIdVGLRTEPNLELLTQMKPSL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 129 ILAPQS-GITREsflQLSALAPV--IAYPD--KPwLTPVKQQVELIAKALGKEAQAEALLRQQQAYIAQVAAenpefngv 203
Cdd:PRK10576   97 ILWSAGyGPSPE---KLARIAPGrgFAFSDgkKP-LAVARKSLVELAQRLNLEAAAETHLAQFDDFIASAKP-------- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 204 RLAyinaASRVGNLSVYVTGDPRVDLLLALGFVLPPQLSGL---NASRGH--F--AAHIGLERADMLDDAELLLSWYSSD 276
Cdd:PRK10576  165 RLA----GRGQRPLLLTSLIDPRHALVFGPNSLFQEVLDELgieNAWQGEtnFwgSTVVGIERLAAYKDADVICFDHGNS 240

                         250       260
                  ....*....|....*....|...
gi 1175509954 277 KARAEVEAMAVIRRLPAMRRGRY 299
Cdd:PRK10576  241 KDMQQLMATPLWQAMPFVRAGRF 263
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 51-201 3.35e-04

Periplasmic binding protein TroA_d. 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: 238561 [Multi-domain]  Cd Length: 186  Bit Score: 41.25  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  51 IESPPKRVVTLGAGAEDWTLSLGVVPIAIephywgGDAQGYLPWFRQALEAQelpLPAIISSYPELDVERLLALKPDLIL 130
Cdd:cd01141     4 IKVPPKRIVVLSPTHVDLLLALDKADKIV------GVSASAYDLNTPAVKER---IDIQVGPTGSLNVELIVALKPDLVI 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1175509954 131 APQSGITR---ESFLQLSALAPVIAYPDKPWltpvkQQVELIAKAL-----GKEAQAEALLRQQQAYIAQVAAENPEFN 201
Cdd:cd01141    75 LYGGFQAQtilDKLEQLGIPVLYVNEYPSPL-----GRAEWIKFAAafygvGKEDKADEAFAQIAGRYRDLAKKVSNLN 148
PRK03379 PRK03379
vitamin B12-transporter protein BtuF; Provisional
 110-198 5.49e-04

vitamin B12-transporter protein BtuF; Provisional


Pssm-ID: 179575 [Multi-domain]  Cd Length: 260  Bit Score: 41.21  E-value: 5.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954 110 ISSYPELDVERLLALKPDLILAPQSGITRESFLQLSALAPVIAYPDkpwltpvKQQVELIAKALGKEAQ----------- 178
Cdd:PRK03379   57 VATWQGMNLERIVALKPDLVLAWRGGNAERQVDQLASLGIKVMWVD-------ATSIEQIANALRQLAPwspqpekaeqa 129

                          90       100
                  ....*....|....*....|
gi 1175509954 179 AEALLRQQQAYIAQVAAENP 198
Cdd:PRK03379  130 AQSLLQQYAALKAQYADKPK 149
PRK14048 PRK14048
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
 1-193 6.23e-03

ferrichrome/ferrioxamine B periplasmic transporter; Provisional


Pssm-ID: 172540 [Multi-domain]  Cd Length: 374  Bit Score: 38.34  E-value: 6.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954   1 MLCEARRLLALVVFLSLGLTgcydPQQTKAQTPpqdgYPVCITTAHGTSCIESPPKRVVTLGAGAEDWTLSLgvvpiaIE 80
Cdd:PRK14048    1 LLLCRRSLVRLVAFLAIAFL----ALSALAEVQ----WPMTVTDAVGREVTIPAPPKAVLLGSGFNLIALSL------IH 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175509954  81 PHY------WGGDAQG-----YLPWFRQALEAQELPLpAIISSYPELDVERLLALKPDL-ILA-----PQSGITRESFLQ 143
Cdd:PRK14048   67 PDPvsllagWSGDMKGdnpeiYESFLRKFPELADVPL-IDDGSGPGLSFETILTLKADLaILAnwqadTEAGQRAIEYLE 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1175509954 144 LSALAPVIAYPDKPWLTPVKQQVELIAKALGKEAQAEALLRQQQAYIAQV 193
Cdd:PRK14048  146 SIGVPVIVVDFNNEALKNTPDNMRLLGKVFEREEQAEDFARFYEERLARI 195
 
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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