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Conserved domains on  [gi|544682550|ref|WP_021114552|]
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iron ABC transporter substrate-binding protein [Glaesserella parasuis]

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 ...
 35-282 6.95e-70

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: 218.74  E-value: 6.95e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  35 AERVQKIISAGNPSDVVLLAVA-PEKLAGFAGFKMqSTSGKLF---PETLQKLETLGRVsGKNSSLSPEKIVALSPDLIV 110
Cdd:cd01147    2 PKPVERVVAAGPGALRLLYALAaPDKIVGVDDAEK-SDEGRPYflaSPELKDLPVIGRG-GRGNTPNYEKIAALKPDVVI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 111 DVGNVSPNYldQAKKTQAHTQVSYVLLDGK--LERTPELLRELGEIVGQTKQAETLAKYAEETLKQAVGSAKNVA----K 184
Cdd:cd01147   80 DVGSDDPTS--IADDLQKKTGIPVVVLDGGdsLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDIPdeekP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 185 TAYLAR----GADGLETGFKGSIhtEAMELVGLKNVVEG-EHKGLAKVSMEQLLQWNPDIIFTQFPEFYQMIWEA----P 255
Cdd:cd01147  158 TVYFGRigtkGAAGLESGLAGSI--EVFELAGGINVADGlGGGGLKEVSPEQILLWNPDVIFLDTGSFYLSLEGYaknrP 235

                        250       260
                 ....*....|....*....|....*..
gi 544682550 256 QWQALDAVKNKQVYLIPHQPFGWLDSP 282
Cdd:cd01147  236 FWQSLKAVKNGRVYLLPALPFNWYDTP 262
 
Name Accession Description Interval E-value
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 35-282 6.95e-70

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: 218.74  E-value: 6.95e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  35 AERVQKIISAGNPSDVVLLAVA-PEKLAGFAGFKMqSTSGKLF---PETLQKLETLGRVsGKNSSLSPEKIVALSPDLIV 110
Cdd:cd01147    2 PKPVERVVAAGPGALRLLYALAaPDKIVGVDDAEK-SDEGRPYflaSPELKDLPVIGRG-GRGNTPNYEKIAALKPDVVI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 111 DVGNVSPNYldQAKKTQAHTQVSYVLLDGK--LERTPELLRELGEIVGQTKQAETLAKYAEETLKQAVGSAKNVA----K 184
Cdd:cd01147   80 DVGSDDPTS--IADDLQKKTGIPVVVLDGGdsLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDIPdeekP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 185 TAYLAR----GADGLETGFKGSIhtEAMELVGLKNVVEG-EHKGLAKVSMEQLLQWNPDIIFTQFPEFYQMIWEA----P 255
Cdd:cd01147  158 TVYFGRigtkGAAGLESGLAGSI--EVFELAGGINVADGlGGGGLKEVSPEQILLWNPDVIFLDTGSFYLSLEGYaknrP 235

                        250       260
                 ....*....|....*....|....*..
gi 544682550 256 QWQALDAVKNKQVYLIPHQPFGWLDSP 282
Cdd:cd01147  236 FWQSLKAVKNGRVYLLPALPFNWYDTP 262
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 40-306 7.45e-42

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 146.30  E-value: 7.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  40 KIISAGNPSDVVLLAV-APEKLAGFAGFKMQStsgklFPET-LQKLETLGRvsgkNSSLSPEKIVALSPDLIV-DVGNVS 116
Cdd:COG0614    2 RIVSLSPSATELLLALgAGDRLVGVSDWGYCD-----YPELeLKDLPVVGG----TGEPNLEAILALKPDLVLaSSSGND 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 117 PNYLDQAKKTQAHTqvsYVLLDGKLERTPELLRELGEIVGQTKQAETLAKYAEETL---KQAVGSAKNVAKTAYLARGAD 193
Cdd:COG0614   73 EEDYEQLEKIGIPV---VVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLaavRARLAGAEERPTVLYEIWSGD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 194 GLETGFKGSIHTEAMELVGLKNVVEGEHKGLAKVSMEQLLQWNPDIIFTQFPEFYQMIWEA--------PQWQALDAVKN 265
Cdd:COG0614  150 PLYTAGGGSFIGELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEalealladPGWQSLPAVKN 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 544682550 266 KQVYLIPHQPFGWldspPSLNRLLGMKWLQHHLsggEPKAF 306
Cdd:COG0614  230 GRVYVVPGDLLSR----PGPRLLLALEDLAKAL---HPELF 263
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 67-272 3.44e-17

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: 79.33  E-value: 3.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550   67 KMQSTSGKLFPETLQKLETLGRVSGKNSSLSPEKIVALSPDLIVDVGNVSPNYLDQAKKTQAHTqVSYVLLDGKLERTpE 146
Cdd:pfam01497  19 SIVGVDAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEELLSLIIPT-VIFESSSTGESLK-E 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  147 LLRELGEIVGQTKQAETL-AKYAEET--LKQAVGSAKNvAKTAYLARGADGLETGFkGSIH--TEAMELVGLKNVV-EGE 220
Cdd:pfam01497  97 QIKQLGELLGLEDEAEELvAEIDSALaaAKKAVPSLTR-KPVLVFGGADGGGYVVA-GSNTyiGDLLRILGIENIAaELS 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 544682550  221 HKGLAKVSMEQLLQWNPDIIFT-----QFPEFYQMIWEAPQWQALDAVKNKQVYLIP 272
Cdd:pfam01497 175 GSEYAPISFEAILSSNPDVIIVsgrdsFTKTGPEFVAANPLWAGLPAVKNGRVYTLP 231
IsdE TIGR03659
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ...
 2-291 2.34e-14

heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins is observed primarily in close proximity with proteins localized to the cell wall and bearing the NEAT (NEAr Transporter, pfam05031) heme-binding domain. IsdE has been shown to bind heme and is involved in the process of scavenging heme for the purpose of obtaining iron.


Pssm-ID: 274706 [Multi-domain]  Cd Length: 289  Bit Score: 72.31  E-value: 2.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550    2 KKFLS---AFALLAFVTSGVSANEqpisTHFGDLPKAERvQKIIsAGNPSDVVLLAVAPEKLAGFAgfkmqsTSGKLFPE 78
Cdd:TIGR03659   1 KKILSlvlLAVLSLGLTGCSSSKE----KSKVSNKKSKE-ERIV-ATSVAVTEILDKLDLDLVGVP------TSQKTLPK 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550   79 TLQKLETLGrvsgknSSLSP--EKIVALSPDLIVDVGNVSPNYldQAKKTQAHTQVSYVLLDgKLERTPELLRELGEIVG 156
Cdd:TIGR03659  69 RYKDVPEVG------NPMSPdmEKIKSLKPTVVLSVTTLEEDL--GPKFKQLGVEATFLNLT-SVDGMKKSITELGEKYG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  157 QTKQAETLAKYAEETLKQAVGSAKNVAK-TAYLARGADG-----LETGFKGSIhteaMELVGLKNVVEGEHKGLAKVSME 230
Cdd:TIGR03659 140 REEQAEKLVKEINEKEAEVKKKVKGKKKpKVLILMGVPGsylvaTENSYIGDL----VKLAGGENVYKGNKQEYLSSNTE 215

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544682550  231 QLLQWNPDIIF-----------TQFPEFYQmiwEAPQWQALDAVKNKQVYLIPHQPFGW---LDSPPSLNRLLGM 291
Cdd:TIGR03659 216 YLLKANPDIILraahgmpdevkKMFDEEFK---TNDIWKHFEAVKNNRVYDLDEELFGMtanLKVAEALDELKKI 287
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
 89-246 1.62e-06

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 49.14  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  89 VSGKNSS-LSPEKIVALSPDLIVdVGNVSPN----YLDQAKKTQAH----TQVSYVlldgklertpellRELGEIVGQTK 159
Cdd:PRK09534 102 VSGGQPFgVNVEAVVGLDPDLVL-APNAVAGdtvtRLREAGITVFHfpaaTSIEDV-------------AEKTATIGRLT 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 160 QAETLAKYAEETLKQAVGSAKNVAK------TAYLARGaDGLETGfKGSIHTEAMELVGLKNVV-EGEHKGLAKVSMEQL 232
Cdd:PRK09534 168 GNCEAAAETNAEMRDRVDAVEDRTAdvddrpRVLYPLG-DGYTAG-GNTFIGALIEAAGGHNVAaDATTDGYPQLSEEVI 245

                        170
                 ....*....|....
gi 544682550 233 LQWNPDIIFTQFPE 246
Cdd:PRK09534 246 VQQDPDVIVVATAS 259
 
Name Accession Description Interval E-value
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 35-282 6.95e-70

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: 218.74  E-value: 6.95e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  35 AERVQKIISAGNPSDVVLLAVA-PEKLAGFAGFKMqSTSGKLF---PETLQKLETLGRVsGKNSSLSPEKIVALSPDLIV 110
Cdd:cd01147    2 PKPVERVVAAGPGALRLLYALAaPDKIVGVDDAEK-SDEGRPYflaSPELKDLPVIGRG-GRGNTPNYEKIAALKPDVVI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 111 DVGNVSPNYldQAKKTQAHTQVSYVLLDGK--LERTPELLRELGEIVGQTKQAETLAKYAEETLKQAVGSAKNVA----K 184
Cdd:cd01147   80 DVGSDDPTS--IADDLQKKTGIPVVVLDGGdsLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDIPdeekP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 185 TAYLAR----GADGLETGFKGSIhtEAMELVGLKNVVEG-EHKGLAKVSMEQLLQWNPDIIFTQFPEFYQMIWEA----P 255
Cdd:cd01147  158 TVYFGRigtkGAAGLESGLAGSI--EVFELAGGINVADGlGGGGLKEVSPEQILLWNPDVIFLDTGSFYLSLEGYaknrP 235

                        250       260
                 ....*....|....*....|....*..
gi 544682550 256 QWQALDAVKNKQVYLIPHQPFGWLDSP 282
Cdd:cd01147  236 FWQSLKAVKNGRVYLLPALPFNWYDTP 262
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 36-298 6.20e-43

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: 149.81  E-value: 6.20e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  36 ERVQKIISAGNPSDVVLLAVAPEKLAgfAGFKMQSTSGKLFPETLQKLETLGRVsGKNSSLSPEKIVALSPDLIVdvgnV 115
Cdd:cd01142   22 DEVKRIAALWGAGNAVVAALGGGKLI--VATTSTVQQEPWLYRLAPSLENVATG-GTGNDVNIEELLALKPDVVI----V 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 116 SPNYLDQAKKTQAHTQVSYVLLDGKLERTPELLRELGEIVGQTKQAETLAKYAEETLKQAVGSAKNVA---KTAYLARGA 192
Cdd:cd01142   95 WSTDGKEAGKAVLRLLNALSLRDAELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAARTKKLPdseRPRVYYAGP 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 193 DGLETGFKGSIHTEAMELVGLKNV-VEGEHKGLAKVSMEQLLQWNPDIIFTQFPEFYQMIWEAPQWQALDAVKNKQVYLI 271
Cdd:cd01142  175 DPLTTDGTGSITNSWIDLAGGINVaSEATKKGSGEVSLEQLLKWNPDVIIVGNADTKAAILADPRWQNLRAVKNGRVYVN 254

                        250       260
                 ....*....|....*....|....*..
gi 544682550 272 PHQPFgWLDSPPSLNRLLGMkWLQHHL 298
Cdd:cd01142  255 PEGAF-WWDRPSAEEALLGL-WLAKTL 279
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 40-306 7.45e-42

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 146.30  E-value: 7.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  40 KIISAGNPSDVVLLAV-APEKLAGFAGFKMQStsgklFPET-LQKLETLGRvsgkNSSLSPEKIVALSPDLIV-DVGNVS 116
Cdd:COG0614    2 RIVSLSPSATELLLALgAGDRLVGVSDWGYCD-----YPELeLKDLPVVGG----TGEPNLEAILALKPDLVLaSSSGND 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 117 PNYLDQAKKTQAHTqvsYVLLDGKLERTPELLRELGEIVGQTKQAETLAKYAEETL---KQAVGSAKNVAKTAYLARGAD 193
Cdd:COG0614   73 EEDYEQLEKIGIPV---VVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLaavRARLAGAEERPTVLYEIWSGD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 194 GLETGFKGSIHTEAMELVGLKNVVEGEHKGLAKVSMEQLLQWNPDIIFTQFPEFYQMIWEA--------PQWQALDAVKN 265
Cdd:COG0614  150 PLYTAGGGSFIGELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEalealladPGWQSLPAVKN 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 544682550 266 KQVYLIPHQPFGWldspPSLNRLLGMKWLQHHLsggEPKAF 306
Cdd:COG0614  230 GRVYVVPGDLLSR----PGPRLLLALEDLAKAL---HPELF 263
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 1-272 1.95e-19

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 87.28  E-value: 1.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550   1 MKKFLSAFALLAFVT------------SGVSANEQPIS-TH-FGDLPKAERVQKIISAGNPS--DVVLLAVAPeklAGFA 64
Cdd:COG4594    1 MKKLLLLLILLLALLllaacgssssdsSSSEAAAGARTvKHaMGETTIPGTPKRVVVLEWSFadALLALGVTP---VGIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  65 gfkmQSTSGKLFPETLQKL----ETLGrvSGKNSSLspEKIVALSPDLIV-DVGNVSPNYlDQAKKTqAHTqVSYVLLDG 139
Cdd:COG4594   78 ----DDNDYDRWVPYLRDLikgvTSVG--TRSQPNL--EAIAALKPDLIIaDKSRHEAIY-DQLSKI-APT-VLFKSRNG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 140 KLERTPELLRELGEIVGQTKQAET-LAKYAE--ETLKQAVGSAKNVAKTAYLARGADGL----ETGFKGSIhteaMELVG 212
Cdd:COG4594  147 DYQENLESFKTIAKALGKEEEAEAvLADHDQriAEAKAKLAAADKGKKVAVGQFRADGLrlytPNSFAGSV----LAALG 222

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544682550 213 LKNVVEG---EHKGLAKVSMEQLLQWNPDIIF-TQF--PEFYQMIWEAPQWQALDAVKNKQVYLIP 272
Cdd:COG4594  223 FENPPKQskdNGYGYSEVSLEQLPALDPDVLFiATYddPSILKEWKNNPLWKNLKAVKNGRVYEVD 288
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 91-289 1.97e-19

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: 86.19  E-value: 1.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  91 GKNSSLSPEKIVALSPDLIVDVGNVSPNYLDQAKKTqAHTqvsyVLLD--GKLERTPELLRELGEIVGQTKQAET-LAKY 167
Cdd:cd01146   51 GTRGQPNLEAIAALKPDLILGSASRHDEIYDQLSQI-APT----VLLDssPWLAEWKENLRLIAKALGKEEEAEKlLAEY 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 168 AE--ETLKQAVGSAKNvaKTAYLARGADG------LETGFKGSIHTEamelVGLKNVVEGE---HKGLAKVSMEQLLQWN 236
Cdd:cd01146  126 DQrlAELRQKLPDKGP--KPVSVVRFSDAgsirlyGPNSFAGSVLED----LGLQNPWAQEttnDSGFATISLERLAKAD 199

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 544682550 237 PDIIFTQF---PEFYQMIWEAPQWQALDAVKNKQVYLIPHQPFGWLDSPPSLNRLL 289
Cdd:cd01146  200 ADVLFVFTyedEELAQALQANPLWQNLPAVKNGRVYVVDDVWWFFGGGLSAARLLL 255
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 67-272 3.44e-17

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: 79.33  E-value: 3.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550   67 KMQSTSGKLFPETLQKLETLGRVSGKNSSLSPEKIVALSPDLIVDVGNVSPNYLDQAKKTQAHTqVSYVLLDGKLERTpE 146
Cdd:pfam01497  19 SIVGVDAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEELLSLIIPT-VIFESSSTGESLK-E 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  147 LLRELGEIVGQTKQAETL-AKYAEET--LKQAVGSAKNvAKTAYLARGADGLETGFkGSIH--TEAMELVGLKNVV-EGE 220
Cdd:pfam01497  97 QIKQLGELLGLEDEAEELvAEIDSALaaAKKAVPSLTR-KPVLVFGGADGGGYVVA-GSNTyiGDLLRILGIENIAaELS 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 544682550  221 HKGLAKVSMEQLLQWNPDIIFT-----QFPEFYQMIWEAPQWQALDAVKNKQVYLIP 272
Cdd:pfam01497 175 GSEYAPISFEAILSSNPDVIIVsgrdsFTKTGPEFVAANPLWAGLPAVKNGRVYTLP 231
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 1-272 3.98e-16

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 77.15  E-value: 3.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550   1 MKKFLSAFALLAFVTSGVSAneqpiSTHFGDlpkAERvqkIISAGnpSDV--VLLAV-APEKLAGfagfkMQSTSgkLFP 77
Cdd:COG4558    1 MKRLALALLLLALAALAAGA-----SVAAAA---AER---IVSLG--GSVteIVYALgAGDRLVG-----VDTTS--TYP 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  78 ETLQKLETLGRVSgknsSLSPEKIVALSPDLIV-DVGNVSPNYLDQAKKtqahTQVSYVLLDGK--LERTPELLRELGEI 154
Cdd:COG4558   61 AAAKALPDVGYMR----QLSAEGILSLKPTLVLaSEGAGPPEVLDQLRA----AGVPVVVVPAApsLEGVLAKIRAVAAA 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 155 VGQTKQAETLAKYAEETLKQAVGSAKNVAKTA----YLARGADGLETGFKGSIHTEAMELVGLKNVVEGeHKGLAKVSME 230
Cdd:COG4558  133 LGVPEAGEALAARLEADLAALAARVAAIGKPPrvlfLLSRGGGRPMVAGRGTAADALIRLAGGVNAAAG-FEGYKPLSAE 211

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 544682550 231 QLLQWNPDIIFTqfpefyqM------------IWEAPQWQALDAVKNKQVYLIP 272
Cdd:COG4558  212 ALIAAAPDVILV-------MtrgleslggvdgLLALPGLAQTPAGKNKRIVAMD 258
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 36-242 3.08e-15

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: 73.08  E-value: 3.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  36 ERVQKIISAGnPSD-VVLLAV-APEKLAGFAGFkmqSTsgklFPETLQKLETLGrvSGKNSSLspEKIVALSPDLIVDVG 113
Cdd:cd01143    1 KEPERIVSLS-PSItEILFALgAGDKIVGVDTY---SN----YPKEVRKKPKVG--SYSNPNV--EKIVALKPDLVIVSS 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 114 NVSPNYLDQAKKtqAHTQVSYVLLDGKLERTPELLRELGEIVGQTKQAETLAKYAEETLKQAVGSAKNVAK-TAYLARGA 192
Cdd:cd01143   69 SSLAELLEKLKD--AGIPVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKsKVYIEVSL 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 544682550 193 DGLETGFKGSIHTEAMELVGLKNVVEGEhKGLAKVSMEQLLQWNPDIIFT 242
Cdd:cd01143  147 GGPYTAGKNTFINELIRLAGAKNIAADS-GGWPQVSPEEILKANPDVIIL 195
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 76-321 4.76e-15

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: 75.04  E-value: 4.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  76 FPEtLQKLETLGrvSGKNSSLSPEKIVALSPDL-IVDVGNVSP----NYLDQAkkTQAHTQVSYVLLDGK-LERTPELLR 149
Cdd:cd01139   65 FPE-IADIPLIG--STYNGDFSVEKVLTLKPDLvILNIWAKTTaeesGILEKL--EQAGIPVVFVDFRQKpLKNTTPSMR 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 150 ELGEIVGQTKQAETLAKYAEETLK----QAVGSAKNVAKTaYLARGADGLE---TGFKGSIHTEAMELVGLKNVVEGEHK 222
Cdd:cd01139  140 LLGKALGREERAEEFIEFYQERIDrirdRLAKINEPKPKV-FIELGAGGPEeccSTYGNGNWGELVDAAGGDNIADGLIP 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 223 G-LAKVSMEQLLQWNPDIIF-----------------------TQfPEFYQMIWEAPQWQALDAVKNKQVYLIPHQpfgW 278
Cdd:cd01139  219 GtSGELNAEYVIAANPEIIIatggnwakdpsgvslgpdgttadAK-ESLLRALLKRPGWSSLQAVKNGRVYALWHQ---F 294

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 544682550 279 LDSPPSLNRLLGM-KWLQhhlsggePKAFI---PE--LKTFYKLFYHID 321
Cdd:cd01139  295 YRSPYNFVALEAFaKWLY-------PELFKdldPEatLQEFHRQFLPVD 336
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 77-272 5.54e-15

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: 73.49  E-value: 5.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  77 PETLQKLEtlgRVSGkNSSLSPEKIVALSPDLIV--DVGNVSPnylDQAKKTQAHTQVsyVLLDGK-LERTPELLRELGE 153
Cdd:cd01144   33 PPEAKKLP---RVGG-FYQLDLERVLALKPDLVIawDDCNVCA---VVDQLRAAGIPV--LVSEPQtLDDILADIRRLGT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 154 IVGQTKQAETLAKYAEETLKQ--AVGSAKNVAKTAYLArGADGLETGFKGSIhTEAMELVGLKNVVEGEHKGLAKVSMEQ 231
Cdd:cd01144  104 LAGRPARAEELAEALRRRLAAlrKQYASKPPPRVFYQE-WIDPLMTAGGDWV-PELIALAGGVNVFADAGERSPQVSWED 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 544682550 232 LLQWNPDIIFTQ---FPEFYQMIWEAPQWQALDAVKNKQVYLIP 272
Cdd:cd01144  182 VLAANPDVIVLSpcgFGFTPAILRKEPAWQALPAVRNGRVYAVD 225
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 39-188 1.75e-14

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: 69.90  E-value: 1.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  39 QKIISAGNPSDVVLLAVAPE-KLAGfagfkmqSTSGKLFPETLQKLETLGRVSGKNSSLSPEKIVALSPDLIVDVGNVSP 117
Cdd:cd00636    1 KRVVALDPGATELLLALGGDdKPVG-------VADPSGYPPEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLE 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544682550 118 NYLDQAKKTQAHTQVSYVLLDGKLERTPELLRELGEIVGQTKQAETLAKYAEETLKQAVGSAKNVAKTAYL 188
Cdd:cd00636   74 AWLDKLSKIAIPVVVVDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVS 144
IsdE TIGR03659
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ...
 2-291 2.34e-14

heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins is observed primarily in close proximity with proteins localized to the cell wall and bearing the NEAT (NEAr Transporter, pfam05031) heme-binding domain. IsdE has been shown to bind heme and is involved in the process of scavenging heme for the purpose of obtaining iron.


Pssm-ID: 274706 [Multi-domain]  Cd Length: 289  Bit Score: 72.31  E-value: 2.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550    2 KKFLS---AFALLAFVTSGVSANEqpisTHFGDLPKAERvQKIIsAGNPSDVVLLAVAPEKLAGFAgfkmqsTSGKLFPE 78
Cdd:TIGR03659   1 KKILSlvlLAVLSLGLTGCSSSKE----KSKVSNKKSKE-ERIV-ATSVAVTEILDKLDLDLVGVP------TSQKTLPK 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550   79 TLQKLETLGrvsgknSSLSP--EKIVALSPDLIVDVGNVSPNYldQAKKTQAHTQVSYVLLDgKLERTPELLRELGEIVG 156
Cdd:TIGR03659  69 RYKDVPEVG------NPMSPdmEKIKSLKPTVVLSVTTLEEDL--GPKFKQLGVEATFLNLT-SVDGMKKSITELGEKYG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  157 QTKQAETLAKYAEETLKQAVGSAKNVAK-TAYLARGADG-----LETGFKGSIhteaMELVGLKNVVEGEHKGLAKVSME 230
Cdd:TIGR03659 140 REEQAEKLVKEINEKEAEVKKKVKGKKKpKVLILMGVPGsylvaTENSYIGDL----VKLAGGENVYKGNKQEYLSSNTE 215

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544682550  231 QLLQWNPDIIF-----------TQFPEFYQmiwEAPQWQALDAVKNKQVYLIPHQPFGW---LDSPPSLNRLLGM 291
Cdd:TIGR03659 216 YLLKANPDIILraahgmpdevkKMFDEEFK---TNDIWKHFEAVKNNRVYDLDEELFGMtanLKVAEALDELKKI 287
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 40-271 2.70e-13

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: 68.51  E-value: 2.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  40 KIISAGNPSDVVLLAVapeklagfaGFKMQSTSGKLFPETLQKLETLGRVSGKNSSLSPEKIVALSPDLIVdVGNVSPNY 119
Cdd:cd01138   10 KRIVALSGETEGLALL---------GIKPVGAASIGGKNPYYKKKTLAKVVGIVDEPNLEKVLELKPDLII-VSSKQEEN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 120 LDQAKKTQAHTQVSYVLLDGKlertpELLRELGEIVGQTKQAET-LAKY------AEETLKQAVGSAKNVAKTA----YL 188
Cdd:cd01138   80 YEKLSKIAPTVPVSYNSSDWE-----EQLKEIGKLLNKEDEAEKwLADYkqkakeAKEKIKKKLGNDKSVAVLRgrkqIY 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 189 ARGADGletGFKGSIHTEAMelvGLK--NVVEGEH--KGLAKVSMEQLLQWNPDIIFTQFP------EFYQmiwEAPQWQ 258
Cdd:cd01138  155 VFGEDG---RGGGPILYADL---GLKapEKVKEIEdkPGYAAISLEVLPEFDADYIFLLFFtgpeakADFE---SLPIWK 225

                        250
                 ....*....|...
gi 544682550 259 ALDAVKNKQVYLI 271
Cdd:cd01138  226 NLPAVKNNHVYIV 238
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 99-272 4.29e-12

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


Pssm-ID: 238560 [Multi-domain]  Cd Length: 270  Bit Score: 65.36  E-value: 4.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  99 EKIVALSPDLIVDVGNVSPNYLDqaKKTQAHTQVSYVLLDGKLERTPELLRELGEIVGQTKQAETLAKYAEETLKQAVGS 178
Cdd:cd01140   66 EAIAALKPDLIIIGGRLAEKYDE--LKKIAPTIDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSA 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 179 AKNvAKTA---------YLARGadglETGFKGSIHteamELVGLKNVVE---GEHKGLAkVSMEQLLQWNPDIIF----- 241
Cdd:cd01140  144 AKG-KKKAlvvlvnggkLSAFG----PGSRFGWLH----DLLGFEPADEnikASSHGQP-VSFEYILEANPDWLFvidrg 213

                        170       180       190
                 ....*....|....*....|....*....|....
gi 544682550 242 ---TQFPEFYQMIWEAPQWQALDAVKNKQVYLIP 272
Cdd:cd01140  214 aaiGAEGSSAKEVLDNDLVKNTTAWKNGKVIYLD 247
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 38-242 2.46e-10

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: 59.59  E-value: 2.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  38 VQKIISAGNPSDVVLLAV-APEKLAGfagfkMQSTSgkLFPETLQKLETLGRVSgknsSLSPEKIVALSPDLIV-DVGNV 115
Cdd:cd01149    1 PERIVSLGGSVTEIVYALgAGDRLVG-----VDSTS--TYPEAAAKLPDVGYMR----QLSAEGVLSLKPTLVIaSDEAG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 116 SPNYLDQAKktQAHTQVSYVLLDGKLERTPELLRELGEIVGQTKQAETLAKYAEETLKQAvgsAKNVA------KTAY-L 188
Cdd:cd01149   70 PPEALDQLR--AAGVPVVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAAL---RKTVAahkkppRVLFlL 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 544682550 189 ARGADGLETGFKGSIHTEAMELVGLKNVVEGeHKGLAKVSMEQLLQWNPDIIFT 242
Cdd:cd01149  145 SHGGGAAMAAGRNTAADAIIALAGAVNAAAG-FRGYKPLSAEALIAAQPDVILV 197
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 39-272 5.49e-10

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: 59.27  E-value: 5.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  39 QKIISAGNPSDVVLLAVAPE-KLAGFAGfkmqsTSGKLFPETLQKLETLGRVSGKNSSLspEKIVALSPDLIV---DVGN 114
Cdd:cd01148   19 QRVVSNDQNTTEMMLALGLQdRMVGTAG-----IDNKDLPELKAKYDKVPELAKKYPSK--ETVLAARPDLVFggwSYGF 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 115 -----VSPNYLdQAKKTQAHTQVSYVLLDGK---LERTPELLRELGEIVGQTKQAETLAKYAEETLKQA---VGSAKNVA 183
Cdd:cd01148   92 dkgglGTPDSL-AELGIKTYILPESCGQRRGeatLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEIsakVKGDGKKV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 184 KTAYLARGADGLETGFKGSIHTEAMELVGLKNVVEGEHKGLAKVSMEQLLQWNPDII----------FTQFPEFYQmiwE 253
Cdd:cd01148  171 AVFVYDSGEDKPFTSGRGGIPNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIviidygdqnaAEQKIKFLK---E 247

                        250
                 ....*....|....*....
gi 544682550 254 APQWQALDAVKNKQVYLIP 272
Cdd:cd01148  248 NPALKNVPAVKNNRFIVLP 266
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
 89-246 1.62e-06

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 49.14  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  89 VSGKNSS-LSPEKIVALSPDLIVdVGNVSPN----YLDQAKKTQAH----TQVSYVlldgklertpellRELGEIVGQTK 159
Cdd:PRK09534 102 VSGGQPFgVNVEAVVGLDPDLVL-APNAVAGdtvtRLREAGITVFHfpaaTSIEDV-------------AEKTATIGRLT 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 160 QAETLAKYAEETLKQAVGSAKNVAK------TAYLARGaDGLETGfKGSIHTEAMELVGLKNVV-EGEHKGLAKVSMEQL 232
Cdd:PRK09534 168 GNCEAAAETNAEMRDRVDAVEDRTAdvddrpRVLYPLG-DGYTAG-GNTFIGALIEAAGGHNVAaDATTDGYPQLSEEVI 245

                        170
                 ....*....|....
gi 544682550 233 LQWNPDIIFTQFPE 246
Cdd:PRK09534 246 VQQDPDVIVVATAS 259
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 74-268 2.47e-06

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 48.52  E-value: 2.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  74 KLFPETLQKLETLGRVsGKNSSLSPEKIVALSPDLIV-DVGNVSPNYldQAKKTQAHTqvsyVLLDGKLERTPELLRE-- 150
Cdd:PRK11411  71 RILPEVRAHLKPWQSV-GTRSQPSLEAIAALKPDLIIaDSSRHAGVY--IALQKIAPT----LLLKSRNETYQENLQSaa 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 151 -LGEIVGqtKQAETLAKYAEEtlKQAVgsaKNVAKTayLARGADGL-----ETGFkgSIHTEA------MELVGLKN-VV 217
Cdd:PRK11411 144 iIGEVLG--KKREMQARIEQH--KERM---AQFASQ--LPKGTRVAfgtsrEQQF--NLHSPEsytgsvLAALGLNVpKA 212

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 544682550 218 EGEHKGLAKVSMEQLLQWNPD-IIFTQFPEfyQMI---WEA-PQWQALDAVKNKQV 268
Cdd:PRK11411 213 PMNGAAMPSISLEQLLALNPDwLLVAHYRQ--ESIvkrWQQdPLWQMLTAAKKQQV 266
PRK14048 PRK14048
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
 60-172 4.39e-05

ferrichrome/ferrioxamine B periplasmic transporter; Provisional


Pssm-ID: 172540 [Multi-domain]  Cd Length: 374  Bit Score: 44.89  E-value: 4.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  60 LAGFAGfKMQSTSGKLFPETLQKLETLGRV----SGKNSSLSPEKIVALSPDLIV--------DVGNVSPNYLDQakktq 127
Cdd:PRK14048  73 LAGWSG-DMKGDNPEIYESFLRKFPELADVplidDGSGPGLSFETILTLKADLAIlanwqadtEAGQRAIEYLES----- 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 544682550 128 ahTQVSYVLLD---GKLERTPELLRELGEIVGQTKQAETLAKYAEETL 172
Cdd:PRK14048 147 --IGVPVIVVDfnnEALKNTPDNMRLLGKVFEREEQAEDFARFYEERL 192
PRK03379 PRK03379
vitamin B12-transporter protein BtuF; Provisional
 76-240 6.64e-05

vitamin B12-transporter protein BtuF; Provisional


Pssm-ID: 179575 [Multi-domain]  Cd Length: 260  Bit Score: 43.91  E-value: 6.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  76 FPETLQKLETLGRVSGKNSslspEKIVALSPDLIVDV--GNvSPNYLDQAkktqAHTQVSYVLLDGK-LERTPELLRELG 152
Cdd:PRK03379  47 YPPQAKKIEQVATWQGMNL----ERIVALKPDLVLAWrgGN-AERQVDQL----ASLGIKVMWVDATsIEQIANALRQLA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550 153 EIVGQTKQAETlakyAEETLKQAVGS-----AKNVAKTAYLARGADGLETGFKGSIHTEAMELVGLKNVVEGEHKGLAKV 227
Cdd:PRK03379 118 PWSPQPEKAEQ----AAQSLLQQYAAlkaqyADKPKKRVFLQFGTNPLFTSGKHSIQSQVLSLCGGENIFADSRVPWPQV 193

                        170
                 ....*....|...
gi 544682550 228 SMEQLLQWNPDII 240
Cdd:PRK03379 194 SREQVLARKPQAI 206
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 71-186 4.02e-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: 40.87  E-value: 4.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682550  71 TSGKLFPETLQKLETLGRVSGKN-SSLSPEKIVALSPDLIVdVGNVSPNYLDQAKKTQAHTQVSYVLLDGKLERTPELLR 149
Cdd:cd01141   34 VSASAYDLNTPAVKERIDIQVGPtGSLNVELIVALKPDLVI-LYGGFQAQTILDKLEQLGIPVLYVNEYPSPLGRAEWIK 112

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 544682550 150 ELGEIVGQTKQAEtlakyAEETLKQAVGSAKNVAKTA 186
Cdd:cd01141  113 FAAAFYGVGKEDK-----ADEAFAQIAGRYRDLAKKV 144
 
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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