NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488302768|ref|WP_002373819|]
View 

MULTISPECIES: iron-hydroxamate ABC transporter substrate-binding protein [Enterococcus]

Protein Classification

iron-hydroxamate ABC transporter substrate-binding protein( domain architecture ID 10100137)

iron-hydroxamate ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of iron(3+)-hydroxamate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 46-295 4.71e-80

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: 243.40  E-value: 4.71e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  46 NKVTVPAKPKRIIASYLEDYLVAL-GEKPVAQWTVGqGSIQDYLAKELKDIPTISYDLPYEAVLKFEPDLLLISSSalvE 124
Cdd:cd01138    1 GEVEIPAKPKRIVALSGETEGLALlGIKPVGAASIG-GKNPYYKKKTLAKVVGIVDEPNLEKVLELKPDLIIVSSK---Q 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 125 GGKYKEYSKIAPTYVVKNgENVTWRDQLEDIATVLDKKEQAKKVLEDYDTLTKGVQEDLGKK-DAGKSAAVLWVtNNQVF 203
Cdd:cd01138   77 EENYEKLSKIAPTVPVSY-NSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKlGNDKSVAVLRG-RKQIY 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 204 MVS-DNRSSGTVLYQDLGLQVPKLVEEISKnaTADWNQVSLEKLAELDADHIFLVNS--DESAPLFQEA-IWKNLPAVKN 279
Cdd:cd01138  155 VFGeDGRGGGPILYADLGLKAPEKVKEIED--KPGYAAISLEVLPEFDADYIFLLFFtgPEAKADFESLpIWKNLPAVKN 232

                        250
                 ....*....|....*.
gi 488302768 280 NQVHTYDKKSSWLYNG 295
Cdd:cd01138  233 NHVYIVDAWVFYFADG 248
 
Name Accession Description Interval E-value
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 46-295 4.71e-80

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: 243.40  E-value: 4.71e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  46 NKVTVPAKPKRIIASYLEDYLVAL-GEKPVAQWTVGqGSIQDYLAKELKDIPTISYDLPYEAVLKFEPDLLLISSSalvE 124
Cdd:cd01138    1 GEVEIPAKPKRIVALSGETEGLALlGIKPVGAASIG-GKNPYYKKKTLAKVVGIVDEPNLEKVLELKPDLIIVSSK---Q 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 125 GGKYKEYSKIAPTYVVKNgENVTWRDQLEDIATVLDKKEQAKKVLEDYDTLTKGVQEDLGKK-DAGKSAAVLWVtNNQVF 203
Cdd:cd01138   77 EENYEKLSKIAPTVPVSY-NSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKlGNDKSVAVLRG-RKQIY 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 204 MVS-DNRSSGTVLYQDLGLQVPKLVEEISKnaTADWNQVSLEKLAELDADHIFLVNS--DESAPLFQEA-IWKNLPAVKN 279
Cdd:cd01138  155 VFGeDGRGGGPILYADLGLKAPEKVKEIED--KPGYAAISLEVLPEFDADYIFLLFFtgPEAKADFESLpIWKNLPAVKN 232

                        250
                 ....*....|....*.
gi 488302768 280 NQVHTYDKKSSWLYNG 295
Cdd:cd01138  233 NHVYIVDAWVFYFADG 248
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 6-312 1.54e-50

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 169.72  E-value: 1.54e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768   6 KTVLIGTTLLLGSFLLGACGNTNKEANNADK---THEVTDTLGnKVTVPAKPKRIIA---SYLEDyLVALGEKPV--AQw 77
Cdd:COG4594    2 KKLLLLLILLLALLLLAACGSSSSDSSSSEAaagARTVKHAMG-ETTIPGTPKRVVVlewSFADA-LLALGVTPVgiAD- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  78 TVGQGSIQDYLAKELKDIPTI----SYDLpyEAVLKFEPDLLLISSSAlvEGGKYKEYSKIAPTyVVKNGENVTWRDQLE 153
Cdd:COG4594   79 DNDYDRWVPYLRDLIKGVTSVgtrsQPNL--EAIAALKPDLIIADKSR--HEAIYDQLSKIAPT-VLFKSRNGDYQENLE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 154 D---IATVLDKKEQAKKVLEDYDTLTKGVQEDLGKKDAGKSAAVLWVTNNQVFMVSDNRSSGTVLyQDLGLQVPKLVEEI 230
Cdd:COG4594  154 SfktIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKGKKVAVGQFRADGLRLYTPNSFAGSVL-AALGFENPPKQSKD 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 231 SKNATAdwnQVSLEKLAELDADHIFLVNSDESAP---LFQEAIWKNLPAVKNNQVHTYDkKSSWLY-NGPIANTQIVEDV 306
Cdd:COG4594  233 NGYGYS---EVSLEQLPALDPDVLFIATYDDPSIlkeWKNNPLWKNLKAVKNGRVYEVD-GDLWTRgRGPLAAELMADDL 308


                 ....*.
gi 488302768 307 KKALLN 312
Cdd:COG4594  309 VEILLK 314
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 60-287 5.25e-20

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


Pssm-ID: 426291 [Multi-domain]  Cd Length: 233  Bit Score: 86.65  E-value: 5.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768   60 SYLEDyLVALGEKPvaQWTVGQGSIQD-YLAKELKDIPTISYD--LPYEAVLKFEPDLLLISSSALVEGgKYKEYSKIAP 136
Cdd:pfam01497   6 AYTEI-LYALGATD--SIVGVDAYTRDpLKADAVAAIVKVGAYgeINVERLAALKPDLVILSTGYLTDE-AEELLSLIIP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  137 TYVVKNGENV-TWRDQLEDIATVLDKKEQAKKVLEDYDTLTKGVQEDLGKKDAgKSAAVLWVTNNQVFMVSDNRSSGTVL 215
Cdd:pfam01497  82 TVIFESSSTGeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTR-KPVLVFGGADGGGYVVAGSNTYIGDL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488302768  216 YQDLGLQvpKLVEEISKNAtadWNQVSLEKLAELDADHIFLVNSDESAPLFQEAI-----WKNLPAVKNNQVHTYDK 287
Cdd:pfam01497 161 LRILGIE--NIAAELSGSE---YAPISFEAILSSNPDVIIVSGRDSFTKTGPEFVaanplWAGLPAVKNGRVYTLPS 232
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 1-310 3.10e-16

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 77.41  E-value: 3.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768   1 MKLLKKTVLIGTTLLLGSFLLGACgntnkeannadkthEVTDTLGnKVTVPAKPKRIIA---SYLeDYLVALGEKPV--- 74
Cdd:PRK11411   1 MLAFIRLLFAGLLLLSGSSHAFAV--------------TVQDEQG-TFTLEKTPQRIVVlelSFV-DALAAVGVSPVgva 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  75 ----------------AQWT-VGqgsiqdylakeLKDIPTIsydlpyEAVLKFEPDLLLISSSAlvEGGKYKEYSKIAPT 137
Cdd:PRK11411  65 ddndakrilpevrahlKPWQsVG-----------TRSQPSL------EAIAALKPDLIIADSSR--HAGVYIALQKIAPT 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 138 YVVKNgENVTWRDQLED---IATVLDKKEQAKKVLEDYDTLTKGVQEDLGKkdaGKSAAVLWVTNNQVFMVSDNRSSGTV 214
Cdd:PRK11411 126 LLLKS-RNETYQENLQSaaiIGEVLGKKREMQARIEQHKERMAQFASQLPK---GTRVAFGTSREQQFNLHSPESYTGSV 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 215 LyQDLGLQVPKLveeisKNATADWNQVSLEKLAELDADHIFLVN-SDESA--PLFQEAIWKNLPAVKNNQVHTYDKKSSW 291
Cdd:PRK11411 202 L-AALGLNVPKA-----PMNGAAMPSISLEQLLALNPDWLLVAHyRQESIvkRWQQDPLWQMLTAAKKQQVASVDSNTWA 275

                        330
                 ....*....|....*....
gi 488302768 292 LYNGPIANTQIVEDVKKAL 310
Cdd:PRK11411 276 RMRGIFAAERIAKDTVKIF 294
IsdE TIGR03659
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ...
 6-308 1.19e-08

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: 54.97  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768    6 KTVLIGTTLLLGSFLLGACGNTNKEANNADKThevtdtlgnkvtvpAKPKRIIASYledylVALGEkpvaqwtvgqgsIQ 85
Cdd:TIGR03659   1 KKILSLVLLAVLSLGLTGCSSSKEKSKVSNKK--------------SKEERIVATS-----VAVTE------------IL 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768   86 DYLAKELKDIPTISYDLP--YEAVLK----FEPDL---------LLISSSALVE--GGKYKEySKIAPTYVvkngeNVTW 148
Cdd:TIGR03659  50 DKLDLDLVGVPTSQKTLPkrYKDVPEvgnpMSPDMekikslkptVVLSVTTLEEdlGPKFKQ-LGVEATFL-----NLTS 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  149 RDQLEDIATVL----DKKEQAKKVLEDYDTLTKGVQEDLGKKDAGKSAAVLWVTNNqvFMVSDNRSSGTVLYQDLGlqvp 224
Cdd:TIGR03659 124 VDGMKKSITELgekyGREEQAEKLVKEINEKEAEVKKKVKGKKKPKVLILMGVPGS--YLVATENSYIGDLVKLAG---- 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  225 klVEEISKNATADWNQVSLEKLAELDADHIFLVNS---DESAPLFQEA-----IWKNLPAVKNNQVHTYDKKsswlYNGP 296
Cdd:TIGR03659 198 --GENVYKGNKQEYLSSNTEYLLKANPDIILRAAHgmpDEVKKMFDEEfktndIWKHFEAVKNNRVYDLDEE----LFGM 271

                         330
                  ....*....|..
gi 488302768  297 IANTQIVEDVKK 308
Cdd:TIGR03659 272 TANLKVAEALDE 283
 
Name Accession Description Interval E-value
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 46-295 4.71e-80

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: 243.40  E-value: 4.71e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  46 NKVTVPAKPKRIIASYLEDYLVAL-GEKPVAQWTVGqGSIQDYLAKELKDIPTISYDLPYEAVLKFEPDLLLISSSalvE 124
Cdd:cd01138    1 GEVEIPAKPKRIVALSGETEGLALlGIKPVGAASIG-GKNPYYKKKTLAKVVGIVDEPNLEKVLELKPDLIIVSSK---Q 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 125 GGKYKEYSKIAPTYVVKNgENVTWRDQLEDIATVLDKKEQAKKVLEDYDTLTKGVQEDLGKK-DAGKSAAVLWVtNNQVF 203
Cdd:cd01138   77 EENYEKLSKIAPTVPVSY-NSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKlGNDKSVAVLRG-RKQIY 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 204 MVS-DNRSSGTVLYQDLGLQVPKLVEEISKnaTADWNQVSLEKLAELDADHIFLVNS--DESAPLFQEA-IWKNLPAVKN 279
Cdd:cd01138  155 VFGeDGRGGGPILYADLGLKAPEKVKEIED--KPGYAAISLEVLPEFDADYIFLLFFtgPEAKADFESLpIWKNLPAVKN 232

                        250
                 ....*....|....*.
gi 488302768 280 NQVHTYDKKSSWLYNG 295
Cdd:cd01138  233 NHVYIVDAWVFYFADG 248
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 6-312 1.54e-50

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 169.72  E-value: 1.54e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768   6 KTVLIGTTLLLGSFLLGACGNTNKEANNADK---THEVTDTLGnKVTVPAKPKRIIA---SYLEDyLVALGEKPV--AQw 77
Cdd:COG4594    2 KKLLLLLILLLALLLLAACGSSSSDSSSSEAaagARTVKHAMG-ETTIPGTPKRVVVlewSFADA-LLALGVTPVgiAD- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  78 TVGQGSIQDYLAKELKDIPTI----SYDLpyEAVLKFEPDLLLISSSAlvEGGKYKEYSKIAPTyVVKNGENVTWRDQLE 153
Cdd:COG4594   79 DNDYDRWVPYLRDLIKGVTSVgtrsQPNL--EAIAALKPDLIIADKSR--HEAIYDQLSKIAPT-VLFKSRNGDYQENLE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 154 D---IATVLDKKEQAKKVLEDYDTLTKGVQEDLGKKDAGKSAAVLWVTNNQVFMVSDNRSSGTVLyQDLGLQVPKLVEEI 230
Cdd:COG4594  154 SfktIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKGKKVAVGQFRADGLRLYTPNSFAGSVL-AALGFENPPKQSKD 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 231 SKNATAdwnQVSLEKLAELDADHIFLVNSDESAP---LFQEAIWKNLPAVKNNQVHTYDkKSSWLY-NGPIANTQIVEDV 306
Cdd:COG4594  233 NGYGYS---EVSLEQLPALDPDVLFIATYDDPSIlkeWKNNPLWKNLKAVKNGRVYEVD-GDLWTRgRGPLAAELMADDL 308


                 ....*.
gi 488302768 307 KKALLN 312
Cdd:COG4594  309 VEILLK 314
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 52-305 1.15e-43

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: 150.13  E-value: 1.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  52 AKPKRIIA---SYLEDyLVALGEKPVAQW-TVGQGSIQDYLAKELKDIPTI--SYDLPYEAVLKFEPDLLLISSSalveG 125
Cdd:cd01146    1 AKPQRIVAldwGALET-LLALGVKPVGVAdTAGYKPWIPEPALPLEGVVDVgtRGQPNLEAIAALKPDLILGSAS----R 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 126 GK--YKEYSKIAPTYVVKNGENVT-WRDQLEDIATVLDKKEQAKKVLEDYDTLTKGVQEDLGKKDaGKSAAVLWVTNNQV 202
Cdd:cd01146   76 HDeiYDQLSQIAPTVLLDSSPWLAeWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKG-PKPVSVVRFSDAGS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 203 FMVSDNRS-SGTVLyQDLGLQVPKLVEEISKNataDWNQVSLEKLAELDADHIFLVnSDESAPLFQE----AIWKNLPAV 277
Cdd:cd01146  155 IRLYGPNSfAGSVL-EDLGLQNPWAQETTNDS---GFATISLERLAKADADVLFVF-TYEDEELAQAlqanPLWQNLPAV 229

                        250       260
                 ....*....|....*....|....*...
gi 488302768 278 KNNQVHTYDkKSSWLYNGPIANTQIVED 305
Cdd:cd01146  230 KNGRVYVVD-DVWWFFGGGLSAARLLLD 256
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 56-310 2.89e-37

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 133.58  E-value: 2.89e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  56 RIIA---SYLEdYLVALGEKP--VAqwtVGQGSIQDYLAKELKDIPTIS--YDLPYEAVLKFEPDLLLISSSALVEGGkY 128
Cdd:COG0614    2 RIVSlspSATE-LLLALGAGDrlVG---VSDWGYCDYPELELKDLPVVGgtGEPNLEAILALKPDLVLASSSGNDEED-Y 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 129 KEYSKI-APTYVVKNGENVTWRDQLEDIATVLDKKEQAKKVLEDYDTLTKGVQEDLGKKDAGKSAAVLWVTNNQVFMVSD 207
Cdd:COG0614   77 EQLEKIgIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAGG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 208 NRSSGTVLyQDLGLQVpklveeISKNATADWNQVSLEKLAELDADHIFLVNSDESAPLFQEAI--------WKNLPAVKN 279
Cdd:COG0614  157 GSFIGELL-ELAGGRN------VAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALealladpgWQSLPAVKN 229

                        250       260       270
                 ....*....|....*....|....*....|.
gi 488302768 280 NQVHTYDkKSSWLYNGPIANtQIVEDVKKAL 310
Cdd:COG0614  230 GRVYVVP-GDLLSRPGPRLL-LALEDLAKAL 258
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 6-310 3.49e-27

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


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 107.96  E-value: 3.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768   6 KTVLIGTTLLLGSFLLGACGNTNK--EANNADKTHEVTDTLGnKVTVPAKPKRIIAsyLE----DYLVALGEKPVAqwtV 79
Cdd:COG4607    2 KKTLLAALALAAALALAACGSSSAaaASAAAAETVTVEHALG-TVEVPKNPKRVVV--FDngalDTLDALGVEVAG---V 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  80 GQGSIQDYLAK----ELKDIPTISYdlP-YEAVLKFEPDLLLISS-SAlvegGKYKEYSKIAPT-YVVKNGENV--TWRD 150
Cdd:COG4607   76 PKGLLPDYLSKyaddKYANVGTLFE--PdLEAIAALKPDLIIIGGrSA----KKYDELSKIAPTiDLTVDGEDYleSLKR 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 151 QLEDIATVLDKKEQAKKVLEDYDTLTKGVQEdlgKKDAGKSAAVLWVTNNQVFMVSDNRSSGtVLYQDLGLqvpKLVEEI 230
Cdd:COG4607  150 NTETLGEIFGKEDEAEELVADLDAKIAALKA---AAAGKGTALIVLTNGGKISAYGPGSRFG-PIHDVLGF---KPADED 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 231 SKNATADwNQVSLEKLAELDADHIFLVNSD-------ESAPLF--QEAIwKNLPAVKNNQVHTYDkKSSWlY---NGPIA 298
Cdd:COG4607  223 IEASTHG-QAISFEFIAEANPDWLFVIDRDaaiggegPAAKQVldNELV-KQTTAWKNGQIVYLD-PDAW-YlagGGIQS 298

                        330
                 ....*....|..
gi 488302768 299 NTQIVEDVKKAL 310
Cdd:COG4607  299 LTEMLDEVADAL 310
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 60-287 5.25e-20

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


Pssm-ID: 426291 [Multi-domain]  Cd Length: 233  Bit Score: 86.65  E-value: 5.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768   60 SYLEDyLVALGEKPvaQWTVGQGSIQD-YLAKELKDIPTISYD--LPYEAVLKFEPDLLLISSSALVEGgKYKEYSKIAP 136
Cdd:pfam01497   6 AYTEI-LYALGATD--SIVGVDAYTRDpLKADAVAAIVKVGAYgeINVERLAALKPDLVILSTGYLTDE-AEELLSLIIP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  137 TYVVKNGENV-TWRDQLEDIATVLDKKEQAKKVLEDYDTLTKGVQEDLGKKDAgKSAAVLWVTNNQVFMVSDNRSSGTVL 215
Cdd:pfam01497  82 TVIFESSSTGeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTR-KPVLVFGGADGGGYVVAGSNTYIGDL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488302768  216 YQDLGLQvpKLVEEISKNAtadWNQVSLEKLAELDADHIFLVNSDESAPLFQEAI-----WKNLPAVKNNQVHTYDK 287
Cdd:pfam01497 161 LRILGIE--NIAAELSGSE---YAPISFEAILSSNPDVIIVSGRDSFTKTGPEFVaanplWAGLPAVKNGRVYTLPS 232
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 37-283 8.45e-18

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: 81.63  E-value: 8.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  37 THEVTDTLGNKVTVPAKPKRIIASYL----EDYLVALGEKPVA-QWTVGQGSIQDYLAKELKDIPTI--SYDLPYEAVLK 109
Cdd:cd01142    7 TRTITDMAGRKVTIPDEVKRIAALWGagnaVVAALGGGKLIVAtTSTVQQEPWLYRLAPSLENVATGgtGNDVNIEELLA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 110 FEPDLLLISSSALVEGGKYKEysKIAPTYVVKNGENVTWRDQLEDIATVLDKKEQAKKVLEDYDTLTKGVQEDLGKKDAG 189
Cdd:cd01142   87 LKPDVVIVWSTDGKEAGKAVL--RLLNALSLRDAELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAARTKKLPDS 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 190 KSAAVLWVTNNQvfMVSDNRSSGTVLYQDL--GLQVpklVEEISKNAtadWNQVSLEKLAELDADHIFLVNSDESAPLFQ 267
Cdd:cd01142  165 ERPRVYYAGPDP--LTTDGTGSITNSWIDLagGINV---ASEATKKG---SGEVSLEQLLKWNPDVIIVGNADTKAAILA 236

                        250
                 ....*....|....*.
gi 488302768 268 EAIWKNLPAVKNNQVH 283
Cdd:cd01142  237 DPRWQNLRAVKNGRVY 252
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 1-310 3.10e-16

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 77.41  E-value: 3.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768   1 MKLLKKTVLIGTTLLLGSFLLGACgntnkeannadkthEVTDTLGnKVTVPAKPKRIIA---SYLeDYLVALGEKPV--- 74
Cdd:PRK11411   1 MLAFIRLLFAGLLLLSGSSHAFAV--------------TVQDEQG-TFTLEKTPQRIVVlelSFV-DALAAVGVSPVgva 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  75 ----------------AQWT-VGqgsiqdylakeLKDIPTIsydlpyEAVLKFEPDLLLISSSAlvEGGKYKEYSKIAPT 137
Cdd:PRK11411  65 ddndakrilpevrahlKPWQsVG-----------TRSQPSL------EAIAALKPDLIIADSSR--HAGVYIALQKIAPT 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 138 YVVKNgENVTWRDQLED---IATVLDKKEQAKKVLEDYDTLTKGVQEDLGKkdaGKSAAVLWVTNNQVFMVSDNRSSGTV 214
Cdd:PRK11411 126 LLLKS-RNETYQENLQSaaiIGEVLGKKREMQARIEQHKERMAQFASQLPK---GTRVAFGTSREQQFNLHSPESYTGSV 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 215 LyQDLGLQVPKLveeisKNATADWNQVSLEKLAELDADHIFLVN-SDESA--PLFQEAIWKNLPAVKNNQVHTYDKKSSW 291
Cdd:PRK11411 202 L-AALGLNVPKA-----PMNGAAMPSISLEQLLALNPDWLLVAHyRQESIvkRWQQDPLWQMLTAAKKQQVASVDSNTWA 275

                        330
                 ....*....|....*....
gi 488302768 292 LYNGPIANTQIVEDVKKAL 310
Cdd:PRK11411 276 RMRGIFAAERIAKDTVKIF 294
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
 12-282 6.04e-16

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 76.94  E-value: 6.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  12 TTLLLGSFLLGACGNTNKEANNADKTHEVTDTLGnKVTVPAKPKRIIAS--YLEDYLVALGEKPVAQWTVGQGSI----Q 85
Cdd:PRK10957   3 YRLALLLLGLLLSGIAAAQASAAGWPRTVTDSRG-SVTLESKPQRIVSTsvTLTGTLLAIDAPVIASGATTPNTRvaddQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  86 DYL------AKE--LKDIPTISYDLpyEAVLKFEPDLLLISS----SALVEggkYKEYSKIAPTYVVkNGENVTWRDQLE 153
Cdd:PRK10957  82 GFFrqwsdvAKErgVEVLYIGEPDA--EAVAAQMPDLIVISAtggdSALAL---YDQLSAIAPTLVI-DYDDKSWQELAT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 154 DIATVLDKKEQAKKVLEDYDTLTKGVQEDLgKKDAGKSAAVLWVTNNQVFMVSDNRSSGTVLYQDLGLQV----PKLVEE 229
Cdd:PRK10957 156 QLGEATGLEKQAAAVIAQFDAQLAEVKAKI-TLPPQPVSALVYNGAGHSANLWTPESAQGQLLEQLGFTLaelpAGLQAS 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488302768 230 ISKNATADWNQVSLEKLAE-LDADHIFLVNSDESA--PLFQEAIWKNLPAVKNNQV 282
Cdd:PRK10957 235 TSQGKRHDIIQLGGENLAAgLNGETLFLFAGDDKDadAFLADPLLANLPAVQNKQV 290
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 46-308 1.93e-15

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: 74.60  E-value: 1.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  46 NKVTVPAKPKRIIASYLE--DYLVALGEKPVAqwtVGQGSIQDYLAKELKDIPTISYDLP----YEAVLKFEPDLLLISS 119
Cdd:cd01140    4 GETKVPKNPEKVVVFDVGalDTLDALGVKVVG---VPKSSTLPEYLKKYKDDKYANVGTLfepdLEAIAALKPDLIIIGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 120 SAlveGGKYKEYSKIAPTYVVKNGENVTW---RDQLEDIATVLDKKEQAKKVLEDYDTLTKGVQedlgKKDAGKSAAVLW 196
Cdd:cd01140   81 RL---AEKYDELKKIAPTIDLGADLKNYLesvKQNIETLGKIFGKEEEAKELVAEIDASIAEAK----SAAKGKKKALVV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 197 VTNNQVFMVSDNRSSGTVLYQDLGlqvpklVEEISKNATAD--WNQVSLEKLAELDADHIFLVNSDE--------SAPLF 266
Cdd:cd01140  154 LVNGGKLSAFGPGSRFGWLHDLLG------FEPADENIKASshGQPVSFEYILEANPDWLFVIDRGAaigaegssAKEVL 227

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 488302768 267 QEAIWKNLPAVKNNQVHTYDKKSSWLYNGPI-ANTQIVEDVKK 308
Cdd:cd01140  228 DNDLVKNTTAWKNGKVIYLDPDLWYLSGGGLeSLKQMIDDLKK 270
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 55-196 1.73e-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: 61.04  E-value: 1.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  55 KRIIASY--LEDYLVALG--EKPVAQWTVGQGSIQDYLAKELKDIPTISYDLPYEAVLKFEPDLLLISSSALVEggKYKE 130
Cdd:cd00636    1 KRVVALDpgATELLLALGgdDKPVGVADPSGYPPEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEA--WLDK 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 131 YSKIA-PTYVVKNGENVT---WRDQLEDIATVLDKKEQAKKVLEDYDTLTKGVQEDLGKKDAGKSAAVLW 196
Cdd:cd00636   79 LSKIAiPVVVVDEASELSlenIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVVG 148
IsdE TIGR03659
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ...
 6-308 1.19e-08

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: 54.97  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768    6 KTVLIGTTLLLGSFLLGACGNTNKEANNADKThevtdtlgnkvtvpAKPKRIIASYledylVALGEkpvaqwtvgqgsIQ 85
Cdd:TIGR03659   1 KKILSLVLLAVLSLGLTGCSSSKEKSKVSNKK--------------SKEERIVATS-----VAVTE------------IL 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768   86 DYLAKELKDIPTISYDLP--YEAVLK----FEPDL---------LLISSSALVE--GGKYKEySKIAPTYVvkngeNVTW 148
Cdd:TIGR03659  50 DKLDLDLVGVPTSQKTLPkrYKDVPEvgnpMSPDMekikslkptVVLSVTTLEEdlGPKFKQ-LGVEATFL-----NLTS 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  149 RDQLEDIATVL----DKKEQAKKVLEDYDTLTKGVQEDLGKKDAGKSAAVLWVTNNqvFMVSDNRSSGTVLYQDLGlqvp 224
Cdd:TIGR03659 124 VDGMKKSITELgekyGREEQAEKLVKEINEKEAEVKKKVKGKKKPKVLILMGVPGS--YLVATENSYIGDLVKLAG---- 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  225 klVEEISKNATADWNQVSLEKLAELDADHIFLVNS---DESAPLFQEA-----IWKNLPAVKNNQVHTYDKKsswlYNGP 296
Cdd:TIGR03659 198 --GENVYKGNKQEYLSSNTEYLLKANPDIILRAAHgmpDEVKKMFDEEfktndIWKHFEAVKNNRVYDLDEE----LFGM 271

                         330
                  ....*....|..
gi 488302768  297 IANTQIVEDVKK 308
Cdd:TIGR03659 272 TANLKVAEALDE 283
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 42-282 2.91e-08

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: 53.88  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  42 DTLGNKVTVPAKPKRI--IASYLEDYLVALG-EKPVAQWTVGQGSIQDYLAKELKDIPTISYDLP-YEAVLKFEPDLLLI 117
Cdd:cd01148    6 ENCGRSVTFDKAPQRVvsNDQNTTEMMLALGlQDRMVGTAGIDNKDLPELKAKYDKVPELAKKYPsKETVLAARPDLVFG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 118 SSS-ALVEGG--------KYKEYSKIAPTYVVKNGENVTWRD---QLEDIATVLDKKEQAKKVLEDYDTLTKGVQEDLgk 185
Cdd:cd01148   86 GWSyGFDKGGlgtpdslaELGIKTYILPESCGQRRGEATLDDvynDIRNLGKIFDVEDRADKLVADLKARLAEISAKV-- 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 186 KDAGKSAAVLWVTNNQvfmvSDNRSSGTV-LYQDL----GLqvpklvEEISKNATADWNQVSLEKLAELDADHIFLVNSD 260
Cdd:cd01148  164 KGDGKKVAVFVYDSGE----DKPFTSGRGgIPNAIitaaGG------RNVFADVDESWTTVSWETVIARNPDVIVIIDYG 233

                        250       260
                 ....*....|....*....|....*....
gi 488302768 261 ESAPLFQEA-------IWKNLPAVKNNQV 282
Cdd:cd01148  234 DQNAAEQKIkflkenpALKNVPAVKNNRF 262
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 39-283 8.81e-08

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: 52.69  E-value: 8.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  39 EVTDTLGNKVTVPAKPKRI-IASYLEDYLVAL--GEKPVAQwTVGQGS-----IQDYLAK------ELKDIPTISY---- 100
Cdd:cd01139    2 TVTDVAGRKVTLDAPVERVlLGEGRQLYALALleGENPFAR-IVGWGGdlkkgDPDTYAKykekfpEIADIPLIGStyng 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 101 DLPYEAVLKFEPDLLLISSSALvEGGKYKEY------SKIAPTYV---VKNGENVTwrDQLEDIATVLDKKEQAKKVLED 171
Cdd:cd01139   81 DFSVEKVLTLKPDLVILNIWAK-TTAEESGIlekleqAGIPVVFVdfrQKPLKNTT--PSMRLLGKALGREERAEEFIEF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 172 YDTLTKGVQEDLGKKDAGKSAAVLWvtnnqvfmVSDNRS---SGTVLYQDLGlqvpKLVEEISKNATAD------WNQVS 242
Cdd:cd01139  158 YQERIDRIRDRLAKINEPKPKVFIE--------LGAGGPeecCSTYGNGNWG----ELVDAAGGDNIADglipgtSGELN 225

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488302768 243 LEKLAELDADHIFL------------------VNSDESAPLFQEAI----WKNLPAVKNNQVH 283
Cdd:cd01139  226 AEYVIAANPEIIIAtggnwakdpsgvslgpdgTTADAKESLLRALLkrpgWSSLQAVKNGRVY 288
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 50-283 1.15e-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: 51.95  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768  50 VPAKPKRIIAS--YLEDYLVALG--EKPV---AQWTVGQGSIQDYLAKELKDIPTI-----SYDLPYEAVLKFEPDLLLI 117
Cdd:cd01147    1 VPKPVERVVAAgpGALRLLYALAapDKIVgvdDAEKSDEGRPYFLASPELKDLPVIgrggrGNTPNYEKIAALKPDVVID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 118 --SSSALVEGGKYKEYSKIAPTYVVKNGENVTWRDQLEDIATVLDKKEQAKKVLEDYDTLTKGVQEDLGKKDAGKSAAVL 195
Cdd:cd01147   81 vgSDDPTSIADDLQKKTGIPVVVLDGGDSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDIPDEEKPTVY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488302768 196 W----VTNNQVFMvSDNRSSGTVLyqdLGLQVPKLVEEISKNATAdwnQVSLEKLAELDADHIFLVNSDESAPLFQEAI- 270
Cdd:cd01147  161 FgrigTKGAAGLE-SGLAGSIEVF---ELAGGINVADGLGGGGLK---EVSPEQILLWNPDVIFLDTGSFYLSLEGYAKn 233

                        250
                 ....*....|....*.
gi 488302768 271 ---WKNLPAVKNNQVH 283
Cdd:cd01147  234 rpfWQSLKAVKNGRVY 249
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH