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Conserved domains on  [gi|736148119|ref|WP_034279589|]
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MULTISPECIES: iron-hydroxamate ABC transporter substrate-binding protein [Bacillus]

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

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List of domain hits

 Name Accession Description Interval E-value
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 46-289 2.72e-90

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: 269.20  E-value: 2.72e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  46 GPVKLPAHPKRVVVLGSYTGNVMSLGVNLVGVDSWSKKNPRFQKKLKNVE--EVSDANVEKIMKLKPDVIIgLSNT--KN 121
Cdd:cd01138    1 GEVEIPAKPKRIVALSGETEGLALLGIKPVGAASIGGKNPYYKKKTLAKVvgIVDEPNLEKVLELKPDLII-VSSKqeEN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 122 VEKLKKIAPTVLFTYNKVDYLQQHIEIGKVLNKEKEAKAWVKDFKKRAAEAGKEIKAKIGEDATVSVFEsGTKDLYVFGD 201
Cdd:cd01138   80 YEKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVLR-GRKQIYVFGE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 202 AWGRGTEILYQAMKLKMPEKVKEKALKAGYYAVSQEVIPEFAGDYMIISKN--SEMDNSYQNSEIYKSIPAVKKHRVYEA 279
Cdd:cd01138  159 DGRGGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADYIFLLFFtgPEAKADFESLPIWKNLPAVKNNHVYIV 238

                        250
                 ....*....|
gi 736148119 280 NAEEFYFNDP 289
Cdd:cd01138  239 DAWVFYFADG 248
 
Name Accession Description Interval E-value
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 46-289 2.72e-90

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: 269.20  E-value: 2.72e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  46 GPVKLPAHPKRVVVLGSYTGNVMSLGVNLVGVDSWSKKNPRFQKKLKNVE--EVSDANVEKIMKLKPDVIIgLSNT--KN 121
Cdd:cd01138    1 GEVEIPAKPKRIVALSGETEGLALLGIKPVGAASIGGKNPYYKKKTLAKVvgIVDEPNLEKVLELKPDLII-VSSKqeEN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 122 VEKLKKIAPTVLFTYNKVDYLQQHIEIGKVLNKEKEAKAWVKDFKKRAAEAGKEIKAKIGEDATVSVFEsGTKDLYVFGD 201
Cdd:cd01138   80 YEKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVLR-GRKQIYVFGE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 202 AWGRGTEILYQAMKLKMPEKVKEKALKAGYYAVSQEVIPEFAGDYMIISKN--SEMDNSYQNSEIYKSIPAVKKHRVYEA 279
Cdd:cd01138  159 DGRGGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADYIFLLFFtgPEAKADFESLPIWKNLPAVKNNHVYIV 238

                        250
                 ....*....|
gi 736148119 280 NAEEFYFNDP 289
Cdd:cd01138  239 DAWVFYFADG 248
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 1-280 1.97e-54

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 179.73  E-value: 1.97e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119   1 MKKILFPLML-IFVLALSACGNSSSsssNKGNQSTSSDKITYQSENGPVKLPAHPKRVVVLG-SYTGNVMSLGVNLVGV- 77
Cdd:COG4594    1 MKKLLLLLILlLALLLLAACGSSSS---DSSSSEAAAGARTVKHAMGETTIPGTPKRVVVLEwSFADALLALGVTPVGIa 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  78 DSWSKKN--PRFQKKLKNVEEV---SDANVEKIMKLKPDVIIGLSN--TKNVEKLKKIAPTVLFTYNKVDY---LQQHIE 147
Cdd:COG4594   78 DDNDYDRwvPYLRDLIKGVTSVgtrSQPNLEAIAALKPDLIIADKSrhEAIYDQLSKIAPTVLFKSRNGDYqenLESFKT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 148 IGKVLNKEKEAKAWVKDFKKRAAEAGKEIKAKiGEDATVSVFESGTKDLYVFGDAWGRGtEILyQAMKLKMPEKVKEKAl 227
Cdd:COG4594  158 IAKALGKEEEAEAVLADHDQRIAEAKAKLAAA-DKGKKVAVGQFRADGLRLYTPNSFAG-SVL-AALGFENPPKQSKDN- 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 736148119 228 KAGYYAVSQEVIPEFAGDYMII--SKNSEMDNSYQNSEIYKSIPAVKKHRVYEAN 280
Cdd:COG4594  234 GYGYSEVSLEQLPALDPDVLFIatYDDPSILKEWKNNPLWKNLKAVKNGRVYEVD 288
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 57-282 8.41e-27

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: 105.14  E-value: 8.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119   57 VVVLGSYTGNVMSLGV--NLVGVDSWSKkNPRFQKKLKNVEEV---SDANVEKIMKLKPDVIIG---LSNTKNVEKLKKI 128
Cdd:pfam01497   1 AALSPAYTEILYALGAtdSIVGVDAYTR-DPLKADAVAAIVKVgayGEINVERLAALKPDLVILstgYLTDEAEELLSLI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  129 APTVLFTYNKV--DYLQQHIEIGKVLNKEKEAKAWVKDFKKRAAEAGKEIKAKIgeDATVSVFESGTKDLYVFGDAWGRG 206
Cdd:pfam01497  80 IPTVIFESSSTgeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLT--RKPVLVFGGADGGGYVVAGSNTYI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  207 TEILyQAMKLKMPEKVKEKalkaGYYA-VSQEVIPEFAGDYMIIS----KNSEMDNSYQNSEIYKSIPAVKKHRVYEANA 281
Cdd:pfam01497 158 GDLL-RILGIENIAAELSG----SEYApISFEAILSSNPDVIIVSgrdsFTKTGPEFVAANPLWAGLPAVKNGRVYTLPS 232


                  .
gi 736148119  282 E 282
Cdd:pfam01497 233 D 233
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 33-282 4.77e-23

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 96.28  E-value: 4.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  33 STSSDKITYQSENGPVKLPAHPKRVVVLG-SYTGNVMSLGVNLVGVDSWSKKN---PRFQKKLKNVEEV---SDANVEKI 105
Cdd:PRK11411  18 SSHAFAVTVQDEQGTFTLEKTPQRIVVLElSFVDALAAVGVSPVGVADDNDAKrilPEVRAHLKPWQSVgtrSQPSLEAI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 106 MKLKPDVIIGLSN--TKNVEKLKKIAPTVLFTYNKVDY---LQQHIEIGKVLNKEKEAKAWVKDFKKRAaeagKEIKAKI 180
Cdd:PRK11411  98 AALKPDLIIADSSrhAGVYIALQKIAPTLLLKSRNETYqenLQSAAIIGEVLGKKREMQARIEQHKERM----AQFASQL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 181 GEDATVSVFESGTKDLYVFGDAWGRGTeiLYQAMKLKMPekvKEKALKAGYYAVSQEVIPEFAGDYMII---SKNSEMDn 257
Cdd:PRK11411 174 PKGTRVAFGTSREQQFNLHSPESYTGS--VLAALGLNVP---KAPMNGAAMPSISLEQLLALNPDWLLVahyRQESIVK- 247

                        250       260
                 ....*....|....*....|....*
gi 736148119 258 SYQNSEIYKSIPAVKKHRVYEANAE 282
Cdd:PRK11411 248 RWQQDPLWQMLTAAKKQQVASVDSN 272
 
Name Accession Description Interval E-value
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 46-289 2.72e-90

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: 269.20  E-value: 2.72e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  46 GPVKLPAHPKRVVVLGSYTGNVMSLGVNLVGVDSWSKKNPRFQKKLKNVE--EVSDANVEKIMKLKPDVIIgLSNT--KN 121
Cdd:cd01138    1 GEVEIPAKPKRIVALSGETEGLALLGIKPVGAASIGGKNPYYKKKTLAKVvgIVDEPNLEKVLELKPDLII-VSSKqeEN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 122 VEKLKKIAPTVLFTYNKVDYLQQHIEIGKVLNKEKEAKAWVKDFKKRAAEAGKEIKAKIGEDATVSVFEsGTKDLYVFGD 201
Cdd:cd01138   80 YEKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVLR-GRKQIYVFGE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 202 AWGRGTEILYQAMKLKMPEKVKEKALKAGYYAVSQEVIPEFAGDYMIISKN--SEMDNSYQNSEIYKSIPAVKKHRVYEA 279
Cdd:cd01138  159 DGRGGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADYIFLLFFtgPEAKADFESLPIWKNLPAVKNNHVYIV 238

                        250
                 ....*....|
gi 736148119 280 NAEEFYFNDP 289
Cdd:cd01138  239 DAWVFYFADG 248
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 1-280 1.97e-54

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 179.73  E-value: 1.97e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119   1 MKKILFPLML-IFVLALSACGNSSSsssNKGNQSTSSDKITYQSENGPVKLPAHPKRVVVLG-SYTGNVMSLGVNLVGV- 77
Cdd:COG4594    1 MKKLLLLLILlLALLLLAACGSSSS---DSSSSEAAAGARTVKHAMGETTIPGTPKRVVVLEwSFADALLALGVTPVGIa 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  78 DSWSKKN--PRFQKKLKNVEEV---SDANVEKIMKLKPDVIIGLSN--TKNVEKLKKIAPTVLFTYNKVDY---LQQHIE 147
Cdd:COG4594   78 DDNDYDRwvPYLRDLIKGVTSVgtrSQPNLEAIAALKPDLIIADKSrhEAIYDQLSKIAPTVLFKSRNGDYqenLESFKT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 148 IGKVLNKEKEAKAWVKDFKKRAAEAGKEIKAKiGEDATVSVFESGTKDLYVFGDAWGRGtEILyQAMKLKMPEKVKEKAl 227
Cdd:COG4594  158 IAKALGKEEEAEAVLADHDQRIAEAKAKLAAA-DKGKKVAVGQFRADGLRLYTPNSFAG-SVL-AALGFENPPKQSKDN- 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 736148119 228 KAGYYAVSQEVIPEFAGDYMII--SKNSEMDNSYQNSEIYKSIPAVKKHRVYEAN 280
Cdd:COG4594  234 GYGYSEVSLEQLPALDPDVLFIatYDDPSILKEWKNNPLWKNLKAVKNGRVYEVD 288
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 52-290 1.16e-40

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: 142.04  E-value: 1.16e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  52 AHPKRVVVLG-SYTGNVMSLGVNLVGVDSWSKKNPRFQKKLKNVEEV------SDANVEKIMKLKPDVIIGLS--NTKNV 122
Cdd:cd01146    1 AKPQRIVALDwGALETLLALGVKPVGVADTAGYKPWIPEPALPLEGVvdvgtrGQPNLEAIAALKPDLILGSAsrHDEIY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 123 EKLKKIAPTVLF-TYNKVDYLQQHIE-IGKVLNKEKEAKAWVKDFKKRAAEAGKEIKAKIGEDATVSVFESGTKdLYVFG 200
Cdd:cd01146   81 DQLSQIAPTVLLdSSPWLAEWKENLRlIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGS-IRLYG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 201 DAWGRGTeILyQAMKLKMPEKVkEKALKAGYYAVSQEVIPEFAGDYMIIS--KNSEMDNSYQNSEIYKSIPAVKKHRVYE 278
Cdd:cd01146  160 PNSFAGS-VL-EDLGLQNPWAQ-ETTNDSGFATISLERLAKADADVLFVFtyEDEELAQALQANPLWQNLPAVKNGRVYV 236

                        250
                 ....*....|..
gi 736148119 279 ANAEEFYFNDPL 290
Cdd:cd01146  237 VDDVWWFFGGGL 248
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 56-294 6.21e-40

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 140.52  E-value: 6.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  56 RVVVLG-SYTGNVMSLGV--NLVGVDSWSKKNPRfQKKLKNVEEVSDA---NVEKIMKLKPDVIIG---LSNTKNVEKLK 126
Cdd:COG0614    2 RIVSLSpSATELLLALGAgdRLVGVSDWGYCDYP-ELELKDLPVVGGTgepNLEAILALKPDLVLAsssGNDEEDYEQLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 127 KI-APTVLFTYNKVDYLQQHIE-IGKVLNKEKEAKAWVKDFKKRAAEAGKEIkAKIGEDATVSVFESGTKDLYVFGDAWG 204
Cdd:COG0614   81 KIgIPVVVLDPRSLEDLYESIRlLGELLGREERAEALIAEYEARLAAVRARL-AGAEERPTVLYEIWSGDPLYTAGGGSF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 205 RGTeiLYQAMKLKMPekvkEKALKAGYYAVSQEVIPEFAGDYMIIS-------KNSEMDNSYQNSEIYKSIPAVKKHRVY 277
Cdd:COG0614  160 IGE--LLELAGGRNV----AADLGGGYPEVSLEQVLALDPDVIILSgggydaeTAEEALEALLADPGWQSLPAVKNGRVY 233

                        250
                 ....*....|....*..
gi 736148119 278 EANAEEFYFNDPLTLEF 294
Cdd:COG0614  234 VVPGDLLSRPGPRLLLA 250
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 1-287 3.24e-32

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


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 121.44  E-value: 3.24e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119   1 MKK-ILFPLMLIFVLALSACGNSSSSssnkGNQSTSSDKITYQSENGPVKLPAHPKRVVVLGSYTGNVMS-LGVNLVGVd 78
Cdd:COG4607    1 MKKtLLAALALAAALALAACGSSSAA----AASAAAAETVTVEHALGTVEVPKNPKRVVVFDNGALDTLDaLGVEVAGV- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  79 swSKKN-PRFQKKLKNvEEVSDA------NVEKIMKLKPDVII--GLSnTKNVEKLKKIAPTVLFTYNKVDYL---QQHI 146
Cdd:COG4607   76 --PKGLlPDYLSKYAD-DKYANVgtlfepDLEAIAALKPDLIIigGRS-AKKYDELSKIAPTIDLTVDGEDYLeslKRNT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 147 E-IGKVLNKEKEAKAWVKDFKKRAAEAgkeiKAKIGEDATV-SVFESGTKdLYVFGDA--WGrgteILYQAMKLKMPEKV 222
Cdd:COG4607  152 EtLGEIFGKEDEAEELVADLDAKIAAL----KAAAAGKGTAlIVLTNGGK-ISAYGPGsrFG----PIHDVLGFKPADED 222

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736148119 223 KEKALKAGyyAVSQEVIPEFAGDYMI-------ISKNSEMDNSYQNSEIYKSIPAVKKHRVYEANAEEFYFN 287
Cdd:COG4607  223 IEASTHGQ--AISFEFIAEANPDWLFvidrdaaIGGEGPAAKQVLDNELVKQTTAWKNGQIVYLDPDAWYLA 292
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 57-282 8.41e-27

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: 105.14  E-value: 8.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119   57 VVVLGSYTGNVMSLGV--NLVGVDSWSKkNPRFQKKLKNVEEV---SDANVEKIMKLKPDVIIG---LSNTKNVEKLKKI 128
Cdd:pfam01497   1 AALSPAYTEILYALGAtdSIVGVDAYTR-DPLKADAVAAIVKVgayGEINVERLAALKPDLVILstgYLTDEAEELLSLI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  129 APTVLFTYNKV--DYLQQHIEIGKVLNKEKEAKAWVKDFKKRAAEAGKEIKAKIgeDATVSVFESGTKDLYVFGDAWGRG 206
Cdd:pfam01497  80 IPTVIFESSSTgeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLT--RKPVLVFGGADGGGYVVAGSNTYI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  207 TEILyQAMKLKMPEKVKEKalkaGYYA-VSQEVIPEFAGDYMIIS----KNSEMDNSYQNSEIYKSIPAVKKHRVYEANA 281
Cdd:pfam01497 158 GDLL-RILGIENIAAELSG----SEYApISFEAILSSNPDVIIVSgrdsFTKTGPEFVAANPLWAGLPAVKNGRVYTLPS 232


                  .
gi 736148119  282 E 282
Cdd:pfam01497 233 D 233
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 33-282 4.77e-23

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 96.28  E-value: 4.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  33 STSSDKITYQSENGPVKLPAHPKRVVVLG-SYTGNVMSLGVNLVGVDSWSKKN---PRFQKKLKNVEEV---SDANVEKI 105
Cdd:PRK11411  18 SSHAFAVTVQDEQGTFTLEKTPQRIVVLElSFVDALAAVGVSPVGVADDNDAKrilPEVRAHLKPWQSVgtrSQPSLEAI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 106 MKLKPDVIIGLSN--TKNVEKLKKIAPTVLFTYNKVDY---LQQHIEIGKVLNKEKEAKAWVKDFKKRAaeagKEIKAKI 180
Cdd:PRK11411  98 AALKPDLIIADSSrhAGVYIALQKIAPTLLLKSRNETYqenLQSAAIIGEVLGKKREMQARIEQHKERM----AQFASQL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 181 GEDATVSVFESGTKDLYVFGDAWGRGTeiLYQAMKLKMPekvKEKALKAGYYAVSQEVIPEFAGDYMII---SKNSEMDn 257
Cdd:PRK11411 174 PKGTRVAFGTSREQQFNLHSPESYTGS--VLAALGLNVP---KAPMNGAAMPSISLEQLLALNPDWLLVahyRQESIVK- 247

                        250       260
                 ....*....|....*....|....*
gi 736148119 258 SYQNSEIYKSIPAVKKHRVYEANAE 282
Cdd:PRK11411 248 RWQQDPLWQMLTAAKKQQVASVDSN 272
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 45-286 4.04e-21

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: 90.40  E-value: 4.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  45 NGPVKLPAHPKRVVVLGSYTGNVMS-LGVNLVGVDSwSKKNPRFQKKLKNVEEVS-----DANVEKIMKLKPDVII-GLS 117
Cdd:cd01140    3 LGETKVPKNPEKVVVFDVGALDTLDaLGVKVVGVPK-SSTLPEYLKKYKDDKYANvgtlfEPDLEAIAALKPDLIIiGGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 118 NTKNVEKLKKIAPTVLFTYNKVDYLQ---QHIE-IGKVLNKEKEAKAWVKDFKKRAAEAGKEIKAKigEDATVsVFESGT 193
Cdd:cd01140   82 LAEKYDELKKIAPTIDLGADLKNYLEsvkQNIEtLGKIFGKEEEAKELVAEIDASIAEAKSAAKGK--KKALV-VLVNGG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 194 KdLYVFGDawGRGTEILYQamKLKMPEKVKEKALKAGYYAVSQEVIPEFAGDY-------MIISKNSEMDNSYQNSEIYK 266
Cdd:cd01140  159 K-LSAFGP--GSRFGWLHD--LLGFEPADENIKASSHGQPVSFEYILEANPDWlfvidrgAAIGAEGSSAKEVLDNDLVK 233

                        250       260
                 ....*....|....*....|
gi 736148119 267 SIPAVKKHRVYEANAEEFYF 286
Cdd:cd01140  234 NTTAWKNGKVIYLDPDLWYL 253
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 55-189 2.33e-20

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: 85.30  E-value: 2.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  55 KRVVVLG-SYTGNVMSLG--VNLVGVDSWSKKNPRFQKKLKNVEEV---SDANVEKIMKLKPDVII--GLSNTKNVEKLK 126
Cdd:cd00636    1 KRVVALDpGATELLLALGgdDKPVGVADPSGYPPEAKALLEKVPDVghgYEPNLEKIAALKPDLIIanGSGLEAWLDKLS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736148119 127 KIA-PTVLFTYNKVDYLQQHIE----IGKVLNKEKEAKAWVKDFKKRAAEAGKEIKAKIGEDATVSVF 189
Cdd:cd00636   81 KIAiPVVVVDEASELSLENIKEsirlIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVVG 148
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 53-201 2.06e-17

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: 78.47  E-value: 2.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  53 HPKRVVVLG-SYTGNVMSLGV--NLVGVDSWSKKNPRFQKKLKnVEEVSDANVEKIMKLKPDVIIG--LSNTKNVEKLKK 127
Cdd:cd01143    2 EPERIVSLSpSITEILFALGAgdKIVGVDTYSNYPKEVRKKPK-VGSYSNPNVEKIVALKPDLVIVssSSLAELLEKLKD 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736148119 128 IAPTVLFTYNKVDY---LQQHIEIGKVLNKEKEAKAWVKDFKKRAAEAGKEIKAKIGEdatVSVFESGTKDLYVFGD 201
Cdd:cd01143   81 AGIPVVVLPAASSLdeiYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKS---KVYIEVSLGGPYTAGK 154
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 48-279 5.23e-17

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: 79.32  E-value: 5.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  48 VKLPAHPKRVVVLGsYTGNVMSLGV----NLVGVDSWSKKNPRFQK---KLKNVEEV---SDANVEKIMKLKPDVIIGLS 117
Cdd:cd01142   18 VTIPDEVKRIAALW-GAGNAVVAALgggkLIVATTSTVQQEPWLYRlapSLENVATGgtgNDVNIEELLALKPDVVIVWS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 118 --NTKNVEKLKKIAPTVLFTYNKVDYLQQHIE-IGKVLNKEKEAKAWVKDFKKRAAeAGKEIKAKIGEDATVSVFesgtk 194
Cdd:cd01142   97 tdGKEAGKAVLRLLNALSLRDAELEEVKLTIAlLGELLGRQEKAEALVAYFDDNLA-YVAARTKKLPDSERPRVY----- 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 195 dlYVFGDAW---GRGTeILYQAMKLKMPEKVKEKALKAGYYAVSQEVI----PEFagdymIISKNSEMDNSYQNSEIYKS 267
Cdd:cd01142  171 --YAGPDPLttdGTGS-ITNSWIDLAGGINVASEATKKGSGEVSLEQLlkwnPDV-----IIVGNADTKAAILADPRWQN 242

                        250
                 ....*....|..
gi 736148119 268 IPAVKKHRVYEA 279
Cdd:cd01142  243 LRAVKNGRVYVN 254
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 56-284 3.20e-16

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: 76.60  E-value: 3.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  56 RVVVLGSYTGN-VMSLGV--NLVGVDS-WSKKNPR----FQKKLKNVEEV------SDANVEKIMKLKPDVII------G 115
Cdd:cd01147    7 RVVAAGPGALRlLYALAApdKIVGVDDaEKSDEGRpyflASPELKDLPVIgrggrgNTPNYEKIAALKPDVVIdvgsddP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 116 LSNTKNVEKLKKIAPTVLFTYNKVDYLQQHIE-IGKVLNKEKEAKAWVKDFKKRAAEAgKEIKAKIGEDATVSVFESGTK 194
Cdd:cd01147   87 TSIADDLQKKTGIPVVVLDGGDSLEDTPEQIRlLGKVLGKEERAEELISFIESILADV-EERTKDIPDEEKPTVYFGRIG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 195 DLYVFGDAWGRGTEIlyQAMKLKMPEKVKEKALKAGYYAVSQEVIPEFAGDYMIISKNS---EMDNSYQNSEIYKSIPAV 271
Cdd:cd01147  166 TKGAAGLESGLAGSI--EVFELAGGINVADGLGGGGLKEVSPEQILLWNPDVIFLDTGSfylSLEGYAKNRPFWQSLKAV 243

                        250
                 ....*....|...
gi 736148119 272 KKHRVYEANAEEF 284
Cdd:cd01147  244 KNGRVYLLPALPF 256
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 39-276 1.46e-12

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: 66.59  E-value: 1.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  39 ITYQSENGPVKLPAHPKRVVVLGSYTGNVM-SLGV--NLVGVDSWSKK-NPRFQKKLKNVEEVS--DANVEKIMKLKPDV 112
Cdd:cd01148    3 LTVENCGRSVTFDKAPQRVVSNDQNTTEMMlALGLqdRMVGTAGIDNKdLPELKAKYDKVPELAkkYPSKETVLAARPDL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 113 IIGLSNTKN-------VEKLKKI-APTVLFT--------YNKVDYLQQHIE-IGKVLNKEKEAKAWVKDFKKRAAEAGKE 175
Cdd:cd01148   83 VFGGWSYGFdkgglgtPDSLAELgIKTYILPescgqrrgEATLDDVYNDIRnLGKIFDVEDRADKLVADLKARLAEISAK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 176 IKaKIGEDATVSVFESGTKDLYVFgdawGRGTeiLYQAMKLKMPEKVKEKALKAGYYAVSQEVI----PEF--AGDYMII 249
Cdd:cd01148  163 VK-GDGKKVAVFVYDSGEDKPFTS----GRGG--IPNAIITAAGGRNVFADVDESWTTVSWETViarnPDVivIIDYGDQ 235

                        250       260
                 ....*....|....*....|....*..
gi 736148119 250 SKNSEMDNSYQNSEIYKSIPAVKKHRV 276
Cdd:cd01148  236 NAAEQKIKFLKENPALKNVPAVKNNRF 262
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 54-160 2.31e-08

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: 53.19  E-value: 2.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  54 PKRVVVLgSYTGNVMSLGV----NLVGVDSWS--KKNPRFQKKLKN-VEEVSDANVEKIMKLKPDVII---GLSNTKNVE 123
Cdd:cd01141    8 PKRIVVL-SPTHVDLLLALdkadKIVGVSASAydLNTPAVKERIDIqVGPTGSLNVELIVALKPDLVIlygGFQAQTILD 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 736148119 124 KLKKIAPTVLFTYNKVDYLqQHIEIGKVL----NKEKEAKA 160
Cdd:cd01141   87 KLEQLGIPVLYVNEYPSPL-GRAEWIKFAaafyGVGKEDKA 126
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 54-271 3.64e-08

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: 53.04  E-value: 3.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  54 PKRVVVLG-SYTGNVMSLGV--NLVGVDSwSKKNPRFQKKLKNVEEVSDANVEKIMKLKPDVIIGLSNT---KNVEKLKK 127
Cdd:cd01149    1 PERIVSLGgSVTEIVYALGAgdRLVGVDS-TSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAgppEALDQLRA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119 128 IAPTVLF---TYNKVDYLQQHIEIGKVLNKEKEAKAWVKDFKKRAAEAGKEIKAKIGEDATVSVFESGTKDLYVFgdawG 204
Cdd:cd01149   80 AGVPVVTvpsTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRVLFLLSHGGGAAMAA----G 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736148119 205 RGTEIlyQAMkLKMPEKVKEKALKAGYYAVSQEVIPEFAGDYMIISKNSEmdNSYQNSEIYKSIPAV 271
Cdd:cd01149  156 RNTAA--DAI-IALAGAVNAAAGFRGYKPLSAEALIAAQPDVILVMSRGL--DAVGGVDGLLKLPGL 217
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 74-203 1.49e-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: 48.45  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  74 LVGVDSWSKKNPRfQKKLKNVEEVSDANVEKIMKLKPDVIIG--LSNTK-NVEKLKKIAPTVLFTYNKV--DYLQQHIEI 148
Cdd:cd01144   23 LVGVTDYCDYPPE-AKKLPRVGGFYQLDLERVLALKPDLVIAwdDCNVCaVVDQLRAAGIPVLVSEPQTldDILADIRRL 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 736148119 149 GKVLNKEKEAKAWVKDFKKRAAEAGKEIKAKigedATVSVF-ESGTKDLYVFGDAW 203
Cdd:cd01144  102 GTLAGRPARAEELAEALRRRLAALRKQYASK----PPPRVFyQEWIDPLMTAGGDW 153
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 48-170 5.08e-04

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: 41.14  E-value: 5.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736148119  48 VKLPAHPKRVVVLGSYTGNVMSLG------VNLVGVDS-WSKKNP----RFQKKLKNVEEV--------SDANVEKIMKL 108
Cdd:cd01139   11 VTLDAPVERVLLGEGRQLYALALLegenpfARIVGWGGdLKKGDPdtyaKYKEKFPEIADIpligstynGDFSVEKVLTL 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736148119 109 KPDVII-------GLSNTKNVEKLKKIAPTVLFT--YNKV-DYLQQHIEI-GKVLNKEKEAKAWVKDFKKRAA 170
Cdd:cd01139   91 KPDLVIlniwaktTAEESGILEKLEQAGIPVVFVdfRQKPlKNTTPSMRLlGKALGREERAEEFIEFYQERID 163
PRK03379 PRK03379
vitamin B12-transporter protein BtuF; Provisional
 47-114 3.31e-03

vitamin B12-transporter protein BtuF; Provisional


Pssm-ID: 179575 [Multi-domain]  Cd Length: 260  Bit Score: 38.51  E-value: 3.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736148119  47 PVKLPAHPkRVVVLG-SYTGNVMSLGVNLVGVDSWSKKNPRFQKklknVEEVSD---ANVEKIMKLKPDVII 114
Cdd:PRK03379  11 PLWLNAAP-RVITLSpANTELAFAAGITPVGVSSYSDYPPQAKK----IEQVATwqgMNLERIVALKPDLVL 77
 
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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