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Conserved domains on  [gi|2777341883|ref|WP_367887737|]
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ABC transporter substrate-binding protein [Pseudogemmatithrix spongiicola]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 11427633)

uncharacterized ABC transporter substrate-binding protein, which functions as the initial receptor in ABC transport of metal ions or other substrates

CATH:  3.40.50.1980
Gene Ontology:  GO:0140359|GO:0055052
PubMed:  26517916|25750732
TCDB:  3.A.1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
52-294 3.42e-66

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


:

Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 208.31  E-value: 3.42e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  52 RVVSLNPVTTELLFALGVGDRAVGRTTWDLF---PEAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLRA 128
Cdd:COG0614     2 RIVSLSPSATELLLALGAGDRLVGVSDWGYCdypELELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDEEDYEQLEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 129 AGIATLTHRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRA-MPRPAEPVRAFWHIW-DAPIMTIGGGSYMS 206
Cdd:COG0614    82 IGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRArLAGAEERPTVLYEIWsGDPLYTAGGGSFIG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 207 ELLEIAGAVNVFADAEQPSPAVSLEEIARRNPDVILAGPNN---------ARKLRANPLWQAVPAVRAGRILVIDTTVVG 277
Cdd:COG0614   162 ELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGydaetaeeaLEALLADPGWQSLPAVKNGRVYVVPGDLLS 241
                         250
                  ....*....|....*..
gi 2777341883 278 RPGVRMGEAARFLRRAL 294
Cdd:COG0614   242 RPGPRLLLALEDLAKAL 258
 
Name Accession Description Interval E-value
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
52-294 3.42e-66

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 208.31  E-value: 3.42e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  52 RVVSLNPVTTELLFALGVGDRAVGRTTWDLF---PEAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLRA 128
Cdd:COG0614     2 RIVSLSPSATELLLALGAGDRLVGVSDWGYCdypELELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDEEDYEQLEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 129 AGIATLTHRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRA-MPRPAEPVRAFWHIW-DAPIMTIGGGSYMS 206
Cdd:COG0614    82 IGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRArLAGAEERPTVLYEIWsGDPLYTAGGGSFIG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 207 ELLEIAGAVNVFADAEQPSPAVSLEEIARRNPDVILAGPNN---------ARKLRANPLWQAVPAVRAGRILVIDTTVVG 277
Cdd:COG0614   162 ELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGydaetaeeaLEALLADPGWQSLPAVKNGRVYVVPGDLLS 241
                         250
                  ....*....|....*..
gi 2777341883 278 RPGVRMGEAARFLRRAL 294
Cdd:COG0614   242 RPGPRLLLALEDLAKAL 258
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
51-290 1.02e-56

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: 183.27  E-value: 1.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  51 QRVVSLNPVTTELLFALGVGDRAVGRTTWDLFPEAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLRAAG 130
Cdd:cd01144     1 MRIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 131 IATLTHRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRAMPRPAEPVRAFWHIWDAPIMTiGGGSYMSELLE 210
Cdd:cd01144    81 IPVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQEWIDPLMT-AGGDWVPELIA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 211 IAGAVNVFADAEQPSPAVSLEEIARRNPDVILAGP----NNARKLRANPLWQAVPAVRAGRILVIDTTVVGRPGVRMGEA 286
Cdd:cd01144   160 LAGGVNVFADAGERSPQVSWEDVLAANPDVIVLSPcgfgFTPAILRKEPAWQALPAVRNGRVYAVDGNWYFRPSPRLVDG 239

                  ....
gi 2777341883 287 ARFL 290
Cdd:cd01144   240 LEQL 243
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
54-272 1.38e-33

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: 122.86  E-value: 1.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  54 VSLNPVTTELLFALGVGDRAVGRTTWDLFPEAAKAVPDL---GPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLrAAG 130
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAIvkvGAYGEINVERLAALKPDLVILSTGYLTDEAEELL-SLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 131 IATLTHRTDK-VADLQRVLPVIAAALGV-DSLGRLVADSVRASVEAVRAMPRPAEPVRAFWHIWD-APIMTIGGGSYMSE 207
Cdd:pfam01497  80 IPTVIFESSStGESLKEQIKQLGELLGLeDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADgGGYVVAGSNTYIGD 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2777341883 208 LLEIAGAVNVFAD-AEQPSPAVSLEEIARRNPDVIL----AGPNNARK--LRANPLWQAVPAVRAGRILVID 272
Cdd:pfam01497 160 LLRILGIENIAAElSGSEYAPISFEAILSSNPDVIIvsgrDSFTKTGPefVAANPLWAGLPAVKNGRVYTLP 231
PRK03379 PRK03379
vitamin B12-transporter protein BtuF; Provisional
50-269 7.88e-25

vitamin B12-transporter protein BtuF; Provisional


Pssm-ID: 179575 [Multi-domain]  Cd Length: 260  Bit Score: 100.53  E-value: 7.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  50 AQRVVSLNPVTTELLFALGVGDRAVgrTTWDLFPEAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLRAA 129
Cdd:PRK03379   17 APRVITLSPANTELAFAAGITPVGV--SSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAWRGGNAERQVDQLASL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 130 GIATLTHRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRAMPRPAEPVRAFWHIWDAPIMTIGGGSYMSELL 209
Cdd:PRK03379   95 GIKVMWVDATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADKPKKRVFLQFGTNPLFTSGKHSIQSQVL 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2777341883 210 EIAGAVNVFADAEQPSPAVSLEEIARRNPDVILAGPNNARKLRANPLWQ---AVPAV--------RAG-RIL 269
Cdd:PRK03379  175 SLCGGENIFADSRVPWPQVSREQVLARKPQAIVITGGPDQIPKIKQFWGpqlKIPVIplnsdwfeRASpRII 246
TroA_like NF038402
helical backbone metal receptor;
52-242 1.67e-19

helical backbone metal receptor;


Pssm-ID: 439691  Cd Length: 219  Bit Score: 84.98  E-value: 1.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  52 RVVSLNPVTTELLfALGVGDRAVGRTTWDLFPeAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLRAAGI 131
Cdd:NF038402    1 RVVSLVPSLTEAI-AATAPELLVGATDWCTHP-ADLDVARVRGTKNPDRAAIAALRPDLVVANQEENRELDVDRLRAAGV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 132 ATLTHRTDKVADlqrvlpviaaalGVDSLGRLVADSVRASV-------EAVRAMPRPAEPVRAFWHIWDAPIMTIGGGSY 204
Cdd:NF038402   79 PVWVTRIETVDE------------ALASLRRLFTEALGVPVpgwldeaEREWAAPAPAPRRRAVVPIWRDPWMVVGRDTF 146
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2777341883 205 MSELLEIAGAVNVFADAEQPSPAVSLEEIARRNPDVIL 242
Cdd:NF038402  147 TGDLLARLGLRNVFADHPERYPHVDLDELDAAGPDLVL 184
 
Name Accession Description Interval E-value
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
52-294 3.42e-66

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 208.31  E-value: 3.42e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  52 RVVSLNPVTTELLFALGVGDRAVGRTTWDLF---PEAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLRA 128
Cdd:COG0614     2 RIVSLSPSATELLLALGAGDRLVGVSDWGYCdypELELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDEEDYEQLEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 129 AGIATLTHRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRA-MPRPAEPVRAFWHIW-DAPIMTIGGGSYMS 206
Cdd:COG0614    82 IGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRArLAGAEERPTVLYEIWsGDPLYTAGGGSFIG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 207 ELLEIAGAVNVFADAEQPSPAVSLEEIARRNPDVILAGPNN---------ARKLRANPLWQAVPAVRAGRILVIDTTVVG 277
Cdd:COG0614   162 ELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGydaetaeeaLEALLADPGWQSLPAVKNGRVYVVPGDLLS 241
                         250
                  ....*....|....*..
gi 2777341883 278 RPGVRMGEAARFLRRAL 294
Cdd:COG0614   242 RPGPRLLLALEDLAKAL 258
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
51-290 1.02e-56

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: 183.27  E-value: 1.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  51 QRVVSLNPVTTELLFALGVGDRAVGRTTWDLFPEAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLRAAG 130
Cdd:cd01144     1 MRIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 131 IATLTHRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRAMPRPAEPVRAFWHIWDAPIMTiGGGSYMSELLE 210
Cdd:cd01144    81 IPVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQEWIDPLMT-AGGDWVPELIA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 211 IAGAVNVFADAEQPSPAVSLEEIARRNPDVILAGP----NNARKLRANPLWQAVPAVRAGRILVIDTTVVGRPGVRMGEA 286
Cdd:cd01144   160 LAGGVNVFADAGERSPQVSWEDVLAANPDVIVLSPcgfgFTPAILRKEPAWQALPAVRNGRVYAVDGNWYFRPSPRLVDG 239

                  ....
gi 2777341883 287 ARFL 290
Cdd:cd01144   240 LEQL 243
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
43-294 1.66e-44

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 153.04  E-value: 1.66e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  43 TSRFARPAQRVVSLNPVTTELLFALGVGDRAVGRTTWDLFPEAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAA 122
Cdd:COG4558    20 ASVAAAAAERIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVGYMRQLSAEGILSLKPTLVLASEGAGPPEV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 123 VQQLRAAGIATLT-HRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRAMP-RPAEPVRAFWhiwdapIMTIG 200
Cdd:COG4558   100 LDQLRAAGVPVVVvPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVaAIGKPPRVLF------LLSRG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 201 GGSYM--------SELLEIAGAVNVFADAEQPSPaVSLEEIARRNPDVIL------AGPNNARKLRANPLWQAVPAVRAG 266
Cdd:COG4558   174 GGRPMvagrgtaaDALIRLAGGVNAAAGFEGYKP-LSAEALIAAAPDVILvmtrglESLGGVDGLLALPGLAQTPAGKNK 252
                         250       260
                  ....*....|....*....|....*...
gi 2777341883 267 RILVIDTTVVGRPGVRMGEAARFLRRAL 294
Cdd:COG4558   253 RIVAMDDLLLLGFGPRTPQAALALAQAL 280
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
48-242 1.55e-40

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: 139.72  E-value: 1.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  48 RPAQRVVSLNPVTTELLFALGVGDRAVGRTTWDLFPEAAKAVPDLGPGMGPNVEAVMGQRPDLVLlyASESNRAAV-QQL 126
Cdd:cd01143     1 KEPERIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVI--VSSSSLAELlEKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 127 RAAGIATL-THRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRAMPRpAEPVRAFWHIWDAP-IMTIGGGSY 204
Cdd:cd01143    79 KDAGIPVVvLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGK-TIKKSKVYIEVSLGgPYTAGKNTF 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2777341883 205 MSELLEIAGAVNVFADAEQpSPAVSLEEIARRNPDVIL 242
Cdd:cd01143   158 INELIRLAGAKNIAADSGG-WPQVSPEEILKANPDVII 194
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
54-272 1.38e-33

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: 122.86  E-value: 1.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  54 VSLNPVTTELLFALGVGDRAVGRTTWDLFPEAAKAVPDL---GPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLrAAG 130
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAIvkvGAYGEINVERLAALKPDLVILSTGYLTDEAEELL-SLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 131 IATLTHRTDK-VADLQRVLPVIAAALGV-DSLGRLVADSVRASVEAVRAMPRPAEPVRAFWHIWD-APIMTIGGGSYMSE 207
Cdd:pfam01497  80 IPTVIFESSStGESLKEQIKQLGELLGLeDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADgGGYVVAGSNTYIGD 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2777341883 208 LLEIAGAVNVFAD-AEQPSPAVSLEEIARRNPDVIL----AGPNNARK--LRANPLWQAVPAVRAGRILVID 272
Cdd:pfam01497 160 LLRILGIENIAAElSGSEYAPISFEAILSSNPDVIIvsgrDSFTKTGPefVAANPLWAGLPAVKNGRVYTLP 231
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
35-290 4.18e-31

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: 117.84  E-value: 4.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  35 TVIDDFGDTSRFARPAQRVVSLNPVTTELLFALGVGDRAVGRT---TWD-----LFPEAAKaVPDLGPGMGPNVEAVMGQ 106
Cdd:cd01142     9 TITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTstvQQEpwlyrLAPSLEN-VATGGTGNDVNIEELLAL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 107 RPDLVLLYAS---ESNRAAVQQLRAAGIatlthrtdKVADLQRVLPVIAAaLGVDSLGRLVADS----VRASVEAVRAMP 179
Cdd:cd01142    88 KPDVVIVWSTdgkEAGKAVLRLLNALSL--------RDAELEEVKLTIAL-LGELLGRQEKAEAlvayFDDNLAYVAART 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 180 R--PAEPVRAFWHIWDAPIMTIGGGSYMSELLEIAGAVNVFADAEQP-SPAVSLEEIARRNPDVILAG-PNNARKLRANP 255
Cdd:cd01142   159 KklPDSERPRVYYAGPDPLTTDGTGSITNSWIDLAGGINVASEATKKgSGEVSLEQLLKWNPDVIIVGnADTKAAILADP 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2777341883 256 LWQAVPAVRAGRILVIDTTVV--GRPGVRMG----EAARFL 290
Cdd:cd01142   239 RWQNLRAVKNGRVYVNPEGAFwwDRPSAEEAllglWLAKTL 279
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
37-272 4.45e-31

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: 117.82  E-value: 4.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  37 IDDFGDTSRFARPAQRVVSLNPVTTELLFALGVGDRAVGRTTWD-----LFPEAAKAVPDLGPGMgPNVEAVMGQRPDLV 111
Cdd:cd01148     5 VENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAGIDnkdlpELKAKYDKVPELAKKY-PSKETVLAARPDLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 112 LLYASESNR----AAVQQLRAAGIATLTHRTDKVadlQRVLPVIAAALGVD--SLGR----------LVADSvRASVEAV 175
Cdd:cd01148    84 FGGWSYGFDkgglGTPDSLAELGIKTYILPESCG---QRRGEATLDDVYNDirNLGKifdvedradkLVADL-KARLAEI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 176 RA-MPRPAEPVRAFWHIW--DAPiMTIGGGSYMSELLEIAGAVNVFADAEQPSPAVSLEEIARRNPDVILA-------GP 245
Cdd:cd01148   160 SAkVKGDGKKVAVFVYDSgeDKP-FTSGRGGIPNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIVIidygdqnAA 238
                         250       260
                  ....*....|....*....|....*...
gi 2777341883 246 NNARK-LRANPLWQAVPAVRAGRILVID 272
Cdd:cd01148   239 EQKIKfLKENPALKNVPAVKNNRFIVLP 266
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
50-272 7.89e-29

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: 110.43  E-value: 7.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  50 AQRVVSLNPVTTELLFALGVGDRAVGRTTWDLFPEAAKAVPDLGPGMGPNVEAVMGQRPDLVLlyASESN--RAAVQQLR 127
Cdd:cd01149     1 PERIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVI--ASDEAgpPEALDQLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 128 AAGIATLThrTDKVADLQRVLP---VIAAALGVDSLGRLVADSVRASVEAVRAMP--RPAEPVRAFWHIWDA-PIMTIGG 201
Cdd:cd01149    79 AAGVPVVT--VPSTPTLDGLLTkirQVAQALGVPEKGEALAQEVRQRLAALRKTVaaHKKPPRVLFLLSHGGgAAMAAGR 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2777341883 202 GSYMSELLEIAGAVNVfADAEQPSPAVSLEEIARRNPDVIL------AGPNNARKLRANPLWQAVPAVRAGRILVID 272
Cdd:cd01149   157 NTAADAIIALAGAVNA-AAGFRGYKPLSAEALIAAQPDVILvmsrglDAVGGVDGLLKLPGLAQTPAGRNKRILAMD 232
PRK03379 PRK03379
vitamin B12-transporter protein BtuF; Provisional
50-269 7.88e-25

vitamin B12-transporter protein BtuF; Provisional


Pssm-ID: 179575 [Multi-domain]  Cd Length: 260  Bit Score: 100.53  E-value: 7.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  50 AQRVVSLNPVTTELLFALGVGDRAVgrTTWDLFPEAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLRAA 129
Cdd:PRK03379   17 APRVITLSPANTELAFAAGITPVGV--SSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAWRGGNAERQVDQLASL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 130 GIATLTHRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRAMPRPAEPVRAFWHIWDAPIMTIGGGSYMSELL 209
Cdd:PRK03379   95 GIKVMWVDATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADKPKKRVFLQFGTNPLFTSGKHSIQSQVL 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2777341883 210 EIAGAVNVFADAEQPSPAVSLEEIARRNPDVILAGPNNARKLRANPLWQ---AVPAV--------RAG-RIL 269
Cdd:PRK03379  175 SLCGGENIFADSRVPWPQVSREQVLARKPQAIVITGGPDQIPKIKQFWGpqlKIPVIplnsdwfeRASpRII 246
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
49-292 8.35e-22

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: 91.96  E-value: 8.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  49 PAQRVVSLNPVTTELLFALGVGDRAVGrTTWDLFP------EAAKAVPDLGPGMGPNVEAVMGQRPDLVLlyASES-NRA 121
Cdd:cd01146     2 KPQRIVALDWGALETLLALGVKPVGVA-DTAGYKPwipepaLPLEGVVDVGTRGQPNLEAIAALKPDLIL--GSASrHDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 122 AVQQLRAagIA---TLTHRTDkVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRA-MPRPAEPVRAFWHIWDAPIM 197
Cdd:cd01146    79 IYDQLSQ--IAptvLLDSSPW-LAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQkLPDKGPKPVSVVRFSDAGSI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 198 TI-GGGSYMSELLEIAGAVNVFADAE---QPSPAVSLEEIARRNPDVIL----AGPNNARKLRANPLWQAVPAVRAGRIL 269
Cdd:cd01146   156 RLyGPNSFAGSVLEDLGLQNPWAQETtndSGFATISLERLAKADADVLFvftyEDEELAQALQANPLWQNLPAVKNGRVY 235
                         250       260
                  ....*....|....*....|...
gi 2777341883 270 VIDTTVVGRPGVRMgeAARFLRR 292
Cdd:cd01146   236 VVDDVWWFFGGGLS--AARLLLD 256
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
46-270 2.49e-20

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: 88.16  E-value: 2.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  46 FARPAQRVVSLNPVTTELLFALGVGDRAVG----------RTTWDLFPEAAKaVPDLGPGMG---PNVEAVMGQRPDLVL 112
Cdd:cd01147     1 VPKPVERVVAAGPGALRLLYALAAPDKIVGvddaeksdegRPYFLASPELKD-LPVIGRGGRgntPNYEKIAALKPDVVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 113 L---YASESNRAAVQQlrAAGIA-TLTHRTDKVADLQRVLPVIAAALGVDSLGRLVAD---SVRASVEAVRAMPRPAEPV 185
Cdd:cd01147    80 DvgsDDPTSIADDLQK--KTGIPvVVLDGGDSLEDTPEQIRLLGKVLGKEERAEELISfieSILADVEERTKDIPDEEKP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 186 RAFWhiwdAPIMTIGGGSYMS------ELLEIAGAVNVFADAEQPSPA-VSLEEIARRNPDVILAGPNN-----ARKLRA 253
Cdd:cd01147   158 TVYF----GRIGTKGAAGLESglagsiEVFELAGGINVADGLGGGGLKeVSPEQILLWNPDVIFLDTGSfylslEGYAKN 233
                         250
                  ....*....|....*..
gi 2777341883 254 NPLWQAVPAVRAGRILV 270
Cdd:cd01147   234 RPFWQSLKAVKNGRVYL 250
TroA_like NF038402
helical backbone metal receptor;
52-242 1.67e-19

helical backbone metal receptor;


Pssm-ID: 439691  Cd Length: 219  Bit Score: 84.98  E-value: 1.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  52 RVVSLNPVTTELLfALGVGDRAVGRTTWDLFPeAAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAVQQLRAAGI 131
Cdd:NF038402    1 RVVSLVPSLTEAI-AATAPELLVGATDWCTHP-ADLDVARVRGTKNPDRAAIAALRPDLVVANQEENRELDVDRLRAAGV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 132 ATLTHRTDKVADlqrvlpviaaalGVDSLGRLVADSVRASV-------EAVRAMPRPAEPVRAFWHIWDAPIMTIGGGSY 204
Cdd:NF038402   79 PVWVTRIETVDE------------ALASLRRLFTEALGVPVpgwldeaEREWAAPAPAPRRRAVVPIWRDPWMVVGRDTF 146
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2777341883 205 MSELLEIAGAVNVFADAEQPSPAVSLEEIARRNPDVIL 242
Cdd:NF038402  147 TGDLLARLGLRNVFADHPERYPHVDLDELDAAGPDLVL 184
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
31-272 3.39e-17

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 80.35  E-value: 3.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  31 AFSHTVIDDFGDTSRFARPaQRVVSLNPVTTELLFALGV-----GDRAVGRTTWDLFPEAAKAVPDLGPGMGPNVEAVMG 105
Cdd:COG4594    34 AGARTVKHAMGETTIPGTP-KRVVVLEWSFADALLALGVtpvgiADDNDYDRWVPYLRDLIKGVTSVGTRSQPNLEAIAA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 106 QRPDLVLlyASESNRAAV-QQLRAagIA-TLT--HRTDKVADLQRVLPVIAAALGVDSLGRLV-------ADSVRASVEA 174
Cdd:COG4594   113 LKPDLII--ADKSRHEAIyDQLSK--IApTVLfkSRNGDYQENLESFKTIAKALGKEEEAEAVladhdqrIAEAKAKLAA 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 175 VRAmPRPAEPVRAFwhiwdAPIMTI-GGGSYMSELLEIAGAVNVFADAEQPSPA---VSLEEIARRNPDVILAG----PN 246
Cdd:COG4594   189 ADK-GKKVAVGQFR-----ADGLRLyTPNSFAGSVLAALGFENPPKQSKDNGYGyseVSLEQLPALDPDVLFIAtyddPS 262
                         250       260
                  ....*....|....*....|....*.
gi 2777341883 247 NARKLRANPLWQAVPAVRAGRILVID 272
Cdd:COG4594   263 ILKEWKNNPLWKNLKAVKNGRVYEVD 288
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
48-296 3.50e-16

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 78.03  E-value: 3.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  48 RPAqRVVSLNPVTTELLFALGVGDRAVGRTTWDLFPEAAKAVPDL--GPGMGPNVEAVMGQRPDLVLLYASESNRAaVQQ 125
Cdd:PRK09534   59 RPE-RVVTLNPSAAQTMWELGARDRVVGVTQYASYLDGAEERTNVsgGQPFGVNVEAVVGLDPDLVLAPNAVAGDT-VTR 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 126 LRAAGI--------ATLTHRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRAMPRpaepvrAFWHIWDApiM 197
Cdd:PRK09534  137 LREAGItvfhfpaaTSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADVDDRPR------VLYPLGDG--Y 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 198 TIGGGSYMSELLEIAGAVNVFADAEQPS-PAVSLEEIARRNPDVILAGPNNARKLRANPlWQAVPAVRAGRILVIDTTVV 276
Cdd:PRK09534  209 TAGGNTFIGALIEAAGGHNVAADATTDGyPQLSEEVIVQQDPDVIVVATASALVAETEP-YASTTAGETGNVVTVNVNHI 287
                         250       260
                  ....*....|....*....|
gi 2777341883 277 GRPGVRMGEAARFLRRALVD 296
Cdd:PRK09534  288 NQPAPRIVESMATMATAFHN 307
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
51-188 3.97e-15

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: 71.05  E-value: 3.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  51 QRVVSLNPVTTELLFALGVGDRAVGRTTWDLFPEAAKA----VPDLGPGMGPNVEAVMGQRPDLVlLYASESNRAAVQQL 126
Cdd:cd00636     1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKAllekVPDVGHGYEPNLEKIAALKPDLI-IANGSGLEAWLDKL 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2777341883 127 RAAGIATLTHRTDKVADLQRVLP---VIAAALGVDSLGRLVADSVRASVEAVRAMPRPAEPVRAF 188
Cdd:cd00636    80 SKIAIPVVVVDEASELSLENIKEsirLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVS 144
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
48-220 5.31e-14

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: 68.99  E-value: 5.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  48 RPAQRVVSLNPVTTELLFALGVGDRAVGRTTWDLFPE----AAKAVPDLGPGMGPNVEAVMGQRPDLVLLYASESNRAAV 123
Cdd:cd01141     6 VPPKRIVVLSPTHVDLLLALDKADKIVGVSASAYDLNtpavKERIDIQVGPTGSLNVELIVALKPDLVILYGGFQAQTIL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 124 QQLRAAGIATLThrTDKVAD-LQRVLPVIAAALGVDSLGRLVADSVRASVEAVR-----AMPRPAEPVRAFWHIWDAPIM 197
Cdd:cd01141    86 DKLEQLGIPVLY--VNEYPSpLGRAEWIKFAAAFYGVGKEDKADEAFAQIAGRYrdlakKVSNLNKPTVAIGKPVKGLWY 163
                         170       180
                  ....*....|....*....|...
gi 2777341883 198 TIGGGSYMSELLEIAGAVNVFAD 220
Cdd:cd01141   164 MPGGNSYVAKMLRDAGGRYLSAE 186
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
38-272 2.17e-13

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: 68.82  E-value: 2.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  38 DDFGDTSRFARPaQRVVSLNPVTTELLFALGVgdRAVGRTTWDLFPEAAKAV-----PDLGPGMGPNVEAVMGQRPDLVL 112
Cdd:cd01140     1 HALGETKVPKNP-EKVVVFDVGALDTLDALGV--KVVGVPKSSTLPEYLKKYkddkyANVGTLFEPDLEAIAALKPDLII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 113 LyaseSNRAAvqqlraagiatlthrtDKVADLQRVLPVIAAALG-----------VDSLGR----------LVADsVRAS 171
Cdd:cd01140    78 I----GGRLA----------------EKYDELKKIAPTIDLGADlknylesvkqnIETLGKifgkeeeakeLVAE-IDAS 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 172 VEAVRAMPRPAEPVRAFWHIwDAPIMTIGGGSYMSELLEIAGAVNVFADAEQPSP--AVSLEEIARRNPDVIL------- 242
Cdd:cd01140   137 IAEAKSAAKGKKKALVVLVN-GGKLSAFGPGSRFGWLHDLLGFEPADENIKASSHgqPVSFEYILEANPDWLFvidrgaa 215
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2777341883 243 --AGPNNARKLRANPLWQAVPAVRAGRILVID 272
Cdd:cd01140   216 igAEGSSAKEVLDNDLVKNTTAWKNGKVIYLD 247
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
16-272 7.90e-09

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


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 55.57  E-value: 7.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  16 LAACtGQERAATGGPAFSHTV-IDDFGDTSRFARPAQRVVSLNPVTTELLFALGVGDRAVGRttwDLFPE-----AAKAV 89
Cdd:COG4607    17 LAAC-GSSSAAAASAAAAETVtVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVEVAGVPK---GLLPDylskyADDKY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  90 PDLGPGMGPNVEAVMGQRPDLVLLyaseSNRAAvqqlraagiatlthrtDKVADLQRVLPVIaaALGVDS---------- 159
Cdd:COG4607    93 ANVGTLFEPDLEAIAALKPDLIII----GGRSA----------------KKYDELSKIAPTI--DLTVDGedyleslkrn 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 160 ---LGR----------LVADsVRASVEAVRAMPRPAEPVRAfwhiwdapIMTIGG-------GSYMSELLEIAGAVNVFA 219
Cdd:COG4607   151 tetLGEifgkedeaeeLVAD-LDAKIAALKAAAAGKGTALI--------VLTNGGkisaygpGSRFGPIHDVLGFKPADE 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2777341883 220 DAE-----QPspaVSLEEIARRNPDVIL---------AGPNNARKLRANPLWQAVPAVRAGRILVID 272
Cdd:COG4607   222 DIEasthgQA---ISFEFIAEANPDWLFvidrdaaigGEGPAAKQVLDNELVKQTTAWKNGQIVYLD 285
PRK10576 PRK10576
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
50-267 2.23e-08

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


Pssm-ID: 236719  Cd Length: 292  Bit Score: 54.25  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  50 AQRVVSLNPVTTELLFALGVGDRAVGRT----TWDLFPEAAKAVPDLGPGMGPNVEAVMGQRPDLVLLyaSESNRAAVQQ 125
Cdd:PRK10576   32 PNRIVALEWLPVELLLALGVTPYGVADThnyrLWVSEPALPDSVIDVGLRTEPNLELLTQMKPSLILW--SAGYGPSPEK 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 126 LRAagIA-----TLTHRTDKVADLQRVLPVIAAALGVDSLGRLVADSVRASVEAVRA--MPRPAEPVRAFWHIWDAPIMT 198
Cdd:PRK10576  110 LAR--IApgrgfAFSDGKKPLAVARKSLVELAQRLNLEAAAETHLAQFDDFIASAKPrlAGRGQRPLLLTSLIDPRHALV 187
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2777341883 199 IGGGSYMSELLEIAGAVNVFADAEQ--PSPAVSLEEIAR-RNPDVILAGPNNAR---KLRANPLWQAVPAVRAGR 267
Cdd:PRK10576  188 FGPNSLFQEVLDELGIENAWQGETNfwGSTVVGIERLAAyKDADVICFDHGNSKdmqQLMATPLWQAMPFVRAGR 262
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
35-268 3.48e-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: 53.85  E-value: 3.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  35 TVIDDFGDTSRFARPAQRVV--------SLNPVTTELLFALGVG---DRAVGRT-TWDL----FPEAAKaVPDLGPGMGP 98
Cdd:cd01139     2 TVTDVAGRKVTLDAPVERVLlgegrqlyALALLEGENPFARIVGwggDLKKGDPdTYAKykekFPEIAD-IPLIGSTYNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  99 --NVEAVMGQRPDLVLL----YASESNRAAVQQLRAAGI---------ATLTHRTDKVadlqRVLpviAAALGVDSLGRL 163
Cdd:cd01139    81 dfSVEKVLTLKPDLVILniwaKTTAEESGILEKLEQAGIpvvfvdfrqKPLKNTTPSM----RLL---GKALGREERAEE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 164 VADSVRASVEAVRA------MPRPAEPVRAFWHIWDAPIMTIGGGSyMSELLEIAGAVNVfADAEQPSP--AVSLEEIAR 235
Cdd:cd01139   154 FIEFYQERIDRIRDrlakinEPKPKVFIELGAGGPEECCSTYGNGN-WGELVDAAGGDNI-ADGLIPGTsgELNAEYVIA 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2777341883 236 RNPD-VILAGPNNA----------------------RKLRANPLWQAVPAVRAGRI 268
Cdd:cd01139   232 ANPEiIIATGGNWAkdpsgvslgpdgttadakesllRALLKRPGWSSLQAVKNGRV 287
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
200-272 2.18e-06

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 48.52  E-value: 2.18e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2777341883 200 GGGSYMSELLEIAG-AVNVFADAEQPSPAVSLEEIARRNPDVILAG----PNNARKLRANPLWQAVPAVRAGRILVID 272
Cdd:PRK11411  193 SPESYTGSVLAALGlNVPKAPMNGAAMPSISLEQLLALNPDWLLVAhyrqESIVKRWQQDPLWQMLTAAKKQQVASVD 270
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
98-268 8.84e-03

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 37.26  E-value: 8.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883  98 PNVEAVMGQRPDLVLLYAS--ESNRAAVQQLRAAGIATLTHRTDKvaDLQRVLPVIAAALGVDSLGRLVADSVRASVEAV 175
Cdd:PRK10957  104 PDAEAVAAQMPDLIVISATggDSALALYDQLSAIAPTLVIDYDDK--SWQELATQLGEATGLEKQAAAVIAQFDAQLAEV 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341883 176 RA-MPRPAEPVRAFWHIWDAPIMTIG-GGSYMSELLEIAGavnvFADAEQPsPAVSLEEIARRNPDVILAGPNN------ 247
Cdd:PRK10957  182 KAkITLPPQPVSALVYNGAGHSANLWtPESAQGQLLEQLG----FTLAELP-AGLQASTSQGKRHDIIQLGGENlaagln 256
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2777341883 248 -------------ARKLRANPLWQAVPAVRAGRI 268
Cdd:PRK10957  257 getlflfagddkdADAFLADPLLANLPAVQNKQV 290
 
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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