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Conserved domains on  [gi|739617621|ref|WP_037474204|]
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MULTISPECIES: cobalamin-binding protein [Shewanella]

Protein Classification

cobalamin-binding protein( domain architecture ID 10100151)

cobalamin-binding protein BtuF is part of the ABC transporter complex BtuCDF involved in the import of vitamin B12; it binds vitamin B12 and delivers it to the periplasmic surface of BtuC

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 1-243 6.99e-97

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: 283.42  E-value: 6.99e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   1 MRIVALSPHAVEMLFAIGAGQQIVATTDYADFPEAAKAIPRIGGYYGIQIERVIELNPDLVVVWDTGNRSEDIEQLTKLG 80
Cdd:cd01144    1 MRIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  81 YRIYGSDPKTLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRENAAKPEIKVFYQLWSEPLMTVAQNsWIQQLLE 160
Cdd:cd01144   81 IPVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQEWIDPLMTAGGD-WVPELIA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621 161 VCHGNNVFKDSSSPYPQVSMENVLLSQPEVIIKTDEKGDGKR---LNWSQWQEIPAVKMEQIYTLNADILHRATPRALEG 237
Cdd:cd01144  160 LAGGVNVFADAGERSPQVSWEDVLAANPDVIVLSPCGFGFTPailRKEPAWQALPAVRNGRVYAVDGNWYFRPSPRLVDG 239


                 ....*.
gi 739617621 238 VEAICK 243
Cdd:cd01144  240 LEQLAA 245
 
Name Accession Description Interval E-value
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 1-243 6.99e-97

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: 283.42  E-value: 6.99e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   1 MRIVALSPHAVEMLFAIGAGQQIVATTDYADFPEAAKAIPRIGGYYGIQIERVIELNPDLVVVWDTGNRSEDIEQLTKLG 80
Cdd:cd01144    1 MRIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  81 YRIYGSDPKTLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRENAAKPEIKVFYQLWSEPLMTVAQNsWIQQLLE 160
Cdd:cd01144   81 IPVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQEWIDPLMTAGGD-WVPELIA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621 161 VCHGNNVFKDSSSPYPQVSMENVLLSQPEVIIKTDEKGDGKR---LNWSQWQEIPAVKMEQIYTLNADILHRATPRALEG 237
Cdd:cd01144  160 LAGGVNVFADAGERSPQVSWEDVLAANPDVIVLSPCGFGFTPailRKEPAWQALPAVRNGRVYAVDGNWYFRPSPRLVDG 239


                 ....*.
gi 739617621 238 VEAICK 243
Cdd:cd01144  240 LEQLAA 245
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 1-245 1.01e-77

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 235.66  E-value: 1.01e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   1 MRIVALSPHAVEMLFAIGAGQQIVATTD--YADFPE-AAKAIPRIGGYYGIQIERVIELNPDLVVVWDTGNRSEDIEQLT 77
Cdd:COG0614    1 MRIVSLSPSATELLLALGAGDRLVGVSDwgYCDYPElELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDEEDYEQLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  78 KLGYRIYGSDPKTLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRENAAKPE-IKVFYQLWS-EPLMTVAQNSWI 155
Cdd:COG0614   81 KIGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEErPTVLYEIWSgDPLYTAGGGSFI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621 156 QQLLEVCHGNNVFKDSSSPYPQVSMENVLLSQPEVIIKTDEKGDGKR--------LNWSQWQEIPAVKMEQIYTLNADIL 227
Cdd:COG0614  161 GELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETaeealealLADPGWQSLPAVKNGRVYVVPGDLL 240

                        250
                 ....*....|....*...
gi 739617621 228 HRATPRALEGVEAICKVL 245
Cdd:COG0614  241 SRPGPRLLLALEDLAKAL 258
PRK03379 PRK03379
vitamin B12-transporter protein BtuF; Provisional
 2-246 5.70e-60

vitamin B12-transporter protein BtuF; Provisional


Pssm-ID: 179575 [Multi-domain]  Cd Length: 260  Bit Score: 190.28  E-value: 5.70e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   2 RIVALSPHAVEMLFAIGAGQqiVATTDYADFPEAAKAIPRIGGYYGIQIERVIELNPDLVVVWDTGNRSEDIEQLTKLGY 81
Cdd:PRK03379  19 RVITLSPANTELAFAAGITP--VGVSSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAWRGGNAERQVDQLASLGI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  82 RIYGSDPKTLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRENAAKPEIKVFYQLWSEPLMTVAQNSWIQQLLEV 161
Cdd:PRK03379  97 KVMWVDATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADKPKKRVFLQFGTNPLFTSGKHSIQSQVLSL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621 162 CHGNNVFKDSSSPYPQVSMENVLLSQPEVIIKTdekGDGKRLNWSQ--WQEIPAVKmeqIYTLNADILHRATPRALEGVE 239
Cdd:PRK03379 177 CGGENIFADSRVPWPQVSREQVLARKPQAIVIT---GGPDQIPKIKqfWGPQLKIP---VIPLNSDWFERASPRIILAAQ 250


                 ....*..
gi 739617621 240 AICKVLD 246
Cdd:PRK03379 251 QLCNALS 257
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 4-225 1.88e-24

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: 97.44  E-value: 1.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621    4 VALSPHAVEMLFAIGAGQQIVATTDYADFPEAAK---AIPRIGGYYGIQIERVIELNPDLVVVwDTGNRSEDIEQLTKLG 80
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADavaAIVKVGAYGEINVERLAALKPDLVIL-STGYLTDEAEELLSLI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   81 YR--IYGSDPkTLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRENA--AKPEIKVFYQLWSEPLMTVAQNSWIQ 156
Cdd:pfam01497  80 IPtvIFESSS-TGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPslTRKPVLVFGGADGGGYVVAGSNTYIG 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739617621  157 QLLEVCHGNNVFKDSS-SPYPQVSMENVLLSQPEVIIKTDEKGDGKR-----LNWSQWQEIPAVKMEQIYTLNAD 225
Cdd:pfam01497 159 DLLRILGIENIAAELSgSEYAPISFEAILSSNPDVIIVSGRDSFTKTgpefvAANPLWAGLPAVKNGRVYTLPSD 233
TroA_like NF038402
helical backbone metal receptor;
2-196 3.79e-10

helical backbone metal receptor;


Pssm-ID: 439691  Cd Length: 219  Bit Score: 58.02  E-value: 3.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   2 RIVALSPHAVEMLfAIGAGQQIVATTDYADFPeAAKAIPRIGGYYGIQIERVIELNPDLVVVWDTGNRSEDIEQLTKLGY 81
Cdd:NF038402   1 RVVSLVPSLTEAI-AATAPELLVGATDWCTHP-ADLDVARVRGTKNPDRAAIAALRPDLVVANQEENRELDVDRLRAAGV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  82 RIYGSDPKTLEgiaEELEQLGRLTGhrqQAGEVAA-DYRQQLATLRRENAAKPEIKVFYQLWSEPLMTVAQNSWIQQLLE 160
Cdd:NF038402  79 PVWVTRIETVD---EALASLRRLFT---EALGVPVpGWLDEAEREWAAPAPAPRRRAVVPIWRDPWMVVGRDTFTGDLLA 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 739617621 161 VCHGNNVFKDSSSPYPQVSMENVLLSQPEVIIKTDE 196
Cdd:NF038402 153 RLGLRNVFADHPERYPHVDLDELDAAGPDLVLLPDE 188
 
Name Accession Description Interval E-value
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 1-243 6.99e-97

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: 283.42  E-value: 6.99e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   1 MRIVALSPHAVEMLFAIGAGQQIVATTDYADFPEAAKAIPRIGGYYGIQIERVIELNPDLVVVWDTGNRSEDIEQLTKLG 80
Cdd:cd01144    1 MRIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  81 YRIYGSDPKTLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRENAAKPEIKVFYQLWSEPLMTVAQNsWIQQLLE 160
Cdd:cd01144   81 IPVLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQEWIDPLMTAGGD-WVPELIA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621 161 VCHGNNVFKDSSSPYPQVSMENVLLSQPEVIIKTDEKGDGKR---LNWSQWQEIPAVKMEQIYTLNADILHRATPRALEG 237
Cdd:cd01144  160 LAGGVNVFADAGERSPQVSWEDVLAANPDVIVLSPCGFGFTPailRKEPAWQALPAVRNGRVYAVDGNWYFRPSPRLVDG 239


                 ....*.
gi 739617621 238 VEAICK 243
Cdd:cd01144  240 LEQLAA 245
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 1-245 1.01e-77

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 235.66  E-value: 1.01e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   1 MRIVALSPHAVEMLFAIGAGQQIVATTD--YADFPE-AAKAIPRIGGYYGIQIERVIELNPDLVVVWDTGNRSEDIEQLT 77
Cdd:COG0614    1 MRIVSLSPSATELLLALGAGDRLVGVSDwgYCDYPElELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDEEDYEQLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  78 KLGYRIYGSDPKTLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRENAAKPE-IKVFYQLWS-EPLMTVAQNSWI 155
Cdd:COG0614   81 KIGIPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEErPTVLYEIWSgDPLYTAGGGSFI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621 156 QQLLEVCHGNNVFKDSSSPYPQVSMENVLLSQPEVIIKTDEKGDGKR--------LNWSQWQEIPAVKMEQIYTLNADIL 227
Cdd:COG0614  161 GELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETaeealealLADPGWQSLPAVKNGRVYVVPGDLL 240

                        250
                 ....*....|....*...
gi 739617621 228 HRATPRALEGVEAICKVL 245
Cdd:COG0614  241 SRPGPRLLLALEDLAKAL 258
PRK03379 PRK03379
vitamin B12-transporter protein BtuF; Provisional
 2-246 5.70e-60

vitamin B12-transporter protein BtuF; Provisional


Pssm-ID: 179575 [Multi-domain]  Cd Length: 260  Bit Score: 190.28  E-value: 5.70e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   2 RIVALSPHAVEMLFAIGAGQqiVATTDYADFPEAAKAIPRIGGYYGIQIERVIELNPDLVVVWDTGNRSEDIEQLTKLGY 81
Cdd:PRK03379  19 RVITLSPANTELAFAAGITP--VGVSSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAWRGGNAERQVDQLASLGI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  82 RIYGSDPKTLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRENAAKPEIKVFYQLWSEPLMTVAQNSWIQQLLEV 161
Cdd:PRK03379  97 KVMWVDATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADKPKKRVFLQFGTNPLFTSGKHSIQSQVLSL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621 162 CHGNNVFKDSSSPYPQVSMENVLLSQPEVIIKTdekGDGKRLNWSQ--WQEIPAVKmeqIYTLNADILHRATPRALEGVE 239
Cdd:PRK03379 177 CGGENIFADSRVPWPQVSREQVLARKPQAIVIT---GGPDQIPKIKqfWGPQLKIP---VIPLNSDWFERASPRIILAAQ 250


                 ....*..
gi 739617621 240 AICKVLD 246
Cdd:PRK03379 251 QLCNALS 257
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 2-192 8.88e-49

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: 159.37  E-value: 8.88e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   2 RIVALSPHAVEMLFAIGAGQQIVATTDYADFPEAAKAIPRIGGYYGIQIERVIELNPDLVVVwDTGNRSEDIEQLTKLGY 81
Cdd:cd01143    5 RIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIV-SSSSLAELLEKLKDAGI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  82 R-IYGSDPKTLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRENAAKPEIKVFYQLWSEPLMTVAQNSWIQQLLE 160
Cdd:cd01143   84 PvVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSKVYIEVSLGGPYTAGKNTFINELIR 163

                        170       180       190
                 ....*....|....*....|....*....|..
gi 739617621 161 VCHGNNVFKDSSSpYPQVSMENVLLSQPEVII 192
Cdd:cd01143  164 LAGAKNIAADSGG-WPQVSPEEILKANPDVII 194
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 2-248 7.82e-40

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 139.17  E-value: 7.82e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   2 RIVALSPHAVEMLFAIGAGQQIVATTDYADFPEAAKAIPRIGGYYGIQIERVIELNPDLVVVWDTGNRSEDIEQLTKLGY 81
Cdd:COG4558   29 RIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVGYMRQLSAEGILSLKPTLVLASEGAGPPEVLDQLRAAGV 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  82 RIYG-SDPKTLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRENAAKPE-IKV-FYQLWSEPLMTVA-QNSWIQQ 157
Cdd:COG4558  109 PVVVvPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVAAIGKpPRVlFLLSRGGGRPMVAgRGTAADA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621 158 LLEVCHGNNVFKDSSSpYPQVSMENVLLSQPEVIIKTDEKGDG----KRLnwsqWQ-----EIPAVKMEQIYTLNADILH 228
Cdd:COG4558  189 LIRLAGGVNAAAGFEG-YKPLSAEALIAAAPDVILVMTRGLESlggvDGL----LAlpglaQTPAGKNKRIVAMDDLLLL 263

                        250       260
                 ....*....|....*....|
gi 739617621 229 RATPRALEGVEAICKVLDKA 248
Cdd:COG4558  264 GFGPRTPQAALALAQALYPA 283
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 2-223 4.77e-27

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: 104.27  E-value: 4.77e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   2 RIVALSPHAVEMLFAIGAGQQIVATTDYADFPEAAKAIPRIGGYYGIQIERVIELNPDLVVVWDTGNRSEDIEQLTKLGY 81
Cdd:cd01149    3 RIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAGPPEALDQLRAAGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  82 R-IYGSDPKTLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRENAA-KPEIKVFYQLWSE--PLMTVAQNSWIQQ 157
Cdd:cd01149   83 PvVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAhKKPPRVLFLLSHGggAAMAAGRNTAADA 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739617621 158 LLEVCHGNNVfKDSSSPYPQVSMENVLLSQPEVIIKTD--EKGDGKRLNWSQ---WQEIPAVKMEQIYTLN 223
Cdd:cd01149  163 IIALAGAVNA-AAGFRGYKPLSAEALIAAQPDVILVMSrgLDAVGGVDGLLKlpgLAQTPAGRNKRILAMD 232
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 1-142 1.63e-26

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: 100.33  E-value: 1.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   1 MRIVALSPHAVEMLFAIGAGQQIVATTDYADFPEAAKA----IPRIGGYYGIQIERVIELNPDLVVVWDTGNrSEDIEQL 76
Cdd:cd00636    1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKAllekVPDVGHGYEPNLEKIAALKPDLIIANGSGL-EAWLDKL 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739617621  77 TKLGYRIYGSDPK---TLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRENAAKPEIKVFYQLW 142
Cdd:cd00636   80 SKIAIPVVVVDEAselSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVVG 148
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 2-222 1.76e-26

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: 103.57  E-value: 1.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   2 RIVALSPHAVEMLFAIGAGQQIVATTD---------YADFPEAAKAIPRIGGYYG---IQIERVIELNPDLVVVWDTGNR 69
Cdd:cd01147    7 RVVAAGPGALRLLYALAAPDKIVGVDDaeksdegrpYFLASPELKDLPVIGRGGRgntPNYEKIAALKPDVVIDVGSDDP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  70 S---EDIEQLTKLGYrIYGSDPKTLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRR--ENAAKPEIKVFYQLWSE 144
Cdd:cd01147   87 TsiaDDLQKKTGIPV-VVLDGGDSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEErtKDIPDEEKPTVYFGRIG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621 145 P-----LMTVAQNSwiQQLLEVCHGNNVFKDSSSPY-PQVSMENVLLSQPEVIIKTD----EKGDGKRLNWSQWQEIPAV 214
Cdd:cd01147  166 TkgaagLESGLAGS--IEVFELAGGINVADGLGGGGlKEVSPEQILLWNPDVIFLDTgsfyLSLEGYAKNRPFWQSLKAV 243


                 ....*...
gi 739617621 215 KMEQIYTL 222
Cdd:cd01147  244 KNGRVYLL 251
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 2-241 1.13e-25

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: 101.65  E-value: 1.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   2 RIVALSPHAVEMLFAIGAGQQIVATT--DYADFPE---AAKAIPRIGGYYgIQIERVIELNPDLVVV-WDTGNRSE---D 72
Cdd:cd01148   20 RVVSNDQNTTEMMLALGLQDRMVGTAgiDNKDLPElkaKYDKVPELAKKY-PSKETVLAARPDLVFGgWSYGFDKGglgT 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  73 IEQLTKLGYRIY------GSDPK--TLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLR-RENAAKPEIKVFYQLWS 143
Cdd:cd01148   99 PDSLAELGIKTYilpescGQRRGeaTLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISaKVKGDGKKVAVFVYDSG 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621 144 EP-LMTVAQNSWIQQLLEVCHGNNVFKDSSSPYPQVSMENVLLSQPEVI--IKTDEKGDGKRL-----NWSQWQEIPAVK 215
Cdd:cd01148  179 EDkPFTSGRGGIPNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIviIDYGDQNAAEQKikflkENPALKNVPAVK 258

                        250       260
                 ....*....|....*....|....*.
gi 739617621 216 MEQIYTLNADILHrATPRALEGVEAI 241
Cdd:cd01148  259 NNRFIVLPLAEAT-PGIRNVDAIEKL 283
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 2-220 1.34e-25

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: 101.66  E-value: 1.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   2 RIVALSPHAVEMLFAIGAGQQIVATTDYA----DFPEAA---KAIPRIGGYYGIQIERVIELNPDLVVVWDTGNRSEDIE 74
Cdd:cd01142   26 RIAALWGAGNAVVAALGGGKLIVATTSTVqqepWLYRLApslENVATGGTGNDVNIEELLALKPDVVIVWSTDGKEAGKA 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  75 QLTKLGYRIYGSDpkTLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRENAAKPE---IKVFYQLwSEPLMTVAQ 151
Cdd:cd01142  106 VLRLLNALSLRDA--ELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAARTKKLPDserPRVYYAG-PDPLTTDGT 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621 152 NSWIQQLLEVCHGNNVFKDSS-SPYPQVSMENVLLSQPEVIIKTDEKGDGKRLNWSQWQEIPAVKMEQIY 220
Cdd:cd01142  183 GSITNSWIDLAGGINVASEATkKGSGEVSLEQLLKWNPDVIIVGNADTKAAILADPRWQNLRAVKNGRVY 252
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 4-225 1.88e-24

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: 97.44  E-value: 1.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621    4 VALSPHAVEMLFAIGAGQQIVATTDYADFPEAAK---AIPRIGGYYGIQIERVIELNPDLVVVwDTGNRSEDIEQLTKLG 80
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADavaAIVKVGAYGEINVERLAALKPDLVIL-STGYLTDEAEELLSLI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   81 YR--IYGSDPkTLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRENA--AKPEIKVFYQLWSEPLMTVAQNSWIQ 156
Cdd:pfam01497  80 IPtvIFESSS-TGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPslTRKPVLVFGGADGGGYVVAGSNTYIG 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739617621  157 QLLEVCHGNNVFKDSS-SPYPQVSMENVLLSQPEVIIKTDEKGDGKR-----LNWSQWQEIPAVKMEQIYTLNAD 225
Cdd:pfam01497 159 DLLRILGIENIAAELSgSEYAPISFEAILSSNPDVIIVSGRDSFTKTgpefvAANPLWAGLPAVKNGRVYTLPSD 233
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
 2-241 1.47e-22

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 94.59  E-value: 1.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   2 RIVALSPHAVEMLFAIGAGQQIVATTDYADFPEAAKAIPRIGGY--YGIQIERVIELNPDLVVVWDTgNRSEDIEQLTKL 79
Cdd:PRK09534  62 RVVTLNPSAAQTMWELGARDRVVGVTQYASYLDGAEERTNVSGGqpFGVNVEAVVGLDPDLVLAPNA-VAGDTVTRLREA 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  80 GYRIYGSDPKT-LEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRENAA---KPeiKVFYQLWSEplMTVAQNSWI 155
Cdd:PRK09534 141 GITVFHFPAATsIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADvddRP--RVLYPLGDG--YTAGGNTFI 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621 156 QQLLEVCHGNNVFKDSS-SPYPQVSMENVLLSQPEVIIKTDEkgDGKRLNWSQWQEIPAVKMEQIYTLNADILHRATPRA 234
Cdd:PRK09534 217 GALIEAAGGHNVAADATtDGYPQLSEEVIVQQDPDVIVVATA--SALVAETEPYASTTAGETGNVVTVNVNHINQPAPRI 294


                 ....*..
gi 739617621 235 LEGVEAI 241
Cdd:PRK09534 295 VESMATM 301
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 2-226 3.86e-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: 91.58  E-value: 3.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   2 RIVALSPHAVEMLFAIGAgqQIVATTDYADF-------PEAAKAIPRIGGYYGIQIERVIELNPDLvVVWDTGNRSEDIE 74
Cdd:cd01146    5 RIVALDWGALETLLALGV--KPVGVADTAGYkpwipepALPLEGVVDVGTRGQPNLEAIAALKPDL-ILGSASRHDEIYD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  75 QLTKLGYRIYGSDPKTLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRENAAKPEIKVFYQLWSEP--LMTVAQN 152
Cdd:cd01146   82 QLSQIAPTVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAgsIRLYGPN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621 153 SWIQQLLEvCHG-NNVFKDSS---SPYPQVSMENVLLSQPEVIIKTDEKGDGKRLNWSQ---WQEIPAVKMEQIYTLNAD 225
Cdd:cd01146  162 SFAGSVLE-DLGlQNPWAQETtndSGFATISLERLAKADADVLFVFTYEDEELAQALQAnplWQNLPAVKNGRVYVVDDV 240


                 .
gi 739617621 226 I 226
Cdd:cd01146  241 W 241
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 30-222 1.49e-20

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: 88.90  E-value: 1.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  30 ADFPEAAKaIPRIGGYY--GIQIERVIELNPDLVVV--W--DTGNRSEDIEQLTKLGYRIYGSD--PKTLEGIAEELEQL 101
Cdd:cd01139   63 EKFPEIAD-IPLIGSTYngDFSVEKVLTLKPDLVILniWakTTAEESGILEKLEQAGIPVVFVDfrQKPLKNTTPSMRLL 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621 102 GRLTGHRQQAGEVAADYRQQLATLRRENAA--KPEIKVFYQL---WSEPLMTVAQNSWIQQLLEVCHGNNVFKD-SSSPY 175
Cdd:cd01139  142 GKALGREERAEEFIEFYQERIDRIRDRLAKinEPKPKVFIELgagGPEECCSTYGNGNWGELVDAAGGDNIADGlIPGTS 221

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739617621 176 PQVSMENVLLSQPEVIIKTDEKGDGKR----------------------LNWSQWQEIPAVKMEQIYTL 222
Cdd:cd01139  222 GELNAEYVIAANPEIIIATGGNWAKDPsgvslgpdgttadakesllralLKRPGWSSLQAVKNGRVYAL 290
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 2-225 2.73e-15

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: 73.14  E-value: 2.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   2 RIVALSpHAVEMLFAIGAgqQIVATTDYADF-PEAAKAIPRIGGYYG--IQIERVIELNPDLVVVWDTgnRSEDIEQLTK 78
Cdd:cd01138   11 RIVALS-GETEGLALLGI--KPVGAASIGGKnPYYKKKTLAKVVGIVdePNLEKVLELKPDLIIVSSK--QEENYEKLSK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  79 LGYRIYGSDpkTLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRE--NAAKPEIKVFY-----QLWSEPLMTVAQ 151
Cdd:cd01138   86 IAPTVPVSY--NSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKikKKLGNDKSVAVlrgrkQIYVFGEDGRGG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621 152 NSWIQQLLEVCHGNNVFKDSSSP-YPQVSMENVllsqPE------VIIKTDEKGDGKRLNWSQ-WQEIPAVKMEQIYTLN 223
Cdd:cd01138  164 GPILYADLGLKAPEKVKEIEDKPgYAAISLEVL----PEfdadyiFLLFFTGPEAKADFESLPiWKNLPAVKNNHVYIVD 239


                 ..
gi 739617621 224 AD 225
Cdd:cd01138  240 AW 241
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 2-146 3.89e-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: 68.60  E-value: 3.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   2 RIVALSPHAVEMLFAIGAGQQIVATTDYADF---PEAAKAIPRIGGY-YGIQIERVIELNPDLVVVWDTGNRSEDIEQLT 77
Cdd:cd01141   10 RIVVLSPTHVDLLLALDKADKIVGVSASAYDlntPAVKERIDIQVGPtGSLNVELIVALKPDLVILYGGFQAQTILDKLE 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739617621  78 KLGYRI-YGSDPKTLEGIAEELEQLGRLTGHRQQA------GEVAADYRQQLATLRRENaaKPE---IKVFYQLWSEPL 146
Cdd:cd01141   90 QLGIPVlYVNEYPSPLGRAEWIKFAAAFYGVGKEDkadeafAQIAGRYRDLAKKVSNLN--KPTvaiGKPVKGLWYMPG 166
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 2-225 3.11e-12

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


Pssm-ID: 238560 [Multi-domain]  Cd Length: 270  Bit Score: 64.59  E-value: 3.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   2 RIVALSPHAVEMLFAIGAGqqIVATTDYADFPEAAKA-----IPRIGGYYGIQIERVIELNPDLVVVwdTGNRSEDIEQL 76
Cdd:cd01140   14 KVVVFDVGALDTLDALGVK--VVGVPKSSTLPEYLKKykddkYANVGTLFEPDLEAIAALKPDLIII--GGRLAEKYDEL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  77 TKLGYRIY-GSDPK-TLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRENAAKPeiKVFYQLWSEP-LMTVAQNS 153
Cdd:cd01140   90 KKIAPTIDlGADLKnYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKK--KALVVLVNGGkLSAFGPGS 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621 154 ---WIQQLLEVchgNNVFKD--SSSPYPQVSMENVLLSQPEVI--------IKTDEKGDGKRLNWSQWQEIPAVKMEQIY 220
Cdd:cd01140  168 rfgWLHDLLGF---EPADENikASSHGQPVSFEYILEANPDWLfvidrgaaIGAEGSSAKEVLDNDLVKNTTAWKNGKVI 244


                 ....*
gi 739617621 221 TLNAD 225
Cdd:cd01140  245 YLDPD 249
TroA_like NF038402
helical backbone metal receptor;
2-196 3.79e-10

helical backbone metal receptor;


Pssm-ID: 439691  Cd Length: 219  Bit Score: 58.02  E-value: 3.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   2 RIVALSPHAVEMLfAIGAGQQIVATTDYADFPeAAKAIPRIGGYYGIQIERVIELNPDLVVVWDTGNRSEDIEQLTKLGY 81
Cdd:NF038402   1 RVVSLVPSLTEAI-AATAPELLVGATDWCTHP-ADLDVARVRGTKNPDRAAIAALRPDLVVANQEENRELDVDRLRAAGV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  82 RIYGSDPKTLEgiaEELEQLGRLTGhrqQAGEVAA-DYRQQLATLRRENAAKPEIKVFYQLWSEPLMTVAQNSWIQQLLE 160
Cdd:NF038402  79 PVWVTRIETVD---EALASLRRLFT---EALGVPVpGWLDEAEREWAAPAPAPRRRAVVPIWRDPWMVVGRDTFTGDLLA 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 739617621 161 VCHGNNVFKDSSSPYPQVSMENVLLSQPEVIIKTDE 196
Cdd:NF038402 153 RLGLRNVFADHPERYPHVDLDELDAAGPDLVLLPDE 188
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 2-230 2.96e-09

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 56.47  E-value: 2.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621   2 RIVALSPHAVEMLFAIGAgqQIVATTDYADFPEAAKAI-PRIGGYYGI------QIERVIELNPDLVVVwdTGNRSEDI- 73
Cdd:COG4594   54 RVVVLEWSFADALLALGV--TPVGIADDNDYDRWVPYLrDLIKGVTSVgtrsqpNLEAIAALKPDLIIA--DKSRHEAIy 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  74 EQLTKLGYRI-YGSDPKTLEGIAEELEQLGRLTGHRQQAGEVAADYRQQLATLRRENAAKPE-----IKVFY--QLWsep 145
Cdd:COG4594  130 DQLSKIAPTVlFKSRNGDYQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKgkkvaVGQFRadGLR--- 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621 146 LMTvaQNSWIQQLLEVCHGNNVFKDS---SSPYPQVSMENVLLSQPEVIIKTDEKGDGKRLNWSQ---WQEIPAVKMEQI 219
Cdd:COG4594  207 LYT--PNSFAGSVLAALGFENPPKQSkdnGYGYSEVSLEQLPALDPDVLFIATYDDPSILKEWKNnplWKNLKAVKNGRV 284

                        250
                 ....*....|.
gi 739617621 220 YTLNADILHRA 230
Cdd:COG4594  285 YEVDGDLWTRG 295
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
 50-126 2.24e-06

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 47.66  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  50 IERVIELNPDLVVVWDTGNRS--EDIEQLTKLGYRI---YGSdpKTLEGIAEeleQLGRLTGHRQQAGEVAADYRQQLAT 124
Cdd:PRK10957 106 AEAVAAQMPDLIVISATGGDSalALYDQLSAIAPTLvidYDD--KSWQELAT---QLGEATGLEKQAAAVIAQFDAQLAE 180


                 ..
gi 739617621 125 LR 126
Cdd:PRK10957 181 VK 182
PRK14048 PRK14048
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
 32-134 4.12e-03

ferrichrome/ferrioxamine B periplasmic transporter; Provisional


Pssm-ID: 172540 [Multi-domain]  Cd Length: 374  Bit Score: 37.96  E-value: 4.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739617621  32 FPEAAKaIPRI--GGYYGIQIERVIELNPDLVVVWDTGNRSED----IEQLTKLGYRIYGSD--PKTLEGIAEELEQLGR 103
Cdd:PRK14048  95 FPELAD-VPLIddGSGPGLSFETILTLKADLAILANWQADTEAgqraIEYLESIGVPVIVVDfnNEALKNTPDNMRLLGK 173

                         90       100       110
                 ....*....|....*....|....*....|.
gi 739617621 104 LTGHRQQAGEVAADYRQQLATLRRENAAKPE 134
Cdd:PRK14048 174 VFEREEQAEDFARFYEERLARIRDRVAKHSE 204
 
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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