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Conserved domains on  [gi|488391442|ref|WP_002460827|]
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MULTISPECIES: ABC transporter substrate-binding protein [Staphylococcus]

Protein Classification

TroA family protein( domain architecture ID 513)

TroA family protein; most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TroA-like super family cl00262
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 45-288 5.28e-50

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.


The actual alignment was detected with superfamily member cd01138:

Pssm-ID: 469696 [Multi-domain]  Cd Length: 248  Bit Score: 165.97  E-value: 5.28e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  45 NKVKIPKNPKRIAVLHPTYVGALVKfGHKPIAVPKFVAKNKVLNKAT--KGIKRIDNTSVEQVAKVKPDLIITSKGDK-N 121
Cdd:cd01138    1 GEVEIPAKPKRIVALSGETEGLALL-GIKPVGAASIGGKNPYYKKKTlaKVVGIVDEPNLEKVLELKPDLIIVSSKQEeN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 122 YGKLKKIAPTYVFDANQSSYKDTTKKLAQLVNEQHKANQWLKHWEKQLAKDKKALAPMIkGKTASVLQ-QTPKGIMAFSN 200
Cdd:cd01138   80 YEKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKL-GNDKSVAVlRGRKQIYVFGE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 201 HMGRGTEIIYEGYGLKQPKALKQATQKKVATPINEEQFPEYIGD-IAVIAQQGNK-SPQFEQTQFWKSLNAVKKHRVIKF 278
Cdd:cd01138  159 DGRGGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADyIFLLFFTGPEaKADFESLPIWKNLPAVKNNHVYIV 238

                        250
                 ....*....|
gi 488391442 279 DVSETQYNDP 288
Cdd:cd01138  239 DAWVFYFADG 248
 
Name Accession Description Interval E-value
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 45-288 5.28e-50

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: 165.97  E-value: 5.28e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  45 NKVKIPKNPKRIAVLHPTYVGALVKfGHKPIAVPKFVAKNKVLNKAT--KGIKRIDNTSVEQVAKVKPDLIITSKGDK-N 121
Cdd:cd01138    1 GEVEIPAKPKRIVALSGETEGLALL-GIKPVGAASIGGKNPYYKKKTlaKVVGIVDEPNLEKVLELKPDLIIVSSKQEeN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 122 YGKLKKIAPTYVFDANQSSYKDTTKKLAQLVNEQHKANQWLKHWEKQLAKDKKALAPMIkGKTASVLQ-QTPKGIMAFSN 200
Cdd:cd01138   80 YEKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKL-GNDKSVAVlRGRKQIYVFGE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 201 HMGRGTEIIYEGYGLKQPKALKQATQKKVATPINEEQFPEYIGD-IAVIAQQGNK-SPQFEQTQFWKSLNAVKKHRVIKF 278
Cdd:cd01138  159 DGRGGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADyIFLLFFTGPEaKADFESLPIWKNLPAVKNNHVYIV 238

                        250
                 ....*....|
gi 488391442 279 DVSETQYNDP 288
Cdd:cd01138  239 DAWVFYFADG 248
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 1-279 5.78e-47

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 160.09  E-value: 5.78e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442   1 MKR--FIILTLCTILFLAACNSNDNHERAKdhSNTKAMRTVTMDDGnKVKIPKNPKRIAVLHPTYVGALVKFGHKPIAVP 78
Cdd:COG4594    1 MKKllLLLILLLALLLLAACGSSSSDSSSS--EAAAGARTVKHAMG-ETTIPGTPKRVVVLEWSFADALLALGVTPVGIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  79 KFVAKNKVLNKATKGIKriDNTSV--------EQVAKVKPDLIITSKGD--KNYGKLKKIAPTYVFDANQSSYKDT---T 145
Cdd:COG4594   78 DDNDYDRWVPYLRDLIK--GVTSVgtrsqpnlEAIAALKPDLIIADKSRheAIYDQLSKIAPTVLFKSRNGDYQENlesF 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 146 KKLAQLVNEQHKANQWLKHWEKQLAKDKKALAPMIKGKTASVLQQTPKGIMAFSNHMGRGteIIYEGYGLKQPKALKQaT 225
Cdd:COG4594  156 KTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKGKKVAVGQFRADGLRLYTPNSFAG--SVLAALGFENPPKQSK-D 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488391442 226 QKKVATPINEEQFPEYIGDIAVIAQQGNKSP--QFEQTQFWKSLNAVKKHRVIKFD 279
Cdd:COG4594  233 NGYGYSEVSLEQLPALDPDVLFIATYDDPSIlkEWKNNPLWKNLKAVKNGRVYEVD 288
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 57-276 1.89e-20

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


Pssm-ID: 426291 [Multi-domain]  Cd Length: 233  Bit Score: 87.81  E-value: 1.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442   57 AVLHPTYVGALVKFGHKPIAVPKFV-AKNKVLNKATKGIKRIDNT---SVEQVAKVKPDLIITSKG---DKNYGKLKKIA 129
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGVDAyTRDPLKADAVAAIVKVGAYgeiNVERLAALKPDLVILSTGyltDEAEELLSLII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  130 PT--YVFDANQSSYKDTTKKLAQLVNEQHKANQWLKHWEKQLAKDKKAlAPMIKGKTASVLQQTPKGI-MAFSNhMGRGT 206
Cdd:pfam01497  81 PTviFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKA-VPSLTRKPVLVFGGADGGGyVVAGS-NTYIG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  207 EI--------IYEGYGLKQpkalkqatqkkvATPINEEQFPEYIGDIAVIAQQGNKSP----QFEQTQFWKSLNAVKKHR 274
Cdd:pfam01497 159 DLlrilgienIAAELSGSE------------YAPISFEAILSSNPDVIIVSGRDSFTKtgpeFVAANPLWAGLPAVKNGR 226


                  ..
gi 488391442  275 VI 276
Cdd:pfam01497 227 VY 228
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 1-279 3.45e-19

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 85.88  E-value: 3.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442   1 MKRFIILTLCTILFLAAcnsndnherakdhSNTKAMRTVTmDDGNKVKIPKNPKRIAVLHPTYVGALVKFGHKPIAVPKF 80
Cdd:PRK11411   1 MLAFIRLLFAGLLLLSG-------------SSHAFAVTVQ-DEQGTFTLEKTPQRIVVLELSFVDALAAVGVSPVGVADD 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  81 VAKNKVLNKATKGIKRIDNT------SVEQVAKVKPDLII--TSKGDKNYGKLKKIAPTYVFDANQSSYK---DTTKKLA 149
Cdd:PRK11411  67 NDAKRILPEVRAHLKPWQSVgtrsqpSLEAIAALKPDLIIadSSRHAGVYIALQKIAPTLLLKSRNETYQenlQSAAIIG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 150 QLVNEQ-------HKANQWLKHWEKQLAKDKKALAPMIKGKTASVlqQTPKGimafsnhmgrgteiiYEG-----YGLKQ 217
Cdd:PRK11411 147 EVLGKKremqariEQHKERMAQFASQLPKGTRVAFGTSREQQFNL--HSPES---------------YTGsvlaaLGLNV 209

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488391442 218 PKAlkQATQKKVAtPINEEQF----PEYIgdIAVIAQQGNKSPQFEQTQFWKSLNAVKKHRVIKFD 279
Cdd:PRK11411 210 PKA--PMNGAAMP-SISLEQLlalnPDWL--LVAHYRQESIVKRWQQDPLWQMLTAAKKQQVASVD 270
 
Name Accession Description Interval E-value
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 45-288 5.28e-50

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: 165.97  E-value: 5.28e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  45 NKVKIPKNPKRIAVLHPTYVGALVKfGHKPIAVPKFVAKNKVLNKAT--KGIKRIDNTSVEQVAKVKPDLIITSKGDK-N 121
Cdd:cd01138    1 GEVEIPAKPKRIVALSGETEGLALL-GIKPVGAASIGGKNPYYKKKTlaKVVGIVDEPNLEKVLELKPDLIIVSSKQEeN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 122 YGKLKKIAPTYVFDANQSSYKDTTKKLAQLVNEQHKANQWLKHWEKQLAKDKKALAPMIkGKTASVLQ-QTPKGIMAFSN 200
Cdd:cd01138   80 YEKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKL-GNDKSVAVlRGRKQIYVFGE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 201 HMGRGTEIIYEGYGLKQPKALKQATQKKVATPINEEQFPEYIGD-IAVIAQQGNK-SPQFEQTQFWKSLNAVKKHRVIKF 278
Cdd:cd01138  159 DGRGGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADyIFLLFFTGPEaKADFESLPIWKNLPAVKNNHVYIV 238

                        250
                 ....*....|
gi 488391442 279 DVSETQYNDP 288
Cdd:cd01138  239 DAWVFYFADG 248
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 1-279 5.78e-47

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 160.09  E-value: 5.78e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442   1 MKR--FIILTLCTILFLAACNSNDNHERAKdhSNTKAMRTVTMDDGnKVKIPKNPKRIAVLHPTYVGALVKFGHKPIAVP 78
Cdd:COG4594    1 MKKllLLLILLLALLLLAACGSSSSDSSSS--EAAAGARTVKHAMG-ETTIPGTPKRVVVLEWSFADALLALGVTPVGIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  79 KFVAKNKVLNKATKGIKriDNTSV--------EQVAKVKPDLIITSKGD--KNYGKLKKIAPTYVFDANQSSYKDT---T 145
Cdd:COG4594   78 DDNDYDRWVPYLRDLIK--GVTSVgtrsqpnlEAIAALKPDLIIADKSRheAIYDQLSKIAPTVLFKSRNGDYQENlesF 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 146 KKLAQLVNEQHKANQWLKHWEKQLAKDKKALAPMIKGKTASVLQQTPKGIMAFSNHMGRGteIIYEGYGLKQPKALKQaT 225
Cdd:COG4594  156 KTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKGKKVAVGQFRADGLRLYTPNSFAG--SVLAALGFENPPKQSK-D 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488391442 226 QKKVATPINEEQFPEYIGDIAVIAQQGNKSP--QFEQTQFWKSLNAVKKHRVIKFD 279
Cdd:COG4594  233 NGYGYSEVSLEQLPALDPDVLFIATYDDPSIlkEWKNNPLWKNLKAVKNGRVYEVD 288
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 51-293 4.86e-37

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: 132.79  E-value: 4.86e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  51 KNPKRIAVLHPTYVGALVKFGHKPIAVPKFVAKNKVLNKA---TKGIKRIDNT---SVEQVAKVKPDLIITSK--GDKNY 122
Cdd:cd01146    1 AKPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPalpLEGVVDVGTRgqpNLEAIAALKPDLILGSAsrHDEIY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 123 GKLKKIAPTYVFD--ANQSSYKDTTKKLAQLVNEQHKANQWLKHWEKQLAKDKKALAPmIKGKTASVLQ-QTPKGIMAFS 199
Cdd:cd01146   81 DQLSQIAPTVLLDssPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPD-KGPKPVSVVRfSDAGSIRLYG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 200 NHMGRGTeiIYEGYGLKQPKALKQaTQKKVATPINEEQFPEYIGDIAVIAQQGNKS--PQFEQTQFWKSLNAVKKHRVIK 277
Cdd:cd01146  160 PNSFAGS--VLEDLGLQNPWAQET-TNDSGFATISLERLAKADADVLFVFTYEDEElaQALQANPLWQNLPAVKNGRVYV 236

                        250
                 ....*....|....*.
gi 488391442 278 FDVSETQYNDPISLER 293
Cdd:cd01146  237 VDDVWWFFGGGLSAAR 252
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 1-276 3.27e-23

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


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 96.79  E-value: 3.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442   1 MKRFI--ILTLCTILFLAACNSNDNherAKDHSNTKAMRTVTMDDGnKVKIPKNPKRIAVLHPTYVGALVKFGHKPIAVP 78
Cdd:COG4607    1 MKKTLlaALALAAALALAACGSSSA---AAASAAAAETVTVEHALG-TVEVPKNPKRVVVFDNGALDTLDALGVEVAGVP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  79 KFV--------AKNKVLNKATkgIKRIDntsVEQVAKVKPDLIITS-KGDKNYGKLKKIAPTYVFDANQSSYKDTTKK-- 147
Cdd:COG4607   77 KGLlpdylskyADDKYANVGT--LFEPD---LEAIAALKPDLIIIGgRSAKKYDELSKIAPTIDLTVDGEDYLESLKRnt 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 148 --LAQLVNEQHKANQWLKHWEKQLAKDKKALApmiKGKTASVLQQTPKGIMAFSNhmGRGTEIIYEGYGLKQpkALKQAt 225
Cdd:COG4607  152 etLGEIFGKEDEAEELVADLDAKIAALKAAAA---GKGTALIVLTNGGKISAYGP--GSRFGPIHDVLGFKP--ADEDI- 223

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488391442 226 qkKVAT---PINeeqfPEYIGDI-----------AVIAQQGNKSPQFEQTQFWKSLNAVKKHRVI 276
Cdd:COG4607  224 --EASThgqAIS----FEFIAEAnpdwlfvidrdAAIGGEGPAAKQVLDNELVKQTTAWKNGQIV 282
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 55-302 1.54e-22

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 94.29  E-value: 1.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  55 RIAVLHPTYVGALVKFGHKP----IAVPKFVAKNKVLNKATKGIKRIDNTSVEQVAKVKPDLIITSKG---DKNYGKLKK 127
Cdd:COG0614    2 RIVSLSPSATELLLALGAGDrlvgVSDWGYCDYPELELKDLPVVGGTGEPNLEAILALKPDLVLASSSgndEEDYEQLEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 128 I-APTYVFDA-NQSSYKDTTKKLAQLVNEQHKANQWLKHWEKQLAKDKKALAPMIKGKTASVLQQTPKGIMAFSNHMGRG 205
Cdd:COG0614   82 IgIPVVVLDPrSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAGGGSFIG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 206 TeiIYEGYGLKQPkalkQATQKKVATPINEEQFPEYIGDIAVIAQQGNKSP-------QFEQTQFWKSLNAVKKHRVIKF 278
Cdd:COG0614  162 E--LLELAGGRNV----AADLGGGYPEVSLEQVLALDPDVIILSGGGYDAEtaeealeALLADPGWQSLPAVKNGRVYVV 235

                        250       260
                 ....*....|....*....|....
gi 488391442 279 DVSETQYNDPISLErQRDIFYKAL 302
Cdd:COG0614  236 PGDLLSRPGPRLLL-ALEDLAKAL 258
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 57-276 1.89e-20

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


Pssm-ID: 426291 [Multi-domain]  Cd Length: 233  Bit Score: 87.81  E-value: 1.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442   57 AVLHPTYVGALVKFGHKPIAVPKFV-AKNKVLNKATKGIKRIDNT---SVEQVAKVKPDLIITSKG---DKNYGKLKKIA 129
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGVDAyTRDPLKADAVAAIVKVGAYgeiNVERLAALKPDLVILSTGyltDEAEELLSLII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  130 PT--YVFDANQSSYKDTTKKLAQLVNEQHKANQWLKHWEKQLAKDKKAlAPMIKGKTASVLQQTPKGI-MAFSNhMGRGT 206
Cdd:pfam01497  81 PTviFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKA-VPSLTRKPVLVFGGADGGGyVVAGS-NTYIG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  207 EI--------IYEGYGLKQpkalkqatqkkvATPINEEQFPEYIGDIAVIAQQGNKSP----QFEQTQFWKSLNAVKKHR 274
Cdd:pfam01497 159 DLlrilgienIAAELSGSE------------YAPISFEAILSSNPDVIIVSGRDSFTKtgpeFVAANPLWAGLPAVKNGR 226


                  ..
gi 488391442  275 VI 276
Cdd:pfam01497 227 VY 228
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 1-279 3.45e-19

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 85.88  E-value: 3.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442   1 MKRFIILTLCTILFLAAcnsndnherakdhSNTKAMRTVTmDDGNKVKIPKNPKRIAVLHPTYVGALVKFGHKPIAVPKF 80
Cdd:PRK11411   1 MLAFIRLLFAGLLLLSG-------------SSHAFAVTVQ-DEQGTFTLEKTPQRIVVLELSFVDALAAVGVSPVGVADD 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  81 VAKNKVLNKATKGIKRIDNT------SVEQVAKVKPDLII--TSKGDKNYGKLKKIAPTYVFDANQSSYK---DTTKKLA 149
Cdd:PRK11411  67 NDAKRILPEVRAHLKPWQSVgtrsqpSLEAIAALKPDLIIadSSRHAGVYIALQKIAPTLLLKSRNETYQenlQSAAIIG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 150 QLVNEQ-------HKANQWLKHWEKQLAKDKKALAPMIKGKTASVlqQTPKGimafsnhmgrgteiiYEG-----YGLKQ 217
Cdd:PRK11411 147 EVLGKKremqariEQHKERMAQFASQLPKGTRVAFGTSREQQFNL--HSPES---------------YTGsvlaaLGLNV 209

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488391442 218 PKAlkQATQKKVAtPINEEQF----PEYIgdIAVIAQQGNKSPQFEQTQFWKSLNAVKKHRVIKFD 279
Cdd:PRK11411 210 PKA--PMNGAAMP-SISLEQLlalnPDWL--LVAHYRQESIVKRWQQDPLWQMLTAAKKQQVASVD 270
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 45-279 2.30e-16

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: 77.30  E-value: 2.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  45 NKVKIPKNPKRIAVLHPTYVGALVKFGHKPIAVPKFvaknKVLNKATKGIKRIDNTSV--------EQVAKVKPDLIITS 116
Cdd:cd01140    4 GETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPKS----STLPEYLKKYKDDKYANVgtlfepdlEAIAALKPDLIIIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 117 K-GDKNYGKLKKIAPTYVFDANQSSY----KDTTKKLAQLVNEQHKANQWLKHWEKQLAKDKKALApmiKGKTASVLQQT 191
Cdd:cd01140   80 GrLAEKYDELKKIAPTIDLGADLKNYlesvKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAK---GKKKALVVLVN 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 192 PKGIMAFSNhmGRGTEIIYEGYGLKQpkALKQATQKKVATPINeeqfPEYIGDI-----------AVIAQQGNKSPQFEQ 260
Cdd:cd01140  157 GGKLSAFGP--GSRFGWLHDLLGFEP--ADENIKASSHGQPVS----FEYILEAnpdwlfvidrgAAIGAEGSSAKEVLD 228

                        250
                 ....*....|....*....
gi 488391442 261 TQFWKSLNAVKKHRVIKFD 279
Cdd:cd01140  229 NDLVKNTTAWKNGKVIYLD 247
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 37-276 2.41e-15

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: 74.70  E-value: 2.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  37 RTVTMDDGNKVKIPKNPKRIAVLHPTYVGALVKFGHKP--IAVPKFVAKNKVLNKATKGIKRI------DNTSVEQVAKV 108
Cdd:cd01142    8 RTITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKliVATTSTVQQEPWLYRLAPSLENVatggtgNDVNIEELLAL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 109 KPDLIITSKGDKNYGKLKKIAPTYVF---DANQSSYKDTTKKLAQLVNEQHKANQWLKHWEKQLAKDKKALAPMIKGKTA 185
Cdd:cd01142   88 KPDVVIVWSTDGKEAGKAVLRLLNALslrDAELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAARTKKLPDSERP 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 186 SVLQQTPKGImafsNHMGRGT---EIIYEGYGLkqpKALKQATQKKVATpINEEQFPEYIGDIaVIAQQGNKSPQFEQTQ 262
Cdd:cd01142  168 RVYYAGPDPL----TTDGTGSitnSWIDLAGGI---NVASEATKKGSGE-VSLEQLLKWNPDV-IIVGNADTKAAILADP 238

                        250
                 ....*....|....
gi 488391442 263 FWKSLNAVKKHRVI 276
Cdd:cd01142  239 RWQNLRAVKNGRVY 252
FepB COG4592
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport ...
 3-275 2.48e-15

ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443649 [Multi-domain]  Cd Length: 330  Bit Score: 74.98  E-value: 2.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442   3 RFIILTLCTILFLAACNSNDNHERAKDHSNTK-AMRTVTMDDGnKVKIPKNPKRIAVLHPTYVGALVKFGHKPIA----V 77
Cdd:COG4592    7 AAAAALLAAALLLAGCSSADSTASGTSTAAAGgWPRTVTTEKG-TVTLPAKPQRIVSTSVTLTGSLLAIDAPVVAsgatT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  78 PKFVAKNKVL-----NKATK-GIKRI---DNTSVEQVAKVKPDLII--TSKGD---KNYGKLKKIAPTYVFDANQSSYKD 143
Cdd:COG4592   86 PNNVTDDQGFfrqwaDVAKErGVKRLyigLEPNAEAIAAAAPDLIIgsATGGDsalDLYDQLSAIAPTLVVNYDDKSWQE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 144 TTKKLAQLVNEQHKANQWLKHWEKQLAKDKKALAPMiKGKTASVLQQTPKGIMAFSNhmGRGTEIIYEGYGLK---QPKA 220
Cdd:COG4592  166 LATQLGEATGHEAQADAVIAAFDARVAEVKAAITLP-PQPVSALVYNEDGGANLWTP--ESAQGQLLQALGFTlapLPAE 242

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 221 LKQATQKKVAT---PINEEQFPEYI-GD-IAVIAQQGNKSPQFEQTQFWKSLNAVKKHRV 275
Cdd:COG4592  243 LATSTSQGKRGdivQLSGENLAAALtGPtLFLFAADDKDVDALKADPLLAHLPAVQAGRV 302
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 54-177 4.34e-13

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: 65.66  E-value: 4.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  54 KRIAVLHPTYVGALVKFG--HKPIAVPKFVAKNKVLNKATKGIKRIDNT---SVEQVAKVKPDLIITSK--GDKNYGKLK 126
Cdd:cd00636    1 KRVVALDPGATELLLALGgdDKPVGVADPSGYPPEAKALLEKVPDVGHGyepNLEKIAALKPDLIIANGsgLEAWLDKLS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488391442 127 KIA-PTYVFDANQSS----YKDTTKKLAQLVNEQHKANQWLKHWEKQLAKDKKALA 177
Cdd:cd00636   81 KIAiPVVVVDEASELslenIKESIRLIGKALGKEENAEELIAELDARLAELRAKLA 136
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 51-201 1.28e-11

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: 62.68  E-value: 1.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  51 KNPKRIAVLHPTYVGALVKFG--HKPIAVPKFVAKNKVLNKATKgIKRIDNTSVEQVAKVKPDLIITSKGDK--NYGKLK 126
Cdd:cd01143    1 KEPERIVSLSPSITEILFALGagDKIVGVDTYSNYPKEVRKKPK-VGSYSNPNVEKIVALKPDLVIVSSSSLaeLLEKLK 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488391442 127 KIAPTYVFDANQSSYKDTTK---KLAQLVNEQHKANQwLKHWEKQLAKDKKALAPMIKGKTASVLQQTPkGIMAFSNH 201
Cdd:cd01143   80 DAGIPVVVLPAASSLDEIYDqieLIGKITGAEEEAEK-LVKEMKQKIDKVKDKGKTIKKSKVYIEVSLG-GPYTAGKN 155
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
 3-178 1.06e-08

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 55.36  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442   3 RFIILTLCTILFLAACNSndnherAKDHSNTKAmRTVTMDDGnKVKIPKNPKRIAVLHPTYVGALVKFGHKPIA-----V 77
Cdd:PRK10957   2 LYRLALLLLGLLLSGIAA------AQASAAGWP-RTVTDSRG-SVTLESKPQRIVSTSVTLTGTLLAIDAPVIAsgattP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  78 PKFVAKNKVLNK------ATKGIKRIDNTSV--EQVAKVKPDLIITSK--GD---KNYGKLKKIAPTYVFDANQSSYKDT 144
Cdd:PRK10957  74 NTRVADDQGFFRqwsdvaKERGVEVLYIGEPdaEAVAAQMPDLIVISAtgGDsalALYDQLSAIAPTLVIDYDDKSWQEL 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 488391442 145 TKKLAQLVNEQHKANQWLKHWEKQLAKDKKALAP 178
Cdd:PRK10957 154 ATQLGEATGLEKQAAAVIAQFDAQLAEVKAKITL 187
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 49-176 1.21e-06

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: 48.19  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  49 IPKNPKRIAVLHPTYVGALVKFG--HKPIAVPKFvaKNKVLNKATKGIKRID-----NTSVEQVAKVKPDLIITSKGDKN 121
Cdd:cd01141    4 IKVPPKRIVVLSPTHVDLLLALDkaDKIVGVSAS--AYDLNTPAVKERIDIQvgptgSLNVELIVALKPDLVILYGGFQA 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488391442 122 YG---KLKKIAPTYVFDANQSSYK---DTTKKLAQLVNE--QHKANQWLKHWE---KQLAKDKKAL 176
Cdd:cd01141   82 QTildKLEQLGIPVLYVNEYPSPLgraEWIKFAAAFYGVgkEDKADEAFAQIAgryRDLAKKVSNL 147
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 38-193 2.55e-04

Periplasmic binding protein TroA_f. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238559 [Multi-domain]  Cd Length: 342  Bit Score: 42.29  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  38 TVTMDDGNKVKIPKNPKRI-----------AVLHPTYVGALVKF----GHKPIavPKFVAKNKVLNKATKGIKRIDNT-- 100
Cdd:cd01139    2 TVTDVAGRKVTLDAPVERVllgegrqlyalALLEGENPFARIVGwggdLKKGD--PDTYAKYKEKFPEIADIPLIGSTyn 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 101 ---SVEQVAKVKPDLIITSKGDKNYG-------KLKKIAPTYVF-DANQSSYKDTTKK---LAQLVNEQHKANQWLKHWE 166
Cdd:cd01139   80 gdfSVEKVLTLKPDLVILNIWAKTTAeesgileKLEQAGIPVVFvDFRQKPLKNTTPSmrlLGKALGREERAEEFIEFYQ 159

                        170       180
                 ....*....|....*....|....*..
gi 488391442 167 KQLAKdkkalapmIKGKTASVLQQTPK 193
Cdd:cd01139  160 ERIDR--------IRDRLAKINEPKPK 178
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 49-286 4.78e-04

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: 40.78  E-value: 4.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442  49 IPKNPKRIAVLHP------TYVGALVK------FGHKPIAVPKFVAKNKVLNKATKG-IKRIDNTSVEQVAKVKPDLIIT 115
Cdd:cd01147    1 VPKPVERVVAAGPgalrllYALAAPDKivgvddAEKSDEGRPYFLASPELKDLPVIGrGGRGNTPNYEKIAALKPDVVID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 116 SKGDknygklkkiAPTYVFDANQS---------SYKD-------TTKKLAQLVNEQHKANQ---WLKHWEKQLAKDKKAL 176
Cdd:cd01147   81 VGSD---------DPTSIADDLQKktgipvvvlDGGDsledtpeQIRLLGKVLGKEERAEElisFIESILADVEERTKDI 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 177 APMIKgKT---ASVLQQTPKGIMafsnhmgrGTEIIY----EGYGLKQpkaLKQATQKKVATPINEEQF----PEYI--- 242
Cdd:cd01147  152 PDEEK-PTvyfGRIGTKGAAGLE--------SGLAGSievfELAGGIN---VADGLGGGGLKEVSPEQIllwnPDVIfld 219

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 488391442 243 -GDIAVIAQQGNKSPQFeqtqfWKSLNAVKKHRVikFDVSETQYN 286
Cdd:cd01147  220 tGSFYLSLEGYAKNRPF-----WQSLKAVKNGRV--YLLPALPFN 257
PRK10576 PRK10576
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
103-178 6.64e-04

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


Pssm-ID: 236719  Cd Length: 292  Bit Score: 40.77  E-value: 6.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488391442 103 EQVAKVKPDLIITSKGdknYG----KLKKIAPTYVFDANQSSYKDTTKK-----LAQLVNEQHKANQWLKHWEKQLAKDK 173
Cdd:PRK10576  87 ELLTQMKPSLILWSAG---YGpspeKLARIAPGRGFAFSDGKKPLAVARkslveLAQRLNLEAAAETHLAQFDDFIASAK 163


                 ....*
gi 488391442 174 KALAP 178
Cdd:PRK10576 164 PRLAG 168
 
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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