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Conserved domains on  [gi|312433998|ref|NP_001186078|]
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lactotransferrin isoform 2 [Homo sapiens]

Protein Classification

PBP2_transferrin_N and PBP2_transferrin_C domain-containing protein( domain architecture ID 11995175)

PBP2_transferrin_N and PBP2_transferrin_C domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP2_transferrin_C cd13617
The C-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; ...
317-650 0e+00

The C-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helices and beta sheets domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor.


:

Pssm-ID: 270335  Cd Length: 331  Bit Score: 676.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 317 RARVVWCAVGEQELRKCNQWSGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVYTAGKCGLVPVLAENYKSQQSS 396
Cdd:cd13617    1 RKRVVWCAVGHEEKLKCDQWSVNSGGKVECASASTTEDCIAKILKGEADAMSLDGGYVYTAGKCGLVPVLAENYKSSDSS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 397 DPDpnCVDRPVEGYLAVAVVRRSDTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLFNQTGSCKFDEYFSQSCAPGSDPRS 476
Cdd:cd13617   81 SPD--CVDRPEEGYLAVAVVKKSDSDLTWNNLKGKKSCHTAVGRTAGWNIPMGLIYNQTGSCKFDEFFSQSCAPGSDPNS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 477 NLCALCIGDEQGENKCVPNSNERYYGYTGAFRCLAENaGDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKRK 556
Cdd:cd13617  159 SLCALCIGSGEGLNKCVPNSKEKYYGYTGAFRCLVEK-GDVAFVKHQTVLQNTDGKNPEDWAKDLKEEDFELLCLDGTRK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 557 PVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSETKNLLFNDNTECLARLHGKTTYEK 636
Cdd:cd13617  238 PVTEARSCHLARAPNHAVVSRPDKAACVKQILLHQQALFGRNGSDCSDKFCLFQSETKDLLFNDNTECLAKLHGKTTYEK 317
                        330
                 ....*....|....
gi 312433998 637 YLGPQYVAGITNLK 650
Cdd:cd13617  318 YLGPEYVTAITNLR 331
Transferrin pfam00405
Transferrin;
1-308 0e+00

Transferrin;


:

Pssm-ID: 395328 [Multi-domain]  Cd Length: 328  Bit Score: 625.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998    1 MRKVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKGGSFQ 80
Cdd:pfam00405  21 MRKVGGPSLSCVKKASYLDCIQAIAANEADAVTLDGGLVFEAGLAPYKLKPVAAEVYGTKEEPQTHYYAVAVVKKGSNFQ 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998   81 LNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENKCAFSS 160
Cdd:pfam00405 101 LNQLQGKKSCHTGLGRSAGWNIPIGLLRPYLPWTGPREPLEKAVAKFFSGSCVPGADKTAFPNLCRLCAGDGANKCACSP 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998  161 QEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKED 240
Cdd:pfam00405 181 LEPYFGYSGAFKCLKDGAGDVAFVKHSTVFENLPDKADRDQYELLCRDNTRKPVDEYKDCHLAQVPSHAVVARSVNGKED 260
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312433998  241 AIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRK 308
Cdd:pfam00405 261 LIWELLNQAQEKFGKDKSSDFQLFSSPHGQKDLLFKDSAIGFLRIPSKMDSGLYLGYEYVTAIQNLRE 328
 
Name Accession Description Interval E-value
PBP2_transferrin_C cd13617
The C-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; ...
317-650 0e+00

The C-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helices and beta sheets domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor.


Pssm-ID: 270335  Cd Length: 331  Bit Score: 676.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 317 RARVVWCAVGEQELRKCNQWSGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVYTAGKCGLVPVLAENYKSQQSS 396
Cdd:cd13617    1 RKRVVWCAVGHEEKLKCDQWSVNSGGKVECASASTTEDCIAKILKGEADAMSLDGGYVYTAGKCGLVPVLAENYKSSDSS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 397 DPDpnCVDRPVEGYLAVAVVRRSDTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLFNQTGSCKFDEYFSQSCAPGSDPRS 476
Cdd:cd13617   81 SPD--CVDRPEEGYLAVAVVKKSDSDLTWNNLKGKKSCHTAVGRTAGWNIPMGLIYNQTGSCKFDEFFSQSCAPGSDPNS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 477 NLCALCIGDEQGENKCVPNSNERYYGYTGAFRCLAENaGDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKRK 556
Cdd:cd13617  159 SLCALCIGSGEGLNKCVPNSKEKYYGYTGAFRCLVEK-GDVAFVKHQTVLQNTDGKNPEDWAKDLKEEDFELLCLDGTRK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 557 PVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSETKNLLFNDNTECLARLHGKTTYEK 636
Cdd:cd13617  238 PVTEARSCHLARAPNHAVVSRPDKAACVKQILLHQQALFGRNGSDCSDKFCLFQSETKDLLFNDNTECLAKLHGKTTYEK 317
                        330
                 ....*....|....
gi 312433998 637 YLGPQYVAGITNLK 650
Cdd:cd13617  318 YLGPEYVTAITNLR 331
Transferrin pfam00405
Transferrin;
1-308 0e+00

Transferrin;


Pssm-ID: 395328 [Multi-domain]  Cd Length: 328  Bit Score: 625.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998    1 MRKVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKGGSFQ 80
Cdd:pfam00405  21 MRKVGGPSLSCVKKASYLDCIQAIAANEADAVTLDGGLVFEAGLAPYKLKPVAAEVYGTKEEPQTHYYAVAVVKKGSNFQ 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998   81 LNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENKCAFSS 160
Cdd:pfam00405 101 LNQLQGKKSCHTGLGRSAGWNIPIGLLRPYLPWTGPREPLEKAVAKFFSGSCVPGADKTAFPNLCRLCAGDGANKCACSP 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998  161 QEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKED 240
Cdd:pfam00405 181 LEPYFGYSGAFKCLKDGAGDVAFVKHSTVFENLPDKADRDQYELLCRDNTRKPVDEYKDCHLAQVPSHAVVARSVNGKED 260
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312433998  241 AIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRK 308
Cdd:pfam00405 261 LIWELLNQAQEKFGKDKSSDFQLFSSPHGQKDLLFKDSAIGFLRIPSKMDSGLYLGYEYVTAIQNLRE 328
PBP2_transferrin_N cd13618
The N-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; ...
1-307 0e+00

The N-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helices and beta sheets domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor.


Pssm-ID: 270336  Cd Length: 324  Bit Score: 604.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998   1 MRKVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKGGSFQ 80
Cdd:cd13618   22 MKKVDGPSVSCVKKASYLDCIRAIAANEADAVTLDGGLVYEAGLAPYKLKPVAAEVYGSKEDPQTHYYAVAVVKKGSGFQ 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998  81 LNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRlcaGTGENKCAFSS 160
Cdd:cd13618  102 LNQLQGKKSCHTGLGRSAGWNIPIGTLRPDLPWTEPREPLEKAVARFFSASCVPGADGGQFPQLCR---GKGEPKCACSS 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 161 QEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKED 240
Cdd:cd13618  179 QEPYFGYSGAFKCLKDGAGDVAFVKHSTVFENLPDKADRDQYELLCLDNTRKPVDEYKDCHLARVPSHAVVARSVNGKED 258
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312433998 241 AIWNLLRQAQEKFGKDKSPKFQLFGSPsGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLR 307
Cdd:cd13618  259 LIWELLNQAQEHFGKDKSSEFQLFSSP-HGKDLLFKDSAIGFLRVPPRMDSGLYLGYEYVTAIRNLR 324
TR_FER smart00094
Transferrin;
320-651 5.20e-176

Transferrin;


Pssm-ID: 214514  Cd Length: 332  Bit Score: 503.76  E-value: 5.20e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998   320 VVWCAVGEQELRKCNQWSGLSEG----SVTCSSASTTEDCIALVLKGEADAMSLDGGYVYTAGKCG-LVPVLAENYKSQq 394
Cdd:smart00094   1 VRWCAVSNAEKSKCDQWSVNSRGrdvpALECVSASSTEECIKAIQKGEADAVTLDGGDVYTAGKPYnLVPVFAENYGSE- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998   395 ssdpdpncvDRPVEGYLAVAVVRRSDTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLFNQ----TGSCKFDE----YFSQ 466
Cdd:smart00094  80 ---------EEPETGYYAVAVVKKGSAIFTWNQLRGKKSCHTGVGRTAGWNIPMGLLYNKlvirPPNCPFEKavskFFSA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998   467 SCAPGSDP---RSNLCALCIGDeqgeNKCVPNSNERYYGYTGAFRCLAENAGDVAFVKDVTVLQNTDGNNNEAWAKDLKL 543
Cdd:smart00094 151 SCAPGADKpdpNSNLCALCAGD----NKCACSSHEPYYGYSGAFRCLAEGAGDVAFVKHSTVFENTDGKNGADWAKNLKR 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998   544 ADFALLCLDGKRKPVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGsdcPDKFCLFQSET-KNLLFNDNT 622
Cdd:smart00094 227 DDYELLCLDGTRKPVTEYKNCHLARVPSHAVVARKDKKEDVIWELLNQQQKFGKDK---PSLFQLFGSPTgKDLLFKDSA 303
                          330       340
                   ....*....|....*....|....*....
gi 312433998   623 ECLARLHGKTTYEKYLGPQYVAGITNLKK 651
Cdd:smart00094 304 KCLAKIPPKTDYELYLGEEYVTAIQNLRK 332
TR_FER smart00094
Transferrin;
1-308 3.85e-167

Transferrin;


Pssm-ID: 214514  Cd Length: 332  Bit Score: 481.42  E-value: 3.85e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998     1 MRKVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGlAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKG-GSF 79
Cdd:smart00094  21 SRGRDVPALECVSASSTEECIKAIQKGEADAVTLDGGDVYTAG-KPYNLVPVFAENYGSEEEPETGYYAVAVVKKGsAIF 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998    80 QLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKG-QFPNLCRLCAGTgeNKCAF 158
Cdd:smart00094 100 TWNQLRGKKSCHTGVGRTAGWNIPMGLLYNKLVIRPPNCPFEKAVSKFFSASCAPGADKPdPNSNLCALCAGD--NKCAC 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998   159 SSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEA--------ERDEYELLCPDNTRKPVDKFKDCHLARVPSHAV 230
Cdd:smart00094 178 SSHEPYYGYSGAFRCLAEGAGDVAFVKHSTVFENTDGKNgadwaknlKRDDYELLCLDGTRKPVTEYKNCHLARVPSHAV 257
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312433998   231 VARSVNgKEDAIWNLLRQAQeKFGKDKSPKFQLFGSPsGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRK 308
Cdd:smart00094 258 VARKDK-KEDVIWELLNQQQ-KFGKDKPSLFQLFGSP-TGKDLLFKDSAKCLAKIPPKTDYELYLGEEYVTAIQNLRK 332
Transferrin pfam00405
Transferrin;
320-651 1.35e-96

Transferrin;


Pssm-ID: 395328 [Multi-domain]  Cd Length: 328  Bit Score: 300.15  E-value: 1.35e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998  320 VVWCAVGEQELRKCNQWSGL--SEG--SVTCSSASTTEDCIALVLKGEADAMSLDGGYVYTAGKC--GLVPVLAENYKSQ 393
Cdd:pfam00405   1 VRWCAVSNPEATKCGNWRDNmrKVGgpSLSCVKKASYLDCIQAIAANEADAVTLDGGLVFEAGLApyKLKPVAAEVYGTK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998  394 QSsdpdpncvdrPVEGYLAVAVVRRSdTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLF---NQTGSCKFDE-----YFS 465
Cdd:pfam00405  81 EE----------PQTHYYAVAVVKKG-SNFQLNQLQGKKSCHTGLGRSAGWNIPIGLLRpylPWTGPREPLEkavakFFS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998  466 QSCAPGSDPRS--NLCALCIGDeqGENKCVPNSNERYYGYTGAFRCLAENAGDVAFVKDVTVLQNTDGNNNeawaKDlkl 543
Cdd:pfam00405 150 GSCVPGADKTAfpNLCRLCAGD--GANKCACSPLEPYFGYSGAFKCLKDGAGDVAFVKHSTVFENLPDKAD----RD--- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998  544 aDFALLCLDGKRKPVTEARSCHLAMAPNHAVVSRMD--KVERLKQVLLHQQAKFGRNGSdcpDKFCLFQSE--TKNLLFN 619
Cdd:pfam00405 221 -QYELLCRDNTRKPVDEYKDCHLAQVPSHAVVARSVngKEDLIWELLNQAQEKFGKDKS---SDFQLFSSPhgQKDLLFK 296
                         330       340       350
                  ....*....|....*....|....*....|..
gi 312433998  620 DNTECLARLHGKTTYEKYLGPQYVAGITNLKK 651
Cdd:pfam00405 297 DSAIGFLRIPSKMDSGLYLGYEYVTAIQNLRE 328
 
Name Accession Description Interval E-value
PBP2_transferrin_C cd13617
The C-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; ...
317-650 0e+00

The C-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helices and beta sheets domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor.


Pssm-ID: 270335  Cd Length: 331  Bit Score: 676.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 317 RARVVWCAVGEQELRKCNQWSGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVYTAGKCGLVPVLAENYKSQQSS 396
Cdd:cd13617    1 RKRVVWCAVGHEEKLKCDQWSVNSGGKVECASASTTEDCIAKILKGEADAMSLDGGYVYTAGKCGLVPVLAENYKSSDSS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 397 DPDpnCVDRPVEGYLAVAVVRRSDTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLFNQTGSCKFDEYFSQSCAPGSDPRS 476
Cdd:cd13617   81 SPD--CVDRPEEGYLAVAVVKKSDSDLTWNNLKGKKSCHTAVGRTAGWNIPMGLIYNQTGSCKFDEFFSQSCAPGSDPNS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 477 NLCALCIGDEQGENKCVPNSNERYYGYTGAFRCLAENaGDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKRK 556
Cdd:cd13617  159 SLCALCIGSGEGLNKCVPNSKEKYYGYTGAFRCLVEK-GDVAFVKHQTVLQNTDGKNPEDWAKDLKEEDFELLCLDGTRK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 557 PVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSETKNLLFNDNTECLARLHGKTTYEK 636
Cdd:cd13617  238 PVTEARSCHLARAPNHAVVSRPDKAACVKQILLHQQALFGRNGSDCSDKFCLFQSETKDLLFNDNTECLAKLHGKTTYEK 317
                        330
                 ....*....|....
gi 312433998 637 YLGPQYVAGITNLK 650
Cdd:cd13617  318 YLGPEYVTAITNLR 331
Transferrin pfam00405
Transferrin;
1-308 0e+00

Transferrin;


Pssm-ID: 395328 [Multi-domain]  Cd Length: 328  Bit Score: 625.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998    1 MRKVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKGGSFQ 80
Cdd:pfam00405  21 MRKVGGPSLSCVKKASYLDCIQAIAANEADAVTLDGGLVFEAGLAPYKLKPVAAEVYGTKEEPQTHYYAVAVVKKGSNFQ 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998   81 LNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENKCAFSS 160
Cdd:pfam00405 101 LNQLQGKKSCHTGLGRSAGWNIPIGLLRPYLPWTGPREPLEKAVAKFFSGSCVPGADKTAFPNLCRLCAGDGANKCACSP 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998  161 QEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKED 240
Cdd:pfam00405 181 LEPYFGYSGAFKCLKDGAGDVAFVKHSTVFENLPDKADRDQYELLCRDNTRKPVDEYKDCHLAQVPSHAVVARSVNGKED 260
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312433998  241 AIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRK 308
Cdd:pfam00405 261 LIWELLNQAQEKFGKDKSSDFQLFSSPHGQKDLLFKDSAIGFLRIPSKMDSGLYLGYEYVTAIQNLRE 328
PBP2_transferrin_N cd13618
The N-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; ...
1-307 0e+00

The N-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helices and beta sheets domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor.


Pssm-ID: 270336  Cd Length: 324  Bit Score: 604.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998   1 MRKVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKGGSFQ 80
Cdd:cd13618   22 MKKVDGPSVSCVKKASYLDCIRAIAANEADAVTLDGGLVYEAGLAPYKLKPVAAEVYGSKEDPQTHYYAVAVVKKGSGFQ 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998  81 LNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRlcaGTGENKCAFSS 160
Cdd:cd13618  102 LNQLQGKKSCHTGLGRSAGWNIPIGTLRPDLPWTEPREPLEKAVARFFSASCVPGADGGQFPQLCR---GKGEPKCACSS 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 161 QEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKED 240
Cdd:cd13618  179 QEPYFGYSGAFKCLKDGAGDVAFVKHSTVFENLPDKADRDQYELLCLDNTRKPVDEYKDCHLARVPSHAVVARSVNGKED 258
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312433998 241 AIWNLLRQAQEKFGKDKSPKFQLFGSPsGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLR 307
Cdd:cd13618  259 LIWELLNQAQEHFGKDKSSEFQLFSSP-HGKDLLFKDSAIGFLRVPPRMDSGLYLGYEYVTAIRNLR 324
TR_FER smart00094
Transferrin;
320-651 5.20e-176

Transferrin;


Pssm-ID: 214514  Cd Length: 332  Bit Score: 503.76  E-value: 5.20e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998   320 VVWCAVGEQELRKCNQWSGLSEG----SVTCSSASTTEDCIALVLKGEADAMSLDGGYVYTAGKCG-LVPVLAENYKSQq 394
Cdd:smart00094   1 VRWCAVSNAEKSKCDQWSVNSRGrdvpALECVSASSTEECIKAIQKGEADAVTLDGGDVYTAGKPYnLVPVFAENYGSE- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998   395 ssdpdpncvDRPVEGYLAVAVVRRSDTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLFNQ----TGSCKFDE----YFSQ 466
Cdd:smart00094  80 ---------EEPETGYYAVAVVKKGSAIFTWNQLRGKKSCHTGVGRTAGWNIPMGLLYNKlvirPPNCPFEKavskFFSA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998   467 SCAPGSDP---RSNLCALCIGDeqgeNKCVPNSNERYYGYTGAFRCLAENAGDVAFVKDVTVLQNTDGNNNEAWAKDLKL 543
Cdd:smart00094 151 SCAPGADKpdpNSNLCALCAGD----NKCACSSHEPYYGYSGAFRCLAEGAGDVAFVKHSTVFENTDGKNGADWAKNLKR 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998   544 ADFALLCLDGKRKPVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGsdcPDKFCLFQSET-KNLLFNDNT 622
Cdd:smart00094 227 DDYELLCLDGTRKPVTEYKNCHLARVPSHAVVARKDKKEDVIWELLNQQQKFGKDK---PSLFQLFGSPTgKDLLFKDSA 303
                          330       340
                   ....*....|....*....|....*....
gi 312433998   623 ECLARLHGKTTYEKYLGPQYVAGITNLKK 651
Cdd:smart00094 304 KCLAKIPPKTDYELYLGEEYVTAIQNLRK 332
TR_FER smart00094
Transferrin;
1-308 3.85e-167

Transferrin;


Pssm-ID: 214514  Cd Length: 332  Bit Score: 481.42  E-value: 3.85e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998     1 MRKVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGlAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKG-GSF 79
Cdd:smart00094  21 SRGRDVPALECVSASSTEECIKAIQKGEADAVTLDGGDVYTAG-KPYNLVPVFAENYGSEEEPETGYYAVAVVKKGsAIF 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998    80 QLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKG-QFPNLCRLCAGTgeNKCAF 158
Cdd:smart00094 100 TWNQLRGKKSCHTGVGRTAGWNIPMGLLYNKLVIRPPNCPFEKAVSKFFSASCAPGADKPdPNSNLCALCAGD--NKCAC 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998   159 SSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEA--------ERDEYELLCPDNTRKPVDKFKDCHLARVPSHAV 230
Cdd:smart00094 178 SSHEPYYGYSGAFRCLAEGAGDVAFVKHSTVFENTDGKNgadwaknlKRDDYELLCLDGTRKPVTEYKNCHLARVPSHAV 257
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312433998   231 VARSVNgKEDAIWNLLRQAQeKFGKDKSPKFQLFGSPsGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRK 308
Cdd:smart00094 258 VARKDK-KEDVIWELLNQQQ-KFGKDKPSLFQLFGSP-TGKDLLFKDSAKCLAKIPPKTDYELYLGEEYVTAIQNLRK 332
PBP2_transferrin cd13529
Transferrin family of the type 2 periplasmic-binding protein superfamily; Transferrins are ...
7-307 9.35e-107

Transferrin family of the type 2 periplasmic-binding protein superfamily; Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helical and beta sheet domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor.


Pssm-ID: 270247  Cd Length: 298  Bit Score: 325.51  E-value: 9.35e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998   7 PPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLApYKLRPVAAEVYGTErqPRTHYYAVAVVKKGGSFQ-LNELQ 85
Cdd:cd13529   29 PSLECVKATSREECMKAIKNGTADFVTLDGGDVYTAGKD-YNLKPIAAELYGDE--GEASYYAVAVVKKSSNITsLKDLR 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998  86 GLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPgadkgqfpnlcrlcagtgenkcafssqepyf 165
Cdd:cd13529  106 GKKSCHTGYGRTAGWNVPIGYLLENGLISPVTCNYIKAVSSFFSSSCVP------------------------------- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 166 sysGAFKCLRDGAGDVAFIRESTVFE----DLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNG--KE 239
Cdd:cd13529  155 ---GALRCLLEGAGDVAFVKHTTVKDntggSWADNINPDDYELLCPDGTRAPVSEYKSCNLGKVPSHAVVTRSDTSqsDR 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312433998 240 DAIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSgLYLGSGYFTAIQNLR 307
Cdd:cd13529  232 NEVQKLLLAAQELFGNKPRSFFMFYGSFNGGKNLLFSDSTKGLVGVPDQKTS-EYLGMEYFSAIRSSR 298
Transferrin pfam00405
Transferrin;
320-651 1.35e-96

Transferrin;


Pssm-ID: 395328 [Multi-domain]  Cd Length: 328  Bit Score: 300.15  E-value: 1.35e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998  320 VVWCAVGEQELRKCNQWSGL--SEG--SVTCSSASTTEDCIALVLKGEADAMSLDGGYVYTAGKC--GLVPVLAENYKSQ 393
Cdd:pfam00405   1 VRWCAVSNPEATKCGNWRDNmrKVGgpSLSCVKKASYLDCIQAIAANEADAVTLDGGLVFEAGLApyKLKPVAAEVYGTK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998  394 QSsdpdpncvdrPVEGYLAVAVVRRSdTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLF---NQTGSCKFDE-----YFS 465
Cdd:pfam00405  81 EE----------PQTHYYAVAVVKKG-SNFQLNQLQGKKSCHTGLGRSAGWNIPIGLLRpylPWTGPREPLEkavakFFS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998  466 QSCAPGSDPRS--NLCALCIGDeqGENKCVPNSNERYYGYTGAFRCLAENAGDVAFVKDVTVLQNTDGNNNeawaKDlkl 543
Cdd:pfam00405 150 GSCVPGADKTAfpNLCRLCAGD--GANKCACSPLEPYFGYSGAFKCLKDGAGDVAFVKHSTVFENLPDKAD----RD--- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998  544 aDFALLCLDGKRKPVTEARSCHLAMAPNHAVVSRMD--KVERLKQVLLHQQAKFGRNGSdcpDKFCLFQSE--TKNLLFN 619
Cdd:pfam00405 221 -QYELLCRDNTRKPVDEYKDCHLAQVPSHAVVARSVngKEDLIWELLNQAQEKFGKDKS---SDFQLFSSPhgQKDLLFK 296
                         330       340       350
                  ....*....|....*....|....*....|..
gi 312433998  620 DNTECLARLHGKTTYEKYLGPQYVAGITNLKK 651
Cdd:pfam00405 297 DSAIGFLRIPSKMDSGLYLGYEYVTAIQNLRE 328
PBP2_transferrin_N cd13618
The N-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; ...
320-650 1.03e-87

The N-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helices and beta sheets domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor.


Pssm-ID: 270336  Cd Length: 324  Bit Score: 277.00  E-value: 1.03e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 320 VVWCAVGEQELRKCNQW----SGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVYTAGKC--GLVPVLAENYKSQ 393
Cdd:cd13618    2 VRWCAVSEPEATKCQSFrdnmKKVDGPSVSCVKKASYLDCIRAIAANEADAVTLDGGLVYEAGLApyKLKPVAAEVYGSK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 394 QSSDPDpncvdrpvegYLAVAVVRRSdTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLF---NQTGSCKFDE-----YFS 465
Cdd:cd13618   82 EDPQTH----------YYAVAVVKKG-SGFQLNQLQGKKSCHTGLGRSAGWNIPIGTLRpdlPWTEPREPLEkavarFFS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 466 QSCAPGSDPRSNLCaLCIGdeQGENKCVPNSNERYYGYTGAFRCLAENAGDVAFVKDVTVlqntdgnnNEAWAKDLKLAD 545
Cdd:cd13618  151 ASCVPGADGGQFPQ-LCRG--KGEPKCACSSQEPYFGYSGAFKCLKDGAGDVAFVKHSTV--------FENLPDKADRDQ 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 546 FALLCLDGKRKPVTEARSCHLAMAPNHAVVSR-MDKVERLKQVLLHQ-QAKFGRNGSdcpDKFCLFQSE-TKNLLFNDNT 622
Cdd:cd13618  220 YELLCLDNTRKPVDEYKDCHLARVPSHAVVARsVNGKEDLIWELLNQaQEHFGKDKS---SEFQLFSSPhGKDLLFKDSA 296
                        330       340
                 ....*....|....*....|....*...
gi 312433998 623 ECLARLHGKTTYEKYLGPQYVAGITNLK 650
Cdd:cd13618  297 IGFLRVPPRMDSGLYLGYEYVTAIRNLR 324
PBP2_transferrin_C cd13617
The C-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; ...
4-307 1.03e-87

The C-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helices and beta sheets domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor.


Pssm-ID: 270335  Cd Length: 331  Bit Score: 277.36  E-value: 1.03e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998   4 VRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLApyKLRPVAAEVYGTERQ--------PRTHYYAVAVVKK 75
Cdd:cd13617   23 NSGGKVECASASTTEDCIAKILKGEADAMSLDGGYVYTAGKC--GLVPVLAENYKSSDSsspdcvdrPEEGYLAVAVVKK 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998  76 G-GSFQLNELQGLKSCHTGLRRTAGWNVPIGTLrpfLNWTGppepiEAAVARFFSASCVPGADKGQfpNLCRLCAGTGEN 154
Cdd:cd13617  101 SdSDLTWNNLKGKKSCHTAVGRTAGWNIPMGLI---YNQTG-----SCKFDEFFSQSCAPGSDPNS--SLCALCIGSGEG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 155 --KCAFSSQEPYFSYSGAFKCLRDgAGDVAFIRESTVFEDLSDEA--------ERDEYELLCPDNTRKPVDKFKDCHLAR 224
Cdd:cd13617  171 lnKCVPNSKEKYYGYTGAFRCLVE-KGDVAFVKHQTVLQNTDGKNpedwakdlKEEDFELLCLDGTRKPVTEARSCHLAR 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 225 VPSHAVVARSvnGKEDAIWNLLRQAQEKFGK---DKSPKFQLFgsPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFT 301
Cdd:cd13617  250 APNHAVVSRP--DKAACVKQILLHQQALFGRngsDCSDKFCLF--QSETKDLLFNDNTECLAKLHGKTTYEKYLGPEYVT 325

                 ....*.
gi 312433998 302 AIQNLR 307
Cdd:cd13617  326 AITNLR 331
PBP2_transferrin cd13529
Transferrin family of the type 2 periplasmic-binding protein superfamily; Transferrins are ...
319-650 5.07e-85

Transferrin family of the type 2 periplasmic-binding protein superfamily; Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helical and beta sheet domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor.


Pssm-ID: 270247  Cd Length: 298  Bit Score: 268.89  E-value: 5.07e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 319 RVVWCAVGEQELRKCNQWSG-----LSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVYTAGKC-GLVPVLAENYKs 392
Cdd:cd13529    1 TVRWCVVSEAELKKCEALQKaaysrGIRPSLECVKATSREECMKAIKNGTADFVTLDGGDVYTAGKDyNLKPIAAELYG- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 393 qqssdpdpncvDRPVEGYLAVAVVRRSDTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLFNQ----TGSCK----FDEYF 464
Cdd:cd13529   80 -----------DEGEASYYAVAVVKKSSNITSLKDLRGKKSCHTGYGRTAGWNVPIGYLLENglisPVTCNyikaVSSFF 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 465 SQSCAPGsdprsnlcalcigdeqgenkcvpnsneryygytgAFRCLAENAGDVAFVKDVTVLQNTDGNnneaWAKDLKLA 544
Cdd:cd13529  149 SSSCVPG----------------------------------ALRCLLEGAGDVAFVKHTTVKDNTGGS----WADNINPD 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 545 DFALLCLDGKRKPVTEARSCHLAMAPNHAVVSRMD----KVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSEtKNLLFND 620
Cdd:cd13529  191 DYELLCPDGTRAPVSEYKSCNLGKVPSHAVVTRSDtsqsDRNEVQKLLLAAQELFGNKPRSFFMFYGSFNGG-KNLLFSD 269
                        330       340       350
                 ....*....|....*....|....*....|
gi 312433998 621 NTECLARLhGKTTYEKYLGPQYVAGITNLK 650
Cdd:cd13529  270 STKGLVGV-PDQKTSEYLGMEYFSAIRSSR 298
PBP2_PhnD_like cd01071
Substrate binding domain of phosphonate uptake system-like, a member of the type 2 ...
356-456 6.64e-03

Substrate binding domain of phosphonate uptake system-like, a member of the type 2 periplasmic-binding fold superfamily; This family includes alkylphosphonate binding domain PhnD. These domains are found in PhnD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. PhnD is the periplasmic binding component of an ABC-type phosphonate uptake system (PhnCDE) that recognizes and binds phosphonate. PhnD belongs to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. The PBP2 have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270232 [Multi-domain]  Cd Length: 253  Bit Score: 38.78  E-value: 6.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433998 356 IALVLKGEADAMSLD-GGYVYTAGKCGLVPVLAENYKSQqssdpdpncvdrpvEGYLAVAVVRRSDTSLTWNSVKGKKSC 434
Cdd:cd01071   50 VEAMRNGKVDIAWLGpASYVLAHDRAGAEALATEVRDGS--------------PGYYSVIIVRKDSPIKSLEDLKGKTVA 115
                         90       100
                 ....*....|....*....|..
gi 312433998 435 HTAVDRTAGWNIPMGLLFNQTG 456
Cdd:cd01071  116 FVDPSSTSGYLFPRAMLKDAGI 137
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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