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Conserved domains on  [gi|2060249233|gb|QXE98548|]
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surface protein p113, partial [Plasmodium falciparum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gal_Rha_Lectin_like-P113_rpt2 cd22848
second galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and ...
 44-139 5.67e-44

second galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar proteins; P113 is an abundant glycosylphosphatidylinositol (GPI)-anchored merozoite surface protein that tethers the RH5:CyRPA:RIPR complex to the merozoite surface. The N-terminal region of P113 contains two closely interacting domains, which resemble the galactose/rhamnose-binding lectin domains found in proteins such as sea urchin egg lectin (SUEL), plant beta-galactosidases, mammalian latrophilins, and catfish rhamnose-binding lectin (SAL) eggs. Due to the lack of rhamnose-binding key residues, the galactose/rhamnose-binding lectin-like domains of P113 do not form a binding pocket for rhamnose. Therefore, P113 is unlikely to act as a rhamnose-binding lectin. This model corresponds to the second galactose/rhamnose binding lectin-like domain of P113.


:

Pssm-ID: 438705  Cd Length: 96  Bit Score: 153.49  E-value: 5.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  44 SFILDEAFIQYFFFIKNKNEEPVICKDGNINIKSALLHSPFCEIKLKDISEYIRKKCDNNKECLIDPLDVQKNLLNEEDP 123
Cdd:cd22848     1 SFILDEAFIQYFFFIKNKNNDPVVCKDGNININSATLHSPFCEIKLKDISSYIRKKCDNNKECLINPLDVQKNLLNEENP 80

                          90
                  ....*....|....*.
gi 2060249233 124 CYINNSYVSVNVVCNK 139
Cdd:cd22848    81 CYINNSYVSVNVVCNK 96
Gal_Rha_Lectin super family cl45893
Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed ...
 1-41 4.85e-14

Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed from a four-stranded antiparallel beta-sheet which packs against an alpha-helix. It was originally described as galactose-binding lectin domain since it was found in a galactose-binding sea urchin egg lectin (SUEL). SUEL was first isolated as a D-galactoside binding lectin, it was later shown that it binds to L-rhamnose preferentially. Galactose/rhamnose-binding lectin domain is also found in many rhamnose-binding lectins, such as Oncorhynchus keta L-rhamnose-binding lectins (CSLs) and Silurus asotus rhamnose-binding lectin (SAL). In addition, the superfamily includes many SUEL/CSLs/SAL homologous proteins, such as plant beta-galactosidases, mammalian latrophilins, Caenorhabditis elegans protein EVA-1 and its homolog, human protein EVA-1 homolog C (also known as C21orf63). Due to the lack of galactose/rhamnose-binding key residues, some superfamily members may not form a binding pocket for galactose/rhamnose. Therefore, they are unlikely to act as galactose/rhamnose-binding lectins.


The actual alignment was detected with superfamily member cd22847:

Pssm-ID: 459238  Cd Length: 98  Bit Score: 68.57  E-value: 4.85e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2060249233   1 YFFEYELRKKTQSFRNKNSIEISECVESEQNEVKTSTTCLL 41
Cdd:cd22847    58 YYFDYIFNKKFYKLRNSSSIYVDECIDSNENEIKNTFTCAL 98
2A1904 super family cl36772
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 642-821 1.01e-06

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


The actual alignment was detected with superfamily member TIGR00927:

Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 52.69  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  642 SESNNENKEKTSDDATHK-ETQEKSDQEPSQNIQEDNSDEKHAENEENVEQIEtdsnVSEEANDENKDNMQTTTDEGTEE 720
Cdd:TIGR00927  653 TEAEGENGEESGGEAEQEgETETKGENESEGEIPAERKGEQEGEGEIEAKEAD----HKGETEAEEVEHEGETEAEGTED 728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  721 lqqndedaESLTKENSKSEEQENEDSTDAEAIDKEEVETEEKGKDEQKKDEQKEQDEEEDGEKENKHKSSETTNETVTDI 800
Cdd:TIGR00927  729 --------EGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGK 800

                          170       180
                   ....*....|....*....|.
gi 2060249233  801 EENKNEVKGEEHLQGSEQSIE 821
Cdd:TIGR00927  801 VEHEGETEAGEKDEHEGQSET 821
 
Name Accession Description Interval E-value
Gal_Rha_Lectin_like-P113_rpt2 cd22848
second galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and ...
 44-139 5.67e-44

second galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar proteins; P113 is an abundant glycosylphosphatidylinositol (GPI)-anchored merozoite surface protein that tethers the RH5:CyRPA:RIPR complex to the merozoite surface. The N-terminal region of P113 contains two closely interacting domains, which resemble the galactose/rhamnose-binding lectin domains found in proteins such as sea urchin egg lectin (SUEL), plant beta-galactosidases, mammalian latrophilins, and catfish rhamnose-binding lectin (SAL) eggs. Due to the lack of rhamnose-binding key residues, the galactose/rhamnose-binding lectin-like domains of P113 do not form a binding pocket for rhamnose. Therefore, P113 is unlikely to act as a rhamnose-binding lectin. This model corresponds to the second galactose/rhamnose binding lectin-like domain of P113.


Pssm-ID: 438705  Cd Length: 96  Bit Score: 153.49  E-value: 5.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  44 SFILDEAFIQYFFFIKNKNEEPVICKDGNINIKSALLHSPFCEIKLKDISEYIRKKCDNNKECLIDPLDVQKNLLNEEDP 123
Cdd:cd22848     1 SFILDEAFIQYFFFIKNKNNDPVVCKDGNININSATLHSPFCEIKLKDISSYIRKKCDNNKECLINPLDVQKNLLNEENP 80

                          90
                  ....*....|....*.
gi 2060249233 124 CYINNSYVSVNVVCNK 139
Cdd:cd22848    81 CYINNSYVSVNVVCNK 96
Gal_Rha_Lectin_like_P113_rpt1 cd22847
first galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and ...
 1-41 4.85e-14

first galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar proteins; P113 is an abundant glycosylphosphatidylinositol (GPI)-anchored merozoite surface protein that tethers the RH5:CyRPA:RIPR complex to the merozoite surface. The N-terminal region of P113 contains two closely interacting domains, which resemble the galactose/rhamnose-binding lectin domains found in proteins such as sea urchin egg lectin (SUEL), plant beta-galactosidases, mammalian latrophilins, and catfish rhamnose-binding lectin (SAL) eggs. Due to the lack of rhamnose-binding key residues, the galactose/rhamnose-binding lectin-like domains of P113 do not form a binding pocket for rhamnose. Therefore, P113 is unlikely to act as a rhamnose-binding lectin. This model corresponds to the first galactose/rhamnose binding lectin-like domain of P113.


Pssm-ID: 438704  Cd Length: 98  Bit Score: 68.57  E-value: 4.85e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2060249233   1 YFFEYELRKKTQSFRNKNSIEISECVESEQNEVKTSTTCLL 41
Cdd:cd22847    58 YYFDYIFNKKFYKLRNSSSIYVDECIDSNENEIKNTFTCAL 98
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 642-821 1.01e-06

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 52.69  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  642 SESNNENKEKTSDDATHK-ETQEKSDQEPSQNIQEDNSDEKHAENEENVEQIEtdsnVSEEANDENKDNMQTTTDEGTEE 720
Cdd:TIGR00927  653 TEAEGENGEESGGEAEQEgETETKGENESEGEIPAERKGEQEGEGEIEAKEAD----HKGETEAEEVEHEGETEAEGTED 728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  721 lqqndedaESLTKENSKSEEQENEDSTDAEAIDKEEVETEEKGKDEQKKDEQKEQDEEEDGEKENKHKSSETTNETVTDI 800
Cdd:TIGR00927  729 --------EGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGK 800

                          170       180
                   ....*....|....*....|.
gi 2060249233  801 EENKNEVKGEEHLQGSEQSIE 821
Cdd:TIGR00927  801 VEHEGETEAGEKDEHEGQSET 821
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 563-812 4.49e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 50.56  E-value: 4.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  563 NALYEKAQSYNLQKLFNDSNdFLKKYAIMGNSfDDGDEVFGSQSSNFNIFDSNNTDQNNEQEQPKQDDQLLNNNNDDVLS 642
Cdd:PTZ00341   871 EGLDEKKLKKRAESLKKLAN-AIEKYAGGGKK-DKKAKKKDAKDLSGNIAHEINLINKELKNQNENVPEHLKEHAEANIE 948

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  643 ESNNENKEKTSDDATHKETQEKSDQEPSQNIQE---DNSDEKHAEN---------EENVEQiETDSNVSEEANDENKDNM 710
Cdd:PTZ00341   949 EDAEENVEEDAEENVEENVEENVEENVEENVEEnveENVEENVEENveenveeniEENVEE-NVEENIEENVEEYDEENV 1027

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  711 QTTTDEGTEELQQNDEDAESLTKENSKSEEQENEDSTDAEAIDKEEVETEEKGKDEQKKDEQKEQDEEEDGEKEN-KHKS 789
Cdd:PTZ00341  1028 EEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEENIEENIEENVEENVEENVEEIEENVEENvEENA 1107

                          250       260
                   ....*....|....*....|...
gi 2060249233  790 SETTNETVTDIEENKNEVKGEEH 812
Cdd:PTZ00341  1108 EENAEENAEENAEEYDDENPEEH 1130
DMP1 pfam07263
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 618-753 9.78e-04

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 42.61  E-value: 9.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233 618 DQNNEQEQPKQDDQLLNNNNDDVLSESNNENKEKTSDDATHKETQEKSDQEPSQNIQEDN-SDEKHAENEENVEQIETDS 696
Cdd:pfam07263 328 DSQNSQDPSSESSQEADLPSQESSSESQEEVVSESRGDNPDNTSSSEEDQEDSDSSEEDSlSTFSSSESESREEQADSES 407

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2060249233 697 NVSEEANDENKDNMQTTTDEGTEELQQNDEDAESLTKENSKSEEQENEDSTDAEAID 753
Cdd:pfam07263 408 NESLRSSEESPESSEDENSSSQEGLQSHSASTESQSEESQSEQDSQSEEDDESDSQD 464
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 593-746 5.64e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 40.28  E-value: 5.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233 593 NSFDDGDEVFGSQSSNFNIFDSNNTDQNNEQEQPKQDDQLLNNNNDDVLSESNNENKEKTSDDATHKETQEKSDQEPSQN 672
Cdd:NF033609  711 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 790

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2060249233 673 IQEDNSDEKHAENEENVEQIETDSNVSEEANDENKDNMQTTTDEGTEELQQNDEDAESLTKENSKSEEQENEDS 746
Cdd:NF033609  791 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDS 864
CobT2 COG4547
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ...
 687-763 6.50e-03

Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 443611 [Multi-domain]  Cd Length: 608  Bit Score: 40.16  E-value: 6.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233 687 ENVEQIETDSNVSEEANDENKDNMQTTTDEGTEELQQNDEDAES----LTKENSKSEEQENEDSTDAEAIDKEEVETEEK 762
Cdd:COG4547   206 DLAEELGEDEDEEDEDDEDDSGEQEEDEEDGEDEDEESDEGAEAedaeASGDDAEEGESEAAEAESDEMAEEAEGEDSEE 285


                  .
gi 2060249233 763 G 763
Cdd:COG4547   286 P 286
 
Name Accession Description Interval E-value
Gal_Rha_Lectin_like-P113_rpt2 cd22848
second galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and ...
 44-139 5.67e-44

second galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar proteins; P113 is an abundant glycosylphosphatidylinositol (GPI)-anchored merozoite surface protein that tethers the RH5:CyRPA:RIPR complex to the merozoite surface. The N-terminal region of P113 contains two closely interacting domains, which resemble the galactose/rhamnose-binding lectin domains found in proteins such as sea urchin egg lectin (SUEL), plant beta-galactosidases, mammalian latrophilins, and catfish rhamnose-binding lectin (SAL) eggs. Due to the lack of rhamnose-binding key residues, the galactose/rhamnose-binding lectin-like domains of P113 do not form a binding pocket for rhamnose. Therefore, P113 is unlikely to act as a rhamnose-binding lectin. This model corresponds to the second galactose/rhamnose binding lectin-like domain of P113.


Pssm-ID: 438705  Cd Length: 96  Bit Score: 153.49  E-value: 5.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  44 SFILDEAFIQYFFFIKNKNEEPVICKDGNINIKSALLHSPFCEIKLKDISEYIRKKCDNNKECLIDPLDVQKNLLNEEDP 123
Cdd:cd22848     1 SFILDEAFIQYFFFIKNKNNDPVVCKDGNININSATLHSPFCEIKLKDISSYIRKKCDNNKECLINPLDVQKNLLNEENP 80

                          90
                  ....*....|....*.
gi 2060249233 124 CYINNSYVSVNVVCNK 139
Cdd:cd22848    81 CYINNSYVSVNVVCNK 96
Gal_Rha_Lectin-like_P113 cd22843
galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar ...
 53-137 1.33e-17

galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar proteins; P113 is an abundant glycosylphosphatidylinositol (GPI)-anchored merozoite surface protein that tethers the RH5:CyRPA:RIPR complex to the merozoite surface. The N-terminal region of P113 contains two closely interacting domains, which resemble the galactose/rhamnose-binding lectin domains found in proteins such as sea urchin egg lectin (SUEL), plant beta-galactosidases, mammalian latrophilins, and catfish rhamnose-binding lectin (SAL) eggs. Due to the lack of rhamnose-binding key residues, the galactose/rhamnose binding lectin-like domains of P113 do not form a binding pocket for rhamnose. Therefore, P113 is unlikely to act as a rhamnose-binding lectin. This model corresponds to galactose/rhamnose binding lectin-like domain of P113.


Pssm-ID: 438700 [Multi-domain]  Cd Length: 89  Bit Score: 78.25  E-value: 1.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  53 QYFFFIKNKNEEPVICK-DGNINIKSALLHSPFCEIKL--------KDISEYIRKKCDNNKECLIDPLDVQknllnEEDP 123
Cdd:cd22843     1 PHTAFVCFGQEVTIHCPgDGNISIKSATYGYNNSNVCIycnsfncdKDITSPVNKKCCGKNTCVLTVSDIL-----EGNP 75

                          90
                  ....*....|....
gi 2060249233 124 CYINNSYVSVNVVC 137
Cdd:cd22843    76 CGIGNSYIRVVYTC 89
Gal_Rha_Lectin_like_P113_rpt1 cd22847
first galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and ...
 1-41 4.85e-14

first galactose/rhamnose binding lectin-like domain found in Plasmodium falciparum P113 and similar proteins; P113 is an abundant glycosylphosphatidylinositol (GPI)-anchored merozoite surface protein that tethers the RH5:CyRPA:RIPR complex to the merozoite surface. The N-terminal region of P113 contains two closely interacting domains, which resemble the galactose/rhamnose-binding lectin domains found in proteins such as sea urchin egg lectin (SUEL), plant beta-galactosidases, mammalian latrophilins, and catfish rhamnose-binding lectin (SAL) eggs. Due to the lack of rhamnose-binding key residues, the galactose/rhamnose-binding lectin-like domains of P113 do not form a binding pocket for rhamnose. Therefore, P113 is unlikely to act as a rhamnose-binding lectin. This model corresponds to the first galactose/rhamnose binding lectin-like domain of P113.


Pssm-ID: 438704  Cd Length: 98  Bit Score: 68.57  E-value: 4.85e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2060249233   1 YFFEYELRKKTQSFRNKNSIEISECVESEQNEVKTSTTCLL 41
Cdd:cd22847    58 YYFDYIFNKKFYKLRNSSSIYVDECIDSNENEIKNTFTCAL 98
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 642-821 1.01e-06

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 52.69  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  642 SESNNENKEKTSDDATHK-ETQEKSDQEPSQNIQEDNSDEKHAENEENVEQIEtdsnVSEEANDENKDNMQTTTDEGTEE 720
Cdd:TIGR00927  653 TEAEGENGEESGGEAEQEgETETKGENESEGEIPAERKGEQEGEGEIEAKEAD----HKGETEAEEVEHEGETEAEGTED 728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  721 lqqndedaESLTKENSKSEEQENEDSTDAEAIDKEEVETEEKGKDEQKKDEQKEQDEEEDGEKENKHKSSETTNETVTDI 800
Cdd:TIGR00927  729 --------EGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDEGAEGK 800

                          170       180
                   ....*....|....*....|.
gi 2060249233  801 EENKNEVKGEEHLQGSEQSIE 821
Cdd:TIGR00927  801 VEHEGETEAGEKDEHEGQSET 821
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 563-812 4.49e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 50.56  E-value: 4.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  563 NALYEKAQSYNLQKLFNDSNdFLKKYAIMGNSfDDGDEVFGSQSSNFNIFDSNNTDQNNEQEQPKQDDQLLNNNNDDVLS 642
Cdd:PTZ00341   871 EGLDEKKLKKRAESLKKLAN-AIEKYAGGGKK-DKKAKKKDAKDLSGNIAHEINLINKELKNQNENVPEHLKEHAEANIE 948

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  643 ESNNENKEKTSDDATHKETQEKSDQEPSQNIQE---DNSDEKHAEN---------EENVEQiETDSNVSEEANDENKDNM 710
Cdd:PTZ00341   949 EDAEENVEEDAEENVEENVEENVEENVEENVEEnveENVEENVEENveenveeniEENVEE-NVEENIEENVEEYDEENV 1027

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  711 QTTTDEGTEELQQNDEDAESLTKENSKSEEQENEDSTDAEAIDKEEVETEEKGKDEQKKDEQKEQDEEEDGEKEN-KHKS 789
Cdd:PTZ00341  1028 EEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEENIEENIEENVEENVEENVEEIEENVEENvEENA 1107

                          250       260
                   ....*....|....*....|...
gi 2060249233  790 SETTNETVTDIEENKNEVKGEEH 812
Cdd:PTZ00341  1108 EENAEENAEENAEEYDDENPEEH 1130
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 621-826 4.85e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 47.09  E-value: 4.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  621 NEQEQPKQDDQLLNNNNDDVLSESNNENKEKTSDDATH--KETQEKSDQEPSQNIQEDNSDEKHAENEENVEQietdsNV 698
Cdd:PTZ00341   901 KDKKAKKKDAKDLSGNIAHEINLINKELKNQNENVPEHlkEHAEANIEEDAEENVEEDAEENVEENVEENVEE-----NV 975

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  699 SEEANDENKDNMQTTTDEGTEElqQNDEDAESLTKENSKSEEQENEDSTDAEAIDKEEVETEEKGKDEQKKDEQKEQDEE 778
Cdd:PTZ00341   976 EENVEENVEENVEENVEENVEE--NVEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENV 1053

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2060249233  779 EDGEKENKHKSSEttnETVTDIEENKNEVKGEEHLQGSEQSIEASESS 826
Cdd:PTZ00341  1054 EENIEENIEEYDE---ENVEEIEENIEENIEENVEENVEENVEEIEEN 1098
PHA00435 PHA00435
capsid assembly protein
 654-763 4.38e-04

capsid assembly protein


Pssm-ID: 222792  Cd Length: 306  Bit Score: 43.29  E-value: 4.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233 654 DDATHKETQEKSDqEPSQNiqednsDEKHAENEENVEQIETDSNVSEEANDENKDNMQTTTDEGTEELQQNDEDAESLTK 733
Cdd:PHA00435   42 DDAIELAEPETSD-DPYGN------PDPFGEDDEGRIEVRISEDGEEEEVEEGEEDEEEEGEEESEEFEPLGDTPEELTE 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2060249233 734 ENSKSEEQEN----------EDSTDAEAIDKEEVETEEKG 763
Cdd:PHA00435  115 ASEQLEEHEEgfqamveqavERGLSAETITRIQAEYEEEG 154
Gal_Rha_Lectin cd22823
Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed ...
 68-137 7.55e-04

Galactose/rhamnose-binding lectin domain; Galactose/rhamnose-binding lectin domain is formed from a four-stranded antiparallel beta-sheet which packs against an alpha-helix. It was originally described as galactose-binding lectin domain since it was found in a galactose-binding sea urchin egg lectin (SUEL). SUEL was first isolated as a D-galactoside binding lectin, it was later shown that it binds to L-rhamnose preferentially. Galactose/rhamnose-binding lectin domain is also found in many rhamnose-binding lectins, such as Oncorhynchus keta L-rhamnose-binding lectins (CSLs) and Silurus asotus rhamnose-binding lectin (SAL). In addition, the superfamily includes many SUEL/CSLs/SAL homologous proteins, such as plant beta-galactosidases, mammalian latrophilins, Caenorhabditis elegans protein EVA-1 and its homolog, human protein EVA-1 homolog C (also known as C21orf63). Due to the lack of galactose/rhamnose-binding key residues, some superfamily members may not form a binding pocket for galactose/rhamnose. Therefore, they are unlikely to act as galactose/rhamnose-binding lectins.


Pssm-ID: 438682 [Multi-domain]  Cd Length: 91  Bit Score: 39.41  E-value: 7.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  68 CKDG-NINIKSAL-------------LHSPFCEIKLKDISEYIRKKCDNNKECLIDPLDVqknllNEEDPCYINNSYVSV 133
Cdd:cd22823    13 CPSGqVIKILSAFygrtdgttcccgpNNTSDTNCCSPDVLDIVKELCDGKQSCSVPASNS-----VFGDPCPGTSKYLEV 87


                  ....
gi 2060249233 134 NVVC 137
Cdd:cd22823    88 TYTC 91
DMP1 pfam07263
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 618-753 9.78e-04

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 42.61  E-value: 9.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233 618 DQNNEQEQPKQDDQLLNNNNDDVLSESNNENKEKTSDDATHKETQEKSDQEPSQNIQEDN-SDEKHAENEENVEQIETDS 696
Cdd:pfam07263 328 DSQNSQDPSSESSQEADLPSQESSSESQEEVVSESRGDNPDNTSSSEEDQEDSDSSEEDSlSTFSSSESESREEQADSES 407

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2060249233 697 NVSEEANDENKDNMQTTTDEGTEELQQNDEDAESLTKENSKSEEQENEDSTDAEAID 753
Cdd:pfam07263 408 NESLRSSEESPESSEDENSSSQEGLQSHSASTESQSEESQSEQDSQSEEDDESDSQD 464
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 593-746 5.64e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 40.28  E-value: 5.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233 593 NSFDDGDEVFGSQSSNFNIFDSNNTDQNNEQEQPKQDDQLLNNNNDDVLSESNNENKEKTSDDATHKETQEKSDQEPSQN 672
Cdd:NF033609  711 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 790

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2060249233 673 IQEDNSDEKHAENEENVEQIETDSNVSEEANDENKDNMQTTTDEGTEELQQNDEDAESLTKENSKSEEQENEDS 746
Cdd:NF033609  791 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDS 864
CobT2 COG4547
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ...
 687-763 6.50e-03

Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 443611 [Multi-domain]  Cd Length: 608  Bit Score: 40.16  E-value: 6.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233 687 ENVEQIETDSNVSEEANDENKDNMQTTTDEGTEELQQNDEDAES----LTKENSKSEEQENEDSTDAEAIDKEEVETEEK 762
Cdd:COG4547   206 DLAEELGEDEDEEDEDDEDDSGEQEEDEEDGEDEDEESDEGAEAedaeASGDDAEEGESEAAEAESDEMAEEAEGEDSEE 285


                  .
gi 2060249233 763 G 763
Cdd:COG4547   286 P 286
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
 546-821 8.03e-03

GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227519 [Multi-domain]  Cd Length: 1077  Bit Score: 39.72  E-value: 8.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  546 KRINEKEKDIDRrmavynaLYEKAQSYNLQKLFNDSNDFLKKYAIMGNSFDDGDEVFGSQSSNFNIFDSNNTDQNNEQEQ 625
Cdd:COG5192    416 KAIAEETSREDE-------LSFDDSDVSTSDENEDVDFTGKKGAINNEDESDNEEVAFDSDSQFDESEGNLRWKEGLASK 488

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  626 PKQDDQLLNNNN------DDVLSESNNENKEKTSDDATHKETQEKSDQEPSQNIQEDNSDEKHAENEENVEQIETD---- 695
Cdd:COG5192    489 LAYSQSGKRGRNiqkifyDESLSPEECIEEYKGESAKSSESDLVVQDEPEDFFDVSKVANESISSNHEKLMESEFEelkk 568

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  696 --SNVSEEANDENKDNMqTTTDEGTEELQQNDEDAESLTKENSKSE-EQENEDST-------DAEAIDKEEVETEEKGKD 765
Cdd:COG5192    569 kwSSLAQLKSRFQKDAT-LDSIEGEEELIQDDEKGNFEDLEDEENSsDNEMEESRgssvtaeNEESADEVDYETEREENA 647

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2060249233  766 EQKKDEQKEQDEEEDGEKENKHKSSETTNETVTDIEENKNEVKGEEHLQGSEQSIE 821
Cdd:COG5192    648 RKKEELRGNFELEERGDPEKKDVDWYTEEKRKIEEQLKINRSEFETMVPESRVVIE 703
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 643-825 8.17e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 39.98  E-value: 8.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  643 ESNNENKEKTSDDATHKETQEKSDQEPSQNIQEDNSD-EKHAENEENVEQIETDSNVSEEANDENKDNMQTTTDEGTEEL 721
Cdd:TIGR00927  712 AEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEaEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEM 791

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233  722 QQNDEDAESLTKENSKSEEQENEDSTDAEAIDKE---EVETEEKGKDEQKKDEQKEQDEEEDGEKENKHKSSETTNETVT 798
Cdd:TIGR00927  792 KGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDtevKDETGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEE 871

                          170       180       190
                   ....*....|....*....|....*....|
gi 2060249233  799 DIEENKNEVKGEEHLQGSEQ---SIEASES 825
Cdd:TIGR00927  872 EEEEEEEEEEEEEEEEEENEeplSLEWPET 901
PRK08581 PRK08581
amidase domain-containing protein;
614-749 8.91e-03

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 39.77  E-value: 8.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2060249233 614 SNNTDQNNEQEQPKQDDQLLNNNNDDVLSESNNENKEKTSDDATHKETQEKSDQE------------PSQNIQEDNSDEK 681
Cdd:PRK08581   33 DSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNTSNQDNNDKKFSTIDSSTSDsnniidfiyknlPQTNINQLLTKNK 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2060249233 682 HAENEENVEQIE----TDSNVSE------EANDENKDNMQTTTDEGTEELQQNDEDAESLT-KENSKSEEQENEDSTDA 749
Cdd:PRK08581  113 YDDNYSLTTLIQnlfnLNSDISDyeqprnSEKSTNDSNKNSDSSIKNDTDTQSSKQDKADNqKAPSSNNTKPSTSNKQP 191
 
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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