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Conserved domains on  [gi|28574694|ref|NP_523473|]
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mitochondrial ribosomal protein S2 [Drosophila melanogaster]

Protein Classification

uS2m family ribosomal protein( domain architecture ID 10105542)

uS2m family ribosomal protein such as yeast mitochondrial 37S ribosomal protein mrp4, and homo sapiens mitochondrial 28S ribosomal protein S2.

Gene Ontology:  GO:0003735|GO:0006412
PubMed:  24524803

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
RPS2 cd01425
Ribosomal protein S2 (RPS2), involved in formation of the translation initiation complex, ...
63-238 1.16e-67

Ribosomal protein S2 (RPS2), involved in formation of the translation initiation complex, where it might contact the messenger RNA and several components of the ribosome. It has been shown that in Escherichia coli RPS2 is essential for the binding of ribosomal protein S1 to the 30s ribosomal subunit. In humans, most likely in all vertebrates, and perhaps in all metazoans, the protein also functions as the 67 kDa laminin receptor (LAMR1 or 67LR), which is formed from a 37 kDa precursor, and is overexpressed in many tumors. 67LR is a cell surface receptor which interacts with a variety of ligands, laminin-1 and others. It is assumed that the ligand interactions are mediated via the conserved C-terminus, which becomes extracellular as the protein undergoes conformational changes which are not well understood. Specifically, a conserved palindromic motif, LMWWML, may participate in the interactions. 67LR plays essential roles in the adhesion of cells to the basement membrane and subsequent signalling events, and has been linked to several diseases. Some evidence also suggests that the precursor of 67LR, 37LRP is also present in the nucleus in animals, where it appears associated with histones.


:

Pssm-ID: 100106  Cd Length: 193  Bit Score: 207.82  E-value: 1.16e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694  63 LFNARVHYGHKEGSLDDRMRPYLFGSRLGHLIFDLDKTASHLRDALNFAAHIAFRDGIILFFNRNAMNSHLVERKAQEAG 142
Cdd:cd01425   1 LLEAGVHLGHKTRRWNPKMKPYIYGERNGIHIIDLEKTLEKLRLALNFIANIAAKGGKILFVGTKPQAQRAVKKFAERTG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694 143 EFSHTRFWRGGIFTNANVQFDAVTR---------------------LPDLCIFLNTQNNvmaqHTAVRDAAKMAIPTIGI 201
Cdd:cd01425  81 SFYVNGRWLGGTLTNWKTIRKSIKRlkklekekleknlggikdmfrLPDLVIVLDPRKE----HQAIREASKLGIPVIAI 156
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 28574694 202 VDSNCNPNLITYPVPGNDDSPAAVELYCNLFKEAILR 238
Cdd:cd01425 157 VDTNCDPDLIDYPIPANDDSIRSIALILWLLARAILE 193
 
Name Accession Description Interval E-value
RPS2 cd01425
Ribosomal protein S2 (RPS2), involved in formation of the translation initiation complex, ...
63-238 1.16e-67

Ribosomal protein S2 (RPS2), involved in formation of the translation initiation complex, where it might contact the messenger RNA and several components of the ribosome. It has been shown that in Escherichia coli RPS2 is essential for the binding of ribosomal protein S1 to the 30s ribosomal subunit. In humans, most likely in all vertebrates, and perhaps in all metazoans, the protein also functions as the 67 kDa laminin receptor (LAMR1 or 67LR), which is formed from a 37 kDa precursor, and is overexpressed in many tumors. 67LR is a cell surface receptor which interacts with a variety of ligands, laminin-1 and others. It is assumed that the ligand interactions are mediated via the conserved C-terminus, which becomes extracellular as the protein undergoes conformational changes which are not well understood. Specifically, a conserved palindromic motif, LMWWML, may participate in the interactions. 67LR plays essential roles in the adhesion of cells to the basement membrane and subsequent signalling events, and has been linked to several diseases. Some evidence also suggests that the precursor of 67LR, 37LRP is also present in the nucleus in animals, where it appears associated with histones.


Pssm-ID: 100106  Cd Length: 193  Bit Score: 207.82  E-value: 1.16e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694  63 LFNARVHYGHKEGSLDDRMRPYLFGSRLGHLIFDLDKTASHLRDALNFAAHIAFRDGIILFFNRNAMNSHLVERKAQEAG 142
Cdd:cd01425   1 LLEAGVHLGHKTRRWNPKMKPYIYGERNGIHIIDLEKTLEKLRLALNFIANIAAKGGKILFVGTKPQAQRAVKKFAERTG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694 143 EFSHTRFWRGGIFTNANVQFDAVTR---------------------LPDLCIFLNTQNNvmaqHTAVRDAAKMAIPTIGI 201
Cdd:cd01425  81 SFYVNGRWLGGTLTNWKTIRKSIKRlkklekekleknlggikdmfrLPDLVIVLDPRKE----HQAIREASKLGIPVIAI 156
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 28574694 202 VDSNCNPNLITYPVPGNDDSPAAVELYCNLFKEAILR 238
Cdd:cd01425 157 VDTNCDPDLIDYPIPANDDSIRSIALILWLLARAILE 193
Ribosomal_S2 pfam00318
Ribosomal protein S2;
66-239 2.97e-43

Ribosomal protein S2;


Pssm-ID: 459759  Cd Length: 216  Bit Score: 146.04  E-value: 2.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694    66 ARVHYGHKEGSLDDRMRPYLFGSRLGHLIFDLDKTASHLRDALNFAAHIAFRDGIILFFN--RNAMNShlVERKAQEAGE 143
Cdd:pfam00318   4 AGVHFGHQTRRWNPKMKPYIFGERNGIHIIDLEKTLPLLRRAYKVVREVAAKGGKILFVGtkKQAQEA--IKEAAKRCGM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694   144 FSHTRFWRGGIFTN------------------ANVQFDAVT-------------------------RLPDLCIFLNTQNN 180
Cdd:pfam00318  82 YYVNERWLGGMLTNfktirksikrlkeleemeEDGTFEDLTkkealtlkrerekleknlggikdmkRLPDLLFVLDPNKE 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 28574694   181 vmaqHTAVRDAAKMAIPTIGIVDSNCNPNLITYPVPGNDDSPAAVELYCNLFKEAILRG 239
Cdd:pfam00318 162 ----KIAVKEARKLGIPVIGIVDTNCDPDLVDYPIPGNDDAIRSIKLILGVLADAIIEG 216
rpsB_bact TIGR01011
ribosomal protein S2, bacterial type; This model describes the bacterial, ribosomal, and ...
59-242 2.97e-43

ribosomal protein S2, bacterial type; This model describes the bacterial, ribosomal, and chloroplast forms of ribosomal protein S2. TIGR01012 describes the archaeal and cytosolic forms. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 130084  Cd Length: 225  Bit Score: 146.31  E-value: 2.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694    59 TVRDLFNARVHYGHKEGSLDDRMRPYLFGSRLGHLIFDLDKTASHLRDALNFAAHIAFRDGIILFFNRNAMNSHLVERKA 138
Cdd:TIGR01011   3 SMKDLLEAGVHFGHQTRRWNPKMKPFIFGERNGIHIIDLQKTLQLLKEAYNFVKDVAANGGKILFVGTKKQAKEIIKEEA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694   139 QEAGEFSHTRFWRGGIFTN------------------ANVQFDAVT-------------------------RLPDLCIFL 175
Cdd:TIGR01011  83 ERCGMFYVNQRWLGGMLTNfktirksikklkklekmeEDGTFDDLTkkealmlsrekeklekslggikdmkKLPDLLFVI 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574694   176 NTQNnvmaQHTAVRDAAKMAIPTIGIVDSNCNPNLITYPVPGNDDSPAAVELYCNLFKEAILRGKRE 242
Cdd:TIGR01011 163 DPVK----EKIAVAEARKLGIPVVAIVDTNCDPDLVDYPIPGNDDAIRSIRLLTNLIADAVLEGKQE 225
RpsB COG0052
Ribosomal protein S2 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S2 ...
58-245 9.08e-43

Ribosomal protein S2 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S2 is part of the Pathway/BioSystem: Ribosome 30S subunit


Pssm-ID: 439822  Cd Length: 253  Bit Score: 146.02  E-value: 9.08e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694  58 FTVRDLFNARVHYGHKEGSLDDRMRPYLFGSRLG-HlIFDLDKTASHLRDALNFAAHIAFRDGIILFF--NRNAmnSHLV 134
Cdd:COG0052   4 VTMKQLLEAGVHFGHQTRRWNPKMKPYIFGERNGiH-IIDLQKTVPLLEEAYNFVRDVAANGGKILFVgtKKQA--QEII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694 135 ERKAQEAGEFSHTRFWRGGIFTN------------------ANVQFDAVT-------------------------RLPDl 171
Cdd:COG0052  81 AEEAERCGMPYVNERWLGGMLTNfktirksikrlkelekmeEDGTFEKLTkkealmlrrerekleknlggikdmkRLPD- 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28574694 172 CIFLNtqnNVMAQHTAVRDAAKMAIPTIGIVDSNCNPNLITYPVPGNDDSPAAVELYCNLFKEAILRGKRERRQ 245
Cdd:COG0052 160 ALFVV---DPKKEHIAVKEARKLGIPVVAIVDTNCDPDGVDYPIPGNDDAIRSIKLITSKIADAILEGKQGRKA 230
rpsB PRK05299
30S ribosomal protein S2; Provisional
58-245 4.17e-40

30S ribosomal protein S2; Provisional


Pssm-ID: 235396  Cd Length: 258  Bit Score: 139.14  E-value: 4.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694   58 FTVRDLFNARVHYGHKEGSLDDRMRPYLFGSRLGHLIFDLDKTASHLRDALNFAAHIAFRDGIILFF--NRNAmnSHLVE 135
Cdd:PRK05299   4 VSMKQLLEAGVHFGHQTRRWNPKMKPYIFGERNGIHIIDLQKTVPMLDEAYNFVRDVAANGGKILFVgtKKQA--QEAIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694  136 RKAQEAGEFSHTRFWRGGIFTN------------------ANVQFDAVT-------------------------RLPDLc 172
Cdd:PRK05299  82 EEAERCGMPYVNHRWLGGMLTNfktirksikrlkelekmeEDGTFEKLTkkealmltreleklekslggikdmgGLPDA- 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574694  173 IFLNTQNNvmaQHTAVRDAAKMAIPTIGIVDSNCNPNLITYPVPGNDDSPAAVELYCNLFKEAILRGKRERRQ 245
Cdd:PRK05299 161 LFVVDPNK---EHIAVKEARKLGIPVVAIVDTNCDPDGVDYPIPGNDDAIRSIKLYTSKIADAILEGRQGRLA 230
 
Name Accession Description Interval E-value
RPS2 cd01425
Ribosomal protein S2 (RPS2), involved in formation of the translation initiation complex, ...
63-238 1.16e-67

Ribosomal protein S2 (RPS2), involved in formation of the translation initiation complex, where it might contact the messenger RNA and several components of the ribosome. It has been shown that in Escherichia coli RPS2 is essential for the binding of ribosomal protein S1 to the 30s ribosomal subunit. In humans, most likely in all vertebrates, and perhaps in all metazoans, the protein also functions as the 67 kDa laminin receptor (LAMR1 or 67LR), which is formed from a 37 kDa precursor, and is overexpressed in many tumors. 67LR is a cell surface receptor which interacts with a variety of ligands, laminin-1 and others. It is assumed that the ligand interactions are mediated via the conserved C-terminus, which becomes extracellular as the protein undergoes conformational changes which are not well understood. Specifically, a conserved palindromic motif, LMWWML, may participate in the interactions. 67LR plays essential roles in the adhesion of cells to the basement membrane and subsequent signalling events, and has been linked to several diseases. Some evidence also suggests that the precursor of 67LR, 37LRP is also present in the nucleus in animals, where it appears associated with histones.


Pssm-ID: 100106  Cd Length: 193  Bit Score: 207.82  E-value: 1.16e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694  63 LFNARVHYGHKEGSLDDRMRPYLFGSRLGHLIFDLDKTASHLRDALNFAAHIAFRDGIILFFNRNAMNSHLVERKAQEAG 142
Cdd:cd01425   1 LLEAGVHLGHKTRRWNPKMKPYIYGERNGIHIIDLEKTLEKLRLALNFIANIAAKGGKILFVGTKPQAQRAVKKFAERTG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694 143 EFSHTRFWRGGIFTNANVQFDAVTR---------------------LPDLCIFLNTQNNvmaqHTAVRDAAKMAIPTIGI 201
Cdd:cd01425  81 SFYVNGRWLGGTLTNWKTIRKSIKRlkklekekleknlggikdmfrLPDLVIVLDPRKE----HQAIREASKLGIPVIAI 156
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 28574694 202 VDSNCNPNLITYPVPGNDDSPAAVELYCNLFKEAILR 238
Cdd:cd01425 157 VDTNCDPDLIDYPIPANDDSIRSIALILWLLARAILE 193
Ribosomal_S2 pfam00318
Ribosomal protein S2;
66-239 2.97e-43

Ribosomal protein S2;


Pssm-ID: 459759  Cd Length: 216  Bit Score: 146.04  E-value: 2.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694    66 ARVHYGHKEGSLDDRMRPYLFGSRLGHLIFDLDKTASHLRDALNFAAHIAFRDGIILFFN--RNAMNShlVERKAQEAGE 143
Cdd:pfam00318   4 AGVHFGHQTRRWNPKMKPYIFGERNGIHIIDLEKTLPLLRRAYKVVREVAAKGGKILFVGtkKQAQEA--IKEAAKRCGM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694   144 FSHTRFWRGGIFTN------------------ANVQFDAVT-------------------------RLPDLCIFLNTQNN 180
Cdd:pfam00318  82 YYVNERWLGGMLTNfktirksikrlkeleemeEDGTFEDLTkkealtlkrerekleknlggikdmkRLPDLLFVLDPNKE 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 28574694   181 vmaqHTAVRDAAKMAIPTIGIVDSNCNPNLITYPVPGNDDSPAAVELYCNLFKEAILRG 239
Cdd:pfam00318 162 ----KIAVKEARKLGIPVIGIVDTNCDPDLVDYPIPGNDDAIRSIKLILGVLADAIIEG 216
rpsB_bact TIGR01011
ribosomal protein S2, bacterial type; This model describes the bacterial, ribosomal, and ...
59-242 2.97e-43

ribosomal protein S2, bacterial type; This model describes the bacterial, ribosomal, and chloroplast forms of ribosomal protein S2. TIGR01012 describes the archaeal and cytosolic forms. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 130084  Cd Length: 225  Bit Score: 146.31  E-value: 2.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694    59 TVRDLFNARVHYGHKEGSLDDRMRPYLFGSRLGHLIFDLDKTASHLRDALNFAAHIAFRDGIILFFNRNAMNSHLVERKA 138
Cdd:TIGR01011   3 SMKDLLEAGVHFGHQTRRWNPKMKPFIFGERNGIHIIDLQKTLQLLKEAYNFVKDVAANGGKILFVGTKKQAKEIIKEEA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694   139 QEAGEFSHTRFWRGGIFTN------------------ANVQFDAVT-------------------------RLPDLCIFL 175
Cdd:TIGR01011  83 ERCGMFYVNQRWLGGMLTNfktirksikklkklekmeEDGTFDDLTkkealmlsrekeklekslggikdmkKLPDLLFVI 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574694   176 NTQNnvmaQHTAVRDAAKMAIPTIGIVDSNCNPNLITYPVPGNDDSPAAVELYCNLFKEAILRGKRE 242
Cdd:TIGR01011 163 DPVK----EKIAVAEARKLGIPVVAIVDTNCDPDLVDYPIPGNDDAIRSIRLLTNLIADAVLEGKQE 225
RpsB COG0052
Ribosomal protein S2 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S2 ...
58-245 9.08e-43

Ribosomal protein S2 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S2 is part of the Pathway/BioSystem: Ribosome 30S subunit


Pssm-ID: 439822  Cd Length: 253  Bit Score: 146.02  E-value: 9.08e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694  58 FTVRDLFNARVHYGHKEGSLDDRMRPYLFGSRLG-HlIFDLDKTASHLRDALNFAAHIAFRDGIILFF--NRNAmnSHLV 134
Cdd:COG0052   4 VTMKQLLEAGVHFGHQTRRWNPKMKPYIFGERNGiH-IIDLQKTVPLLEEAYNFVRDVAANGGKILFVgtKKQA--QEII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694 135 ERKAQEAGEFSHTRFWRGGIFTN------------------ANVQFDAVT-------------------------RLPDl 171
Cdd:COG0052  81 AEEAERCGMPYVNERWLGGMLTNfktirksikrlkelekmeEDGTFEKLTkkealmlrrerekleknlggikdmkRLPD- 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28574694 172 CIFLNtqnNVMAQHTAVRDAAKMAIPTIGIVDSNCNPNLITYPVPGNDDSPAAVELYCNLFKEAILRGKRERRQ 245
Cdd:COG0052 160 ALFVV---DPKKEHIAVKEARKLGIPVVAIVDTNCDPDGVDYPIPGNDDAIRSIKLITSKIADAILEGKQGRKA 230
rpsB PRK05299
30S ribosomal protein S2; Provisional
58-245 4.17e-40

30S ribosomal protein S2; Provisional


Pssm-ID: 235396  Cd Length: 258  Bit Score: 139.14  E-value: 4.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694   58 FTVRDLFNARVHYGHKEGSLDDRMRPYLFGSRLGHLIFDLDKTASHLRDALNFAAHIAFRDGIILFF--NRNAmnSHLVE 135
Cdd:PRK05299   4 VSMKQLLEAGVHFGHQTRRWNPKMKPYIFGERNGIHIIDLQKTVPMLDEAYNFVRDVAANGGKILFVgtKKQA--QEAIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694  136 RKAQEAGEFSHTRFWRGGIFTN------------------ANVQFDAVT-------------------------RLPDLc 172
Cdd:PRK05299  82 EEAERCGMPYVNHRWLGGMLTNfktirksikrlkelekmeEDGTFEKLTkkealmltreleklekslggikdmgGLPDA- 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574694  173 IFLNTQNNvmaQHTAVRDAAKMAIPTIGIVDSNCNPNLITYPVPGNDDSPAAVELYCNLFKEAILRGKRERRQ 245
Cdd:PRK05299 161 LFVVDPNK---EHIAVKEARKLGIPVVAIVDTNCDPDGVDYPIPGNDDAIRSIKLYTSKIADAILEGRQGRLA 230
rps2 CHL00067
ribosomal protein S2
62-240 6.08e-33

ribosomal protein S2


Pssm-ID: 177007  Cd Length: 230  Bit Score: 119.95  E-value: 6.08e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694   62 DLFNARVHYGHKEGSLDDRMRPYLFGSRLGHLIFDLDKTASHLRDALNFAAHIAFRDGIILFFNRNAMNSHLVERKAQEA 141
Cdd:CHL00067  12 EMLEAGVHFGHQTRKWNPKMAPYIYAERNGIHIINLVQTARFLSEACDLVFDAASKGKKFLFVGTKKQAADLVASAAIRA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694  142 GEFSHTRFWRGGIFTN------------------ANVQFD-------AV------------------TRLPDLCIFLNTQ 178
Cdd:CHL00067  92 RCHYVNKRWLGGMLTNwsttktrlqklrdlrmeeKTGLFNrlpkkeaAIlkrqlsrlekylggikymTKLPDIVIIIDQQ 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574694  179 NNVmaqhTAVRDAAKMAIPTIGIVDSNCNPNLITYPVPGNDDSPAAVELYCNLFKEAILRGK 240
Cdd:CHL00067 172 EEY----TALRECRKLGIPTISILDTNCDPDLADIPIPANDDAIASIKLILNKLTTAICEGR 229
rpsB PRK12311
30S ribosomal protein S2;
61-239 5.70e-25

30S ribosomal protein S2;


Pssm-ID: 183428 [Multi-domain]  Cd Length: 326  Bit Score: 101.00  E-value: 5.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694   61 RDLFNARVHYGHKEGSLDDRMRPYLFGSRLGHLIFDLDKTASHLRDALNFAAHIAFRDGIILFFNRNAMNSHLVERKAQE 140
Cdd:PRK12311   2 RQLLEAGVHFGHQSHRWNPKMAPYIFGTRNNIHIIDLAQTVPLLHRALQAVSDTVAKGGRVLFVGTKRQAQDAVADAAKR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574694  141 AGEFSHTRFWRGGIFTNANVQFDAVTRL-------------------------------------------PDLCIFLNT 177
Cdd:PRK12311  82 SAQYFVNSRWLGGTLTNWKTISGSIQRLrkldevlssgeangytkkerltlqrerdkldralggikdmgglPDLLFVIDT 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574694  178 QNnvmaQHTAVRDAAKMAIPTIGIVDSNCNPNLITYPVPGNDDSPAAVELYCNLFKEAILRG 239
Cdd:PRK12311 162 NK----EDIAIQEAQRLGIPVAAIVDTNCDPDGITYPVPGNDDAGRAIALYCDLIARAAIDG 219
 
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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