NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958656189|ref|XP_038941011|]
View 

phosphoribosyl pyrophosphate synthase-associated protein 2 isoform X6 [Rattus norvegicus]

Protein Classification

ribose-phosphate diphosphokinase( domain architecture ID 11421473)

ribose-phosphate diphosphokinase catalyzes the transfer of the pyrophosphoryl group from ATP to the 1-hydroxyl of ribose-5-phosphate to form the the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP)

CATH:  3.40.50.2020
EC:  2.7.6.1
Gene Ontology:  GO:0002189|GO:0000287|GO:0004749|GO:0005524|GO:0009156|GO:0016301|GO:0016310|GO:0006015|GO:0009165
PubMed:  11751055|7593598

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 20-224 9.54e-73

Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis


:

Pssm-ID: 440230 [Multi-domain]  Cd Length: 311  Bit Score: 224.17  E-value: 9.54e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  20 LVLFSANSNsscMELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYACKTS 99
Cdd:COG0462     4 LKIFSGNAN---PELAEEIAEYLGVPLGKAEVRRFSDGEIYVRIEESVRGRDVFVIQSTSPPVNDNLMELLIMIDALKRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189 100 CAKSIIGVIPYFPYSKQ-CKMRKRGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQEEip 178
Cdd:COG0462    81 SARRITAVIPYYGYARQdRKFRPREPITAKLVADLLEAAGADRVLTVDLHAPQIQGFFDIPVDHLYAAPLLADYIKSK-- 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958656189 179 DYRNAVIVakSP--ASAKRAQSFAERLRLGIAVIHGE---AQDAESDLVDG 224
Cdd:COG0462   159 DLEDLVVV--SPdvGGVKRARAFAKRLGAPLAIIDKRrpgANEVEVMNIIG 207
 
Name Accession Description Interval E-value
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 20-224 9.54e-73

Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis


Pssm-ID: 440230 [Multi-domain]  Cd Length: 311  Bit Score: 224.17  E-value: 9.54e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  20 LVLFSANSNsscMELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYACKTS 99
Cdd:COG0462     4 LKIFSGNAN---PELAEEIAEYLGVPLGKAEVRRFSDGEIYVRIEESVRGRDVFVIQSTSPPVNDNLMELLIMIDALKRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189 100 CAKSIIGVIPYFPYSKQ-CKMRKRGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQEEip 178
Cdd:COG0462    81 SARRITAVIPYYGYARQdRKFRPREPITAKLVADLLEAAGADRVLTVDLHAPQIQGFFDIPVDHLYAAPLLADYIKSK-- 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958656189 179 DYRNAVIVakSP--ASAKRAQSFAERLRLGIAVIHGE---AQDAESDLVDG 224
Cdd:COG0462   159 DLEDLVVV--SPdvGGVKRARAFAKRLGAPLAIIDKRrpgANEVEVMNIIG 207
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
20-210 2.62e-65

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 204.97  E-value: 2.62e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  20 LVLFSANSNsscMELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYACKTS 99
Cdd:PRK01259    1 MKLFAGNAN---PELAEKIAKYLGIPLGKASVGRFSDGEISVEINENVRGKDVFIIQSTCAPTNDNLMELLIMIDALKRA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189 100 CAKSIIGVIPYFPYSKQ-CKMRKRGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQEEip 178
Cdd:PRK01259   78 SAGRITAVIPYFGYARQdRKARSRVPITAKLVANLLETAGADRVLTMDLHADQIQGFFDIPVDNLYGSPILLEDIKQK-- 155

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1958656189 179 DYRNAVIVakSP--ASAKRAQSFAERLRLGIAVI 210
Cdd:PRK01259  156 NLENLVVV--SPdvGGVVRARALAKRLDADLAII 187
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 20-220 5.94e-61

ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In some systems, close homologs lacking enzymatic activity exist and perform regulatory functions. The model is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273523 [Multi-domain]  Cd Length: 308  Bit Score: 194.03  E-value: 5.94e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  20 LVLFSANSNSscmELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFII-QTVSKDVNTTIMELLIMVYACKT 98
Cdd:TIGR01251   1 MKIFSGSSNQ---ELAQKVAKNLGLPLGDVEVKRFPDGELYVRINESVRGKDVFIIqQSTSAPVNDNLMELLIMIDALKR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  99 SCAKSIIGVIPYFPYSKQCKMRKRG-SIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQEEI 177
Cdd:TIGR01251  78 ASAKSITAVIPYYGYARQDKKFKSRePISAKLVANLLETAGADRVLTVDLHSPQIQGFFDVPVDNLYASPVLAEYLKKKI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958656189 178 PDyrNAVIVAKSPASAKRAQSFAERLRLGIAVIHGEAQDAESD 220
Cdd:TIGR01251 158 LD--NPVVVSPDAGGVERAKKVADALGCPLAIIDKRRISATNE 198
Pribosyltran_N pfam13793
N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found ...
 20-138 2.53e-55

N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found N-terminal to the Pribosyltran, pfam00156.


Pssm-ID: 433483 [Multi-domain]  Cd Length: 117  Bit Score: 172.99  E-value: 2.53e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  20 LVLFSANSNsscMELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYACKTS 99
Cdd:pfam13793   1 LKIFSGNSN---PELAEKIAKRLGIPLGKATVSRFSDGEIYVRIEESVRGKDVFIIQSTCPPVNDNLMELLIMIDALKRA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958656189 100 CAKSIIGVIPYFPYSKQCKM-RKRGSIVSKLLASMMCKAG 138
Cdd:pfam13793  78 SAKRITAVIPYFGYARQDRKdKPREPITAKLVADLLEAAG 117
FERM_F1_Myo10_like cd17110
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in unconventional ...
 8-80 5.71e-03

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in unconventional myosin-X and similar proteins; Myosin-X, also termed myosin-10 (Myo10), is an untraditional member of myosin superfamily. It is an actin-based motor protein that plays a critical role in diverse cellular motile events, such as filopodia formation/extension, phagocytosis, cell migration, and mitotic spindle maintenance, as well as a number of disease states including cancer metastasis and pathogen infection. Myosin-X functions as an important regulator of cytoskeleton that modulates cell motilities in many different cellular contexts. It regulates neuronal radial migration through interacting with N-cadherin. Like other unconventional myosins, Myosin-X is composed of a conserved motor head, a neck region and a variable tail. The neck region consists of three IQ motifs (light chain-binding sites), and a predicted stalk of coiled coil. The tail contains three PEST regions, three PH domains, a MyTH4 domain, and a FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Amoebozoan Dictyostelium discoideum myosin VII (DdMyo7) and uncharacterized pleckstrin homology domain-containing family H member 3 (PLEKHH3) are also included in this family. Like metazoan Myo10, DdMyo7 is essential for the extension of filopodia, plasma membrane protrusions filled with parallel bundles of F-actin.


Pssm-ID: 340630  Cd Length: 97  Bit Score: 35.44  E-value: 5.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656189   8 ELETKMNITKGGLVLFSANSNSSCMELSKKIAERLGVEMGK--VQVYqepnrETRVQIQESVRGKDVfIIQTVSK 80
Cdd:cd17110     3 ELTVTVTCQGGRTCKVAIDSWTTCGEVSKDLARRLGLERSRngFALF-----ETSGDIERALEAKTR-VVDVLSK 71
 
Name Accession Description Interval E-value
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 20-224 9.54e-73

Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis


Pssm-ID: 440230 [Multi-domain]  Cd Length: 311  Bit Score: 224.17  E-value: 9.54e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  20 LVLFSANSNsscMELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYACKTS 99
Cdd:COG0462     4 LKIFSGNAN---PELAEEIAEYLGVPLGKAEVRRFSDGEIYVRIEESVRGRDVFVIQSTSPPVNDNLMELLIMIDALKRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189 100 CAKSIIGVIPYFPYSKQ-CKMRKRGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQEEip 178
Cdd:COG0462    81 SARRITAVIPYYGYARQdRKFRPREPITAKLVADLLEAAGADRVLTVDLHAPQIQGFFDIPVDHLYAAPLLADYIKSK-- 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958656189 179 DYRNAVIVakSP--ASAKRAQSFAERLRLGIAVIHGE---AQDAESDLVDG 224
Cdd:COG0462   159 DLEDLVVV--SPdvGGVKRARAFAKRLGAPLAIIDKRrpgANEVEVMNIIG 207
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
20-210 2.62e-65

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 204.97  E-value: 2.62e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  20 LVLFSANSNsscMELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYACKTS 99
Cdd:PRK01259    1 MKLFAGNAN---PELAEKIAKYLGIPLGKASVGRFSDGEISVEINENVRGKDVFIIQSTCAPTNDNLMELLIMIDALKRA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189 100 CAKSIIGVIPYFPYSKQ-CKMRKRGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQEEip 178
Cdd:PRK01259   78 SAGRITAVIPYFGYARQdRKARSRVPITAKLVANLLETAGADRVLTMDLHADQIQGFFDIPVDNLYGSPILLEDIKQK-- 155

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1958656189 179 DYRNAVIVakSP--ASAKRAQSFAERLRLGIAVI 210
Cdd:PRK01259  156 NLENLVVV--SPdvGGVVRARALAKRLDADLAII 187
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 20-220 5.94e-61

ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In some systems, close homologs lacking enzymatic activity exist and perform regulatory functions. The model is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273523 [Multi-domain]  Cd Length: 308  Bit Score: 194.03  E-value: 5.94e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  20 LVLFSANSNSscmELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFII-QTVSKDVNTTIMELLIMVYACKT 98
Cdd:TIGR01251   1 MKIFSGSSNQ---ELAQKVAKNLGLPLGDVEVKRFPDGELYVRINESVRGKDVFIIqQSTSAPVNDNLMELLIMIDALKR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  99 SCAKSIIGVIPYFPYSKQCKMRKRG-SIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQEEI 177
Cdd:TIGR01251  78 ASAKSITAVIPYYGYARQDKKFKSRePISAKLVANLLETAGADRVLTVDLHSPQIQGFFDVPVDNLYASPVLAEYLKKKI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958656189 178 PDyrNAVIVAKSPASAKRAQSFAERLRLGIAVIHGEAQDAESD 220
Cdd:TIGR01251 158 LD--NPVVVSPDAGGVERAKKVADALGCPLAIIDKRRISATNE 198
Pribosyltran_N pfam13793
N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found ...
 20-138 2.53e-55

N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found N-terminal to the Pribosyltran, pfam00156.


Pssm-ID: 433483 [Multi-domain]  Cd Length: 117  Bit Score: 172.99  E-value: 2.53e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  20 LVLFSANSNsscMELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYACKTS 99
Cdd:pfam13793   1 LKIFSGNSN---PELAEKIAKRLGIPLGKATVSRFSDGEIYVRIEESVRGKDVFIIQSTCPPVNDNLMELLIMIDALKRA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958656189 100 CAKSIIGVIPYFPYSKQCKM-RKRGSIVSKLLASMMCKAG 138
Cdd:pfam13793  78 SAKRITAVIPYFGYARQDRKdKPREPITAKLVADLLEAAG 117
PRK02269 PRK02269
ribose-phosphate diphosphokinase;
16-210 3.77e-55

ribose-phosphate diphosphokinase;


Pssm-ID: 167353 [Multi-domain]  Cd Length: 320  Bit Score: 179.60  E-value: 3.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  16 TKGGLVLFSANSNsscMELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYA 95
Cdd:PRK02269    2 SYSDLKLFALSSN---KELAEKVAQEIGIELGKSSVRQFSDGEIQVNIEESIRGHHVFILQSTSSPVNDNLMEILIMVDA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  96 CKTSCAKSIIGVIPYFPYSKQ-CKMRKRGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQ 174
Cdd:PRK02269   79 LKRASAESINVVMPYYGYARQdRKARSREPITSKLVANMLEVAGVDRLLTVDLHAAQIQGFFDIPVDHLMGAPLIADYFD 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958656189 175 EEIPDYRNAVIVAKSPASAKRAQSFAERLRLGIAVI 210
Cdd:PRK02269  159 RRGLVGDDVVVVSPDHGGVTRARKLAQFLKTPIAII 194
PRK02458 PRK02458
ribose-phosphate pyrophosphokinase; Provisional
 22-218 2.97e-53

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235039 [Multi-domain]  Cd Length: 323  Bit Score: 174.54  E-value: 2.97e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  22 LFSANSNsscMELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYACKTSCA 101
Cdd:PRK02458   12 LFSLNSN---LEIAEKIAQAAGVPLGKLSSRQFSDGEIMINIEESVRGDDIYIIQSTSFPVNDHLWELLIMIDACKRASA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189 102 KSIIGVIPYFPYSKQCKMRK-RGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQEEIPDY 180
Cdd:PRK02458   89 NTVNVVLPYFGYARQDRIAKpREPITAKLVANMLVKAGVDRVLTLDLHAVQVQGFFDIPVDNLFTVPLFAKHYCKKGLSG 168

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958656189 181 RNAVIVAKSPASAKRAQSFAERLRLGIAVIHGEAQDAE 218
Cdd:PRK02458  169 SDVVVVSPKNSGIKRARSLAEYLDAPIAIIDYAQDDSE 206
PLN02369 PLN02369
ribose-phosphate pyrophosphokinase
 32-222 4.33e-51

ribose-phosphate pyrophosphokinase


Pssm-ID: 215209 [Multi-domain]  Cd Length: 302  Bit Score: 168.33  E-value: 4.33e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  32 MELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYACKTSCAKSIIGVIPYF 111
Cdd:PLN02369    1 PALSQEIACYLGLELGKITIKRFADGEIYVQLQESVRGCDVFLVQPTCPPANENLMELLIMIDACRRASAKRITAVIPYF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189 112 PYSKQ-CKMRKRGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQEEIPDYRNAVIVAKSP 190
Cdd:PLN02369   81 GYARAdRKTQGRESIAAKLVANLITEAGADRVLACDLHSGQSMGYFDIPVDHVYGQPVILDYLASKTISSPDLVVVSPDV 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958656189 191 ASAKRAQSFAERLR-LGIAVI----HGEAQDAESDLV 222
Cdd:PLN02369  161 GGVARARAFAKKLSdAPLAIVdkrrQGHNVAEVMNLI 197
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
34-211 1.06e-45

ribose-phosphate diphosphokinase;


Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 154.72  E-value: 1.06e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  34 LSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYACKTSCAKSIIGVIPYFPY 113
Cdd:PRK03092    1 LAEEVAKELGVEVTPTTAYDFANGEIYVRFEESVRGCDAFVLQSHTAPINKWLMEQLIMIDALKRASAKRITVVLPFYPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189 114 SKQ-CKMRKRGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQEEIPDyRNAVIVAKSPAS 192
Cdd:PRK03092   81 ARQdKKHRGREPISARLVADLFKTAGADRIMTVDLHTAQIQGFFDGPVDHLFAMPLLADYVRDKYDL-DNVTVVSPDAGR 159

                         170       180
                  ....*....|....*....|
gi 1958656189 193 AKRAQSFAERL-RLGIAVIH 211
Cdd:PRK03092  160 VRVAEQWADRLgGAPLAFIH 179
PRK04923 PRK04923
ribose-phosphate diphosphokinase;
20-237 1.53e-44

ribose-phosphate diphosphokinase;


Pssm-ID: 179893 [Multi-domain]  Cd Length: 319  Bit Score: 152.01  E-value: 1.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  20 LVLFSANSNSScmeLSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYACKTS 99
Cdd:PRK04923    7 LLVFSGNANKP---LAQSICKELGVRMGKALVTRFSDGEVQVEIEESVRRQEVFVIQPTCAPSAENLMELLVLIDALKRA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189 100 CAKSIIGVIPYFPYSKQ-CKMRK-RGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQEEI 177
Cdd:PRK04923   84 SAASVTAVIPYFGYSRQdRRMRSsRVPITAKVAAKMISAMGADRVLTVDLHADQIQGFFDVPVDNVYASPLLLADIWRAY 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189 178 pDYRNAVIVAKSPASAKRAQSFAERLrlgiavihgeaQDAESDLVDGRHSPPMVRSVAAI 237
Cdd:PRK04923  164 -GTDNLIVVSPDVGGVVRARAVAKRL-----------DDADLAIIDKRRPRANVATVMNI 211
PRK02812 PRK02812
ribose-phosphate pyrophosphokinase; Provisional
 20-204 1.46e-43

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235072 [Multi-domain]  Cd Length: 330  Bit Score: 149.89  E-value: 1.46e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  20 LVLFSANSNSScmeLSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYACKTS 99
Cdd:PRK02812   22 LRLFSGSSNPA---LAQEVARYLGMDLGPMIRKRFADGELYVQIQESIRGCDVYLIQPTCAPVNDHLMELLIMVDACRRA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189 100 CAKSIIGVIPYFPYSK-QCKMRKRGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQEEip 178
Cdd:PRK02812   99 SARQITAVIPYYGYARaDRKTAGRESITAKLVANLITKAGADRVLAMDLHSAQIQGYFDIPCDHVYGSPVLLDYLASK-- 176

                         170       180
                  ....*....|....*....|....*.
gi 1958656189 179 DYRNAVIVAKSPASAKRAQSFAERLR 204
Cdd:PRK02812  177 NLEDIVVVSPDVGGVARARAFAKKLN 202
PRK00553 PRK00553
ribose-phosphate pyrophosphokinase; Provisional
 12-210 4.80e-41

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 179062 [Multi-domain]  Cd Length: 332  Bit Score: 143.52  E-value: 4.80e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  12 KMNITKGGLVLFSAnsnSSCMELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLI 91
Cdd:PRK00553    2 HLSIDKSNHVIFSL---SKAKKLVDSICRKLSMKPGEIVIQKFADGETYIRFDESVRNKDVVIFQSTCSPVNDSLMELLI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  92 MVYACKTSCAKSIIGVIPYFPYSKQ-CKMRKRGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLL 170
Cdd:PRK00553   79 AIDALKRGSAKSITAILPYYGYARQdRKTAGREPITSKLVADLLTKAGVTRVTLTDIHSDQTQGFFDIPVDILRTYHVFL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958656189 171 QYIQEEIpDYRNAVIVAKSPASAKRAQSFAERLRLGIAVI 210
Cdd:PRK00553  159 SRVLELL-GKKDLVVVSPDYGGVKRARLIAESLELPLAII 197
PTZ00145 PTZ00145
phosphoribosylpyrophosphate synthetase; Provisional
 21-203 2.89e-38

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 240290 [Multi-domain]  Cd Length: 439  Bit Score: 138.47  E-value: 2.89e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  21 VLFSANSNSscmELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYACKTSC 100
Cdd:PTZ00145  121 ILFSGSSNP---LLSKNIADHLGTILGRVHLKRFADGEVSMQFLESIRGKDVYIIQPTCPPVNENLIELLLMISTCRRAS 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189 101 AKSIIGVIPYFPYSKQ-CKMRKRGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFF--NIPVDNLRASPFLLQYIQEEi 177
Cdd:PTZ00145  198 AKKITAVIPYYGYARQdRKLSSRVPISAADVARMIEAMGVDRVVAIDLHSGQIQGFFgpRVPVDNLEAQLIGLDYFTKK- 276

                         170       180
                  ....*....|....*....|....*.
gi 1958656189 178 pDYRNAVIVAKSPASAKRAQSFAERL 203
Cdd:PTZ00145  277 -DLYKPVIVSPDAGGVYRARKFQDGL 301
Pribosyl_synth pfam14572
Phosphoribosyl synthetase-associated domain; This family includes several examples of enzymes ...
 179-244 2.25e-32

Phosphoribosyl synthetase-associated domain; This family includes several examples of enzymes from class EC:2.7.6.1, phosphoribosyl-pyrophosphate transferase.


Pssm-ID: 434046  Cd Length: 184  Bit Score: 116.46  E-value: 2.25e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656189 179 DYRNAVIVAKSPASAKRAQSFAERLRLGIAVIHGEAQDAESDLVDGRHSPPMVRSvAAIHPSLEIP 244
Cdd:pfam14572   1 DYRNAVIVARSPGSAKRATSFAERLRLGIAVIHGEQKEAESDEVDGRQSPPPYRS-RTVSRSLGLP 65
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 29-203 1.57e-28

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 109.23  E-value: 1.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  29 SSCMELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDvNTTIMELLIMVYACKTSCAKSIIGVI 108
Cdd:PRK00934    6 SASQLLASEVARLLNTELALVETKRFPDGELYVRILGEIDGEDVVIISTTYPQ-DENLVELLLLIDALRDEGAKSITLVI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189 109 PYFPYSKQCKMRKRG-SIVSKLLASMMcKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQEeipDYRNAVIVA 187
Cdd:PRK00934   85 PYLGYARQDKRFKPGePISARAIAKII-SAYYDRIITINIHEPSILEFFPIPFINLDAAPLIAEYIGD---KLDDPLVLA 160

                         170
                  ....*....|....*.
gi 1958656189 188 KSPASAKRAQSFAERL 203
Cdd:PRK00934  161 PDKGALELAKEAAEIL 176
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 56-225 2.97e-16

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 76.91  E-value: 2.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  56 NRETRVQIQESVRGKDVFIIQTVS--------------KDVNTTIMELLIMVYACKTScAKSIIGVIPYFPYSKQCKMRK 121
Cdd:PRK06827   64 NGEAKGEILESVRGKDIYILQDVGnysvtynmfgeknhMSPDDHFQDLKRTIDAIRGK-ARRITVIMPFLYESRQHKRKG 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189 122 RGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNI-PVDNLRASPFLLQYIQEEIPDYR----NAVIVAKSPASAKRA 196
Cdd:PRK06827  143 RESLDCALALQELEELGVDNIITFDAHDPRIENAIPLmGFENLYPSYQIIKALLKNEKDLEidkdHLMVISPDTGAMDRA 222

                         170       180
                  ....*....|....*....|....*....
gi 1958656189 197 QSFAERLRLGIAVIHGEaQDaESDLVDGR 225
Cdd:PRK06827  223 KYYASVLGVDLGLFYKR-RD-YSRVVNGR 249
PRK07199 PRK07199
ribose-phosphate diphosphokinase;
33-211 7.53e-13

ribose-phosphate diphosphokinase;


Pssm-ID: 235960 [Multi-domain]  Cd Length: 301  Bit Score: 66.50  E-value: 7.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  33 ELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDvNTTIMELLIMVYACKTSCAKSIIGVIPYFP 112
Cdd:PRK07199   13 AAAGRLAAALGVEVGRIELHRFPDGESYVRLDSPVAGRTVVLVCSLDRP-DEKLLPLLFAAEAARELGARRVGLVAPYLA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189 113 YSKQCKMRKRGSIVS-----KLLAsmmckAGLTHLITMD--LHQ-KEIQGFFNIPVDNLRASPFLLQYIQEEIPDyrnAV 184
Cdd:PRK07199   92 YMRQDIAFHPGEAISqrhfaRLLS-----GSFDRLVTVDphLHRyPSLSEVYPIPAVVLSAAPAIAAWIRAHVPR---PL 163

                         170       180
                  ....*....|....*....|....*..
gi 1958656189 185 IVAKSPASAKRAQSFAERLRLGIAVIH 211
Cdd:PRK07199  164 LIGPDEESEQWVAAVAERAGAPHAVLR 190
PLN02297 PLN02297
ribose-phosphate pyrophosphokinase
 65-199 5.38e-04

ribose-phosphate pyrophosphokinase


Pssm-ID: 177934 [Multi-domain]  Cd Length: 326  Bit Score: 40.44  E-value: 5.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656189  65 ESVRGKDVFIIQTVSKdvNTTIMELLIMVYACKTSCAKSIIGVIPYFPYSKQCKMRKRGSIVSKL-LASM-----MCKAG 138
Cdd:PLN02297   62 HGIRGQHVAFLASFSS--PAVIFEQLSVIYALPKLFVASFTLVLPFFPTGTSERVEREGDVATAFtLARIlsnipISRGG 139

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656189 139 LTHLITMDLHQKEIQGFFNipvDNLRAS-----PFLLQYIQeEIPDYRNAVIVAKSPASAKRAQSF 199
Cdd:PLN02297  140 PTSLVIFDIHALQERFYFG---DNVLPCfesgiPLLKKRLQ-QLPDSDNIVIAFPDDGAWKRFHKQ 201
FERM_F1_Myo10_like cd17110
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in unconventional ...
 8-80 5.71e-03

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in unconventional myosin-X and similar proteins; Myosin-X, also termed myosin-10 (Myo10), is an untraditional member of myosin superfamily. It is an actin-based motor protein that plays a critical role in diverse cellular motile events, such as filopodia formation/extension, phagocytosis, cell migration, and mitotic spindle maintenance, as well as a number of disease states including cancer metastasis and pathogen infection. Myosin-X functions as an important regulator of cytoskeleton that modulates cell motilities in many different cellular contexts. It regulates neuronal radial migration through interacting with N-cadherin. Like other unconventional myosins, Myosin-X is composed of a conserved motor head, a neck region and a variable tail. The neck region consists of three IQ motifs (light chain-binding sites), and a predicted stalk of coiled coil. The tail contains three PEST regions, three PH domains, a MyTH4 domain, and a FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Amoebozoan Dictyostelium discoideum myosin VII (DdMyo7) and uncharacterized pleckstrin homology domain-containing family H member 3 (PLEKHH3) are also included in this family. Like metazoan Myo10, DdMyo7 is essential for the extension of filopodia, plasma membrane protrusions filled with parallel bundles of F-actin.


Pssm-ID: 340630  Cd Length: 97  Bit Score: 35.44  E-value: 5.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958656189   8 ELETKMNITKGGLVLFSANSNSSCMELSKKIAERLGVEMGK--VQVYqepnrETRVQIQESVRGKDVfIIQTVSK 80
Cdd:cd17110     3 ELTVTVTCQGGRTCKVAIDSWTTCGEVSKDLARRLGLERSRngFALF-----ETSGDIERALEAKTR-VVDVLSK 71
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH