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Conserved domains on  [gi|1832123188|gb|KAF4073898|]
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hypothetical protein AMELA_G00248570 [Ameiurus melas]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MFS_NLS1_MFSD2A cd17451
Sodium-dependent lysophosphatidylcholine symporter 1 of the Major Facilitator Superfamily of ...
41-494 0e+00

Sodium-dependent lysophosphatidylcholine symporter 1 of the Major Facilitator Superfamily of transporters; Sodium-dependent lysophosphatidylcholine (LPC) symporter 1 (NLS1) is also called major facilitator superfamily domain-containing protein 2A (MFSD2A). NLS1/MFSD2A is an LPC symporter that plays an essential role for blood-brain barrier formation and function. It also transports the essential omega-3 fatty acid docosahexaenoic acid (DHA), which is essential for normal brain growth and cognitive function, in the form of LPC into the brain across the blood-brain barrier. Inactivating mutations in MFSD2A cause a lethal microcephaly syndrome. NLS1/MFSD2A belongs to the Salmonella enterica Na+/melibiose symporter like (MelB-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


:

Pssm-ID: 341009  Cd Length: 419  Bit Score: 774.76  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   41 KLCYAVGGAPYQITGCALGFFLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTPWTRFGRMMPWIILSTPF 120
Cdd:cd17451      1 KLCYAIGGAPYQITGCALGFFLQIYLLDVAQLDPFYASIILFVGRAWDAITDPTVGFFVSKSPWTRFGRLMPWIIFSTPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  121 AVMSYFLIWYVPPVDQTKVVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYRMTVEVLGTVIGTGIQGQIV 200
Cdd:cd17451     81 AVLSYFLIWFVPDFSQGKVMWYLLFYCLFQTLQTCFHVPYSALTMFISTEQKERDSATAYRMTVEVLGTVLGTAIQGQIV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  201 GMAnapcipvgndlnatfrnsgseanitqpdlsldkvrnAYMIASGVICAIYVLCAITLFCGVKERKENSKVHS-ERMSF 279
Cdd:cd17451    161 GMA------------------------------------AYMIAAGVICAIYVLCAIILFLGVREQREPCELKSqKPVSF 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  280 FRGIRLVMGHGPYAKLVMGFLFTSLAFMLLEGNFALFCSYTLGFRDDFQNVLLVVMLSATLTIPFWQWFLTRFGKKTAVY 359
Cdd:cd17451    205 FKGLKLVMSHGPYIKLITGFLFTSLAFMLLEGNFALFCTYTLGFRNDFQNILLVIMLSATLTIPFWQWFLTRFGKKTAVY 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  360 VGTTIVIPFLITVVLMKSNLIVTYVIAIASGVSIAAAFLLPWSMLPDVVDDFKVLNPESQGHEAIFYSFYVFFTKFASGV 439
Cdd:cd17451    285 IGISSAVPFLILVVLVESNLIVTYVVSVAAGVSVAAAFLLPWSMLPDVVDDFKLKNPDSQGHEAIFYSFYVFFTKFASGV 364
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1832123188  440 SLGISTLSLDFAGYVTRGCTQPKAVDVTLKVLVSAAPVALIFIGLLIFTSYPINE 494
Cdd:cd17451    365 SLGISTLSLDFAGYQTRGCSQPEEVNLTLKMLVSAAPVVLILLGLLLFKLYPIDE 419
nt_trans super family cl00015
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
558-886 1.64e-95

nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.


The actual alignment was detected with superfamily member PRK08560:

Pssm-ID: 469580 [Multi-domain]  Cd Length: 329  Bit Score: 306.79  E-value: 1.64e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  558 DKKFNLITRNLQEVLGEEKLK-LILMERELKVYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAFLDNmKAP 636
Cdd:PRK08560     2 EERLELITRNTEEVVTEEELReLLESKEEPKAYIGFEPSGKIHLGHLLTMNKLADLQKAGFKVTVLLADWHAYLND-KGD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  637 WELLELRVKYYEQVIKAMlesiGVPLDKLKFVKGTEYQLSREYTLDVYRLSSMVTEHDAKKAGAEVVKQVEHPLLSGLLY 716
Cdd:PRK08560    81 LEEIRKVAEYNKKVFEAL----GLDPDKTEFVLGSEFQLDKEYWLLVLKLAKNTTLARARRSMTIMGRRMEEPDVSKLVY 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  717 PGLQALDEEYLKVDAQFGGVDQRKIFTLAEKYLPSLGYTKRIHMMNPMVPGLTGS--KMSSSEEESKIDLLDKKEDIKKK 794
Cdd:PRK08560   157 PLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGgiKMSKSKPGSAIFVHDSPEEIRRK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  795 LKKAFCEPGNIQNNGVLSFVKHVLFPLHSEFAIKRDPKFGGDKVYTFYEELEKDFAEERIHPGDLKASVEVALDKLLDPI 874
Cdd:PRK08560   237 IKKAYCPPGEVEGNPVLEIAKYHIFPRYDPFVIERPEKYGGDLEYESYEELERDYAEGKLHPMDLKNAVAEYLIEILEPV 316
                          330
                   ....*....|..
gi 1832123188  875 RKKFETPELKKL 886
Cdd:PRK08560   317 REYLEEGPELLE 328
PLN02610 super family cl33529
probable methionyl-tRNA synthetase
894-1076 2.91e-59

probable methionyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02610:

Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 218.88  E-value: 2.91e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  894 KNKNAVKVNPKKAEEEdEIIPSRLDLRVGKIVGVEKHPAADTLYLEKIDIGEEQPRTVVSGLVAYVSQEELQDRLVVVLC 973
Cdd:PLN02610   621 GKKAGGGGKSKAAAER-EIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGLVKYIPLEEMQNRKVCVLC 699
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  974 NLKPQKMRGIESQAMLLCASvDGEPKRVEPLDPPEGSAPGERVFVDGYtSGTPDDELKPKKKVFEKIQVDMKISDECIAQ 1053
Cdd:PLN02610   700 NLKPAAMRGIKSQAMVLAAS-NSDHTKVELVEPPESAAVGERVTFPGF-EGEPDDVLNPKKKVWETLQPDLHTNSELVAC 777
                          170       180
                   ....*....|....*....|...
gi 1832123188 1054 WNKKDLITKLGKITCKTLKGGSI 1076
Cdd:PLN02610   778 YKDVPFTTSAGVCKVASIANGSI 800
 
Name Accession Description Interval E-value
MFS_NLS1_MFSD2A cd17451
Sodium-dependent lysophosphatidylcholine symporter 1 of the Major Facilitator Superfamily of ...
41-494 0e+00

Sodium-dependent lysophosphatidylcholine symporter 1 of the Major Facilitator Superfamily of transporters; Sodium-dependent lysophosphatidylcholine (LPC) symporter 1 (NLS1) is also called major facilitator superfamily domain-containing protein 2A (MFSD2A). NLS1/MFSD2A is an LPC symporter that plays an essential role for blood-brain barrier formation and function. It also transports the essential omega-3 fatty acid docosahexaenoic acid (DHA), which is essential for normal brain growth and cognitive function, in the form of LPC into the brain across the blood-brain barrier. Inactivating mutations in MFSD2A cause a lethal microcephaly syndrome. NLS1/MFSD2A belongs to the Salmonella enterica Na+/melibiose symporter like (MelB-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 341009  Cd Length: 419  Bit Score: 774.76  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   41 KLCYAVGGAPYQITGCALGFFLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTPWTRFGRMMPWIILSTPF 120
Cdd:cd17451      1 KLCYAIGGAPYQITGCALGFFLQIYLLDVAQLDPFYASIILFVGRAWDAITDPTVGFFVSKSPWTRFGRLMPWIIFSTPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  121 AVMSYFLIWYVPPVDQTKVVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYRMTVEVLGTVIGTGIQGQIV 200
Cdd:cd17451     81 AVLSYFLIWFVPDFSQGKVMWYLLFYCLFQTLQTCFHVPYSALTMFISTEQKERDSATAYRMTVEVLGTVLGTAIQGQIV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  201 GMAnapcipvgndlnatfrnsgseanitqpdlsldkvrnAYMIASGVICAIYVLCAITLFCGVKERKENSKVHS-ERMSF 279
Cdd:cd17451    161 GMA------------------------------------AYMIAAGVICAIYVLCAIILFLGVREQREPCELKSqKPVSF 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  280 FRGIRLVMGHGPYAKLVMGFLFTSLAFMLLEGNFALFCSYTLGFRDDFQNVLLVVMLSATLTIPFWQWFLTRFGKKTAVY 359
Cdd:cd17451    205 FKGLKLVMSHGPYIKLITGFLFTSLAFMLLEGNFALFCTYTLGFRNDFQNILLVIMLSATLTIPFWQWFLTRFGKKTAVY 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  360 VGTTIVIPFLITVVLMKSNLIVTYVIAIASGVSIAAAFLLPWSMLPDVVDDFKVLNPESQGHEAIFYSFYVFFTKFASGV 439
Cdd:cd17451    285 IGISSAVPFLILVVLVESNLIVTYVVSVAAGVSVAAAFLLPWSMLPDVVDDFKLKNPDSQGHEAIFYSFYVFFTKFASGV 364
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1832123188  440 SLGISTLSLDFAGYVTRGCTQPKAVDVTLKVLVSAAPVALIFIGLLIFTSYPINE 494
Cdd:cd17451    365 SLGISTLSLDFAGYQTRGCSQPEEVNLTLKMLVSAAPVVLILLGLLLFKLYPIDE 419
MFS_2 pfam13347
MFS/sugar transport protein; This family is part of the major facilitator superfamily of ...
43-494 5.05e-113

MFS/sugar transport protein; This family is part of the major facilitator superfamily of membrane transport proteins.


Pssm-ID: 433134 [Multi-domain]  Cd Length: 427  Bit Score: 357.00  E-value: 5.05e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   43 CYAVGGAPYQITGCALGFFLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTPwTRFGRMMPWIILSTPFAV 122
Cdd:pfam13347    1 GYGSGALAAGIKYAGLATYLLYFYTDVLGLSAAAVGLVLLVARLVDAFTDPIVGHIIDRTR-TRWGRRRPWLLLSAIILA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  123 MSYFLIWYVPPVDQ-TKVVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYRMTVEVLGTVIGTGIQGQIVG 201
Cdd:pfam13347   80 VSFILLFTPPELGRaPLFIWLLATYILLRIAYTFFEIPYWSLGPELTRDYDERTSLTSYRSFFSVGGGLLAAALAFPLVL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  202 MANAPCIPvgndlnatfrnsgseanitqpdlsldkvRNAYMIASGVICAIYVLCAITLFCGVKE----RKENSKVHSERM 277
Cdd:pfam13347  160 ILGGTGLE----------------------------RKGYRIFALIGAVLMLLGVIITAAGTKErvsmRSKEDTGQKEAG 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  278 SFFRGIRLVMGHGPYAKLVMGFLFTSLAFMLLEGNFALFCSYTLGFRDDFQNVLLVVMLSATLTIPFWQWFLTRFGKKTA 357
Cdd:pfam13347  212 SLLDMLKEVFRNRAFLILLASFLLAALAMGVLNGLLLYYFRYVLGNGFAASAFPLVFTIGALLGIPLWPPLAKRIGKKNT 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  358 VYVGTTIVIPFLITVVLM-KSNLIVTYVIAIASGVSIAAAFLLPWSMLPDVVDDFKVLNPESqgHEAIFYSFYVFFTKFA 436
Cdd:pfam13347  292 YILGALITIAGFALALLLgPNNTLLFLVLYIIIGFGYGSSFFLPWSMLADVVDYGELRTGKR--REGTFFAMWSFISKLA 369
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1832123188  437 SGVSLGISTLSLDFAGYVTRGCTQPKAVDVTLKVLVSAAPVALIFIGLLIFTSYPINE 494
Cdd:pfam13347  370 TGVGLGVSGLLLSAFGYNAGDSVQSPQAVTAIRLLYAVLPAVLFLVALLLLYFYPLDR 427
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
558-886 1.64e-95

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 306.79  E-value: 1.64e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  558 DKKFNLITRNLQEVLGEEKLK-LILMERELKVYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAFLDNmKAP 636
Cdd:PRK08560     2 EERLELITRNTEEVVTEEELReLLESKEEPKAYIGFEPSGKIHLGHLLTMNKLADLQKAGFKVTVLLADWHAYLND-KGD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  637 WELLELRVKYYEQVIKAMlesiGVPLDKLKFVKGTEYQLSREYTLDVYRLSSMVTEHDAKKAGAEVVKQVEHPLLSGLLY 716
Cdd:PRK08560    81 LEEIRKVAEYNKKVFEAL----GLDPDKTEFVLGSEFQLDKEYWLLVLKLAKNTTLARARRSMTIMGRRMEEPDVSKLVY 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  717 PGLQALDEEYLKVDAQFGGVDQRKIFTLAEKYLPSLGYTKRIHMMNPMVPGLTGS--KMSSSEEESKIDLLDKKEDIKKK 794
Cdd:PRK08560   157 PLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGgiKMSKSKPGSAIFVHDSPEEIRRK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  795 LKKAFCEPGNIQNNGVLSFVKHVLFPLHSEFAIKRDPKFGGDKVYTFYEELEKDFAEERIHPGDLKASVEVALDKLLDPI 874
Cdd:PRK08560   237 IKKAYCPPGEVEGNPVLEIAKYHIFPRYDPFVIERPEKYGGDLEYESYEELERDYAEGKLHPMDLKNAVAEYLIEILEPV 316
                          330
                   ....*....|..
gi 1832123188  875 RKKFETPELKKL 886
Cdd:PRK08560   317 REYLEEGPELLE 328
MelB COG2211
Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism];
30-509 4.90e-92

Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism];


Pssm-ID: 441813 [Multi-domain]  Cd Length: 447  Bit Score: 301.44  E-value: 4.90e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   30 SEEKRHLSVCNKLCYAVGGAPYQITGCALGFFLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTpWTRFGR 109
Cdd:COG2211      1 TAAKKKLSLKEKLAYGLGDLGLNLAFGLLSAYLLYFYTDVLGLSAALVGLILLVARLWDAITDPLIGALSDRT-RTRWGR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  110 MMPWIILSTPFAVMSYFLIWYVPPVDQT-KVVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYRMTVEVLG 188
Cdd:COG2211     80 RRPWILIGAIPLALSFVLLFTAPDLSPTgKLIYALVTYLLLGLAYTLVNIPYSALGAELTPDYEERTRLSSWRFAFAGLG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  189 TVIGTGIQGQIVGManapcipVGNDlnatfrnsgseanitqpdlsldkVRNAYMIASGVICAIYVLCAITLFCGVKERKE 268
Cdd:COG2211    160 GLLASVLPPPLVAA-------FGGD-----------------------AALGYRLTALIFAVLGLLAFLLTFFGTKERPV 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  269 NSKvhsERMSFFRGIRLVMGHGPYAKLVMGFLFTSLAFMLLEGNFALFCSYTLGFRDDFQNVLLVVM-LSATLTIPFWQW 347
Cdd:COG2211    210 PEE---EKVSLKESLKALLKNRPFLLLLLAYLLFFLALALVAALLLYYFKYVLGLSAALVGLLLALYfLAALLGAPLWPR 286
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  348 FLTRFGKKTAVYVGTTI-VIPFLITVVLMKSNLIVTYVIAIASGVSIAAAFLLPWSMLPDVVDDFKVLNPESQghEAIFY 426
Cdd:COG2211    287 LAKRFGKKKAFIIGLLLaALGLLLLFFLGPGNLWLLLVLAALAGIGLGAILVLPWAMLADVVDYDEWKTGRRR--EGLYF 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  427 SFYVFFTKFASGVSLGISTLSLDFAGYVTrGCTQPKAVDVTLKVLVSAAPVALIFIGLLIFTSYPINEKRRQGNRKLLNE 506
Cdd:COG2211    365 GIFTFAIKLGQALAGALAGLLLALFGYVA-GAAQSPSALTGIRLLFFLLPAVLLLLAALLLLFYPLTRERHAEIRAELAA 443

                   ...
gi 1832123188  507 QRE 509
Cdd:COG2211    444 RRA 446
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
586-870 1.56e-79

catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) catalytic core domain. TyrRS is a homodimer which attaches Tyr to the appropriate tRNA. TyrRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formationof the enzyme bound aminoacyl-adenylate. It contains the class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding.


Pssm-ID: 173902 [Multi-domain]  Cd Length: 269  Bit Score: 261.00  E-value: 1.56e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  586 LKVYWGTATTG-KPHVAYFVPMSKIADFLKAGCEVTILFADLHAFLDNMK--------APWELLELRVKYYEQVIKAMLE 656
Cdd:cd00805      1 LKVYIGFDPTApSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSgkseerklLDLELIRENAKYYKKQLKAILD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  657 SIgvPLDKLKFVKGTEYQLSrEYTLDVYRLSSMVTEHDAKKAGAEVVKQ--VEHPLLSGLLYPGLQALDEEYLKVDAQFG 734
Cdd:cd00805     81 FI--PPEKAKFVNNSDWLLS-LYTLDFLRLGKHFTVNRMLRRDAVKVRLeeEEGISFSEFIYPLLQAYDFVYLDVDLQLG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  735 GVDQRKIFTLAEKYLPSLGYTKRIHMMNPMVPGLTGSKM-SSSEEESKIDLLDKKEDIKKKLKKAFCEPgniqnngVLSF 813
Cdd:cd00805    158 GSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGGKMsKSEGNAIWDPVLDSPYDVYQKIRNAFDPD-------VLEF 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1832123188  814 VKHVLFPLHSEfaikrdpkfggdkvytfYEELEKDFAEErIHPGDLKASVEVALDKL 870
Cdd:cd00805    231 LKLFTFLDYEE-----------------IEELEEEHAEG-PLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
583-871 1.33e-61

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 212.14  E-value: 1.33e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  583 ERELKVYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAFL-DNMKAPWELLELRVKYYEQVIKAMLeSIGVP 661
Cdd:pfam00579    3 NRPLRVYSGIDPTGPLHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIgDPSKSPERKLLSRETVLENAIKAQL-ACGLD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  662 LDKLKFVKGTEYQLSREYTLDVYRLSSMVTEHDAKKAGaEVVKQVEHP---LLSGLLYPGLQALDEEYLKVDAQFGGVDQ 738
Cdd:pfam00579   82 PEKAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFK-DVKKRLEQGpgiSLGEFTYPLLQAYDILLLKADLQPGGSDQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  739 RKIFTLAEKYLPSLGY---TKRIHMMNPMVPGLTG-SKMSSSEEESKIDLLDKKEDIKKKLKKAFCEPGNiqNNGVLSFV 814
Cdd:pfam00579  161 WGNIELGRDLARRFNKkifKKPVGLTNPLLTGLDGgKKMSKSAGNSAIFLDDDPESVYKKIQKAYTDPDR--EVRKDLKL 238
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1832123188  815 KHVLFPlhseFAIKRDPKFGGDKVYTFYEELEKDFAEERIHPGDLKASVEVALDKLL 871
Cdd:pfam00579  239 FTFLSN----EEIEILEAELGKSPYREAEELLAREVTGLVHGGDLKKAAAEAVNKLL 291
PLN02610 PLN02610
probable methionyl-tRNA synthetase
894-1076 2.91e-59

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 218.88  E-value: 2.91e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  894 KNKNAVKVNPKKAEEEdEIIPSRLDLRVGKIVGVEKHPAADTLYLEKIDIGEEQPRTVVSGLVAYVSQEELQDRLVVVLC 973
Cdd:PLN02610   621 GKKAGGGGKSKAAAER-EIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGLVKYIPLEEMQNRKVCVLC 699
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  974 NLKPQKMRGIESQAMLLCASvDGEPKRVEPLDPPEGSAPGERVFVDGYtSGTPDDELKPKKKVFEKIQVDMKISDECIAQ 1053
Cdd:PLN02610   700 NLKPAAMRGIKSQAMVLAAS-NSDHTKVELVEPPESAAVGERVTFPGF-EGEPDDVLNPKKKVWETLQPDLHTNSELVAC 777
                          170       180
                   ....*....|....*....|...
gi 1832123188 1054 WNKKDLITKLGKITCKTLKGGSI 1076
Cdd:PLN02610   778 YKDVPFTTSAGVCKVASIANGSI 800
tRNA_bind_EMAP-II_like cd02799
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ...
914-1017 3.28e-57

tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of tRNA binding proteins, including Caenorhabditis elegans methionyl-tRNA synthetase (CeMetRS), human tyrosyl- tRNA synthetase (hTyrRS), Saccharomyces cerevisiae Arc1p, human p43 and EMAP2. CeMetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. A EMAP-II-like cytokine also is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain.


Pssm-ID: 239198 [Multi-domain]  Cd Length: 105  Bit Score: 192.06  E-value: 3.28e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  914 PSRLDLRVGKIVGVEKHPAADTLYLEKIDIGEEQPRTVVSGLVAYVSQEELQDRLVVVLCNLKPQKMRGIESQAMLLCAS 993
Cdd:cd02799      3 PSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLCAS 82
                           90       100
                   ....*....|....*....|....
gi 1832123188  994 VDGEPKrVEPLDPPEGSAPGERVF 1017
Cdd:cd02799     83 NADHEK-VELLEPPEGAKPGERVT 105
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
557-879 6.05e-49

tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up tryptophanyl-tRNA synthetases at scores of 0 and below. The proteins found by this model have a deep split between two groups. One group contains bacterial and organellar eukaryotic examples. The other contains archaeal and cytosolic eukaryotic examples. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272976 [Multi-domain]  Cd Length: 378  Bit Score: 178.74  E-value: 6.05e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  557 PDKKFNLITRNLQEVLGEEKLKLI--LMERELKVYWGTATTG-KPHVAYFVPMSKIADFLKAGCEVTILFADLHAFLDNM 633
Cdd:TIGR00234    1 MNNILLLLTKRGLEVQTPEEEKDLlkLLERPLKLYLGFDPTApSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  634 KAPWELLELR-----VKYYEQVIKAMLESIGVplDKLKFVKGTEYQLSREYTLDVYRLSSMVTEHDAKKAGAEVVKQVEH 708
Cdd:TIGR00234   81 TGKSEVRKILtreevQENAENIKKQIARFLDF--EKAKFVYNSEWLLKLNYTDFIRLLGKIFTVNRMLRRDAFSSRFEEN 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  709 PLLSGLLYPGLQALDEEYLKVDAQFGGVDQ----RKIFTLAEKYLPSLGYTKRIHMMNP---MVPGLTGS-KMSS--SEE 778
Cdd:TIGR00234  159 ISLHEFIYPLLQAYDFVYLNVDLQLGGSDQwfniRKGRDLARENLPSLQFGLTVPLLTPadgEKMGKSLGgAVSLdeGKY 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  779 ESKIDLLDKKEDIKKKLKKAFCEPGN----------------IQNNGVLSFVKHVLFP------------------LHSE 824
Cdd:TIGR00234  239 DFYQKVINTPDELVKKYLKLFTFLGLeeieqlvelkgpnpreVKENLALEITKYVHGPeaalaaeeiseaifsgglNPDE 318
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1832123188  825 FAIKRDPKFGGDKVYTFYEELEKDFAEERIHPGDLK-ASVEVA--LDKLLDPIRKKFE 879
Cdd:TIGR00234  319 VPIFRPEKFGGPITLADLLVLSGLFPSKSEARRDIKnGGVYINgeKVEDLEPIRKELE 376
gph TIGR00792
sugar (Glycoside-Pentoside-Hexuronide) transporter; The Glycoside-Pentoside-Hexuronide (GPH): ...
41-496 1.98e-44

sugar (Glycoside-Pentoside-Hexuronide) transporter; The Glycoside-Pentoside-Hexuronide (GPH):Cation Symporter Family (TC 2.A.2) GPH:cation symporters catalyze uptake of sugars in symport with a monovalent cation (H+ or Na+). Members of this family includes transporters for melibiose, lactose, raffinose, glucuronides, pentosides and isoprimeverose. Mutants of two groups of these symporters (the melibiose permeases of enteric bacteria, and the lactose permease of Streptococcus thermophilus) have been isolated in which altered cation specificity is observed or in which sugar transport is uncoupled from cation symport (i.e., uniport is catalyzed). The various members of the family can use Na+, H+ or Li, Na+ or Li+, H+ or Li+, or only H+ as the symported cation. All of these proteins possess twelve putative transmembrane a-helical spanners. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273270  Cd Length: 437  Bit Score: 167.04  E-value: 1.98e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   41 KLCYAVGGAPYQITGCALGFFLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTPwTRFGRMMPWI-ILSTP 119
Cdd:TIGR00792    1 KLSYGFGDFGNDFIFAIVSTYLLFFYTDVLGLSAAFVGTLFLVARILDAITDPIMGNIVDRTR-TRWGKFRPWLlIGAIP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  120 FAVMSyFLIWYVPPVDQT-KVVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYRMtvevlgtvIGTGIQGQ 198
Cdd:TIGR00792   80 FSIVL-VLLFTTPDFSGTgKLVYAYITYILLGLFYSFVNIPYWSLVPAITLDPRERESLSTFRR--------FGATLGGL 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  199 IVGMAnapCIPVGNDLNATFRNSGseanitqpdlsldkvrnaYMIASGVICAIYVLCAITLFCGVKERKENSKVHSERMS 278
Cdd:TIGR00792  151 LVAVI---VLPLVSYFGGGDDKFG------------------WFMFALVLALIGVVSLIICFFGTKERYSEIPKNIEKKL 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  279 FFRGI-RLVMGHGPYAKLVMGFLFTSLAFMLLEGNFALFCSYTLGFRDDFQNVLLVVMLSATLTIPFWQWFLTRFGKKTA 357
Cdd:TIGR00792  210 SLKQIfKALFKNDQLLILCLAYLFYNLAFNIKNGVQVYYFTYVLGDPELFSYMGSIAIVAGLIGVLLFPRLVKKFGRKIL 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  358 VYVGTTIVIPFLITVVLMKSNLIVTYVIAIASGVSIAAAFLLPWSMLPDVVDDFKVLNpesqGH--EAIFYSFYVFFTKF 435
Cdd:TIGR00792  290 FAGGILLMVLGYLIFFFAGSNLPLILVLIILAGFGQNIVTGLVWALVADTVDYGEWKT----GIraEGLVYSVRTFVRKL 365
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832123188  436 ASGVSLGISTLSLDFAGYVTrGCTQPKAVDVTLKVLVSAAPVALIFIGLLIFTS-YPINEKR 496
Cdd:TIGR00792  366 GQALAGFFVGLILGIIGYVA-NAAQSPITLNGIKILMFAVPALFLLLAAIIIGRfYKLTEKK 426
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
919-1015 6.01e-36

Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1), human tyrosyl-tRNA synthetase, and endothelial-monocyte activating polypeptide II. G4p1 binds specifically to tRNA form a complex with methionyl-tRNA synthetases. In human tyrosyl-tRNA synthetase this domain may direct tRNA to the active site of the enzyme. This domain may perform a common function in tRNA aminoacylation.


Pssm-ID: 396251 [Multi-domain]  Cd Length: 96  Bit Score: 131.21  E-value: 6.01e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  919 LRVGKIVGVEKHPAADTLYLEKIDIGEEQPRTVVSGLVAYVSQEELQDRLVVVLCNLKPQKMRGIESQAMLLCASvDGEP 998
Cdd:pfam01588    1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAE-ELDG 79
                           90
                   ....*....|....*..
gi 1832123188  999 KRVEPLDPPEGSAPGER 1015
Cdd:pfam01588   80 GSVGLLEPPADVPPGTK 96
metG_C_term TIGR00399
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ...
884-1016 3.20e-25

methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model describes a region of the methionyl-tRNA synthetase that is present at the C-terminus of MetG in some species (E. coli, B. subtilis, Thermotoga maritima, Methanobacterium thermoautotrophicum), and as a separate beta chain in Aquifex aeolicus. It is absent in a number of other species (e.g. Mycoplasma genitalium, Mycobacterium tuberculosis), while Pyrococcus horikoshii has both a full length MetG and a second protein homologous to the beta chain only. Proteins hit by this model should be called methionyl-tRNA synthetase beta chain if and only if the model metG hits a separate protein not also hit by this model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273059 [Multi-domain]  Cd Length: 137  Bit Score: 102.12  E-value: 3.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  884 KKLTSLAYPSKNKNAVKVNPKKAEEEDEIIPS-----RLDLRVGKIVGVEKHPAADTLYLEKIDIGEEQpRTVVSGLVAY 958
Cdd:TIGR00399    2 KKIEELKLKGAKKKEKKDEGEKALEPQKETITiddfeKVDLRVGKILKAERVEKSDKLLKLKLDLGDEK-RQIVSGIAGY 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1832123188  959 VSQEELQDRLVVVLCNLKPQKMRGIESQAMLLCASVDGepKRVEPLDPPEGSAPGERV 1016
Cdd:TIGR00399   81 YTPEELVGKKVIVVANLKPAKLFGVKSEGMILAAEDDG--KVLFLLSPDQEAIAGERI 136
PRK09669 PRK09669
putative symporter YagG; Provisional
36-496 4.65e-25

putative symporter YagG; Provisional


Pssm-ID: 236610  Cd Length: 444  Bit Score: 109.81  E-value: 4.65e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   36 LSVCNKLCYAVGGapyqiTGCAL-----GFFLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTPwTRFGRM 110
Cdd:PRK09669     6 LTTKDKIGYGLGD-----TACNLvwqtvMLFLAYFYTDVFGLSAAIMGTMFLVVRVLDAVTDPLMGALVDRTR-TRHGQF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  111 MPWII-LSTPFAVmSYFLIWYVPPVDQT-KVVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYRMTVEVLG 188
Cdd:PRK09669    80 RPYLLwFAIPFGV-VCLLTFYTPDFGATgKIIYACVTYILLSLVYTAINVPYCAMPGAITNDPRERHSLQSWRFALSFIG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  189 tvigtgiqGQIVGMANAPCIPVgndlnatfrnsgseanITQPDlsldkVRNAYMIASGVICAIYVLCAITLFCGVKERKE 268
Cdd:PRK09669   159 --------GLIVSVIALPLVDI----------------LGKGD-----EQKGYFYAMMVMGLLGVVLFFCCFFMTKERYT 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  269 NSKVHSErmSFFRGIRLVMGHGPYaKLVMGFLFTSLAFMLLEGNFAL-FCSYTLGfRDDFQNVLLVVMLSATLTIPFWQW 347
Cdd:PRK09669   210 PEVDNSS--SVWKDLKLLLGNSQW-RIMFIFNVVLLTAVVTRGGATLyYVNYVLL-RPDLATLFLVTGMIAGLFGALLSE 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  348 FLtrFGKKTAVYVGTTIVIPFLITVVLM----KSNLIVTYVIAIASGVSIAAAFLLPWSMLPDVVDdfkVLNPES-QGHE 422
Cdd:PRK09669   286 RL--LGKFDRVRAFKWTIVAFVILSALIffipPSNVWLIFALNILFNFIQNLTTPLQWSMFSDVVD---YEEKRSgRRLD 360
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832123188  423 AIFYSFYVFFTKFasGVSLGISTL--SLDFAGYVTRGCTQPKAVDVTLKVLVSAAPVALIFIGLLIFTSYPINEKR 496
Cdd:PRK09669   361 GLVFSTNLFAIKL--GLAIGGAVVgwILAWVDYVGGAAVQSASVLTTINLLFTVIPGVLFAGMAIILNFYKLNDAR 434
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
907-1013 5.75e-19

tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 92.61  E-value: 5.75e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  907 EEEDEIIPSRLD-LRVGKIVGVEKHPAADTLYLEKIDIGEEqPRTVVSGL-VAYVSQ---EELQDRLVVVLCNLKPQKMR 981
Cdd:COG0073     31 EVEDFEKVGGLDgLRVGKVLEAEPHPNADKLLVLQVDVGEE-TRQIVCGApNVYAGDkvpEALVGAQVPGVVNLKPRKIR 109
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1832123188  982 GIESQAMLLCASVDGEPKRVE-PLDPPEGSAPG 1013
Cdd:COG0073    110 GVESEGMLCSAEELGLGEDHDgILELPEDAPPG 142
 
Name Accession Description Interval E-value
MFS_NLS1_MFSD2A cd17451
Sodium-dependent lysophosphatidylcholine symporter 1 of the Major Facilitator Superfamily of ...
41-494 0e+00

Sodium-dependent lysophosphatidylcholine symporter 1 of the Major Facilitator Superfamily of transporters; Sodium-dependent lysophosphatidylcholine (LPC) symporter 1 (NLS1) is also called major facilitator superfamily domain-containing protein 2A (MFSD2A). NLS1/MFSD2A is an LPC symporter that plays an essential role for blood-brain barrier formation and function. It also transports the essential omega-3 fatty acid docosahexaenoic acid (DHA), which is essential for normal brain growth and cognitive function, in the form of LPC into the brain across the blood-brain barrier. Inactivating mutations in MFSD2A cause a lethal microcephaly syndrome. NLS1/MFSD2A belongs to the Salmonella enterica Na+/melibiose symporter like (MelB-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 341009  Cd Length: 419  Bit Score: 774.76  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   41 KLCYAVGGAPYQITGCALGFFLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTPWTRFGRMMPWIILSTPF 120
Cdd:cd17451      1 KLCYAIGGAPYQITGCALGFFLQIYLLDVAQLDPFYASIILFVGRAWDAITDPTVGFFVSKSPWTRFGRLMPWIIFSTPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  121 AVMSYFLIWYVPPVDQTKVVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYRMTVEVLGTVIGTGIQGQIV 200
Cdd:cd17451     81 AVLSYFLIWFVPDFSQGKVMWYLLFYCLFQTLQTCFHVPYSALTMFISTEQKERDSATAYRMTVEVLGTVLGTAIQGQIV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  201 GMAnapcipvgndlnatfrnsgseanitqpdlsldkvrnAYMIASGVICAIYVLCAITLFCGVKERKENSKVHS-ERMSF 279
Cdd:cd17451    161 GMA------------------------------------AYMIAAGVICAIYVLCAIILFLGVREQREPCELKSqKPVSF 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  280 FRGIRLVMGHGPYAKLVMGFLFTSLAFMLLEGNFALFCSYTLGFRDDFQNVLLVVMLSATLTIPFWQWFLTRFGKKTAVY 359
Cdd:cd17451    205 FKGLKLVMSHGPYIKLITGFLFTSLAFMLLEGNFALFCTYTLGFRNDFQNILLVIMLSATLTIPFWQWFLTRFGKKTAVY 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  360 VGTTIVIPFLITVVLMKSNLIVTYVIAIASGVSIAAAFLLPWSMLPDVVDDFKVLNPESQGHEAIFYSFYVFFTKFASGV 439
Cdd:cd17451    285 IGISSAVPFLILVVLVESNLIVTYVVSVAAGVSVAAAFLLPWSMLPDVVDDFKLKNPDSQGHEAIFYSFYVFFTKFASGV 364
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1832123188  440 SLGISTLSLDFAGYVTRGCTQPKAVDVTLKVLVSAAPVALIFIGLLIFTSYPINE 494
Cdd:cd17451    365 SLGISTLSLDFAGYQTRGCSQPEEVNLTLKMLVSAAPVVLILLGLLLFKLYPIDE 419
MFS_MFSD2 cd17392
Major facilitator superfamily domain-containing protein 2 subfamily; The major facilitator ...
41-494 0e+00

Major facilitator superfamily domain-containing protein 2 subfamily; The major facilitator superfamily domain-containing protein 2 (MFSD2) subfamily is composed of two vertebrate members, MFSD2A amd MFSD2B. MFSD2A is more commonly called sodium-dependent lysophosphatidylcholine symporter 1 (NLS1). It is an LPC symporter that plays an essential role for blood-brain barrier formation and function. Inactivating mutations in MFSD2A cause a lethal microcephaly syndrome. MFSD2B is a potential risk or protect factor in the prognosis of lung adenocarcinoma. The MFSD2 subfamily belongs to the Salmonella enterica Na+/melibiose symporter like (MelB-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340950  Cd Length: 446  Bit Score: 664.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   41 KLCYAVGGAPYQITGCALGFFLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTPWTRFGRMMPWIILSTPF 120
Cdd:cd17392      1 KLCYAIGGAPYQMTSSATGFFLQIFLLDVAQMGAFSVSLILFVGRVWDAVTDPLVGYFISRSQRTGIGRLMPWIVFSTPL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  121 AVMSYFLIWYVPPVDQTKVVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYRMTVEVLGTVIGTGIQGQIV 200
Cdd:cd17392     81 IILAYFFLWFLPPFTSLSGLWYLTFYCLFETFMTCFHVPYSALTMFLGGCQRERDSATAYRMTVEVFGTLMGATIQGQIV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  201 GMANAPCIpvgNDLNATfrnsgsEANITQPDLSLDKVRNAYMIASGVICAIYVLCAITLFCGVKERKENSKVHS-ERMSF 279
Cdd:cd17392    161 GVAHRPRR---QDCTAT------PGTSDHPVTVLPNTRRAYLIAALVVVVLYFVCCSILFLGVKEQPDPLSPASgPGLSY 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  280 FRGIRLVMGHGPYAKLVMGFLFTSLAFMLLEGNFALFCSYTLGFRDDFQNVLLVVMLSATLTIPFWQWFLTRFGKKTAVY 359
Cdd:cd17392    232 LAGLKLVTGHPPYLKLVIGFLFSSLAFQMEQGNFVLFCTHAAGLGDHFQHLVLAILVSATLSIPLWQWVLQRRGKKTTSF 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  360 VGTTIVIPFLITVVLMKSNLIVTYVIAIASGVSIAAAFLLPWSMLPDVVDDFKVLNPESQGHEAIFYSFYVFFTKFASGV 439
Cdd:cd17392    312 IGISAMVPFLILLALVPSNLPVAYVVAVVSGVSLAALFLLPWSMLPDVVDDFQLKNPHCPGLEPIFYSCYVFFTKLGGGL 391
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1832123188  440 SLGISTLSLDFAGYVTRGCTQPKAVDVTLKVLVSAAPVALIFIGLLIFTSYPINE 494
Cdd:cd17392    392 SLGISTLSLHFSGYKAGACKQPEEVVVTLKVLIAPVPICLILAGLVLFYVYPINE 446
MFS_MFSD2B cd17452
Major facilitator superfamily domain-containing protein 2B; Major facilitator superfamily ...
41-494 0e+00

Major facilitator superfamily domain-containing protein 2B; Major facilitator superfamily domain-containing protein 2B (MFSD2B) is closely related to MFSD2A, and their conserved genomic structure suggests that they are derived from the duplication of an ancestral gene. Variations of chromosome 2 gene expressions among patients with lung cancer or non-cancer identified MFSD2B as a potential risk or protect factor in the prognosis of lung adenocarcinoma. MFSD2B belongs to the Salmonella enterica Na+/melibiose symporter like (MelB-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 341010  Cd Length: 416  Bit Score: 607.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   41 KLCYAVGGAPYQITGCALGFFLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTPWTRFGRMMPWIILSTPF 120
Cdd:cd17452      1 KLCYAIGGAPNQVAGSATAFFLQIYLLDIAQITPFQASLVLFVGKAWGAATDPVVGFFISKSKWTKIGRLMPWMLGCTPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  121 AVMSYFLIWYVPPVDQTKVVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYRMTVEVLGTVIGTGIQGQIV 200
Cdd:cd17452     81 IVVSYFFLWFVPPFTTGRFLWYLTFYCLFQALATCFHVPYSALTMFLSTDQRERDSATAYRMTVEVLGTLVGAAVQGQIV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  201 GmanapcipvgndlnatfrnsgseanitqpdlsldkvrNAYMIASGVICAIYVLCAITLFCGVKERKENSKVHSER-MSF 279
Cdd:cd17452    161 A-------------------------------------SAYMIAAGVIGGLYLLCISVLFLGVKERDDPYAPKSGKaIPF 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  280 FRGIRLVMGHGPYAKLVMGFLFTSLAFMLLEGNFALFCSYTLGFRDDFQNVLLVVMLSATLTIPFWQWFLTRFGKKTAvY 359
Cdd:cd17452    204 FKGLSLTMRHGPYLKLTASFLFISAAVQLEQSNFVLFCTHAVDLHDHFQNLVLTILVSAVVSIPFWQWFLQRFGKKAA-A 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  360 VGTTIVIPFLITVVLMkSNLIVTYVIAIASGVSIAAAFLLPWSMLPDVVDDFKVLNPESQGHEAIFYSFYVFFTKFASGV 439
Cdd:cd17452    283 CGISWMIPFAIMLVTI-PNLIVAYVVAFVSGLSIAASLLLPWSMLPDVVDDFRLQNPHGKGLETIFYSSYVFFTKLSAGI 361
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1832123188  440 SLGISTLSLDFAGYVTRGCTQPKAVDVTLKVLVSAAPVALIFIGLLIFTSYPINE 494
Cdd:cd17452    362 ALGISTLSLEFAGYETGACKQPESVVLTLKLLIGAAPTCMILIGLCILMFYPITE 416
MFS_2 pfam13347
MFS/sugar transport protein; This family is part of the major facilitator superfamily of ...
43-494 5.05e-113

MFS/sugar transport protein; This family is part of the major facilitator superfamily of membrane transport proteins.


Pssm-ID: 433134 [Multi-domain]  Cd Length: 427  Bit Score: 357.00  E-value: 5.05e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   43 CYAVGGAPYQITGCALGFFLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTPwTRFGRMMPWIILSTPFAV 122
Cdd:pfam13347    1 GYGSGALAAGIKYAGLATYLLYFYTDVLGLSAAAVGLVLLVARLVDAFTDPIVGHIIDRTR-TRWGRRRPWLLLSAIILA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  123 MSYFLIWYVPPVDQ-TKVVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYRMTVEVLGTVIGTGIQGQIVG 201
Cdd:pfam13347   80 VSFILLFTPPELGRaPLFIWLLATYILLRIAYTFFEIPYWSLGPELTRDYDERTSLTSYRSFFSVGGGLLAAALAFPLVL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  202 MANAPCIPvgndlnatfrnsgseanitqpdlsldkvRNAYMIASGVICAIYVLCAITLFCGVKE----RKENSKVHSERM 277
Cdd:pfam13347  160 ILGGTGLE----------------------------RKGYRIFALIGAVLMLLGVIITAAGTKErvsmRSKEDTGQKEAG 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  278 SFFRGIRLVMGHGPYAKLVMGFLFTSLAFMLLEGNFALFCSYTLGFRDDFQNVLLVVMLSATLTIPFWQWFLTRFGKKTA 357
Cdd:pfam13347  212 SLLDMLKEVFRNRAFLILLASFLLAALAMGVLNGLLLYYFRYVLGNGFAASAFPLVFTIGALLGIPLWPPLAKRIGKKNT 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  358 VYVGTTIVIPFLITVVLM-KSNLIVTYVIAIASGVSIAAAFLLPWSMLPDVVDDFKVLNPESqgHEAIFYSFYVFFTKFA 436
Cdd:pfam13347  292 YILGALITIAGFALALLLgPNNTLLFLVLYIIIGFGYGSSFFLPWSMLADVVDYGELRTGKR--REGTFFAMWSFISKLA 369
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1832123188  437 SGVSLGISTLSLDFAGYVTRGCTQPKAVDVTLKVLVSAAPVALIFIGLLIFTSYPINE 494
Cdd:pfam13347  370 TGVGLGVSGLLLSAFGYNAGDSVQSPQAVTAIRLLYAVLPAVLFLVALLLLYFYPLDR 427
MFS_MelB_like cd17332
Salmonella enterica Na+/melibiose symporter MelB and similar transporters of the Major ...
41-494 1.13e-104

Salmonella enterica Na+/melibiose symporter MelB and similar transporters of the Major Facilitator Superfamily; This family is composed of Salmonella enterica Na+/melibiose symporter MelB, Major Facilitator Superfamily domain-containing proteins, MFSD2 and MFSD12, and other sugar transporters. MelB catalyzes the electrogenic symport of galactosides with Na+, Li+ or H+. The MFSD2 subfamily is composed of two vertebrate members, MFSD2A and MFSD2B. MFSD2A is more commonly called sodium-dependent lysophosphatidylcholine symporter 1 (NLS1). It is an LPC symporter that plays an essential role for blood-brain barrier formation and function. Inactivating mutations in MFSD2A cause a lethal microcephaly syndrome. MFSD2B is a potential risk or protect factor in the prognosis of lung adenocarcinoma. MelB-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340890 [Multi-domain]  Cd Length: 424  Bit Score: 334.57  E-value: 1.13e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   41 KLCYAVGGAPYQITGCALGFFLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTPwTRFGRMMPWIILSTPF 120
Cdd:cd17332      1 KIGYGLGDFGNNLIFQIVSTYLLFFYTDVLGLSAAAAGTIFLVARIIDAINDPLMGYLIDRTR-SRWGRFRPWLLWGAIP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  121 AVMSYFLIWYVPPVDQT-KVVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYRMTVEVLGTVIGTGIQGQI 199
Cdd:cd17332     80 LALLFVLLFTTPDGSGTgKLIYALITYILLDLLYTLVNIPYTALIPELTDDPEERTSLTSWRMFFATIGGLLVTVLPPPL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  200 VGMANAPCIPVGndlnatfrnsgseanitqpdlsldkvrnaYMIASGVICAIYVLCAITLFCGVKERKENSKVHSERMSF 279
Cdd:cd17332    160 VAYFGGGNASRG-----------------------------YFLTALIIGIIGIILLLICFFGTRERVVPPEEEKSKLPL 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  280 FRGIRLVMGHGPYAKLVMGFLFTSLAFMLLEGNFALFCSYTLGFRDDFQNVLLVVMLSATLTIPFWQWFLTRFGKKTAVY 359
Cdd:cd17332    211 LKSLKALLKNRPFLILLLAYLLYFLAFNIVNTVLVYYFKYVLGGRAELVLLLLLILSGALLALLPWPPLKKRFGKKKAFF 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  360 VGTTIVIPF-LITVVLMKSNLIVTYVIAIASGVSIAAAFLLPWSMLPDVVDDFKVLNPesQGHEAIFYSFYVFFTKFASG 438
Cdd:cd17332    291 IGLLLAILGlLLLFFLPPGNLVLILVLAVLAGIGYGGANLLPWAMLADVIDYGELKTG--KRREGIFYSVMTFFRKLGLA 368
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1832123188  439 VSLGISTLSLDFAGYVTRGCTQPKAVDVTLKVLVSAAPVALIFIGLLIFTSYPINE 494
Cdd:cd17332    369 LAGALVGLILSLAGYVANAAAQSASALNGIRLLIAVLPAVLLLLALILMSFYPLDK 424
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
558-886 1.64e-95

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 306.79  E-value: 1.64e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  558 DKKFNLITRNLQEVLGEEKLK-LILMERELKVYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAFLDNmKAP 636
Cdd:PRK08560     2 EERLELITRNTEEVVTEEELReLLESKEEPKAYIGFEPSGKIHLGHLLTMNKLADLQKAGFKVTVLLADWHAYLND-KGD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  637 WELLELRVKYYEQVIKAMlesiGVPLDKLKFVKGTEYQLSREYTLDVYRLSSMVTEHDAKKAGAEVVKQVEHPLLSGLLY 716
Cdd:PRK08560    81 LEEIRKVAEYNKKVFEAL----GLDPDKTEFVLGSEFQLDKEYWLLVLKLAKNTTLARARRSMTIMGRRMEEPDVSKLVY 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  717 PGLQALDEEYLKVDAQFGGVDQRKIFTLAEKYLPSLGYTKRIHMMNPMVPGLTGS--KMSSSEEESKIDLLDKKEDIKKK 794
Cdd:PRK08560   157 PLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGgiKMSKSKPGSAIFVHDSPEEIRRK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  795 LKKAFCEPGNIQNNGVLSFVKHVLFPLHSEFAIKRDPKFGGDKVYTFYEELEKDFAEERIHPGDLKASVEVALDKLLDPI 874
Cdd:PRK08560   237 IKKAYCPPGEVEGNPVLEIAKYHIFPRYDPFVIERPEKYGGDLEYESYEELERDYAEGKLHPMDLKNAVAEYLIEILEPV 316
                          330
                   ....*....|..
gi 1832123188  875 RKKFETPELKKL 886
Cdd:PRK08560   317 REYLEEGPELLE 328
MelB COG2211
Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism];
30-509 4.90e-92

Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism];


Pssm-ID: 441813 [Multi-domain]  Cd Length: 447  Bit Score: 301.44  E-value: 4.90e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   30 SEEKRHLSVCNKLCYAVGGAPYQITGCALGFFLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTpWTRFGR 109
Cdd:COG2211      1 TAAKKKLSLKEKLAYGLGDLGLNLAFGLLSAYLLYFYTDVLGLSAALVGLILLVARLWDAITDPLIGALSDRT-RTRWGR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  110 MMPWIILSTPFAVMSYFLIWYVPPVDQT-KVVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYRMTVEVLG 188
Cdd:COG2211     80 RRPWILIGAIPLALSFVLLFTAPDLSPTgKLIYALVTYLLLGLAYTLVNIPYSALGAELTPDYEERTRLSSWRFAFAGLG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  189 TVIGTGIQGQIVGManapcipVGNDlnatfrnsgseanitqpdlsldkVRNAYMIASGVICAIYVLCAITLFCGVKERKE 268
Cdd:COG2211    160 GLLASVLPPPLVAA-------FGGD-----------------------AALGYRLTALIFAVLGLLAFLLTFFGTKERPV 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  269 NSKvhsERMSFFRGIRLVMGHGPYAKLVMGFLFTSLAFMLLEGNFALFCSYTLGFRDDFQNVLLVVM-LSATLTIPFWQW 347
Cdd:COG2211    210 PEE---EKVSLKESLKALLKNRPFLLLLLAYLLFFLALALVAALLLYYFKYVLGLSAALVGLLLALYfLAALLGAPLWPR 286
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  348 FLTRFGKKTAVYVGTTI-VIPFLITVVLMKSNLIVTYVIAIASGVSIAAAFLLPWSMLPDVVDDFKVLNPESQghEAIFY 426
Cdd:COG2211    287 LAKRFGKKKAFIIGLLLaALGLLLLFFLGPGNLWLLLVLAALAGIGLGAILVLPWAMLADVVDYDEWKTGRRR--EGLYF 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  427 SFYVFFTKFASGVSLGISTLSLDFAGYVTrGCTQPKAVDVTLKVLVSAAPVALIFIGLLIFTSYPINEKRRQGNRKLLNE 506
Cdd:COG2211    365 GIFTFAIKLGQALAGALAGLLLALFGYVA-GAAQSPSALTGIRLLFFLLPAVLLLLAALLLLFYPLTRERHAEIRAELAA 443

                   ...
gi 1832123188  507 QRE 509
Cdd:COG2211    444 RRA 446
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
586-870 1.56e-79

catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) catalytic core domain. TyrRS is a homodimer which attaches Tyr to the appropriate tRNA. TyrRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formationof the enzyme bound aminoacyl-adenylate. It contains the class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding.


Pssm-ID: 173902 [Multi-domain]  Cd Length: 269  Bit Score: 261.00  E-value: 1.56e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  586 LKVYWGTATTG-KPHVAYFVPMSKIADFLKAGCEVTILFADLHAFLDNMK--------APWELLELRVKYYEQVIKAMLE 656
Cdd:cd00805      1 LKVYIGFDPTApSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSgkseerklLDLELIRENAKYYKKQLKAILD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  657 SIgvPLDKLKFVKGTEYQLSrEYTLDVYRLSSMVTEHDAKKAGAEVVKQ--VEHPLLSGLLYPGLQALDEEYLKVDAQFG 734
Cdd:cd00805     81 FI--PPEKAKFVNNSDWLLS-LYTLDFLRLGKHFTVNRMLRRDAVKVRLeeEEGISFSEFIYPLLQAYDFVYLDVDLQLG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  735 GVDQRKIFTLAEKYLPSLGYTKRIHMMNPMVPGLTGSKM-SSSEEESKIDLLDKKEDIKKKLKKAFCEPgniqnngVLSF 813
Cdd:cd00805    158 GSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGGKMsKSEGNAIWDPVLDSPYDVYQKIRNAFDPD-------VLEF 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1832123188  814 VKHVLFPLHSEfaikrdpkfggdkvytfYEELEKDFAEErIHPGDLKASVEVALDKL 870
Cdd:cd00805    231 LKLFTFLDYEE-----------------IEELEEEHAEG-PLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
583-871 1.33e-61

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 212.14  E-value: 1.33e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  583 ERELKVYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAFL-DNMKAPWELLELRVKYYEQVIKAMLeSIGVP 661
Cdd:pfam00579    3 NRPLRVYSGIDPTGPLHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIgDPSKSPERKLLSRETVLENAIKAQL-ACGLD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  662 LDKLKFVKGTEYQLSREYTLDVYRLSSMVTEHDAKKAGaEVVKQVEHP---LLSGLLYPGLQALDEEYLKVDAQFGGVDQ 738
Cdd:pfam00579   82 PEKAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFK-DVKKRLEQGpgiSLGEFTYPLLQAYDILLLKADLQPGGSDQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  739 RKIFTLAEKYLPSLGY---TKRIHMMNPMVPGLTG-SKMSSSEEESKIDLLDKKEDIKKKLKKAFCEPGNiqNNGVLSFV 814
Cdd:pfam00579  161 WGNIELGRDLARRFNKkifKKPVGLTNPLLTGLDGgKKMSKSAGNSAIFLDDDPESVYKKIQKAYTDPDR--EVRKDLKL 238
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1832123188  815 KHVLFPlhseFAIKRDPKFGGDKVYTFYEELEKDFAEERIHPGDLKASVEVALDKLL 871
Cdd:pfam00579  239 FTFLSN----EEIEILEAELGKSPYREAEELLAREVTGLVHGGDLKKAAAEAVNKLL 291
PLN02610 PLN02610
probable methionyl-tRNA synthetase
894-1076 2.91e-59

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 218.88  E-value: 2.91e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  894 KNKNAVKVNPKKAEEEdEIIPSRLDLRVGKIVGVEKHPAADTLYLEKIDIGEEQPRTVVSGLVAYVSQEELQDRLVVVLC 973
Cdd:PLN02610   621 GKKAGGGGKSKAAAER-EIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGLVKYIPLEEMQNRKVCVLC 699
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  974 NLKPQKMRGIESQAMLLCASvDGEPKRVEPLDPPEGSAPGERVFVDGYtSGTPDDELKPKKKVFEKIQVDMKISDECIAQ 1053
Cdd:PLN02610   700 NLKPAAMRGIKSQAMVLAAS-NSDHTKVELVEPPESAAVGERVTFPGF-EGEPDDVLNPKKKVWETLQPDLHTNSELVAC 777
                          170       180
                   ....*....|....*....|...
gi 1832123188 1054 WNKKDLITKLGKITCKTLKGGSI 1076
Cdd:PLN02610   778 YKDVPFTTSAGVCKVASIANGSI 800
tRNA_bind_EMAP-II_like cd02799
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ...
914-1017 3.28e-57

tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of tRNA binding proteins, including Caenorhabditis elegans methionyl-tRNA synthetase (CeMetRS), human tyrosyl- tRNA synthetase (hTyrRS), Saccharomyces cerevisiae Arc1p, human p43 and EMAP2. CeMetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. A EMAP-II-like cytokine also is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain.


Pssm-ID: 239198 [Multi-domain]  Cd Length: 105  Bit Score: 192.06  E-value: 3.28e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  914 PSRLDLRVGKIVGVEKHPAADTLYLEKIDIGEEQPRTVVSGLVAYVSQEELQDRLVVVLCNLKPQKMRGIESQAMLLCAS 993
Cdd:cd02799      3 PSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLCAS 82
                           90       100
                   ....*....|....*....|....
gi 1832123188  994 VDGEPKrVEPLDPPEGSAPGERVF 1017
Cdd:cd02799     83 NADHEK-VELLEPPEGAKPGERVT 105
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
557-879 6.05e-49

tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up tryptophanyl-tRNA synthetases at scores of 0 and below. The proteins found by this model have a deep split between two groups. One group contains bacterial and organellar eukaryotic examples. The other contains archaeal and cytosolic eukaryotic examples. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272976 [Multi-domain]  Cd Length: 378  Bit Score: 178.74  E-value: 6.05e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  557 PDKKFNLITRNLQEVLGEEKLKLI--LMERELKVYWGTATTG-KPHVAYFVPMSKIADFLKAGCEVTILFADLHAFLDNM 633
Cdd:TIGR00234    1 MNNILLLLTKRGLEVQTPEEEKDLlkLLERPLKLYLGFDPTApSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  634 KAPWELLELR-----VKYYEQVIKAMLESIGVplDKLKFVKGTEYQLSREYTLDVYRLSSMVTEHDAKKAGAEVVKQVEH 708
Cdd:TIGR00234   81 TGKSEVRKILtreevQENAENIKKQIARFLDF--EKAKFVYNSEWLLKLNYTDFIRLLGKIFTVNRMLRRDAFSSRFEEN 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  709 PLLSGLLYPGLQALDEEYLKVDAQFGGVDQ----RKIFTLAEKYLPSLGYTKRIHMMNP---MVPGLTGS-KMSS--SEE 778
Cdd:TIGR00234  159 ISLHEFIYPLLQAYDFVYLNVDLQLGGSDQwfniRKGRDLARENLPSLQFGLTVPLLTPadgEKMGKSLGgAVSLdeGKY 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  779 ESKIDLLDKKEDIKKKLKKAFCEPGN----------------IQNNGVLSFVKHVLFP------------------LHSE 824
Cdd:TIGR00234  239 DFYQKVINTPDELVKKYLKLFTFLGLeeieqlvelkgpnpreVKENLALEITKYVHGPeaalaaeeiseaifsgglNPDE 318
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1832123188  825 FAIKRDPKFGGDKVYTFYEELEKDFAEERIHPGDLK-ASVEVA--LDKLLDPIRKKFE 879
Cdd:TIGR00234  319 VPIFRPEKFGGPITLADLLVLSGLFPSKSEARRDIKnGGVYINgeKVEDLEPIRKELE 376
gph TIGR00792
sugar (Glycoside-Pentoside-Hexuronide) transporter; The Glycoside-Pentoside-Hexuronide (GPH): ...
41-496 1.98e-44

sugar (Glycoside-Pentoside-Hexuronide) transporter; The Glycoside-Pentoside-Hexuronide (GPH):Cation Symporter Family (TC 2.A.2) GPH:cation symporters catalyze uptake of sugars in symport with a monovalent cation (H+ or Na+). Members of this family includes transporters for melibiose, lactose, raffinose, glucuronides, pentosides and isoprimeverose. Mutants of two groups of these symporters (the melibiose permeases of enteric bacteria, and the lactose permease of Streptococcus thermophilus) have been isolated in which altered cation specificity is observed or in which sugar transport is uncoupled from cation symport (i.e., uniport is catalyzed). The various members of the family can use Na+, H+ or Li, Na+ or Li+, H+ or Li+, or only H+ as the symported cation. All of these proteins possess twelve putative transmembrane a-helical spanners. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273270  Cd Length: 437  Bit Score: 167.04  E-value: 1.98e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   41 KLCYAVGGAPYQITGCALGFFLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTPwTRFGRMMPWI-ILSTP 119
Cdd:TIGR00792    1 KLSYGFGDFGNDFIFAIVSTYLLFFYTDVLGLSAAFVGTLFLVARILDAITDPIMGNIVDRTR-TRWGKFRPWLlIGAIP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  120 FAVMSyFLIWYVPPVDQT-KVVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYRMtvevlgtvIGTGIQGQ 198
Cdd:TIGR00792   80 FSIVL-VLLFTTPDFSGTgKLVYAYITYILLGLFYSFVNIPYWSLVPAITLDPRERESLSTFRR--------FGATLGGL 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  199 IVGMAnapCIPVGNDLNATFRNSGseanitqpdlsldkvrnaYMIASGVICAIYVLCAITLFCGVKERKENSKVHSERMS 278
Cdd:TIGR00792  151 LVAVI---VLPLVSYFGGGDDKFG------------------WFMFALVLALIGVVSLIICFFGTKERYSEIPKNIEKKL 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  279 FFRGI-RLVMGHGPYAKLVMGFLFTSLAFMLLEGNFALFCSYTLGFRDDFQNVLLVVMLSATLTIPFWQWFLTRFGKKTA 357
Cdd:TIGR00792  210 SLKQIfKALFKNDQLLILCLAYLFYNLAFNIKNGVQVYYFTYVLGDPELFSYMGSIAIVAGLIGVLLFPRLVKKFGRKIL 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  358 VYVGTTIVIPFLITVVLMKSNLIVTYVIAIASGVSIAAAFLLPWSMLPDVVDDFKVLNpesqGH--EAIFYSFYVFFTKF 435
Cdd:TIGR00792  290 FAGGILLMVLGYLIFFFAGSNLPLILVLIILAGFGQNIVTGLVWALVADTVDYGEWKT----GIraEGLVYSVRTFVRKL 365
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832123188  436 ASGVSLGISTLSLDFAGYVTrGCTQPKAVDVTLKVLVSAAPVALIFIGLLIFTS-YPINEKR 496
Cdd:TIGR00792  366 GQALAGFFVGLILGIIGYVA-NAAQSPITLNGIKILMFAVPALFLLLAAIIIGRfYKLTEKK 426
PTZ00126 PTZ00126
tyrosyl-tRNA synthetase; Provisional
552-889 2.63e-44

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 240282 [Multi-domain]  Cd Length: 383  Bit Score: 165.25  E-value: 2.63e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  552 GEEMSPDKKFNLITRNLQEVLGEEKL-KLILMERELKVYWGTATTGKPHVAYFVPMSKIADFL-KAGCEVTILFADLHAF 629
Cdd:PTZ00126    32 QSKLSLEERVKLCLSIGEECIQPEELrELLKLKERPICYDGFEPSGRMHIAQGILKAINVNKLtKAGCVFVFWVADWFAL 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  630 LDNmKAPWELLELRV--KYYEQVIKAmlesIGVPLDKLKFVKGTEY--QLSREYTLDVYRLSSMVTEHDAKKAGAEVVKQ 705
Cdd:PTZ00126   112 LNN-KMGGDLEKIRKvgEYFIEVWKA----AGMDMDNVRFLWASEEinKNPNDYWLRVMDIARSFNITRIKRCSQIMGRS 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  706 V--EHPLlSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTLAEKY--LPSLGYtKRIHMMNPMVPGLT--GSKMSSSEEE 779
Cdd:PTZ00126   187 EgdEQPC-AQILYPCMQCADIFYLKADICQLGMDQRKVNMLAREYcdKKKIKK-KPIILSHHMLPGLLegQEKMSKSDPN 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  780 SKIDLLDKKEDIKKKLKKAFCEPGNIQNNGVLSFVKHVLFPLHSEFAIKRDPKFGGDKVYTFYEELEKDFAEERIHPGDL 859
Cdd:PTZ00126   265 SAIFMEDSEEDVNRKIKKAYCPPGVIEGNPILAYFKSIVFPAFNSFTVLRKEKNGGDVTYTTYEELEKDYLSGALHPGDL 344
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1832123188  860 KASVEVALDKLLDPIRKKFET-PELKKLTSL 889
Cdd:PTZ00126   345 KPALAKYLNLMLQPVRDHFQNnPEAKSLLSE 375
tRNA_bindingDomain cd02153
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in ...
919-1016 7.92e-37

The tRNA binding domain is also known as the Myf domain in literature. This domain is found in a diverse collection of tRNA binding proteins, including prokaryotic phenylalanyl tRNA synthetases (PheRS), methionyl-tRNA synthetases (MetRS), human tyrosyl-tRNA synthetase(hTyrRS), Saccharomyces cerevisiae Arc1p, Thermus thermophilus CsaA, Aquifex aeolicus Trbp111, human p43 and human EMAP-II. PheRS, MetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. The molecular chaperones Trbp111 and CsaA also contain this domain. CsaA has export related activities; Trbp111 is structure-specific recognizing the L-shape of the tRNA fold. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. An EMAP-II-like cytokine is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain. For homodimeric members of this group which include CsaA, Trbp111 and Escherichia coli MetRS this domain acts as a dimerization domain.


Pssm-ID: 239066 [Multi-domain]  Cd Length: 99  Bit Score: 133.80  E-value: 7.92e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  919 LRVGKIVGVEKHPAADTLYLEKIDIGEEQPRTVVSGLVAYVSQEELQDRLVVVLCNLKPQKMRGIESQAMLLCASVDG-E 997
Cdd:cd02153      1 LRVGKIVEAEPHPNADKLYVLKVDIGEEKPRQIVSGAANVYPPEELVGKKVVVAVNLKPKKLRGVESEGMLLSAEELGlE 80
                           90
                   ....*....|....*....
gi 1832123188  998 PKRVEPLDPPEGSAPGERV 1016
Cdd:cd02153     81 EGSVGILELPEDAPVGDRI 99
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
919-1015 6.01e-36

Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1), human tyrosyl-tRNA synthetase, and endothelial-monocyte activating polypeptide II. G4p1 binds specifically to tRNA form a complex with methionyl-tRNA synthetases. In human tyrosyl-tRNA synthetase this domain may direct tRNA to the active site of the enzyme. This domain may perform a common function in tRNA aminoacylation.


Pssm-ID: 396251 [Multi-domain]  Cd Length: 96  Bit Score: 131.21  E-value: 6.01e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  919 LRVGKIVGVEKHPAADTLYLEKIDIGEEQPRTVVSGLVAYVSQEELQDRLVVVLCNLKPQKMRGIESQAMLLCASvDGEP 998
Cdd:pfam01588    1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAE-ELDG 79
                           90
                   ....*....|....*..
gi 1832123188  999 KRVEPLDPPEGSAPGER 1015
Cdd:pfam01588   80 GSVGLLEPPADVPPGTK 96
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
844-1010 2.86e-29

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 124.91  E-value: 2.86e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  844 ELEKDFAEERIHPGDLKASVEVALDKLLDP-IRKKFETPELKKLtslayPSKNKNAVKVNPKKAEEEDEI-IP--SRLDL 919
Cdd:PRK12267   479 EEELTSWESLLEWGGLPAGTKVAKGEPLFPrIDVEEEIAYIKEQ-----MEGSAPKEPEEKEKKPEKPEItIDdfDKVEL 553
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  920 RVGKIVGVEKHPAADTLYLEKIDIGEEQPRTVVSGLVAYVSQEELQDRLVVVLCNLKPQKMRGIESQAMLLCASVDGEPK 999
Cdd:PRK12267   554 RVAEVLEAEKVEKSDKLLKLQVDLGEEEPRQIVSGIAKFYPPEELVGKKVVVVANLKPAKLMGEESQGMILAAEDDGKLT 633
                          170
                   ....*....|..
gi 1832123188 1000 RVEPLDP-PEGS 1010
Cdd:PRK12267   634 LLTVDKEvPNGS 645
metG PRK00133
methionyl-tRNA synthetase; Reviewed
883-1016 6.85e-28

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 121.03  E-value: 6.85e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  883 LKKLTSLAYPSKNKNAVKVNPKKAEEEDEI-IP--SRLDLRVGKIVGVEKHPAADTLYLEKIDIGEEQpRTVVSGLVAYV 959
Cdd:PRK00133   539 IEASKEAAAAKAAAAAAAAPLAEEPIAETIsFDdfAKVDLRVAKIVEAEKVEGADKLLKLTLDLGEET-RQVFSGIKSAY 617
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1832123188  960 SQEELQDRLVVVLCNLKPQKMRGIESQAMLLCASVDGEpkRVEPLDPPEGSAPGERV 1016
Cdd:PRK00133   618 DPEELVGKLVVMVANLAPRKMKFGVSEGMVLAAGPGGG--DLFLLEPDEGAKPGMRV 672
tRNA_bind_EcMetRS_like cd02800
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ...
915-1016 7.38e-28

tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like proteins. This family includes EcMetRS and Aquifex aeolicus Trbp111 (AaTrbp111). This domain has general tRNA binding properties. MetRS aminoacylates methionine transfer RNAs (tRNAmet). AaTrbp111 is structure-specific molecular chaperone recognizing the L-shape of the tRNA fold. AaTrbp111 plays a role in nuclear trafficking of tRNAs. The functional unit of EcMetRs and AaTrbp111 is a homodimer, this domain acts as the dimerization domain.


Pssm-ID: 239199 [Multi-domain]  Cd Length: 105  Bit Score: 108.36  E-value: 7.38e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  915 SRLDLRVGKIVGVEKHPAADTLYLEKIDIGEEqPRTVVSGLVAYVSQEELQDRLVVVLCNLKPQKMRGIESQAMLLCASV 994
Cdd:cd02800      7 AKVDLRVGKVLEAERVEGSDKLLKLTVDLGEE-ERQIVSGIAKFYPPEELVGKKVVVVANLKPRKLRGVESQGMILAAED 85
                           90       100
                   ....*....|....*....|..
gi 1832123188  995 DGEPKRvepLDPPEGSAPGERV 1016
Cdd:cd02800     86 GGKLKL---LTPDEEVEPGSRV 104
tRNA_bind_CsaA cd02798
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export ...
916-1016 1.75e-25

tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export related activities. CsaA has a putative tRNA binding activity. The functional unit of CsaA is a homodimer and this domain acts as a dimerization domain.


Pssm-ID: 239197 [Multi-domain]  Cd Length: 107  Bit Score: 101.93  E-value: 1.75e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  916 RLDLRVGKIVGVEKHP-AADTLYLEKIDIGEEQPRTVVSGLVAYVSQEELQDRLVVVLCNLKPQKMRGIESQAMLLCAsv 994
Cdd:cd02798      8 KVDLRVGTIVEVEDFPeARKPAYKLKVDFGEIGVKQSSAQITKYYKPEELIGRQVVAVVNFPPKQIAGVLSEVLVLGA-- 85
                           90       100
                   ....*....|....*....|..
gi 1832123188  995 DGEPKRVEPLDPPEGSAPGERV 1016
Cdd:cd02798     86 DDEGGEVVLLVPDREVPNGAKV 107
metG_C_term TIGR00399
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ...
884-1016 3.20e-25

methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model describes a region of the methionyl-tRNA synthetase that is present at the C-terminus of MetG in some species (E. coli, B. subtilis, Thermotoga maritima, Methanobacterium thermoautotrophicum), and as a separate beta chain in Aquifex aeolicus. It is absent in a number of other species (e.g. Mycoplasma genitalium, Mycobacterium tuberculosis), while Pyrococcus horikoshii has both a full length MetG and a second protein homologous to the beta chain only. Proteins hit by this model should be called methionyl-tRNA synthetase beta chain if and only if the model metG hits a separate protein not also hit by this model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273059 [Multi-domain]  Cd Length: 137  Bit Score: 102.12  E-value: 3.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  884 KKLTSLAYPSKNKNAVKVNPKKAEEEDEIIPS-----RLDLRVGKIVGVEKHPAADTLYLEKIDIGEEQpRTVVSGLVAY 958
Cdd:TIGR00399    2 KKIEELKLKGAKKKEKKDEGEKALEPQKETITiddfeKVDLRVGKILKAERVEKSDKLLKLKLDLGDEK-RQIVSGIAGY 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1832123188  959 VSQEELQDRLVVVLCNLKPQKMRGIESQAMLLCASVDGepKRVEPLDPPEGSAPGERV 1016
Cdd:TIGR00399   81 YTPEELVGKKVIVVANLKPAKLFGVKSEGMILAAEDDG--KVLFLLSPDQEAIAGERI 136
PRK09669 PRK09669
putative symporter YagG; Provisional
36-496 4.65e-25

putative symporter YagG; Provisional


Pssm-ID: 236610  Cd Length: 444  Bit Score: 109.81  E-value: 4.65e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   36 LSVCNKLCYAVGGapyqiTGCAL-----GFFLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTPwTRFGRM 110
Cdd:PRK09669     6 LTTKDKIGYGLGD-----TACNLvwqtvMLFLAYFYTDVFGLSAAIMGTMFLVVRVLDAVTDPLMGALVDRTR-TRHGQF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  111 MPWII-LSTPFAVmSYFLIWYVPPVDQT-KVVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYRMTVEVLG 188
Cdd:PRK09669    80 RPYLLwFAIPFGV-VCLLTFYTPDFGATgKIIYACVTYILLSLVYTAINVPYCAMPGAITNDPRERHSLQSWRFALSFIG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  189 tvigtgiqGQIVGMANAPCIPVgndlnatfrnsgseanITQPDlsldkVRNAYMIASGVICAIYVLCAITLFCGVKERKE 268
Cdd:PRK09669   159 --------GLIVSVIALPLVDI----------------LGKGD-----EQKGYFYAMMVMGLLGVVLFFCCFFMTKERYT 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  269 NSKVHSErmSFFRGIRLVMGHGPYaKLVMGFLFTSLAFMLLEGNFAL-FCSYTLGfRDDFQNVLLVVMLSATLTIPFWQW 347
Cdd:PRK09669   210 PEVDNSS--SVWKDLKLLLGNSQW-RIMFIFNVVLLTAVVTRGGATLyYVNYVLL-RPDLATLFLVTGMIAGLFGALLSE 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  348 FLtrFGKKTAVYVGTTIVIPFLITVVLM----KSNLIVTYVIAIASGVSIAAAFLLPWSMLPDVVDdfkVLNPES-QGHE 422
Cdd:PRK09669   286 RL--LGKFDRVRAFKWTIVAFVILSALIffipPSNVWLIFALNILFNFIQNLTTPLQWSMFSDVVD---YEEKRSgRRLD 360
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832123188  423 AIFYSFYVFFTKFasGVSLGISTL--SLDFAGYVTRGCTQPKAVDVTLKVLVSAAPVALIFIGLLIFTSYPINEKR 496
Cdd:PRK09669   361 GLVFSTNLFAIKL--GLAIGGAVVgwILAWVDYVGGAAVQSASVLTTINLLFTVIPGVLFAGMAIILNFYKLNDAR 434
PRK10429 PRK10429
melibiose:sodium transporter MelB;
34-527 1.01e-20

melibiose:sodium transporter MelB;


Pssm-ID: 182453  Cd Length: 473  Bit Score: 96.70  E-value: 1.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   34 RHLSVCNKLCYAVGGAPYQITGCALGFFLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTPwTRFGRMMPW 113
Cdd:PRK10429     1 MSISMTTKLSYGFGAFGKDFAIGIVYMYLMYYYTDVVGLSVGLVGTLFLVARIWDAINDPIMGWIVNNTR-SRWGKFKPW 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  114 IILST---PFAVMSYFLIWYVPpvDQTKVVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYRMTVEVLGTV 190
Cdd:PRK10429    80 ILIGTlanSVVLFLLFSAHLFE--GTAQYVFVCVTYILWGMTYTIMDIPFWSLVPTLTLDKREREQLVPYPRFFASLAGF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  191 IGTGIQGQIVGManapcipVGNDlnatFRNSGseanitqpdlsldkvrnaYMIASGVICAIYVLCAITLFCGVKER---K 267
Cdd:PRK10429   158 VTAGFTLPFVNY-------VGGG----DRGFG------------------FQMFTLVLIAFFIVSTIITLRNVHEVyssD 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  268 ENSKVHSERMSFFRGIRLVMGHGPYAKLVMGFLFTSLAFMLLEGNFALFCSYTLGFRDDFQNVLLVVMLSATLTIPFWQW 347
Cdd:PRK10429   209 NQVSAEGSHLTLKDIVALIYKNDQLSCLLGMALAYNIASNIINGFAIYYFTYVIGDADLFPYYLSYAGAANLVTLILFPR 288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  348 FLTRFGKKTaVYVGTTIViPFLITVVLMKSNLIVTYVIAIasgVSIAAAFL-----LPWS----MLPDVVD--DFKVlnp 416
Cdd:PRK10429   289 LVKSLSRRI-LWAGASIF-PVLSCGVLLLMGLAAPHNALL---IVIAGILLnigtaLFWVlqviMVADTVDygEYKL--- 360
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  417 eSQGHEAIFYSFYVFFTKFASGVSLGISTLSLDFAGYVTrGCTQPKAVDVTLKVLVSAAPVALIFIGLLI-FTSYPINE- 494
Cdd:PRK10429   361 -GIRCESIAYSVQTMVVKGGSAFAAFFIGVVLGLIGYVP-NVEQSAQTLLGMQFIMIGLPTLFFMITLVLyFRYYRLNGd 438
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1832123188  495 KRRQGNRKLLNEQRELESPADSSETELVNTGSV 527
Cdd:PRK10429   439 FLRRIQIHLLDKYRKVPPEPVHAEIPVGAVSDV 471
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
907-1013 5.75e-19

tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 92.61  E-value: 5.75e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  907 EEEDEIIPSRLD-LRVGKIVGVEKHPAADTLYLEKIDIGEEqPRTVVSGL-VAYVSQ---EELQDRLVVVLCNLKPQKMR 981
Cdd:COG0073     31 EVEDFEKVGGLDgLRVGKVLEAEPHPNADKLLVLQVDVGEE-TRQIVCGApNVYAGDkvpEALVGAQVPGVVNLKPRKIR 109
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1832123188  982 GIESQAMLLCASVDGEPKRVE-PLDPPEGSAPG 1013
Cdd:COG0073    110 GVESEGMLCSAEELGLGEDHDgILELPEDAPPG 142
PRK09848 PRK09848
glucuronide transporter; Provisional
61-496 3.67e-17

glucuronide transporter; Provisional


Pssm-ID: 182109 [Multi-domain]  Cd Length: 448  Bit Score: 85.61  E-value: 3.67e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   61 FLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTPwTRFGRMMPWIIL-STPFAVMSYFLIWYVPPVDQT-K 138
Cdd:PRK09848    30 FLLSYYTDVAGVGAAAAGTMLLLVRVFDAFADVFAGRVVDSVN-TRWGKFRPFLLFgTAPLMIFSVLVFWVPTDWSHSsK 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  139 VVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYRMtvevlgtvIGTGIQGQIVGMANAPCIpvgndlnatf 218
Cdd:PRK09848   109 VVYAYLTYMGLGLCYSLVNIPYGSLATAMTQQPQSRARLGAARG--------IAASLTFVCLAFLIGPSI---------- 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  219 rNSGSEANitqpdlsLDKVRNAYMIASGVI-CAIYVLCaitlfcgVKERKENSKVHSERMSFFRGIRLVMGHGPYAKLVM 297
Cdd:PRK09848   171 -KNSSPEE-------MVSVYHFWTIVLAIAgMVLYFIC-------FKSTRENVVRIVAQPSLKISLQTLKRNRPLFMLCI 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  298 GflftslAFMLLEGNFAL------FCSYTLGFRDDFQNVLLVVMLSATL-TIPFWQWFLTRFGKKTAVYVGTTI-VIPFL 369
Cdd:PRK09848   236 G------ALCVLISTFAVsasslfYVRYVLNDTGLFTVLVLVQNLVGTVaSAPLVPGMVARIGKKNTFLIGALLgTCGYL 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  370 ITVVLMKSNLIVTYVIAIASGVSIAAAFLLPWSMLPDVVDDFKVLNPESQghEAIFYSFYVFFTKFASGVSLGISTLSLD 449
Cdd:PRK09848   310 LFFWVSVWSLPVALVALAIASIGQGVTMTVMWALEADTVEYGEYLTGVRI--EGLTYSLFSFTRKCGQAIGGSIPAFILG 387
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1832123188  450 FAGYVTRGCTQPKAVdVTLKVLVSAAPVALIFIGLLIFTSYPINEKR 496
Cdd:PRK09848   388 LSGYIANQVQTPEVI-MGIRTSIALVPCGFMLLAFVIIWFYPLTDKK 433
PRK10089 PRK10089
chaperone CsaA;
916-1017 2.03e-16

chaperone CsaA;


Pssm-ID: 182232 [Multi-domain]  Cd Length: 112  Bit Score: 76.02  E-value: 2.03e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  916 RLDLRVGKIVGVEKHPAADTL-YLEKIDIGEE-QPRTVVSGLVAYVSQEELQDRLVVVLCNLKPQKMRGIESQAMLLCAS 993
Cdd:PRK10089    11 KVDIRVGTIVEAEPFPEARKPaYKLWIDFGEEiGVKQSSAQITPHYTPEELIGKQVVAVVNFPPKQIAGFMSEVLVLGFE 90
                           90       100
                   ....*....|....*....|....
gi 1832123188  994 vdGEPKRVEPLDPPEGSAPGERVF 1017
Cdd:PRK10089    91 --DEDGEVVLLTPDRPVPNGVKLV 112
MFS_MFSD12 cd17491
Major facilitator superfamily domain-containing protein 12; Major facilitator superfamily ...
41-491 4.57e-13

Major facilitator superfamily domain-containing protein 12; Major facilitator superfamily domain-containing protein 12 (MFSD12) protein subfamily includes a group of uncharacterized proteins similar to human MFSD2. MFSD2 is composed of two vertebrate members, MFSD2A and MFSD2B. MFSD2A is an LPC symporter that plays an essential role for blood-brain barrier formation and function. MFSD2B is a potential risk or protect factor in the prognosis of lung adenocarcinoma. The MFSD12 subfamily belongs to the Salmonella enterica Na+/melibiose symporter like (MelB-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 341044  Cd Length: 438  Bit Score: 72.68  E-value: 4.57e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   41 KLCYAVGGapYQITGCA-LGF-FLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTPW-TRFGRMMPWIILS 117
Cdd:cd17491      1 RIAYGVGH--VLNDLCAsMWFtYLLVYFHLVLGFSSALAGILLLIGQVADAISTPLVGYESDRTNGcGKYGRRKSWHLIG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  118 TPFAVMSYFLIWYVPP-----VDQT-KVVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYR--MTVevlgt 189
Cdd:cd17491     79 TICVLLSFPFIFNPCLgcsdsTSEWaKLVYYGPFIIIFQFGWAAVQISHLSLIPELTSDEHERVELTALRyaFTV----- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  190 vigtgiqgqivgMANapcIPVGNDLNATFRNSGSEANITQPDLSLDKVRNAYMIASGvicaIYVLCAITLFCGVKERKEN 269
Cdd:cd17491    154 ------------IAN---ITVYLIAWLLLQQSSGDSVNPTSAQDLPIFRNLSLIVVG----IGFLFSLLFHLGTKEPRPP 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  270 SKVHSERMSFFRGIRlvmghGPYAKLV-------MGFLFTSLAFML--LEGN-----FALFCSYTLGFRDDFQNVL-LVV 334
Cdd:cd17491    215 TDLSTTTNEGEEVTA-----PEEPRLTwkewlrePQFYQVALLYMCtrLIVNlsqvyIPLYLTETLQLPKESIAIVpLVM 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  335 MLSATLTiPFWQWFLTRF-GKKTAVYVGTTIVIPFLITVVLMKSNLIVTYVIAIASGVSIAAAFLL--PWSMLPDVVDDF 411
Cdd:cd17491    290 YVSGFLT-SLVMKPINKKiGRKITYLLGLLFVLGFCIWVWFQSGSSRTYEIYGAAVLLGVGSATLLvtSLSMTADLIGTN 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  412 KvlnpESqghEAIFYSFYVFFTKFASGVS-LGISTLsldfagyVTRGCTQPKAVDVTLKVLVSAAPVALIFIGLLIFTSY 490
Cdd:cd17491    369 T----ES---GAFVYGAMSFTDKLSNGIAvLIIQSL-------HPCNTELDECISYYYRVMVVVAGGVAILAGLLLLAFL 434

                   .
gi 1832123188  491 P 491
Cdd:cd17491    435 L 435
PRK11462 PRK11462
putative transporter; Provisional
36-193 2.86e-12

putative transporter; Provisional


Pssm-ID: 183145  Cd Length: 460  Bit Score: 70.35  E-value: 2.86e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   36 LSVCNKLCYAVGGAPYQITGCALGFFLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTPwTRFGRMMPWII 115
Cdd:PRK11462     6 LSVKEKIGYGMGDAASHIIFDNVMLYMMFFYTDIFGIPAGFVGTMFLVARALDAISDPCMGLLADRTR-SRWGKFRPWVL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  116 L-STPFAVMSyFLIWYVPPVDQT-KVVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYRMTVEVLGTVIGT 193
Cdd:PRK11462    85 FgALPFGIVC-VLAYSTPDLSMNgKMIYAAITYTLLTLLYTVVNIPYCALGGVITNDPTQRISLQSWRFVLATAGGMLST 163
PTZ00348 PTZ00348
tyrosyl-tRNA synthetase; Provisional
555-886 3.72e-12

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 173541 [Multi-domain]  Cd Length: 682  Bit Score: 70.70  E-value: 3.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  555 MSPDKKFNLITRNLQEVLGEEKLK-LILMERELKVYWGTATTGKPHVAYFVPMS-KIADFLKAGCEVTILFADLHAFLdN 632
Cdd:PTZ00348     1 MNTDERYKLLRSVGEECIQESELRnLIEKKPLIRCYDGFEPSGRMHIAQGIFKAvNVNKCTQAGCEFVFWVADWFALM-N 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  633 MKAPWELLELRV--KYYEQVIKAMlesiGVPLDKLKFVKGTEYQLSREYT-----LDVYRLSSMVTehdAKKAGAEVVKQ 705
Cdd:PTZ00348    80 DKVGGELEKIRIvgRYLIEVWKAA----GMDMDKVLFLWSSEEITNHANTywrtvLDIGRQNTIAR---IKKCCTIMGKT 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  706 VEHPLLSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTLAEKYLPSLGYT-KRIHMMNPMVPGLTG--SKMSSSEEESKI 782
Cdd:PTZ00348   153 EGTLTAAQVLYPLMQCADIFFLKADICQLGLDQRKVNMLAREYCDLIGRKlKPVILSHHMLAGLKQgqAKMSKSDPDSAI 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  783 DLLDKKEDIKKKLKKAFCePGNIQN----------------NGVLSFVKHVLFPLHSEFAIKrdpkfgGDKVYTFYEELE 846
Cdd:PTZ00348   233 FMEDTEEDVARKIRQAYC-PRVKQSaseitddgapvatddrNPVLDYFQCVVYARPGAVATI------DGTTYATYEDLE 305
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1832123188  847 KDFAEERIHPGDLKASVEVALDKLLDPIRKKF-ETPELKKL 886
Cdd:PTZ00348   306 QAFVSDEVSEEALKSCLIDEVNALLEPVRQHFaSNPEAHEL 346
tRNA_bind_bactPheRS cd02796
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ...
919-989 4.22e-10

tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. PheRS aminoacylate phenylalanine transfer RNAs (tRNAphe). PheRSs belong structurally to class II aminoacyl tRNA synthetases (aaRSs) but, as they aminoacylate the 2'OH of the terminal ribose of tRNA they belong functionally to class 1 aaRSs. This domain has general tRNA binding properties and is believed to direct tRNAphe to the active site of the enzyme.


Pssm-ID: 239196 [Multi-domain]  Cd Length: 103  Bit Score: 57.90  E-value: 4.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  919 LRVGKIVGVEKHPAADTLYLEKIDIGEEQPRTVVSGlvayvSQEELQDRLVVV---------LCNLKPQKMRGIESQAML 989
Cdd:cd02796      1 VVVGKVLEVEPHPNADKLNVCKVDIGENKPLQIVCG-----APNVRAGDKVVValpgavlpgGLKIKKRKLRGVESEGML 75
MFS_SLC45_SUC cd17313
Solute carrier family 45 and similar sugar transporters of the Major Facilitator Superfamily ...
42-430 9.96e-10

Solute carrier family 45 and similar sugar transporters of the Major Facilitator Superfamily of transporters; This group includes the solute carrier 45 (SLC45) family as well as plant sucrose transporters (SUCs or SUTs) and similar proteins such as Schizosaccharomyces pombe general alpha-glucoside permease. the SLC45 family is composed of four (A1-A4) vertebrate proteins as well as related insect proteins such as Drosophila sucrose transporter SCRT or Slc45-1. Members of this group transport sucrose and other sugars like maltose into the cell, with the concomitant uptake of protons (symport system). Plant sucrose transporters are crucial to carbon partitioning, playing a key role in phloem loading/unloading. They play a key role in loading and unloading of sucrose into the phloem and as a result, they control sucrose distribution throughout the whole plant and drive the osmotic flow system in the phloem. They also play a role in the exchange of sucrose between beneficial symbionts (mycorrhiza and Rhizobium) as well as pathogens such as nematodes and parasitic fungi. There are nine sucrose transporter genes in Arabidopsis and five in rice. Vertebrate SLC45 family proteins have been implicated in the regulation of glucose homoeostasis in the brain (SLC45A1), with skin and hair pigmentation (SLC45A2), and with prostate cancer and myelination (SLC45A3). Mutations in SLC45A2, also called MATP (membrane-associated transporter protein) or melanoma antigen AIM1, cause oculocutaneous albinism type 4 (OCA4), an autosomal recessive disorder of melanin biosynthesis that results in congenital hypopigmentation of ocular and cutaneous tissues. The SLC45 family and related sugar transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340871 [Multi-domain]  Cd Length: 421  Bit Score: 61.87  E-value: 9.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   42 LCYAVGGApyqitgcalgfFLQIYLLDVaLLDPFYASVILFVGRAWDAITDPTVGFLVSRTpWTRFGRMMPWIILSTPFA 121
Cdd:cd17313     13 FGWALENS-----------YVPPILQTL-GLSHALIGFVWTLGPILGLFVQPLVGSLSDRC-NSRIGRRRPFILVGAPLA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  122 VMSYFLI----WYVPPVDQTKVVWYLIFYCLFQTL-----QTCFHvPYSALTMFI-SSEQKERDSATAYRMTveVLGTVI 191
Cdd:cd17313     80 ALGLILIpnaaDIGLALGDGPRTWALVLFVLGIVLldfamNVCQG-PVRALLPDLvPPEQRSKANGIINFMG--GLGGVL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  192 GTGIQGqivgmanapcipVGNDLNATFRNSGSEanitqpdlsldkVRNAYMIASgvicAIYVLCAITLFCGVKER--KEN 269
Cdd:cd17313    157 GYLLGA------------ILWDHNWFGFALGGN------------LKVPFYIGA----IILLVCVLVTLFFVKEPplSPE 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  270 SKVHSERMS---FFRGIRLVMGHGPYA--KLVMGFLFTSLAFMLLEGNFALFC-------------SYTLGFRdDFQNVL 331
Cdd:cd17313    209 AGEHSENPSlgeVLKSLLKLLKIMPRSllRLLLVIFFWWIAFFPFELFFTDYMgeevyhgtsaassHYGAGVR-MGAWGL 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  332 LVVMLSATLTIPFWQWFLTRFGKKtAVYVGTTIVIPFLITVVLMKSNLIVTYVIAIASGVSIAAAFLLPWSMLPDVVDDf 411
Cdd:cd17313    288 LIFSLAFLIFSLPIGKLGKKIGRK-KVYLIGLVLFAVGMALMALVHNVTVALVLFALGGIGWATININPYPLVSDYHSE- 365
                          410       420
                   ....*....|....*....|
gi 1832123188  412 kvlNPESQG-HEAIFYSFYV 430
Cdd:cd17313    366 ---SGRGQGtDTGLLNLAIS 382
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
908-993 1.52e-07

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 55.56  E-value: 1.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  908 EEDEIIPSRLDLR---VGKIVGVEKHPAADTLYLEKIDIGEEqPRTVVSG-------LVAYVSQE--ELQDRLVvvlcnL 975
Cdd:PRK00629    31 EVEGVEDVAAGLSgvvVGKVLECEKHPNADKLRVCQVDVGEE-PLQIVCGapnvragDKVPVALPgaVLPGGFK-----I 104
                           90
                   ....*....|....*...
gi 1832123188  976 KPQKMRGIESQAMlLCAS 993
Cdd:PRK00629   105 KKAKLRGVESEGM-LCSA 121
AraJ COG2814
Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism];
247-410 2.28e-05

Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism];


Pssm-ID: 442063 [Multi-domain]  Cd Length: 348  Bit Score: 48.05  E-value: 2.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  247 VICAIYVLCAITLFCGVKERKenskvHSERMSFFRGIRLVMGHGPYAKLVMGFLFTSLAFMLLEGNFALFCSYTLGF-RD 325
Cdd:COG2814    169 VNAVLALLALLLLLRLLPESR-----PAARARLRGSLRELLRRPRLLLLLLLAFLLGFGFFALFTYLPLYLQEVLGLsAS 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  326 DFQNVLLVVMLSATLTIPFWQWFLTRFGKKTAVYVGTTIVIPFLITVVLMkSNLIVTYVIAIASGVSIAAAFLLPWSMLP 405
Cdd:COG2814    244 AAGLLLALFGLGGVLGALLAGRLADRFGRRRLLLIGLLLLALGLLLLALA-GSLWLLLLALFLLGFGFGLLFPLLQALVA 322

                   ....*
gi 1832123188  406 DVVDD 410
Cdd:COG2814    323 ELAPP 327
BtlA COG2270
MFS-type transporter involved in bile tolerance, Atg22 family [General function prediction ...
244-437 1.99e-04

MFS-type transporter involved in bile tolerance, Atg22 family [General function prediction only];


Pssm-ID: 441871 [Multi-domain]  Cd Length: 424  Bit Score: 45.14  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  244 ASGVICAI-YVLCAITLFCGVKERKENSKVHSERMSF--FRGIRLVMGHGPYAKLVMGFLFTSLAF-------MLLEGNF 313
Cdd:COG2270    185 ISFLLTALwWLLFALPLFLFLPERPRPGPAPPRGAVRagFRELRRTLRELRRYRDLLRFLLAYFFYrdgvqtvIAFAGIY 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  314 AlfcSYTLGFR-DDFQNVLLVVMLSATLTIPFWQWFLTRFGKKTAVYVGTTIVIPFLITVVLMKSNLIVtYVIAIASGVS 392
Cdd:COG2270    265 A---AGVLGFStTELIVFGLLVQIVAALGALLFGRLDDRIGPKRVILVSLVIWIVVCLAAYFLTTALAF-WILGLLIGLV 340
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1832123188  393 IAAAFLLPWSMLPDVVddfkvlnPEsqGHEAIFYSFYVFFTKFAS 437
Cdd:COG2270    341 MGGIQALSRSLLARLI-------PP--GREAEFFGLYALSGKAAS 376
NarK COG2223
Nitrate/nitrite transporter NarK [Inorganic ion transport and metabolism];
237-408 5.03e-04

Nitrate/nitrite transporter NarK [Inorganic ion transport and metabolism];


Pssm-ID: 441825 [Multi-domain]  Cd Length: 392  Bit Score: 43.72  E-value: 5.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  237 VRNAYMIASgvicAIYVLCAITLFCGVKERKENSKVHSErmSFFRGIRLVMGHGPYAKLVMGFLFTSLAFMLLEGNFALF 316
Cdd:COG2223    158 WRNAFLILG----ILLLVVAVLAWLFLRDPPAGAAAAAK--ASLRDQLEALRDPRFWLLSLLYFGTFGSFIGFSSWLPPY 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  317 csYTLGFRDDFQNVLLVVM---LSATLTIPFWQWFLTRFGKKTAVYVGTTIVIPFLITVVLMKSNLIVTYVIAIASGVSI 393
Cdd:COG2223    232 --LVDQFGLSAATAGLLAAlfaLLGALGRPLGGWLSDRIGGRRVLLIVFALMALGLLLLALALGSLWLFLVLFLLLGLAL 309
                          170
                   ....*....|....*
gi 1832123188  394 AAAFLLPWSMLPDVV 408
Cdd:COG2223    310 GGGNGAVFALVPDIF 324
MFS_1 pfam07690
Major Facilitator Superfamily;
295-496 1.59e-03

Major Facilitator Superfamily;


Pssm-ID: 429598 [Multi-domain]  Cd Length: 344  Bit Score: 42.02  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  295 LVMGFLFTSLAFMLLEGNFALFCSYTLGF-RDDFQNVLLVVMLSATLTIPFWQWFLTRFGKKTaVYVGTTIVIPFLITVV 373
Cdd:pfam07690    1 LFLAAFLAALGRSLLGPALPLLLAEDLGIsPTEIGLLLTLFSLGYALAQPLAGRLSDRFGRRR-VLLIGLLLFALGLLLL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  374 LMKSNLIVTYVIAIASGVSIAAAFLLPWSMLPDVVDDfkvlnpesqGHEAIFYSFYVFFTKFASGVSLGISTLSLDFAGY 453
Cdd:pfam07690   80 LFASSLWLLLVLRVLQGLGAGALFPAALALIADWFPP---------EERGRALGLVSAGFGLGAALGPLLGGLLASLFGW 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1832123188  454 VTrgctqpkavdvtlkVLVSAAPVALIFIGLLIFTSYPINEKR 496
Cdd:pfam07690  151 RA--------------AFLILAILSLLAAVLLLLPRPPPESKR 179
PTZ00348 PTZ00348
tyrosyl-tRNA synthetase; Provisional
798-905 1.95e-03

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 173541 [Multi-domain]  Cd Length: 682  Bit Score: 42.20  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  798 AFCEPgNIQNNGVLSFVKHVLFPlHSEFAIKRDPKFGGDKVYTFYEELEKDFAEERIHPGDLKASVevaLDKLLD--PIR 875
Cdd:PTZ00348   582 AYSAP-NEEANPVISVAQHLLAQ-QGALSIERGEANGGNVAYNTPEALVADCGSGALHPADLKAAV---SQLLLDrsAAA 656
                           90       100       110
                   ....*....|....*....|....*....|
gi 1832123188  876 KKFETPELKKLTSLAypsknKNAVKVNPKK 905
Cdd:PTZ00348   657 RALLSGELKKNMQTL-----RNAEKKLSKR 681
MFS_MMR_MDR_like cd17321
Methylenomycin A resistance protein (also called MMR peptide) and similar multidrug resistance ...
57-260 2.24e-03

Methylenomycin A resistance protein (also called MMR peptide) and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily; This family is composed of bacterial, fungal, and archaeal multidrug resistance (MDR) transporters including several proteins from Bacilli such as methylenomycin A resistance protein (also called MMR peptide), tetracycline resistance protein (TetB), and lincomycin resistance protein LmrB, as well as fungal proteins such as vacuolar basic amino acid transporters, which are involved in the transport into vacuoles of the basic amino acids histidine, lysine, and arginine in Saccharomyces cerevisiae, and aminotriazole/azole resistance proteins. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. For example, MMR confers resistance to the epoxide antibiotic methylenomycin while TetB resistance to tetracycline by an active tetracycline efflux. MMR-like MDR transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340879 [Multi-domain]  Cd Length: 370  Bit Score: 41.77  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188   57 ALGFFLQIYLLDVALLDPFYASVILFVGRAWDAITDPTVGFLVSRTPwtrfgrmmPWIILSTPFAVMSYFLIWYVpPVDQ 136
Cdd:cd17321    186 GLLFLLPLYLQGVLGYSPLQAGLALLPLALAMLVAAPLAGRLADRFG--------PRLVLVAGLLLTAVGLLLLA-LLGA 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  137 TKVVWYLIFYCLFQTLQTCFHVPYSALTMFISSEQKERDSATAYRMTVEVLGTVIGTGIQGQIVGMANAPCIPVGNDLNA 216
Cdd:cd17321    257 DSSVWLLLPGLVLLGLGLGLFATPLTNAALSSVPKEKAGAASGILNTARQLGGALGVALLGALLTAGLSANLGDSGVAAL 336
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1832123188  217 TFRNSGSEAnitqpdlslDKVRNAyMIASGVICAIYVLCAITLF 260
Cdd:cd17321    337 LSAAAAAFA---------AGFHLA-FLVAAALALLAALLALLLP 370
MFS_ShiA_like cd17369
Shikimate transporter and similar proteins of the Major Facilitator Superfamily; This ...
298-397 3.26e-03

Shikimate transporter and similar proteins of the Major Facilitator Superfamily; This subfamily is composed of Escherichia coli shikimate transporter (ShiA), inner membrane metabolite transport protein YhjE, and other putative metabolite transporters. ShiA is involved in the uptake of shikimate, an aromatic compound involved in siderophore biosynthesis. It has been suggested that YhjE may mediate the uptake of osmoprotectants. The ShiA-like subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340927 [Multi-domain]  Cd Length: 408  Bit Score: 41.36  E-value: 3.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  298 GFLFTSLAFMLLEGNFALFCSYTLGF--------RDDFQNVLLVVMLSATLTIPFWQWFLTRFGKKTAVYVGTTIVIPFL 369
Cdd:cd17369    229 ALLLAIGLRLAENVLFYLFTTFALSYatqtlgvdRSTVLLAVLIASVVAAITIPLFGWLSDRVGRRPVYLAGALLAALFA 308
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1832123188  370 ITVVLM---KSNLIVTYVIAIASGVSIAAAF 397
Cdd:cd17369    309 FPFFWLldtGSTWLIVLAAVVVLGVLHGMMY 339
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
588-773 4.02e-03

tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members of the family have a pfam00458 domain amino-terminal to the region described by this model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272975 [Multi-domain]  Cd Length: 327  Bit Score: 40.78  E-value: 4.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  588 VYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAFLdnmkAPWELLELRVKYYEQVIKAMLeSIGVPLDKLKF 667
Cdd:TIGR00233    5 VLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELFICIADLHAIT----VKQTDPDALRKAREELAADYL-AVGLDPEKTFI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  668 VKGTEYQlsrEYTLDVYRLSSMVTEHDAKKAGAEVVKQVEHPLLSGLL-YPGLQALDEEYLKVDAQFGGVDQRKIFTL-- 744
Cdd:TIGR00233   80 FLQSDYP---EHYELAWLLSCQVTFGELKRMTQFKDKSQAENVPIGLLsYPVLQAADILLYQADLVPVGIDQDQHLELtr 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1832123188  745 --AEK---------YLPSLGYTKrihmMNPMVPGLTGSKM 773
Cdd:TIGR00233  157 dlAERfnkkfknffPKPESLISK----FFPRLMGLSGKKM 192
PRK12285 PRK12285
tryptophanyl-tRNA synthetase; Reviewed
588-773 8.95e-03

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237037 [Multi-domain]  Cd Length: 368  Bit Score: 39.85  E-value: 8.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  588 VYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAFLDNMKAPWELLELRVKYyeqvikaMLESIGVPLDKLKf 667
Cdd:PRK12285    69 VYTGFMPSGPMHIGHKMVFDELKWHQEFGANVYIPIADDEAYAARGLSWEETREWAYEY-------ILDLIALGFDPDK- 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832123188  668 vkgTEYQLSREYTlDVYRLSSMVtehdAKKAGAEVVKQV----EHPLLSGLLYPGLQALDEEYLKVDAQFG------GVD 737
Cdd:PRK12285   141 ---TEIYFQSENI-KVYDLAFEL----AKKVNFSELKAIygftGETNIGHIFYPATQAADILHPQLEEGPKptlvpvGID 212
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1832123188  738 Q----RKIFTLAEKYLPSLGYTKRIHMMNPMVPGLTGSKM 773
Cdd:PRK12285   213 QdphiRLTRDIAERLHGGYGFIKPSSTYHKFMPGLTGGKM 252
 
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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