|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-424 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 823.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 1 MLDLKRIRTDFDAVAAKLKTRGVSEDtLTTLKALDEQRRALLVQTEELKAQRNIASAAIAQAKRQKKDASQQIADMQQLA 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPLD-VDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 81 ANIKAIDAKLADIDQEITSIITVLPNTPHDSVPIGADEEDNVEIRRWGKPRQFDFDIKAHWDLGEALDILDWERGAKVTG 160
Cdd:PRK05431 80 EEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 161 ARFLFYKNLGARLERALYNFMLDEHLKE-GYQEIIPPYMVNHDSMFGTGQYPKFKEDTFELDGTNFVLIPTAEVPLTNYY 239
Cdd:PRK05431 160 SRFYVLKGDGARLERALIQFMLDLHTEEhGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDDLYLIPTAEVPLTNLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 240 RGDIIDGKELPIYFTAMSPSFRSEAGSAGRDTRGLIRLHQFHKVEMVKFAKPETSYEELEKMTANAEHILQKLKLPYRVL 319
Cdd:PRK05431 240 RDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRVV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 320 ALCTGDMGFSAAKTYDLEVWIPAQNTYREISSCSNTEDFQARRAQIRYRDEADGKVKLLHTLNGSGLAVGRTVAAILENY 399
Cdd:PRK05431 320 LLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEGDGKPELVHTLNGSGLAVGRTLVAILENY 399
|
410 420
....*....|....*....|....*
gi 504435268 400 QNEDGSVTIPEVLRPYMGGLELIKP 424
Cdd:PRK05431 400 QQADGSVTIPEVLRPYMGGLEVIPP 424
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1-423 |
0e+00 |
|
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 818.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 1 MLDLKRIRTDFDAVAAKLKTRGVSEDtLTTLKALDEQRRALLVQTEELKAQRNIASAAIAQAKRQKKDASQQIADMQQLA 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLD-VDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 81 ANIKAIDAKLADIDQEITSIITVLPNTPHDSVPIGADEEDNVEIRRWGKPRQFDFDIKAHWDLGEALDILDWERGAKVTG 160
Cdd:COG0172 80 EEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 161 ARFLFYKNLGARLERALYNFMLDEHLKEGYQEIIPPYMVNHDSMFGTGQYPKFKEDTFELDGTNFVLIPTAEVPLTNYYR 240
Cdd:COG0172 160 SRFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGDDLYLIPTAEVPLTNLHR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 241 GDIIDGKELPIYFTAMSPSFRSEAGSAGRDTRGLIRLHQFHKVEMVKFAKPETSYEELEKMTANAEHILQKLKLPYRVLA 320
Cdd:COG0172 240 DEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVVL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 321 LCTGDMGFSAAKTYDLEVWIPAQNTYREISSCSNTEDFQARRAQIRYRDEaDGKVKLLHTLNGSGLAVGRTVAAILENYQ 400
Cdd:COG0172 320 LCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDE-DGKPEFVHTLNGSGLAVGRTLVAILENYQ 398
|
410 420
....*....|....*....|...
gi 504435268 401 NEDGSVTIPEVLRPYMGGLELIK 423
Cdd:COG0172 399 QADGSVRIPEVLRPYMGGLEVIE 421
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-416 |
0e+00 |
|
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. The seryl-tRNA synthetases of two archaeal species, Methanococcus jannaschii and Methanobacterium thermoautotrophicum, differ considerably and are included in a different model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273066 [Multi-domain] Cd Length: 418 Bit Score: 620.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 1 MLDLKRIRTDFDAVAAKLKTRGVSEDTLT-TLKALDEQRRALLVQTEELKAQRNIASAAIAQAKRQKKDASQQI-ADMQQ 78
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGLSVDIDLeKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDKIEEIkKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 79 LAANIKAIDAKLADIDQEITSIITVLPNTPHDSVPIGADEEDNVEIRRWGKPRQFDFDIKAHWDLGEALDILDWERGAKV 158
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 159 TGARFLFYKNLGARLERALYNFMLDEHLKEGYQEIIPPYMVNHDSMFGTGQYPKFKEDTFELDGTNFVLIPTAEVPLTNY 238
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTDLYLIPTAEVPLTNL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 239 YRGDIIDGKELPIYFTAMSPSFRSEAGSAGRDTRGLIRLHQFHKVEMVKFAKPETSYEELEKMTANAEHILQKLKLPYRV 318
Cdd:TIGR00414 241 HRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 319 LALCTGDMGFSAAKTYDLEVWIPAQNTYREISSCSNTEDFQARRAQIRYRDEADGKVKLLHTLNGSGLAVGRTVAAILEN 398
Cdd:TIGR00414 321 VNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNKGKNKYVHTLNGTALAIGRTIVAILEN 400
|
410
....*....|....*...
gi 504435268 399 YQNEDGSVTIPEVLRPYM 416
Cdd:TIGR00414 401 YQTEDGSVEIPEVLRKYL 418
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
120-416 |
0e+00 |
|
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. SerRS synthetase is a homodimer.
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 548.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 120 DNVEIRRWGKPRQFDFDIKAHWDLGEALDILDWERGAKVTGARFLFYKNLGARLERALYNFMLDEHLKEGYQEIIPPYMV 199
Cdd:cd00770 1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 200 NHDSMFGTGQYPKFKEDTFELDGTNFVLIPTAEVPLTNYYRGDIIDGKELPIYFTAMSPSFRSEAGSAGRDTRGLIRLHQ 279
Cdd:cd00770 81 RKEVMEGTGQLPKFDEQLYKVEGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 280 FHKVEMVKFAKPETSYEELEKMTANAEHILQKLKLPYRVLALCTGDMGFSAAKTYDLEVWIPAQNTYREISSCSNTEDFQ 359
Cdd:cd00770 161 FEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDFQ 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 504435268 360 ARRAQIRYRDEADGKVKLLHTLNGSGLAVGRTVAAILENYQNEDGSVTIPEVLRPYM 416
Cdd:cd00770 241 ARRLNIRYRDKKDGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 297
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
217-399 |
6.70e-48 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 161.81 E-value: 6.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 217 TFELDGT-NFVLIPTAEVPLTNYYRGDIIDGKELPIYFTAMSPSFRSEAGsagRDTRGLIRLHQFHKVEMVKFAKPETSY 295
Cdd:pfam00587 2 KVEDENGdELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 296 EELEKMTANAEHILQKLKLPYRVLALCTGDMGFSAAKTYDLEVWIPAQNTYREISSCSNTEDFQARRAQIRYRDEaDGKV 375
Cdd:pfam00587 79 DELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDE-DNES 157
|
170 180
....*....|....*....|....
gi 504435268 376 KLLHTLNGSGLAVGRTVAAILENY 399
Cdd:pfam00587 158 KFPYMIHRAGLGVERFLAAILENN 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-424 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 823.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 1 MLDLKRIRTDFDAVAAKLKTRGVSEDtLTTLKALDEQRRALLVQTEELKAQRNIASAAIAQAKRQKKDASQQIADMQQLA 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPLD-VDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 81 ANIKAIDAKLADIDQEITSIITVLPNTPHDSVPIGADEEDNVEIRRWGKPRQFDFDIKAHWDLGEALDILDWERGAKVTG 160
Cdd:PRK05431 80 EEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 161 ARFLFYKNLGARLERALYNFMLDEHLKE-GYQEIIPPYMVNHDSMFGTGQYPKFKEDTFELDGTNFVLIPTAEVPLTNYY 239
Cdd:PRK05431 160 SRFYVLKGDGARLERALIQFMLDLHTEEhGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDDLYLIPTAEVPLTNLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 240 RGDIIDGKELPIYFTAMSPSFRSEAGSAGRDTRGLIRLHQFHKVEMVKFAKPETSYEELEKMTANAEHILQKLKLPYRVL 319
Cdd:PRK05431 240 RDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRVV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 320 ALCTGDMGFSAAKTYDLEVWIPAQNTYREISSCSNTEDFQARRAQIRYRDEADGKVKLLHTLNGSGLAVGRTVAAILENY 399
Cdd:PRK05431 320 LLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEGDGKPELVHTLNGSGLAVGRTLVAILENY 399
|
410 420
....*....|....*....|....*
gi 504435268 400 QNEDGSVTIPEVLRPYMGGLELIKP 424
Cdd:PRK05431 400 QQADGSVTIPEVLRPYMGGLEVIPP 424
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1-423 |
0e+00 |
|
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 818.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 1 MLDLKRIRTDFDAVAAKLKTRGVSEDtLTTLKALDEQRRALLVQTEELKAQRNIASAAIAQAKRQKKDASQQIADMQQLA 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLD-VDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 81 ANIKAIDAKLADIDQEITSIITVLPNTPHDSVPIGADEEDNVEIRRWGKPRQFDFDIKAHWDLGEALDILDWERGAKVTG 160
Cdd:COG0172 80 EEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 161 ARFLFYKNLGARLERALYNFMLDEHLKEGYQEIIPPYMVNHDSMFGTGQYPKFKEDTFELDGTNFVLIPTAEVPLTNYYR 240
Cdd:COG0172 160 SRFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGDDLYLIPTAEVPLTNLHR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 241 GDIIDGKELPIYFTAMSPSFRSEAGSAGRDTRGLIRLHQFHKVEMVKFAKPETSYEELEKMTANAEHILQKLKLPYRVLA 320
Cdd:COG0172 240 DEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVVL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 321 LCTGDMGFSAAKTYDLEVWIPAQNTYREISSCSNTEDFQARRAQIRYRDEaDGKVKLLHTLNGSGLAVGRTVAAILENYQ 400
Cdd:COG0172 320 LCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDE-DGKPEFVHTLNGSGLAVGRTLVAILENYQ 398
|
410 420
....*....|....*....|...
gi 504435268 401 NEDGSVTIPEVLRPYMGGLELIK 423
Cdd:COG0172 399 QADGSVRIPEVLRPYMGGLEVIE 421
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-416 |
0e+00 |
|
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. The seryl-tRNA synthetases of two archaeal species, Methanococcus jannaschii and Methanobacterium thermoautotrophicum, differ considerably and are included in a different model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273066 [Multi-domain] Cd Length: 418 Bit Score: 620.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 1 MLDLKRIRTDFDAVAAKLKTRGVSEDTLT-TLKALDEQRRALLVQTEELKAQRNIASAAIAQAKRQKKDASQQI-ADMQQ 78
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGLSVDIDLeKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDKIEEIkKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 79 LAANIKAIDAKLADIDQEITSIITVLPNTPHDSVPIGADEEDNVEIRRWGKPRQFDFDIKAHWDLGEALDILDWERGAKV 158
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 159 TGARFLFYKNLGARLERALYNFMLDEHLKEGYQEIIPPYMVNHDSMFGTGQYPKFKEDTFELDGTNFVLIPTAEVPLTNY 238
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTDLYLIPTAEVPLTNL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 239 YRGDIIDGKELPIYFTAMSPSFRSEAGSAGRDTRGLIRLHQFHKVEMVKFAKPETSYEELEKMTANAEHILQKLKLPYRV 318
Cdd:TIGR00414 241 HRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 319 LALCTGDMGFSAAKTYDLEVWIPAQNTYREISSCSNTEDFQARRAQIRYRDEADGKVKLLHTLNGSGLAVGRTVAAILEN 398
Cdd:TIGR00414 321 VNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNKGKNKYVHTLNGTALAIGRTIVAILEN 400
|
410
....*....|....*...
gi 504435268 399 YQNEDGSVTIPEVLRPYM 416
Cdd:TIGR00414 401 YQTEDGSVEIPEVLRKYL 418
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
120-416 |
0e+00 |
|
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. SerRS synthetase is a homodimer.
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 548.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 120 DNVEIRRWGKPRQFDFDIKAHWDLGEALDILDWERGAKVTGARFLFYKNLGARLERALYNFMLDEHLKEGYQEIIPPYMV 199
Cdd:cd00770 1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 200 NHDSMFGTGQYPKFKEDTFELDGTNFVLIPTAEVPLTNYYRGDIIDGKELPIYFTAMSPSFRSEAGSAGRDTRGLIRLHQ 279
Cdd:cd00770 81 RKEVMEGTGQLPKFDEQLYKVEGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 280 FHKVEMVKFAKPETSYEELEKMTANAEHILQKLKLPYRVLALCTGDMGFSAAKTYDLEVWIPAQNTYREISSCSNTEDFQ 359
Cdd:cd00770 161 FEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDFQ 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 504435268 360 ARRAQIRYRDEADGKVKLLHTLNGSGLAVGRTVAAILENYQNEDGSVTIPEVLRPYM 416
Cdd:cd00770 241 ARRLNIRYRDKKDGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 297
|
|
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
1-422 |
1.46e-122 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 363.26 E-value: 1.46e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 1 MLDLKRIRTDF----DAVAAKLKTRGVSEDTLTTLKALDEQRRALLVQTEELKAQRNIASAAIAQAKRQKKDASQQIADM 76
Cdd:PLN02678 1 MLDINLFREEKggdpELIRESQRRRFASVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKEDATELIAET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 77 QQLAANIKAIDAKLADIDQEITSIITVLPNTPHDSVPIGADEEDNVEIRRWGKPRQfDFDIKAHWDLGEALDILDWERGA 156
Cdd:PLN02678 81 KELKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEANNAVVRTWGEKRQ-EPKLKNHVDLVELLGIVDTERGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 157 KVTGARFLFYKNLGARLERALYNFMLDEHLKEGYQEIIPPYMVNHDSMFGTGQYPKFKEDTFEL--DGTNFVLIPTAEVP 234
Cdd:PLN02678 160 DVAGGRGYYLKGAGVLLNQALINFGLAFLRKRGYTPLQTPFFMRKDVMAKCAQLAQFDEELYKVtgEGDDKYLIATSEQP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 235 LTNYYRGDIIDGKELPIYFTAMSPSFRSEAGSAGRDTRGLIRLHQFHKVEMVKFAKPET--SYEELEKMTANAEHILQKL 312
Cdd:PLN02678 240 LCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQFEKVEQFCITSPNGneSWEMHEEMLKNSEDFYQSL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 313 KLPYRVLALCTGDMGFSAAKTYDLEVWIPAQNTYREISSCSNTEDFQARRAQIRYRDE--ADGKVKLLHTLNGSGLAVGR 390
Cdd:PLN02678 320 GIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDYQSRRLEIRYGQKksNEQTKQYVHLLNSTLTATER 399
|
410 420 430
....*....|....*....|....*....|..
gi 504435268 391 TVAAILENYQNEDGsVTIPEVLRPYMGGLELI 422
Cdd:PLN02678 400 TLCCILENYQTEDG-VRVPEVLQPFMGGIEFL 430
|
|
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
2-425 |
4.95e-100 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 307.23 E-value: 4.95e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 2 LDLKRIRTDFDAVAAKLKTRGvSEDTLTTLKALDEQRRALLVQTEELKAQRNiasaAIAQAKRQKKDASQQ---IADMQQ 78
Cdd:PLN02320 67 IDFKWIRDNKEAVAINIRNRN-SNANLELVLELYENMLALQKEVERLRAERN----AVANKMKGKLEPSERqalVEEGKN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 79 LAANIKAIDAKLADIDQEITSIITVLPNTPHDSVPIGAdeEDNVEIRRW-GKPRQFDFDIKAHWDLGEALDILDWERGAK 157
Cdd:PLN02320 142 LKEGLVTLEEDLVKLTDELQLEAQSIPNMTHPDVPVGG--EDSSAVRKEvGSPREFSFPIKDHLQLGKELDLFDFDAAAE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 158 VTGARFLFYKNLGARLERALYNFMLDEHLKEGYQEIIPPYMVNHDSMFGTGQYPKFKE-DTFELDGTNFVLIPTAEVPLT 236
Cdd:PLN02320 220 VSGSKFYYLKNEAVLLEMALVNWTLSEVMKKGFTPLTTPEIVRSSVVEKCGFQPRGDNtQVYSIDGSDQCLIGTAEIPVG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 237 NYYRGDIIDGKELPIYFTAMSPSFRSEAGSAGRDTRGLIRLHQFHKVEMVKFAKPETSYEELEKMTANAEHILQKLKLPY 316
Cdd:PLN02320 300 GIHMDSILLESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESESFHEELIQIEEDLFTSLGLHF 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 317 RVLALCTGDMGFSAAKTYDLEVWIPAQNTYREISSCSNTEDFQARRAQIRYRDE------------ADGKVKLLHTLNGS 384
Cdd:PLN02320 380 KTLDMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTDYQSRRLGIRYRPSeppqtnpkkgkgSLGPTKFVHTLNAT 459
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 504435268 385 GLAVGRTVAAILENYQNEDGSVTIPEVLRPYMGGLELIKPR 425
Cdd:PLN02320 460 ACAVPRMIVCLLENYQQEDGSVVIPEPLRPFMGGLELIKPK 500
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
217-399 |
6.70e-48 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 161.81 E-value: 6.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 217 TFELDGT-NFVLIPTAEVPLTNYYRGDIIDGKELPIYFTAMSPSFRSEAGsagRDTRGLIRLHQFHKVEMVKFAKPETSY 295
Cdd:pfam00587 2 KVEDENGdELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 296 EELEKMTANAEHILQKLKLPYRVLALCTGDMGFSAAKTYDLEVWIPAQNTYREISSCSNTEDFQARRAQIRYRDEaDGKV 375
Cdd:pfam00587 79 DELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDE-DNES 157
|
170 180
....*....|....*....|....
gi 504435268 376 KLLHTLNGSGLAVGRTVAAILENY 399
Cdd:pfam00587 158 KFPYMIHRAGLGVERFLAAILENN 181
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
1-108 |
1.58e-34 |
|
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.
Pssm-ID: 426757 [Multi-domain] Cd Length: 108 Bit Score: 124.24 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 1 MLDLKRIRTDFDAVAAKLKTRGVSEDTLTTLKALDEQRRALLVQTEELKAQRNIASAAIAQAKRQKKDASQQIADMQQLA 80
Cdd:pfam02403 1 MLDIKLIRENPEAVKESLKKRGVDVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKEDADALIAEVKELK 80
|
90 100
....*....|....*....|....*...
gi 504435268 81 ANIKAIDAKLADIDQEITSIITVLPNTP 108
Cdd:pfam02403 81 DELKALEAELKELEAELDKLLLTIPNIP 108
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
170-396 |
3.73e-26 |
|
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238359 [Multi-domain] Cd Length: 235 Bit Score: 105.55 E-value: 3.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 170 GARLERALYNFMLDEHLKEGYQEIIPPYMVNHDSMFGTGQYPKFKEDTF-------ELDGTNFVLIPTAEVPLTNYYRGD 242
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYtfedkgrELRDTDLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 243 IIDGKELPIYFTAMSPSFRSEAGSAgrdtRGLIRLHQFHKVEMVKFAKPETSYEELEKMTANAEHILQKLKLPYRVLALC 322
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGR----RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 323 TGDMGFSAA--------KTYDLEVWIPAQNTYREISSCSNTEDFQARRAQIRYRDEADGKVkllHTLNGSGLAVGRTVAA 394
Cdd:cd00670 157 DPFFGRGGKrgldagreTVVEFELLLPLPGRAKETAVGSANVHLDHFGASFKIDEDGGGRA---HTGCGGAGGEERLVLA 233
|
..
gi 504435268 395 IL 396
Cdd:cd00670 234 LL 235
|
|
| PRK00960 |
PRK00960 |
seryl-tRNA synthetase; Provisional |
165-341 |
3.86e-13 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 234876 [Multi-domain] Cd Length: 517 Bit Score: 70.82 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 165 FYKNLGARLERALYNFMLDEHLKE-GYQEIIPPYMVNHDSMFGTGQ---------Y---PKFKEDTFE------------ 219
Cdd:PRK00960 217 FYTPPMTKLFRAFEKLVIEEVLKPlGFDECLFPKLIPLEVMYKMRYleglpegmyYvcpPKRDPEYFEefvdemmvkkev 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 220 --------LDGTNFVLIPTAEVPLTNYYRGDIIDGKELPIYFTAMS-PSFRSEAGSAgrdtRGLIRLHQFHKVEMVKFAK 290
Cdd:PRK00960 297 pieklkekLRDPGYVLAPAQCEPFYQFFQGETVDVDELPIKFFDRSgWTYRWEGGGA----HGLERVNEFHRIEIVWLGT 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504435268 291 PETSYEELEKMTANAEHILQKLKLPYRVLALCT-----------GDMGFSAAKTYDLEVWIP 341
Cdd:PRK00960 373 PEQVEEIRDELLKYAHILAEKLDLEYWREVGDDpfylegrgledRGIEFPDVPKYEMELWLP 434
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
207-397 |
1.49e-06 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 49.11 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 207 TGQYPKFKEDTFEL---DGTNFVLIPTAEVPLTNYYRGDIIDGKELPIYFTAMSPSFRSEAgsagRDTRGLIRLHQFHKV 283
Cdd:cd00779 67 SGRWDAYGPELLRLkdrHGKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEI----RPRFGLMRGREFLMK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 284 EMVKF-AKPETSYEELEKMTANAEHILQKLKLPYRVLALCTGDMGFSAAKTYDLEVWIPAQNT------------Yreis 350
Cdd:cd00779 143 DAYSFdIDEESLEETYEKMYQAYSRIFKRLGLPFVKVEADSGAIGGSLSHEFHVLSPLKITKGievghifqlgtkY---- 218
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504435268 351 scsnTEDFQArraqirYRDEADGKVKLLHTlnGS-GLAVGRTVAAILE 397
Cdd:cd00779 219 ----SKALGA------TFLDENGKPKPLEM--GCyGIGVSRLLAAIIE 254
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
170-229 |
8.30e-06 |
|
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440210 [Multi-domain] Cd Length: 639 Bit Score: 48.10 E-value: 8.30e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504435268 170 GARLERALYNFMLDEHLKEGYQEIIPPYMVNhDSMFGT-GQYPKFKED--TFELDGTNFVLIP 229
Cdd:COG0441 270 GAIIRRELEDYIREKHRKAGYQEVKTPHILD-RELWETsGHWDHYRENmfPTESDGEEYALKP 331
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
181-397 |
1.75e-05 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 46.21 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 181 MLDEHLKE-GYQEIIPPYMV---------NHDSmFGTGQYPKFKEDTFELDGTNFVLIPTAEVPLTNYYRGDIIDGKELP 250
Cdd:cd00772 41 VLDKMFKEhGAQNALFPFFIlasflekeaEHDE-GFSKELAVFKDAGDEELEEDFALRPTLEENIGEIAAKFIKSWKDLP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 251 IYFTAMSPSFRSEAgsagRDTRGLIRLHQFHKVEMVKF-AKPETSYEELEKMTANAEHILQKL-KLPYRVLALCTGDMGF 328
Cdd:cd00772 120 QHLNQIGNKFRDEI----RPRFGFLRAREFIMKDGHSAhADAEEADEEFLNMLSAYAEIARDLaAIDFIEGEADEGAKFA 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 329 SAAKTYDLEVWIPAQNTYREISSCSNTEDF-QARRAQIRYRDEaDGKVKLLHTlNGSGLAVGRTVAAILE 397
Cdd:cd00772 196 GASKSREFEALMEDGKAKQAETGHIFGEGFaRAFDLKAKFLDK-DGKEKFFEM-GCWGIGISRFIGAIIE 263
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
57-107 |
4.13e-04 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 41.47 E-value: 4.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 504435268 57 AAIAQAKRQKKDASQQIADMQQLAANIKAIDAKLADIDQEITSIITVLPNT 107
Cdd:COG3167 46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELEQQLGELLKQLPSK 96
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
165-339 |
1.31e-03 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 40.91 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 165 FYKNLGARLERALYNFMLDEHLKEGYQEIIPPYMVNHDSMFGTGQYPKFKED--TFELDGTNFVLIPTAEVPLTNYYRGD 242
Cdd:PLN02908 315 FFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENmfVFEIEKQEFGLKPMNCPGHCLMFAHR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 243 IIDGKELPIYFTAMSPSFRSEAGSAgrdTRGLIRLHQFHKVEMVKFAKPETSYEELEKmtanaehILQKLKLPYRVLALc 322
Cdd:PLN02908 395 VRSYRELPLRLADFGVLHRNELSGA---LTGLTRVRRFQQDDAHIFCREDQIKDEVKG-------VLDFLDYVYEVFGF- 463
|
170 180
....*....|....*....|
gi 504435268 323 TGDMGFSA-AKTY--DLEVW 339
Cdd:PLN02908 464 TYELKLSTrPEKYlgDLETW 483
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
23-92 |
1.35e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 1.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 23 VSEDTLTTLKALDEQRRALLVQTEELKAQRNIASAAIAQAKRQKKDASQQIADMQQLAANIKAIDAKLAD 92
Cdd:COG3883 127 IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
4-96 |
7.55e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 4 LKRIRTDFDAVAAKLKTRGVSEDTLTTLKALDEQRRALLVQTE---------ELKAQRNIASAAIAQAKRQKKDASQQIA 74
Cdd:COG4913 254 LEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEleelraelaRLEAELERLEARLDALREELDELEAQIR 333
|
90 100
....*....|....*....|....*..
gi 504435268 75 -----DMQQLAANIKAIDAKLADIDQE 96
Cdd:COG4913 334 gnggdRLEQLEREIERLERELEERERR 360
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
3-101 |
9.18e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 37.96 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504435268 3 DLKRIRTDFDAVAAKLKTRGVSEDTL-TTLKALDEQRRALLVQTEELKAQRNIASAAIAQAKRQKKDASQQIADMQQLAA 81
Cdd:COG4372 88 QLQAAQAELAQAQEELESLQEEAEELqEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
|
90 100
....*....|....*....|..
gi 504435268 82 NIKAIDAKL--ADIDQEITSII 101
Cdd:COG4372 168 ALEQELQALseAEAEQALDELL 189
|
|
| |
