|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 816.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 1 MLDVKMIRQNFAEVQSKLATRGVQKEVlDRFLTLDERRRELLVQTEERKKLRNDVSGEIAALKRAKEDAADKIAQMKEVG 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLDV-DELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 81 SQIKQLDEEIAQIDEDIKEIATTLPNLPNDSVPVGKDEDDNVEVRRWAEPKAFAFEPKPHWEIAEELGILDFERGAKVSG 160
Cdd:COG0172 80 EEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 161 SRFVYYKGLGARLERALYNFMLDQHVyEHGYTEMITPYIVNSQAMFGTGQFPKFKEDVFQLADTDLTLIPTAEVPLTNYY 240
Cdd:COG0172 160 SRFYVLKGDGARLERALIQFMLDLHT-EHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGDDLYLIPTAEVPLTNLH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 241 QGEILEQEQLPAYFTALSPSFRSEAGSAGRDTRGLIRLHQFNKVEMVKFSDADHSYEELEKMTANAEDILQKLNLPYRVL 320
Cdd:COG0172 239 RDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 321 SLCTGDMGFSAAKTYDLEVWIPAQEMYREISSCSNCEDFQARRAMIRYRDQEGKIHYMHTLNGSGLAVGRTVAAVLENYQ 400
Cdd:COG0172 319 LLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDEDGKPEFVHTLNGSGLAVGRTLVAILENYQ 398
|
410 420
....*....|....*....|...
gi 498442821 401 NEDGSVTVPEVLVPYMGGLTKIE 423
Cdd:COG0172 399 QADGSVRIPEVLRPYMGGLEVIE 421
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-425 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 814.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 1 MLDVKMIRQNFAEVQSKLATRGVqKEVLDRFLTLDERRRELLVQTEERKKLRNDVSGEIAALKRAKEDAADKIAQMKEVG 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGF-PLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 81 SQIKQLDEEIAQIDEDIKEIATTLPNLPNDSVPVGKDEDDNVEVRRWAEPKAFAFEPKPHWEIAEELGILDFERGAKVSG 160
Cdd:PRK05431 80 EEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 161 SRFVYYKGLGARLERALYNFMLDQHVYEHGYTEMITPYIVNSQAMFGTGQFPKFKEDVFQLADTDLTLIPTAEVPLTNYY 240
Cdd:PRK05431 160 SRFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDDLYLIPTAEVPLTNLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 241 QGEILEQEQLPAYFTALSPSFRSEAGSAGRDTRGLIRLHQFNKVEMVKFSDADHSYEELEKMTANAEDILQKLNLPYRVL 320
Cdd:PRK05431 240 RDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRVV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 321 SLCTGDMGFSAAKTYDLEVWIPAQEMYREISSCSNCEDFQARRAMIRYRD-QEGKIHYMHTLNGSGLAVGRTVAAVLENY 399
Cdd:PRK05431 320 LLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDeGDGKPELVHTLNGSGLAVGRTLVAILENY 399
|
410 420
....*....|....*....|....*.
gi 498442821 400 QNEDGSVTVPEVLVPYMGGLTKIEKA 425
Cdd:PRK05431 400 QQADGSVTIPEVLRPYMGGLEVIPPK 425
|
|
| 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: 608.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 1 MLDVKMIRQNFAEVQSKLATRGVQKE-VLDRFLTLDERRRELLVQTEERKKLRNDVSGEIAALKRAKEDAADKI-AQMKE 78
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGLSVDiDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDKIEEIkKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 79 VGSQIKQLDEEIAQIDEDIKEIATTLPNLPNDSVPVGKDEDDNVEVRRWAEPKAFAFEPKPHWEIAEELGILDFERGAKV 158
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 159 SGSRFVYYKGLGARLERALYNFMLDQHVyEHGYTEMITPYIVNSQAMFGTGQFPKFKEDVFQLADTDLTLIPTAEVPLTN 238
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLLE-KNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTDLYLIPTAEVPLTN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 239 YYQGEILEQEQLPAYFTALSPSFRSEAGSAGRDTRGLIRLHQFNKVEMVKFSDADHSYEELEKMTANAEDILQKLNLPYR 318
Cdd:TIGR00414 240 LHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 319 VLSLCTGDMGFSAAKTYDLEVWIPAQEMYREISSCSNCEDFQARRAMIRYRDQE-GKIHYMHTLNGSGLAVGRTVAAVLE 397
Cdd:TIGR00414 320 VVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNkGKNKYVHTLNGTALAIGRTIVAILE 399
|
410
....*....|....*....
gi 498442821 398 NYQNEDGSVTVPEVLVPYM 416
Cdd:TIGR00414 400 NYQTEDGSVEIPEVLRKYL 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: 536.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 120 DNVEVRRWAEPKAFAFEPKPHWEIAEELGILDFERGAKVSGSRFVYYKGLGARLERALYNFMLDQHvYEHGYTEMITPYI 199
Cdd:cd00770 1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFL-TKRGFTPVIPPFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 200 VNSQAMFGTGQFPKFKEDVFQLADTDLTLIPTAEVPLTNYYQGEILEQEQLPAYFTALSPSFRSEAGSAGRDTRGLIRLH 279
Cdd:cd00770 80 VRKEVMEGTGQLPKFDEQLYKVEGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 280 QFNKVEMVKFSDADHSYEELEKMTANAEDILQKLNLPYRVLSLCTGDMGFSAAKTYDLEVWIPAQEMYREISSCSNCEDF 359
Cdd:cd00770 160 QFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 498442821 360 QARRAMIRYRDQE-GKIHYMHTLNGSGLAVGRTVAAVLENYQNEDGSVTVPEVLVPYM 416
Cdd:cd00770 240 QARRLNIRYRDKKdGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 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 ... |
223-399 |
3.19e-47 |
|
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: 159.88 E-value: 3.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 223 DTDLTLIPTAEVPLTNYYQGEILEQEQLPAYFTALSPSFRSEAGsagRDTRGLIRLHQFNKVEMVKFSDADHSYEELEKM 302
Cdd:pfam00587 8 GDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 303 TANAEDILQKLNLPYRVLSLCTGDMGFSAAKTYDLEVWIPAQEMYREISSCSNCEDFQARRAMIRYRDQEGKIHYMHTLN 382
Cdd:pfam00587 85 IKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNESKFPYMIH 164
|
170
....*....|....*..
gi 498442821 383 GSGLAVGRTVAAVLENY 399
Cdd:pfam00587 165 RAGLGVERFLAAILENN 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 816.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 1 MLDVKMIRQNFAEVQSKLATRGVQKEVlDRFLTLDERRRELLVQTEERKKLRNDVSGEIAALKRAKEDAADKIAQMKEVG 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLDV-DELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 81 SQIKQLDEEIAQIDEDIKEIATTLPNLPNDSVPVGKDEDDNVEVRRWAEPKAFAFEPKPHWEIAEELGILDFERGAKVSG 160
Cdd:COG0172 80 EEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 161 SRFVYYKGLGARLERALYNFMLDQHVyEHGYTEMITPYIVNSQAMFGTGQFPKFKEDVFQLADTDLTLIPTAEVPLTNYY 240
Cdd:COG0172 160 SRFYVLKGDGARLERALIQFMLDLHT-EHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGDDLYLIPTAEVPLTNLH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 241 QGEILEQEQLPAYFTALSPSFRSEAGSAGRDTRGLIRLHQFNKVEMVKFSDADHSYEELEKMTANAEDILQKLNLPYRVL 320
Cdd:COG0172 239 RDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 321 SLCTGDMGFSAAKTYDLEVWIPAQEMYREISSCSNCEDFQARRAMIRYRDQEGKIHYMHTLNGSGLAVGRTVAAVLENYQ 400
Cdd:COG0172 319 LLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDEDGKPEFVHTLNGSGLAVGRTLVAILENYQ 398
|
410 420
....*....|....*....|...
gi 498442821 401 NEDGSVTVPEVLVPYMGGLTKIE 423
Cdd:COG0172 399 QADGSVRIPEVLRPYMGGLEVIE 421
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-425 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 814.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 1 MLDVKMIRQNFAEVQSKLATRGVqKEVLDRFLTLDERRRELLVQTEERKKLRNDVSGEIAALKRAKEDAADKIAQMKEVG 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGF-PLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 81 SQIKQLDEEIAQIDEDIKEIATTLPNLPNDSVPVGKDEDDNVEVRRWAEPKAFAFEPKPHWEIAEELGILDFERGAKVSG 160
Cdd:PRK05431 80 EEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 161 SRFVYYKGLGARLERALYNFMLDQHVYEHGYTEMITPYIVNSQAMFGTGQFPKFKEDVFQLADTDLTLIPTAEVPLTNYY 240
Cdd:PRK05431 160 SRFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDDLYLIPTAEVPLTNLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 241 QGEILEQEQLPAYFTALSPSFRSEAGSAGRDTRGLIRLHQFNKVEMVKFSDADHSYEELEKMTANAEDILQKLNLPYRVL 320
Cdd:PRK05431 240 RDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRVV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 321 SLCTGDMGFSAAKTYDLEVWIPAQEMYREISSCSNCEDFQARRAMIRYRD-QEGKIHYMHTLNGSGLAVGRTVAAVLENY 399
Cdd:PRK05431 320 LLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDeGDGKPELVHTLNGSGLAVGRTLVAILENY 399
|
410 420
....*....|....*....|....*.
gi 498442821 400 QNEDGSVTVPEVLVPYMGGLTKIEKA 425
Cdd:PRK05431 400 QQADGSVTIPEVLRPYMGGLEVIPPK 425
|
|
| 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: 608.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 1 MLDVKMIRQNFAEVQSKLATRGVQKE-VLDRFLTLDERRRELLVQTEERKKLRNDVSGEIAALKRAKEDAADKI-AQMKE 78
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGLSVDiDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDKIEEIkKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 79 VGSQIKQLDEEIAQIDEDIKEIATTLPNLPNDSVPVGKDEDDNVEVRRWAEPKAFAFEPKPHWEIAEELGILDFERGAKV 158
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 159 SGSRFVYYKGLGARLERALYNFMLDQHVyEHGYTEMITPYIVNSQAMFGTGQFPKFKEDVFQLADTDLTLIPTAEVPLTN 238
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLLE-KNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTDLYLIPTAEVPLTN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 239 YYQGEILEQEQLPAYFTALSPSFRSEAGSAGRDTRGLIRLHQFNKVEMVKFSDADHSYEELEKMTANAEDILQKLNLPYR 318
Cdd:TIGR00414 240 LHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 319 VLSLCTGDMGFSAAKTYDLEVWIPAQEMYREISSCSNCEDFQARRAMIRYRDQE-GKIHYMHTLNGSGLAVGRTVAAVLE 397
Cdd:TIGR00414 320 VVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNkGKNKYVHTLNGTALAIGRTIVAILE 399
|
410
....*....|....*....
gi 498442821 398 NYQNEDGSVTVPEVLVPYM 416
Cdd:TIGR00414 400 NYQTEDGSVEIPEVLRKYL 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: 536.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 120 DNVEVRRWAEPKAFAFEPKPHWEIAEELGILDFERGAKVSGSRFVYYKGLGARLERALYNFMLDQHvYEHGYTEMITPYI 199
Cdd:cd00770 1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFL-TKRGFTPVIPPFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 200 VNSQAMFGTGQFPKFKEDVFQLADTDLTLIPTAEVPLTNYYQGEILEQEQLPAYFTALSPSFRSEAGSAGRDTRGLIRLH 279
Cdd:cd00770 80 VRKEVMEGTGQLPKFDEQLYKVEGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 280 QFNKVEMVKFSDADHSYEELEKMTANAEDILQKLNLPYRVLSLCTGDMGFSAAKTYDLEVWIPAQEMYREISSCSNCEDF 359
Cdd:cd00770 160 QFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 498442821 360 QARRAMIRYRDQE-GKIHYMHTLNGSGLAVGRTVAAVLENYQNEDGSVTVPEVLVPYM 416
Cdd:cd00770 240 QARRLNIRYRDKKdGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 297
|
|
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
1-420 |
7.60e-121 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 358.63 E-value: 7.60e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 1 MLDVKMIRQ----NFAEVQSKLATRGVQKEVLDRFLTLDERRRELLVQTEERKKLRNDVSGEIAALKRAKEDAADKIAQM 76
Cdd:PLN02678 1 MLDINLFREekggDPELIRESQRRRFASVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKEDATELIAET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 77 KEVGSQIKQLDEEIAQIDEDIKEIATTLPNLPNDSVPVGKDEDDNVEVRRWAEPKafaFEPKP--HWEIAEELGILDFER 154
Cdd:PLN02678 81 KELKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEANNAVVRTWGEKR---QEPKLknHVDLVELLGIVDTER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 155 GAKVSGSRFVYYKGLGARLERALYNFMLDqHVYEHGYTEMITPYIVNSQAMFGTGQFPKFKEDVFQLADT--DLTLIPTA 232
Cdd:PLN02678 158 GADVAGGRGYYLKGAGVLLNQALINFGLA-FLRKRGYTPLQTPFFMRKDVMAKCAQLAQFDEELYKVTGEgdDKYLIATS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 233 EVPLTNYYQGEILEQEQLPAYFTALSPSFRSEAGSAGRDTRGLIRLHQFNKVEM--VKFSDADHSYEELEKMTANAEDIL 310
Cdd:PLN02678 237 EQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQFEKVEQfcITSPNGNESWEMHEEMLKNSEDFY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 311 QKLNLPYRVLSLCTGDMGFSAAKTYDLEVWIPAQEMYREISSCSNCEDFQARRAMIRYRDQ---EGKIHYMHTLNGSGLA 387
Cdd:PLN02678 317 QSLGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDYQSRRLEIRYGQKksnEQTKQYVHLLNSTLTA 396
|
410 420 430
....*....|....*....|....*....|...
gi 498442821 388 VGRTVAAVLENYQNEDGsVTVPEVLVPYMGGLT 420
Cdd:PLN02678 397 TERTLCCILENYQTEDG-VRVPEVLQPFMGGIE 428
|
|
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
2-422 |
4.27e-92 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 286.82 E-value: 4.27e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 2 LDVKMIRQNFAEVQSKLATRGVQKEvLDRFLTLDERRRELLVQTEERKKLRNDVSGEIaalkRAKEDAADKIAQMKEvGS 81
Cdd:PLN02320 67 IDFKWIRDNKEAVAINIRNRNSNAN-LELVLELYENMLALQKEVERLRAERNAVANKM----KGKLEPSERQALVEE-GK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 82 QIKQ----LDEEIAQIDEDIKEIATTLPNLPNDSVPVGkDEDDNVEVRRWAEPKAFAFEPKPHWEIAEELGILDFERGAK 157
Cdd:PLN02320 141 NLKEglvtLEEDLVKLTDELQLEAQSIPNMTHPDVPVG-GEDSSAVRKEVGSPREFSFPIKDHLQLGKELDLFDFDAAAE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 158 VSGSRFVYYKGLGARLERALYNFMLDQhVYEHGYTEMITPYIVNSQAMFGTGQFPKFKE-DVFQLADTDLTLIPTAEVPL 236
Cdd:PLN02320 220 VSGSKFYYLKNEAVLLEMALVNWTLSE-VMKKGFTPLTTPEIVRSSVVEKCGFQPRGDNtQVYSIDGSDQCLIGTAEIPV 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 237 TNYYQGEILEQEQLPAYFTALSPSFRSEAGSAGRDTRGLIRLHQFNKVEMVKFSDADHSYEELEKMTANAEDILQKLNLP 316
Cdd:PLN02320 299 GGIHMDSILLESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESESFHEELIQIEEDLFTSLGLH 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 317 YRVLSLCTGDMGFSAAKTYDLEVWIPAQEMYREISSCSNCEDFQARRAMIRYRDQE-------------GKIHYMHTLNG 383
Cdd:PLN02320 379 FKTLDMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTDYQSRRLGIRYRPSEppqtnpkkgkgslGPTKFVHTLNA 458
|
410 420 430
....*....|....*....|....*....|....*....
gi 498442821 384 SGLAVGRTVAAVLENYQNEDGSVTVPEVLVPYMGGLTKI 422
Cdd:PLN02320 459 TACAVPRMIVCLLENYQQEDGSVVIPEPLRPFMGGLELI 497
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
223-399 |
3.19e-47 |
|
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: 159.88 E-value: 3.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 223 DTDLTLIPTAEVPLTNYYQGEILEQEQLPAYFTALSPSFRSEAGsagRDTRGLIRLHQFNKVEMVKFSDADHSYEELEKM 302
Cdd:pfam00587 8 GDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 303 TANAEDILQKLNLPYRVLSLCTGDMGFSAAKTYDLEVWIPAQEMYREISSCSNCEDFQARRAMIRYRDQEGKIHYMHTLN 382
Cdd:pfam00587 85 IKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNESKFPYMIH 164
|
170
....*....|....*..
gi 498442821 383 GSGLAVGRTVAAVLENY 399
Cdd:pfam00587 165 RAGLGVERFLAAILENN 181
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
1-108 |
2.86e-35 |
|
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: 126.16 E-value: 2.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 1 MLDVKMIRQNFAEVQSKLATRGVQKEVLDRFLTLDERRRELLVQTEERKKLRNDVSGEIAALKRAKEDAADKIAQMKEVG 80
Cdd:pfam02403 1 MLDIKLIRENPEAVKESLKKRGVDVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKEDADALIAEVKELK 80
|
90 100
....*....|....*....|....*...
gi 498442821 81 SQIKQLDEEIAQIDEDIKEIATTLPNLP 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 |
8.80e-23 |
|
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: 96.31 E-value: 8.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 170 GARLERALYNFMLDQHVyEHGYTEMITPYIVNSQAMFGTGQFPKFKEDVFQLAD-------TDLTLIPTAEVPLTNYYQG 242
Cdd:cd00670 1 GTALWRALERFLDDRMA-EYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDkgrelrdTDLVLRPAACEPIYQIFSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 243 EILEQEQLPAYFTALSPSFRSEAGSAgrdtRGLIRLHQFNKVEMVKFSDADHSYEELEKMTANAEDILQKLNLPYRVLSL 322
Cdd:cd00670 80 EILSYRALPLRLDQIGPCFRHEPSGR----RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 323 CTGDMGFSAA--------KTYDLEVWIPAQEMYREISSCSNCEDFQARRAMIRyRDQEGKIHYMHTLNGSGLaVGRTVAA 394
Cdd:cd00670 156 DDPFFGRGGKrgldagreTVVEFELLLPLPGRAKETAVGSANVHLDHFGASFK-IDEDGGGRAHTGCGGAGG-EERLVLA 233
|
..
gi 498442821 395 VL 396
Cdd:cd00670 234 LL 235
|
|
| PRK00960 |
PRK00960 |
seryl-tRNA synthetase; Provisional |
93-342 |
4.16e-08 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 234876 [Multi-domain] Cd Length: 517 Bit Score: 55.03 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 93 IDEDIKEIATTLPNLPNDSVPVGKDEDDNVEVRRwaEPKAFAFEPKPHwEIAEELGILdfERGAkvSGSRFVYYKGLgAR 172
Cdd:PRK00960 153 IDRAIKLVEEKLEKLEDLTFYVGKAEPGTIVSES--KKREITFDGDPT-EEAEKLGWV--KRFP--GRGQWFYTPPM-TK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 173 LERALYNFMLDQHVYEHGYTEMITPYIVNSQAMFGTGQF------------PKFKEDVFQ-------------------- 220
Cdd:PRK00960 225 LFRAFEKLVIEEVLKPLGFDECLFPKLIPLEVMYKMRYLeglpegmyyvcpPKRDPEYFEefvdemmvkkevpieklkek 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 221 LADTDLTLIPTAEVPLTNYYQGEILEQEQLPAYFTALS-PSFRSEAGSAgrdtRGLIRLHQFNKVEMVKFSDADHSYEEL 299
Cdd:PRK00960 305 LRDPGYVLAPAQCEPFYQFFQGETVDVDELPIKFFDRSgWTYRWEGGGA----HGLERVNEFHRIEIVWLGTPEQVEEIR 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 498442821 300 EKMTANAEDILQKLNLPYRVLSLCT-----------GDMGFSAAKTYDLEVWIP 342
Cdd:PRK00960 381 DELLKYAHILAEKLDLEYWREVGDDpfylegrgledRGIEFPDVPKYEMELWLP 434
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
181-397 |
4.06e-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.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 48.13 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 181 MLDQHVYEHGYTEMITPYIVNSQAMFGTGQFPK--------FKEDVFQLADTDLTLIPTAEVPLTNYYQGEILEQEQLPA 252
Cdd:cd00772 41 VLDKMFKEHGAQNALFPFFILASFLEKEAEHDEgfskelavFKDAGDEELEEDFALRPTLEENIGEIAAKFIKSWKDLPQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 253 YFTALSPSFRSEAgsagRDTRGLIRLHQFNKVEMVKF-SDADHSYEELEKMTANAEDILQKL-NLPYRVLSLCTGDMGFS 330
Cdd:cd00772 121 HLNQIGNKFRDEI----RPRFGFLRAREFIMKDGHSAhADAEEADEEFLNMLSAYAEIARDLaAIDFIEGEADEGAKFAG 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498442821 331 AAKTYDLEVWIP-AQEMYREISSCSNCEDFQARRAMIRYRDQEGKIHYMHTlNGSGLAVGRTVAAVLE 397
Cdd:cd00772 197 ASKSREFEALMEdGKAKQAETGHIFGEGFARAFDLKAKFLDKDGKEKFFEM-GCWGIGISRFIGAIIE 263
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
182-328 |
1.06e-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. 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: 46.80 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 182 LDQHVYEHGYTEMITPyIVNSQAMF-GTGQFPKFKEDVFQLAD---TDLTLIPTAEVPLTNYYQGEILEQEQLPAYFTAL 257
Cdd:cd00779 41 IREEMNKIGAQEILMP-ILQPAELWkESGRWDAYGPELLRLKDrhgKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQI 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498442821 258 SPSFRSEAgsagRDTRGLIRLHQFNKVEMVKF-SDADHSYEELEKMTANAEDILQKLNLPYRVLSLCTGDMG 328
Cdd:cd00779 120 QTKFRDEI----RPRFGLMRGREFLMKDAYSFdIDEESLEETYEKMYQAYSRIFKRLGLPFVKVEADSGAIG 187
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
7-122 |
2.07e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 7 IRQNFAEVQSKLatrgvQKEVLDRFLTLDERRRELLVQTEERKKLRNDVSgEIAALKRAKEDaadkiaQMKEVGSQIKQL 86
Cdd:pfam15921 108 LRQSVIDLQTKL-----QEMQMERDAMADIRRRESQSQEDLRNQLQNTVH-ELEAAKCLKED------MLEDSNTQIEQL 175
|
90 100 110
....*....|....*....|....*....|....*...
gi 498442821 87 DEEIAQIDEDIKEIATTLPNLPNDSvpvGKD--EDDNV 122
Cdd:pfam15921 176 RKMMLSHEGVLQEIRSILVDFEEAS---GKKiyEHDSM 210
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2-105 |
5.62e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 2 LDVKMIRQNFAEVQSKLATRGVQKEV--LDRFLTLDERRR-----ELLVQTEERKKLRNDVSGEIAALKRAKEDAADKIA 74
Cdd:COG1579 66 LEIEEVEARIKKYEEQLGNVRNNKEYeaLQKEIESLKRRIsdledEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
90 100 110
....*....|....*....|....*....|.
gi 498442821 75 QMKEvgsQIKQLDEEIAQIDEDIKEIATTLP 105
Cdd:COG1579 146 ELDE---ELAELEAELEELEAEREELAAKIP 173
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7-104 |
3.85e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 7 IRQNFAEVQSKLATRGVQKEVLDRfLTLDERRRELLVQTEERKKLRNDVSG---EIAALKRAKEDAADKIAQMKEV---- 79
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAA-LRLWFAQRRLELLEAELEELRAELARleaELERLEARLDALREELDELEAQirgn 335
|
90 100
....*....|....*....|....*.
gi 498442821 80 -GSQIKQLDEEIAQIDEDIKEIATTL 104
Cdd:COG4913 336 gGDRLEQLEREIERLERELEERERRR 361
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
4-108 |
4.38e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.98 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 4 VKMIRQNFAEVQSKLATRGVQKEVLDRFLT-LDERRRELLVQTEERKKLrndvsgeIAALKRAKEDAADKIAQMKEvgsQ 82
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAeLEEERAALEALKAERQKL-------LARLEKELAELAAELAELQQ---E 221
|
90 100
....*....|....*....|....*.
gi 498442821 83 IKQLDEEIAQIDEDIKEIATTLPNLP 108
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTPAAG 247
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
25-116 |
8.76e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 37.97 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498442821 25 KEVLDRFLTLDERRRELLVQ----TEERKKLRNDVSGEIAALKRAKEDAADKIAQMKEVGSQIKQLDEEIAQIDEDIKEI 100
Cdd:COG1340 18 EELREEIEELKEKRDELNEElkelAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDEL 97
|
90
....*....|....*.
gi 498442821 101 ATTLPNLPNDSVPVGK 116
Cdd:COG1340 98 RKELAELNKAGGSIDK 113
|
|
| |
