|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
331-717 |
1.48e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 331 KKAQE--DSAELARWEEENRRFEKQKNEAREKRKREEEQEERQFKESLKLLDESRREKERK---LQELLLRQKEEAEEEA 405
Cdd:PTZ00121 1516 KKAEEakKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKnmaLRKAEEAKKAEEARIE 1595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 406 LRRLANDSEIEQKLEKIRYENEQKA----LQNDHENSIQLQLLKDGGQKERQEIEDRRIKE-----KNEHEKRIKEQDNQ 476
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIkaeeLKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEeenkiKAAEEAKKAEEDKK 1675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 477 FIENQRQHEIEENERKMEFERKQTEHE--EKLQQMYEQFERDREEMQRQHQERADKMKQqweqimmmIKHKMWNDiieRN 554
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKkaEELKKKEAEEKKKAEELKKAEEENKIKAEE--------AKKEAEED---KK 1744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 555 WTNRLNVLRSANKKVAELFNRFFTEISIIQREIEK--SEDISMERKRVSIVLNTLTNSLKQEKELMTEEMKNLQIQYDNT 632
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAviEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDS 1824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 633 GKSFVWKIKESVeivayecgIFENVLREYSNKIQQKTLTSFDHDSITKTIKWQF----DNLSKFSRNIPTLAELKQNYSS 708
Cdd:PTZ00121 1825 KEMEDSAIKEVA--------DSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFnkekDLKEDDEEEIEEADEIEKIDKD 1896
|
....*....
gi 392921127 709 DMQNNTSSD 717
Cdd:PTZ00121 1897 DIEREIPNN 1905
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
379-632 |
3.94e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.51 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 379 LDESRREKERKLQELLLRQKEEAEEEALRRLandsEIEQKLEKIRYENE----QKALQNDHENSIQLQLLKDGG----QK 450
Cdd:pfam17380 355 QEERKRELERIRQEEIAMEISRMRELERLQM----ERQQKNERVRQELEaarkVKILEEERQRKIQQQKVEMEQiraeQE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 451 ERQEIEDRRIKEKNEHE-KRIKEQdnqfiENQRQHEIEEnERKMEFERKQTEHEeklqqmyeqFERDREEMQRQHQERAD 529
Cdd:pfam17380 431 EARQREVRRLEEERAREmERVRLE-----EQERQQQVER-LRQQEEERKRKKLE---------LEKEKRDRKRAEEQRRK 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 530 KMKQQWEQ-IMMMIKHKMWNDIIERNWTNRLN-VLRSANKKVAELFNRFFTEISIIQREIEKSEDISMERKRVsivlntl 607
Cdd:pfam17380 496 ILEKELEErKQAMIEEERKRKLLEKEMEERQKaIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRL------- 568
|
250 260
....*....|....*....|....*..
gi 392921127 608 tNSLKQEKELMTE--EMKNLQIQYDNT 632
Cdd:pfam17380 569 -EAMEREREMMRQivESEKARAEYEAT 594
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
330-540 |
5.15e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 330 NKKAQEDSAELARWEEENRRFEKQKNEAREKRKREEEQEERQFKESLKL---LDESRREKERKLQELLLRQKEEAEEEAL 406
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELeeeLEELEEELEEAEEELEEAEAELAEAEEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 407 RRLANDSEIEQKLEKIRYENEQKALQNDHENsIQLQLLKDGGQKERQEIEDRRIKEKNEHEKRIKEQDNQFIENQRQHEI 486
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAE-LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 392921127 487 EENERKMEFERKQTEHEEKLQQMYEQFERDREEMQRQHQERADKMKQQWEQIMM 540
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
432-534 |
9.19e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.79 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 432 QNDHENSIqLQLLKDGGQKERQEIEDRRIKEKNEHEKRIKEQDNQFIE-----NQRQHE--IEENERKMEFERKQTEHEe 504
Cdd:cd16269 179 KEAEAEAI-LQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEqkledQERSYEehLRQLKEKMEEERENLLKE- 256
|
90 100 110
....*....|....*....|....*....|.
gi 392921127 505 kLQQMYEQFERDREEMQRQ-HQERADKMKQQ 534
Cdd:cd16269 257 -QERALESKLKEQEALLEEgFKEQAELLQEE 286
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
380-630 |
9.95e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 380 DESRREKERKLQELLLRQKEEAEEEALRRLANDSEIEQKLEKIRYENEQ-------------------KALQNDHENSIQ 440
Cdd:TIGR02169 214 QALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISElekrleeieqlleelnkkiKDLGEEEQLRVK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 441 LQLLKDGGQKERQEiedRRIKEKNEHEKRIKEQDNQFIE--NQRQHEIEENERKMEFERKQ----TEHEEKLQQMYEQFE 514
Cdd:TIGR02169 294 EKIGELEAEIASLE---RSIAEKERELEDAEERLAKLEAeiDKLLAEIEELEREIEEERKRrdklTEEYAELKEELEDLR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 515 RDREEMQRQHQERADKMKQQWEQIMMMiKHKMwnDIIERNWTNRLNVLRSANKKVAEL----------FNRFFTEISIIQ 584
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKLEKL-KREI--NELKRELDRLQEELQRLSEELADLnaaiagieakINELEEEKEDKA 447
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 392921127 585 REIEKSEDISMERKRVSIVLNTLTNSLKQEKELMTEEMKNLQIQYD 630
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
331-717 |
1.48e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 331 KKAQE--DSAELARWEEENRRFEKQKNEAREKRKREEEQEERQFKESLKLLDESRREKERK---LQELLLRQKEEAEEEA 405
Cdd:PTZ00121 1516 KKAEEakKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKnmaLRKAEEAKKAEEARIE 1595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 406 LRRLANDSEIEQKLEKIRYENEQKA----LQNDHENSIQLQLLKDGGQKERQEIEDRRIKE-----KNEHEKRIKEQDNQ 476
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIkaeeLKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEeenkiKAAEEAKKAEEDKK 1675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 477 FIENQRQHEIEENERKMEFERKQTEHE--EKLQQMYEQFERDREEMQRQHQERADKMKQqweqimmmIKHKMWNDiieRN 554
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKkaEELKKKEAEEKKKAEELKKAEEENKIKAEE--------AKKEAEED---KK 1744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 555 WTNRLNVLRSANKKVAELFNRFFTEISIIQREIEK--SEDISMERKRVSIVLNTLTNSLKQEKELMTEEMKNLQIQYDNT 632
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAviEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDS 1824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 633 GKSFVWKIKESVeivayecgIFENVLREYSNKIQQKTLTSFDHDSITKTIKWQF----DNLSKFSRNIPTLAELKQNYSS 708
Cdd:PTZ00121 1825 KEMEDSAIKEVA--------DSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFnkekDLKEDDEEEIEEADEIEKIDKD 1896
|
....*....
gi 392921127 709 DMQNNTSSD 717
Cdd:PTZ00121 1897 DIEREIPNN 1905
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
379-632 |
3.94e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.51 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 379 LDESRREKERKLQELLLRQKEEAEEEALRRLandsEIEQKLEKIRYENE----QKALQNDHENSIQLQLLKDGG----QK 450
Cdd:pfam17380 355 QEERKRELERIRQEEIAMEISRMRELERLQM----ERQQKNERVRQELEaarkVKILEEERQRKIQQQKVEMEQiraeQE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 451 ERQEIEDRRIKEKNEHE-KRIKEQdnqfiENQRQHEIEEnERKMEFERKQTEHEeklqqmyeqFERDREEMQRQHQERAD 529
Cdd:pfam17380 431 EARQREVRRLEEERAREmERVRLE-----EQERQQQVER-LRQQEEERKRKKLE---------LEKEKRDRKRAEEQRRK 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 530 KMKQQWEQ-IMMMIKHKMWNDIIERNWTNRLN-VLRSANKKVAELFNRFFTEISIIQREIEKSEDISMERKRVsivlntl 607
Cdd:pfam17380 496 ILEKELEErKQAMIEEERKRKLLEKEMEERQKaIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRL------- 568
|
250 260
....*....|....*....|....*..
gi 392921127 608 tNSLKQEKELMTE--EMKNLQIQYDNT 632
Cdd:pfam17380 569 -EAMEREREMMRQivESEKARAEYEAT 594
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
330-540 |
5.15e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 330 NKKAQEDSAELARWEEENRRFEKQKNEAREKRKREEEQEERQFKESLKL---LDESRREKERKLQELLLRQKEEAEEEAL 406
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELeeeLEELEEELEEAEEELEEAEAELAEAEEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 407 RRLANDSEIEQKLEKIRYENEQKALQNDHENsIQLQLLKDGGQKERQEIEDRRIKEKNEHEKRIKEQDNQFIENQRQHEI 486
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAE-LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 392921127 487 EENERKMEFERKQTEHEEKLQQMYEQFERDREEMQRQHQERADKMKQQWEQIMM 540
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
436-539 |
9.05e-06 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 46.19 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 436 ENSIQLQLLKDGGQKERQEIEDRRIKEKNEHEKRIKEQ------DNQFIENQRQHEIEENERKMEFERKQTEHEEklQQM 509
Cdd:pfam05672 18 EKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEErarreeEARRLEEERRREEEERQRKAEEEAEEREQRE--QEE 95
|
90 100 110
....*....|....*....|....*....|
gi 392921127 510 YEQFERDREEMQRQHQERADKMKQQWEQIM 539
Cdd:pfam05672 96 QERLQKQKEEAEAKAREEAERQRQEREKIM 125
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
340-529 |
1.33e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 340 LARWEEENRRFEKQKNEAREKRKREEEQEERQFKESLKL------LDESRREKERKLQELLLRQKEEAEEEALRRLANDS 413
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELeelrleLEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 414 EIEQKLEKIRYENEQKALQNDHENSIQLQLLKDGGQKERQEIEDRRIKEKNEHEKRIKEQDNQFIENQRQHEiEENERKM 493
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE-ELAEELL 389
|
170 180 190
....*....|....*....|....*....|....*.
gi 392921127 494 EFERKQTEHEEKLQQMYEQFERDREEMQRQHQERAD 529
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
329-534 |
1.38e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 329 SNKKAQEDSAELARwEEENRRFEKQKNEAREKRKREEEQEERQFKESLKLLDESRREKERKLQELLLRQKEEAE---EEA 405
Cdd:COG1196 263 AELEAELEELRLEL-EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELeeeLEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 406 LRRLANDSEIEQKLEKIRYENEQKALQNDHENSIQLQLLKDGGQKERQEIEDRRIKEKN--EHEKRIKEQDNQFIENQRQ 483
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqlEELEEAEEALLERLERLEE 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 392921127 484 HEIEENERKMEFERKQTEHEEKLQQMYEQFERDREEMQRQHQERADKMKQQ 534
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
321-511 |
4.84e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 321 NNWRDnsgSNKKAQEDSAELARWEEENRRFEKQKNEAREKRKREEEQEERQFKESLKLLDESRREKERKLQ-----ELLL 395
Cdd:pfam02029 143 NKWST---EVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQngeeeVTKL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 396 RQKEEAEEEALRRLANDS-------EIEQKLEKIRYENEQKA-------LQNDHENSIQLQLLKdggqKERQEieDRRIK 461
Cdd:pfam02029 220 KVTTKRRQGGLSQSQEREeeaevflEAEQKLEELRRRRQEKEseefeklRQKQQEAELELEELK----KKREE--RRKLL 293
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 392921127 462 EknEHEKRIKEQdnqfiENQRQHEIEENERKM--EFERKQTEHEEKLQQMYE 511
Cdd:pfam02029 294 E--EEEQRRKQE-----EAERKLREEEEKRRMkeEIERRRAEAAEKRQKLPE 338
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
447-534 |
1.46e-04 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 45.50 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 447 GGQKERQEIEDRRIKEKNEHEKRIKEQdnqfIENQRQHEIEENERKMEFERKQTEHEEKLQQMYEQFERDREEMQRQHQE 526
Cdd:PTZ00266 427 GGRVDKDHAERARIEKENAHRKALEMK----ILEKKRIERLEREERERLERERMERIERERLERERLERERLERDRLERD 502
|
....*...
gi 392921127 527 RADKMKQQ 534
Cdd:PTZ00266 503 RLDRLERE 510
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
324-631 |
2.15e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 324 RDNSGSNKKAQEDSAELARWEEENRRFEKQKNEAREKRKREEEQEERQFKESLKLLDESRREKERKLQELLLRQKEEAEE 403
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 404 EALRRLANDSEIEQKLEKIRYENEQKALQNDHENSIQLQLLKDggQKERQEIEDRRIKEKNEHEK----RIKEQDNQFIE 479
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE--AEEAKKAEELKKKEAEEKKKaeelKKAEEENKIKA 1732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 480 NQRQHEIEENERKMEFERKQTEHEEKLQQMYEQFERDREEMQRQHQ--------ERADKMKQQWEQIMMMIKHKMWNdII 551
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEavieeeldEEDEKRRMEVDKKIKDIFDNFAN-II 1811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 552 ERNWTNRLNV------LRSANKKVAELFNRFFTEISIIQREIEKSEDISMERKRVSIVLNTLTNSLKQEKELMTEEMKNL 625
Cdd:PTZ00121 1812 EGGKEGNLVIndskemEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
....*.
gi 392921127 626 QIQYDN 631
Cdd:PTZ00121 1892 KIDKDD 1897
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
351-626 |
3.78e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 351 EKQKNEAREKRKREEEQEERQFKESLKLLDESRREKERKLQELLLRQKEEAEEEALRrlandSEIEQKLEKIRyenEQKA 430
Cdd:COG1196 206 ERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL-----AELEAELEELR---LELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 431 LQNDHENSIQLQLLKDGGQKERQEIEDRRIKEKNEHEKRIKEQDNQFIENQRQHEIEENERKMEFERKQTEHEEKLQQMY 510
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 511 EQFERDREEMQRQHQERADKMKQQweqimmmikhkmwndiiERNWTNRLNVLRSANKKVAELFNRFFTEISIIQREIEKS 590
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEEL-----------------EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
250 260 270
....*....|....*....|....*....|....*.
gi 392921127 591 EDISMERKRVSIVLNTLTNSLKQEKELMTEEMKNLQ 626
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
418-526 |
5.30e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.21 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 418 KLEKIRYENEQKALQNDHENSIQLQLLKdggQKERQEIEDRRIKEKNEHEKRIKEQDNQfIENQR----QHEIEENERKM 493
Cdd:pfam09731 293 HREIDQLSKKLAELKKREEKHIERALEK---QKEELDKLAEELSARLEEVRAADEAQLR-LEFERereeIRESYEEKLRT 368
|
90 100 110
....*....|....*....|....*....|...
gi 392921127 494 EFERKQTEHEEKLQQMYEQFErdrEEMQRQHQE 526
Cdd:pfam09731 369 ELERQAEAHEEHLKDVLVEQE---IELQREFLQ 398
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
432-534 |
9.19e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.79 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 432 QNDHENSIqLQLLKDGGQKERQEIEDRRIKEKNEHEKRIKEQDNQFIE-----NQRQHE--IEENERKMEFERKQTEHEe 504
Cdd:cd16269 179 KEAEAEAI-LQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEqkledQERSYEehLRQLKEKMEEERENLLKE- 256
|
90 100 110
....*....|....*....|....*....|.
gi 392921127 505 kLQQMYEQFERDREEMQRQ-HQERADKMKQQ 534
Cdd:cd16269 257 -QERALESKLKEQEALLEEgFKEQAELLQEE 286
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
380-630 |
9.95e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 380 DESRREKERKLQELLLRQKEEAEEEALRRLANDSEIEQKLEKIRYENEQ-------------------KALQNDHENSIQ 440
Cdd:TIGR02169 214 QALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISElekrleeieqlleelnkkiKDLGEEEQLRVK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 441 LQLLKDGGQKERQEiedRRIKEKNEHEKRIKEQDNQFIE--NQRQHEIEENERKMEFERKQ----TEHEEKLQQMYEQFE 514
Cdd:TIGR02169 294 EKIGELEAEIASLE---RSIAEKERELEDAEERLAKLEAeiDKLLAEIEELEREIEEERKRrdklTEEYAELKEELEDLR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 515 RDREEMQRQHQERADKMKQQWEQIMMMiKHKMwnDIIERNWTNRLNVLRSANKKVAEL----------FNRFFTEISIIQ 584
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKLEKL-KREI--NELKRELDRLQEELQRLSEELADLnaaiagieakINELEEEKEDKA 447
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 392921127 585 REIEKSEDISMERKRVSIVLNTLTNSLKQEKELMTEEMKNLQIQYD 630
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
378-540 |
1.13e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 378 LLDESRREKERKLQELLLRQKEEAEEEALRRLANDSEIEQKLEKIRYENEQKALQNDHENSIQLQLLKDGGQKERQEIED 457
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 458 RRIKEKNEHEKRIKEQDNQFIENQRQHEIEENERKMEFerkqtEHEEKLQQMYEQFERDREEMQRQHQERADKMKQQWEQ 537
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKL-----QEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
...
gi 392921127 538 IMM 540
Cdd:pfam02463 321 KEK 323
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
383-539 |
1.13e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.83 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 383 RREKERKLQELLLRQKEEAEEEALRRLANDSEIEQKLEKIRY---------ENEQKALQnDHENSIQLQLLKDGGQKERQ 453
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYrqeleeqieEREQKRQE-EYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 454 EIEDRRIKEKNEHEKRIKEQDNQFIENQRQHEIEENERKMEFERKQTEHEEKLQQMYEQFERDREEMQRQHQERADKMKQ 533
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRA 191
|
....*.
gi 392921127 534 QWEQIM 539
Cdd:pfam13868 192 QQEKAQ 197
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
317-537 |
1.19e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 317 SGIYNNWRDNSGSNKKAQEDSAELARWEEENRRFEKQKneareKRKREEEQEERQFkeslKLLDESRREKERKLQELLLR 396
Cdd:pfam15709 322 KALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEE-----QRRLQQEQLERAE----KMREELELEQQRRFEEIRLR 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 397 QKEEAEEEALRrlandSEIEQKLEKIRYENEQKALQNDHENSIQLQLLkdggQKERQEIEDRRIKEKnehEKRIKEQDNQ 476
Cdd:pfam15709 393 KQRLEEERQRQ-----EEEERKQRLQLQAAQERARQQQEEFRRKLQEL----QRKKQQEEAERAEAE---KQRQKELEMQ 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392921127 477 FIENQ-RQHEIEENERkMEFERKQTEHEEKLQQMYEQFERDREEMQRQHQERAdkMKQQWEQ 537
Cdd:pfam15709 461 LAEEQkRLMEMAEEER-LEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEA--MKQAQEQ 519
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
377-536 |
2.09e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.06 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 377 KLLDESRREKERklQELLLRQKEEAEeealrrlandseiEQKLEKIRYENEQKALQNDHENSIQLQLLKDGGQKERQEIE 456
Cdd:pfam13868 89 RQEEYEEKLQER--EQMDEIVERIQE-------------EDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 457 DRRI----KEKNEHEKRIKEQDNQfIENQRQHEIEENERKMEFERKQTEHEEKLQQMYEQFERDREEMQRQHQERADKMK 532
Cdd:pfam13868 154 DERIleylKEKAEREEEREAEREE-IEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKAR 232
|
....
gi 392921127 533 QQWE 536
Cdd:pfam13868 233 QRQE 236
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
469-537 |
6.62e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.40 E-value: 6.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392921127 469 RIKEQ--DNQFIENQRQHEIEENERkmEFERKQTEHEEKLQQMyEQFERDREEMQRQHQERADKMKQQWEQ 537
Cdd:PRK09510 66 RQQQQqkSAKRAEEQRKKKEQQQAE--ELQQKQAAEQERLKQL-EKERLAAQEQKKQAEEAAKQAALKQKQ 133
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
331-628 |
7.30e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.95 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 331 KKAQEDSAELARWEEENRRFEKQKnearekrKREEEQEERQFKESLKLLDE-----------SRREKERKLQELLLRQKE 399
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELKL-------KEQAKKALEYYQLKEKLELEeeyllyldylkLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 400 EAEEEALRRLANDSEIEQKLEKIRYENEQKALQNDHENSIQLQLLKDGGQK---ERQEIEDRRIKEKNEHEKR---IKEQ 473
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELlklERRKVDDEEKLKESEKEKKkaeKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 474 DNQFIENQRQHEIEENERKMEFERKQTEHEEKLQQMYEQFERDREEMQRQHQERADKMKQQWEQIMMMIkhkmwnDIIER 553
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK------SEEEK 405
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392921127 554 NWTNRLNVLRSANKKVAELFNRFFTEISIIQREIEKSEDISMERKRVSIVLNTLTNSLKQEKELMTEEMKNLQIQ 628
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
386-538 |
8.25e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 386 KERKLQELLLRQKEEAEEEALRRLANDSEIEQKLEKIryENEQKALQND---HENSIQLQLLKDGGQKERQEIED----- 457
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEEL--EAELEELREElekLEKLLQLLPLYQELEALEAELAElperl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 458 ----RRIKEKNEHEKRIKEQDNQFIENQRQHEIEENERKMEFERKQTEHEEKLQQMYEQFERDREEMQRQhQERADKMKQ 533
Cdd:COG4717 149 eeleERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA-QEELEELEE 227
|
....*
gi 392921127 534 QWEQI 538
Cdd:COG4717 228 ELEQL 232
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
449-525 |
9.14e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 39.64 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392921127 449 QKERQEIEDRRIKEKNEHEKRiKEQDNQfienQRQHEIEENERKMEfERKQTEHEEKLQ-------QMYEQFERDREEMQ 521
Cdd:PRK10811 645 QAQQQTAETRESQQAEVTEKA-RTQDEQ----QQAPRRERQRRRND-EKRQAQQEAKALnveeqsvQETEQEERVQQVQP 718
|
....
gi 392921127 522 RQHQ 525
Cdd:PRK10811 719 RRKQ 722
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
449-526 |
9.82e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 37.34 E-value: 9.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392921127 449 QKERQEIEDRRIKEKNEHEKRIKEQDNQFIENQRQHEIEENERKMEFERkQTEHEEKLQQMYEQFERDREEMQRQHQE 526
Cdd:pfam15346 57 ELEREREAELEEERRKEEEERKKREELERILEENNRKIEEAQRKEAEER-LAMLEEQRRMKEERQRREKEEEEREKRE 133
|
|
| |
