|
Name |
Accession |
Description |
Interval |
E-value |
| SCAPER_N |
pfam16501 |
S phase cyclin A-associated protein in the endoplasmic reticulum; SCAPER_N is a short highly ... |
88-185 |
3.66e-55 |
|
S phase cyclin A-associated protein in the endoplasmic reticulum; SCAPER_N is a short highly conserved region close to the N-terminus. SCAPER is localized to the endoplasmic reticulum and is a substrate for cyclin A/Cdk2. It associates with cyclin A and localizes to the ER. One theory suggests that SCAPER functions to create a local high concentration of cyclin A2 in the cytoplasm. Alternatively, SCAPER might be acting to sequester a portion of cellular cyclin A2 that could then be readily available for nuclear translocation, which may be needed for exit from G0 phase.
Pssm-ID: 406813 Cd Length: 98 Bit Score: 186.46 E-value: 3.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 88 KTRHPRKIDLRARYWAFLFDNLRRAVDEIYVTCESDQSVVECKEVLMMLDYYVRDFKALIDWIQLQEKLEKTDAQSRPTS 167
Cdd:pfam16501 1 STGRDKKSELRARYWAFLFDNLQRAVDEIYQTCESDESVVECKEVIMVLDNYTRDFKALIEWFRLKWDYENTPPPQRPTS 80
|
90
....*....|....*...
gi 672062331 168 LAWEVKKMSPGRHVIQSP 185
Cdd:pfam16501 81 LAWEVRKSSPGKSVNKSP 98
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
540-788 |
9.05e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 9.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 540 KRTIAESKKKYEEKHMKAQQLREKLREEkSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKA 619
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 620 QEEEAKVNEIAFINTL-EAQNKRHDVLSKLKEYEQRLNELqeerqrRQEEKQARDEAVQERKRALEAERQARVEELLTKR 698
Cdd:COG1196 331 ELEELEEELEELEEELeEAEEELEEAEAELAEAEEALLEA------EAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 699 KEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQkKIQLKHDESIRRHMEQIEQRKEKAAELSSGR 778
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA-ELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250
....*....|
gi 672062331 779 HASTDYAPKL 788
Cdd:COG1196 484 EELAEAAARL 493
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
532-918 |
1.11e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.17 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 532 EKLSSPSRKRTIAESKKKYEEKHMKAQQLREK--LREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKRE 609
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAaeAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 610 VqlQAIVKKAQEEEAKVNEiafINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEA------------VQ 677
Cdd:PTZ00121 1393 A--DEAKKKAEEDKKKADE---LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAeeakkaeeakkkAE 1467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 678 ERKRALEAERQA----RVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKH 753
Cdd:PTZ00121 1468 EAKKADEAKKKAeeakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 754 DESIRRHMEQIEQRKEKAAElsSGRHASTDYAPKLTPYERKKQCSlcNVLIASEVYLFSHIKGKKHQQAVR-ENSSIQGR 832
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAE--EAKKAEEDKNMALRKAEEAKKAE--EARIEEVMKLYEEEKKMKAEEAKKaEEAKIKAE 1623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 833 ELSDEEVEHLSLKKYVVDIVIESAAPPEPMKDGEERQKNKKKAKKIKARMNTRAKEYENSVETKNSGSESPYK-AKLQRL 911
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKeAEEAKK 1703
|
....*..
gi 672062331 912 AKDLVKQ 918
Cdd:PTZ00121 1704 AEELKKK 1710
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
544-773 |
3.51e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.24 E-value: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 544 AESKKKYEEKHmKAQQLReKLREEKSLKLQKLLEREKDVRKWKEELLDQ--RRRMMEEKLLHAEFKREVQLQAivKKAQE 621
Cdd:PTZ00121 1542 AEEKKKADELK-KAEELK-KAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEEKKMKAEEA--KKAEE 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 622 EEAKVNEIafiNTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARD--EAVQERKRALE---AERQARVEELLT 696
Cdd:PTZ00121 1618 AKIKAEEL---KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEakKAEEDKKKAEEakkAEEDEKKAAEAL 1694
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672062331 697 KRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 773
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
556-773 |
5.65e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 556 KAQQLREKLRE-EKSLKLQKLLEREKDVRKWKEELLDQRRRmmEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEiafint 634
Cdd:COG1196 214 RYRELKEELKElEAELLLLKLRELEAELEELEAELEELEAE--LEELEAELAELEAELEELRLELEELELELEE------ 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 635 leAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQ------ARDEAVQERKRALEAERQARVEELLTKRKEQEARIEQQ 708
Cdd:COG1196 286 --AQAEEYELLAELARLEQDIARLEERRRELEERLEeleeelAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672062331 709 RQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 773
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
539-776 |
6.99e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 539 RKRTIAESKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKK 618
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 619 AQEEEAKVNEIAFintLEAQNKRHDVLSKLKEYEQRLNELQEERqrrqeEKQARDEAVQERKRALEAERQARVEELLTKR 698
Cdd:COG1196 341 ELEEELEEAEEEL---EEAEAELAEAEEALLEAEAELAEAEEEL-----EELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672062331 699 KEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHD-ESIRRHMEQIEQRKEKAAELSS 776
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELlEEAALLEAALAELLEELAEAAA 491
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
426-770 |
3.88e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 426 AKKEELADRLEK---ANEEAIASAIAEEEQLTREIEA--EENNDINIETDNDSDFSASMGSgslsfcgmslDWNDVLADY 500
Cdd:PRK02224 359 EELREEAAELESeleEAREAVEDRREEIEELEEEIEElrERFGDAPVDLGNAEDFLEELRE----------ERDELRERE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 501 EARESWRQNTSwGDIVEEEPARLPGHGIHMHEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKL--------REEKSLKL 572
Cdd:PRK02224 429 AELEATLRTAR-ERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVeeveerleRAEDLVEA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 573 QKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKR----------EVQLQAIVKKAQEEEAKVNEIAFIN--------T 634
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELReraaeleaeaEEKREAAAEAEEEAEEAREEVAELNsklaelkeR 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 635 LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQ---ERKRALEAERQ-ARVEELLTKRKEQEARIEQQRQ 710
Cdd:PRK02224 588 IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAekrERKRELEAEFDeARIEEAREDKERAEEYLEQVEE 667
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672062331 711 EkekaredaarerardreerLAALTaaqqEAMEELQKKI-----QLKHDESIRRHMEQIEQRKEK 770
Cdd:PRK02224 668 K-------------------LDELR----EERDDLQAEIgavenELEELEELRERREALENRVEA 709
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
540-943 |
4.99e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 4.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 540 KRTIAESKKKYEEKHmKAQQLREKLREEKslKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLqaiVKKA 619
Cdd:PTZ00121 1469 AKKADEAKKKAEEAK-KADEAKKKAEEAK--KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE---AKKA 1542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 620 qEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELqeerQRRQEEKQARDEAVQERKRALEAERQARVEELltkRK 699
Cdd:PTZ00121 1543 -EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL----RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA---KK 1614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 700 EQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDEsirrhmeqiEQRKEKAAELSSGRH 779
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA---------EEDKKKAEEAKKAEE 1685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 780 ASTDYAPKLTPYERKKQcslcnvlIASEVYLFSHIKGKKHQQAVR--ENSSIQGRELSDEEVEhlslkkyvvdiviESAA 857
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAK-------KAEELKKKEAEEKKKAEELKKaeEENKIKAEEAKKEAEE-------------DKKK 1745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 858 PPEPMKDGEERQKNKKKAKKIKARMNTRAKEYENSVETKNSGSESPYKAKLQRLAKDLVKQLQVQDSGS-----WVNNKA 932
Cdd:PTZ00121 1746 AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGkegnlVINDSK 1825
|
410
....*....|.
gi 672062331 933 SALDRTLGEIA 943
Cdd:PTZ00121 1826 EMEDSAIKEVA 1836
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
539-773 |
5.96e-10 |
|
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: 62.63 E-value: 5.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 539 RKRTIAESKKKYEEKHMKAQQLREKL------REEKSLKLQKLLEREKD-----VRKWKEE-LLDQRRRMMEEKLLHAEF 606
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELeeqieeREQKRQEEYEEKLQEREqmdeiVERIQEEdQAEAEEKLEKQRQLREEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 607 KREVQLQAIVKKAQEEEAKVNE---IAFINTLEAQNKRHDVLSKLKEY--EQRLNELQEERQRRQEEKQARDEAVQER-K 680
Cdd:pfam13868 133 DEFNEEQAEWKELEKEEEREEDeriLEYLKEKAEREEEREAEREEIEEekEREIARLRAQQEKAQDEKAERDELRAKLyQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 681 RALEAERQARVEELLTKRKEQEARI----EQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKK--IQLKHD 754
Cdd:pfam13868 213 EEQERKERQKEREEAEKKARQRQELqqarEEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRrmKRLEHR 292
|
250
....*....|....*....
gi 672062331 755 ESIRRHMEQIEQRKEKAAE 773
Cdd:pfam13868 293 RELEKQIEEREEQRAAERE 311
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
538-767 |
8.89e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 8.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 538 SRKRTIAESKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWKEEL--LDQRRRMMEEKLLHAEFKREVQLQAI 615
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELeeAEEELEEAEAELAEAEEALLEAEAEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 616 VKKAQEEEAKVNEIafintLEAQNKRHDVLSKLKEYEQRLNELQEERQRrQEEKQARDEAVQERKRALEAERQARVEELL 695
Cdd:COG1196 375 AEAEEELEELAEEL-----LEALRAAAELAAQLEELEEAEEALLERLER-LEEELEELEEALAELEEEEEEEEEALEEAA 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672062331 696 TKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQR 767
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
593-773 |
1.32e-09 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 62.49 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 593 RRRMMEEKLLHAEFKREvqlqAIVKKAQEE-EAKVNEIafinTLEAQNKRHDVLSKL-KEYEQRLNELQEERQRRQEEKQ 670
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAK----RILEEAKKEaEAIKKEA----LLEAKEEIHKLRNEFeKELRERRNELQKLEKRLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 671 A---RDEAVQERKRALEAERQ---ARVEELLTKRKEQEARIEQQRQEKEKaredaarerardreerLAALTA--AQQEAM 742
Cdd:PRK12704 97 NldrKLELLEKREEELEKKEKeleQKQQELEKKEEELEELIEEQLQELER----------------ISGLTAeeAKEILL 160
|
170 180 190
....*....|....*....|....*....|.
gi 672062331 743 EELQKKIQLKHDESIRRHMEQIEQRKEKAAE 773
Cdd:PRK12704 161 EKVEEEARHEAAVLIKEIEEEAKEEADKKAK 191
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
533-713 |
3.21e-09 |
|
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: 61.68 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 533 KLSSPSRKRTIAESKKKYEEKHMKAQQLRE----KLREEKSLKLQKL----LEREKDVRKWKEELLDQRRRMMEeklLHA 604
Cdd:pfam17380 405 KILEEERQRKIQQQKVEMEQIRAEQEEARQrevrRLEEERAREMERVrleeQERQQQVERLRQQEEERKRKKLE---LEK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 605 EFKREVQLQAIVKKAQEEEAKVNEIAFIntlEAQNKRHDVLsklKEYEQRLNELQEerqrrqeeKQARDEAVQERKRALE 684
Cdd:pfam17380 482 EKRDRKRAEEQRRKILEKELEERKQAMI---EEERKRKLLE---KEMEERQKAIYE--------EERRREAEEERRKQQE 547
|
170 180
....*....|....*....|....*....
gi 672062331 685 AERQARVEELLTKRKEQEARIEQQRQEKE 713
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEAMERERE 576
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
540-773 |
5.73e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 540 KRTIAESKKKYEEKHMKAQQLREKLRE-EKSL--KLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEF-KREVQLQAI 615
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEkEKELeeVLREINEISSELPELREELEKLEKEVKELEELKEEIeELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 616 VKKAQEEEAKVNEI-AFINTLEAQnkrhdvLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQE------RKRALEAERQ 688
Cdd:PRK03918 251 EGSKRKLEEKIRELeERIEELKKE------IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDElreiekRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 689 ArVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAaltAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRK 768
Cdd:PRK03918 325 G-IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA---KAKKEELERLKKRLTGLTPEKLEKELEELEKAK 400
|
....*
gi 672062331 769 EKAAE 773
Cdd:PRK03918 401 EEIEE 405
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
546-773 |
1.18e-08 |
|
chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 546 SKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ--LQAIVKKAQEEE 623
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEekLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 624 AKVNEIAFINtLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEkQARDEAVQERKRALEAERQARVEELLTKRKEQEA 703
Cdd:TIGR02168 281 EEIEELQKEL-YALANEISRLEQQKQILRERLANLERQLEELEAQ-LEELESKLDELAEELAELEEKLEELKEELESLEA 358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672062331 704 RIEQQRQEKEkaredaarerardreeRLAALTAAQQEAMEELQKKI-QLKHD--------ESIRRHMEQIEQRKEKAAE 773
Cdd:TIGR02168 359 ELEELEAELE----------------ELESRLEELEEQLETLRSKVaQLELQiaslnneiERLEARLERLEDRRERLQQ 421
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
412-714 |
2.19e-08 |
|
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: 58.93 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 412 SNVSAADWSMAEVLAKKEELADRLEKANEEaiasaIAEEEQLTREIEAEENNDINIETDNDSDFSAsmgsgslsfcgMSL 491
Cdd:TIGR02169 709 QELSDASRKIGEIEKEIEQLEQEEEKLKER-----LEELEEDLSSLEQEIENVKSELKELEARIEE-----------LEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 492 DWNDV---LADYEARES---WRQNTSWGDIVEEEPARLPGHGIHMHEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLR 565
Cdd:TIGR02169 773 DLHKLeeaLNDLEARLShsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 566 EEK----SLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLlhaefKREVQLQAIVKKAQEEEAKVnEIAFINTLEAQNKR 641
Cdd:TIGR02169 853 EKEienlNGKKEELEEELEELEAALRDLESRLGDLKKERD-----ELEAQLRELERKIEELEAQI-EKKRKRLSELKAKL 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 642 HDVLSKLKEYEQRLNELQEERQRRQEEK--QARDEAVQERKRALE----------AERQARVEELLTK-------RKEQE 702
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEIPEEELSLEdvQAELQRVEEEIRALEpvnmlaiqeyEEVLKRLDELKEKrakleeeRKAIL 1006
|
330
....*....|..
gi 672062331 703 ARIEQQRQEKEK 714
Cdd:TIGR02169 1007 ERIEEYEKKKRE 1018
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
539-773 |
2.20e-08 |
|
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: 57.62 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 539 RKRTIAESKK-KYEEKHMK---AQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLL-HAEFKRE-VQL 612
Cdd:pfam13868 24 RDAQIAEKKRiKAEEKEEErrlDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEeYEEKLQErEQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 613 QAIVKKAQEEEAKVNEIAFI---NTLEAQNKRHDVLSKLKEYE-QRLNELQEERQRRQEEKQARDEAVQERKRALEAERQ 688
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEkqrQLREEIDEFNEEQAEWKELEkEEEREEDERILEYLKEKAEREEEREAEREEIEEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 689 ARVEELLtkrkEQEARIEQQRQEKEKaredaarerardreeRLAALTAAQQEA------MEELQKKIQLKHD--ESIRRH 760
Cdd:pfam13868 184 REIARLR----AQQEKAQDEKAERDE---------------LRAKLYQEEQERkerqkeREEAEKKARQRQElqQAREEQ 244
|
250
....*....|...
gi 672062331 761 MEQIEQRKEKAAE 773
Cdd:pfam13868 245 IELKERRLAEEAE 257
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
537-955 |
4.06e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 537 PSRKRTIAESKKK------YEEKHMKAQQLR--EKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEkllhAEFKR 608
Cdd:PTZ00121 1074 PSYKDFDFDAKEDnradeaTEEAFGKAEEAKktETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEE----ARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 609 EVQLQAIVKKAqeEEAKVNEIAfintLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQ 688
Cdd:PTZ00121 1150 DAKRVEIARKA--EDARKAEEA----RKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDA 1223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 689 ARVEELL----TKRKEQEA-RIEQQRQEKEKAREDAARERARDREErlAALTAAQQEAMEELQKKIQLKHDESIRRHME- 762
Cdd:PTZ00121 1224 KKAEAVKkaeeAKKDAEEAkKAEEERNNEEIRKFEEARMAHFARRQ--AAIKAEEARKADELKKAEEKKKADEAKKAEEk 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 763 -QIEQRKEKAAELSSGRHASTDY--------APKLTPYERKKqcslcnvliASEVYLFSHIKGKKHQQAVRENSSIQGRE 833
Cdd:PTZ00121 1302 kKADEAKKKAEEAKKADEAKKKAeeakkkadAAKKKAEEAKK---------AAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 834 LSDEEVEHLSLKKYVvdiviESAAPPEPMKDGEERQKNKKKAKKIKARMNTRAKEYENSVETKNSGSESPYKAKLQRLAK 913
Cdd:PTZ00121 1373 KEEAKKKADAAKKKA-----EEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD 1447
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 672062331 914 DLVKQLQVQDSGSWVNNKASAlDRTLGEIARILEKENVADQI 955
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEE-AKKADEAKKKAEEAKKADEA 1488
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
440-955 |
1.31e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 440 EEAIASAIAEEEQLTREIeaeenNDINIETDNDSDFSASMGSGSLSFCGMSLDWNDVLADYEARESWRQNTSWGdivEEE 519
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDI-----IDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFG---KAE 1101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 520 PARLPGHGIHMHEKLSSPSRKRtiAESKKKYEEKHmKAQQLR--EKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMM 597
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKK--AEDARKAEEAR-KAEDARkaEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKA 1178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 598 EEKLLHAEFKR--EVQLQAIVKKAQ-----EEEAKVNEI-AFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEK 669
Cdd:PTZ00121 1179 EAARKAEEVRKaeELRKAEDARKAEaarkaEEERKAEEArKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 670 QARDEAVQERKRALEAERQARVEELLT---KRKEQEARieqQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQ 746
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKaeeKKKADEAK---KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK 1335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 747 KKIQ--LKHDESIRRHMEQIEQRKEKAAELSSGRHASTDYAPKLTPYERKKqcslcnvliASEVYLFSHIKgKKHQQAVR 824
Cdd:PTZ00121 1336 KKAEeaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK---------AEEKKKADEAK-KKAEEDKK 1405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 825 ENSSIQGRELSDEEVEHLSLKKYvvdiviESAAPPEPMKDGEERQknkkkakkikarmntRAKEYENSVETKNSGSESPY 904
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAE------EKKKADEAKKKAEEAK---------------KADEAKKKAEEAKKAEEAKK 1464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 672062331 905 KAKLQRLAKDLVKQLQVQDSGSWVNNKASALDRTLGEIARILEKENVADQI 955
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
538-773 |
2.08e-07 |
|
chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 538 SRKRTIAESKKKYEEKHMKAQQLREKLREekslKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ------ 611
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAE----LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleeri 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 612 --LQAIVKKAQEEEAKVNEiafiNTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALeAERQA 689
Cdd:TIGR02168 750 aqLSKELTELEAEIEELEE----RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-ANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 690 RVEELLTKRKEQEARIEQQRQEKEKaredaarerARDREERLAALTAAQQEAMEELQKKIQLKHDE--SIRRHMEQIEQR 767
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEE---------LSEDIESLAAEIEELEELIEELESELEALLNEraSLEEALALLRSE 895
|
....*.
gi 672062331 768 KEKAAE 773
Cdd:TIGR02168 896 LEELSE 901
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
543-773 |
3.05e-07 |
|
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: 55.36 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 543 IAESKKK----YEEKHMKAQQLREKLREEKSLKLQ--KLLEREKD-----VRKWKEELLDQRRRMMEEKLLHAEFKREVQ 611
Cdd:pfam02463 164 GSRLKRKkkeaLKKLIEETENLAELIIDLEELKLQelKLKEQAKKaleyyQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 612 ------------LQAIVKKAQEEEAKVNEIAFINT--LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQ 677
Cdd:pfam02463 244 ellrdeqeeiesSKQEIEKEEEKLAQVLKENKEEEkeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 678 ERKRALEAERQARVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQ--EAMEELQKKIQLKH-D 754
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERlsSAAKLKEEELELKSeE 403
|
250
....*....|....*....
gi 672062331 755 ESIRRHMEQIEQRKEKAAE 773
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLK 422
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
422-710 |
5.68e-07 |
|
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: 54.30 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 422 AEVLAKKEELADRLEK--ANEEAIASAIAEEEQLTREIEAEENNDINIETDNDSDFSASMGS--GSLSFCgmsldwNDVL 497
Cdd:TIGR02169 244 RQLASLEEELEKLTEEisELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASleRSIAEK------EREL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 498 ADYEARESwrqntswgdIVEEEPARLpghgihmheklsspsrKRTIAESKKKYEEKHMKAQQLRE---KLREEKSLKLQK 574
Cdd:TIGR02169 318 EDAEERLA---------KLEAEIDKL----------------LAEIEELEREIEEERKRRDKLTEeyaELKEELEDLRAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 575 LLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREV-QLQAIVKKAQEEEAKVNE-----IAFINTLEAQNKrhDVLSKL 648
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREINELKRELdRLQEELQRLSEELADLNAaiagiEAKINELEEEKE--DKALEI 450
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672062331 649 KEYEQRLNELqeerqrrqeekQARDEAVQERKRALEAErQARVEELLTKRKEQEARIEQQRQ 710
Cdd:TIGR02169 451 KKQEWKLEQL-----------AADLSKYEQELYDLKEE-YDRVEKELSKLQRELAEAEAQAR 500
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
546-773 |
6.41e-07 |
|
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: 53.97 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 546 SKKKYEEKHMKAQQlrEKLREEKSLKLQKLLEREK--DVRKWKEELLDQRRRM-MEEKLLHAEFKREVQ-LQAIVKKAQE 621
Cdd:pfam17380 285 SERQQQEKFEKMEQ--ERLRQEKEEKAREVERRRKleEAEKARQAEMDRQAAIyAEQERMAMERERELErIRQEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 622 EEAKVNEIAFINT---------LEAQNKRHDVLSKLK-------EYEQRLNELQEERQRRQEEKQARDEAVQERKRALEA 685
Cdd:pfam17380 363 ERIRQEEIAMEISrmrelerlqMERQQKNERVRQELEaarkvkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 686 ERQARVEELLTKRKEQEARIEQQRQ-EKEKAREDAARERARDreerlaaltaaQQEAMEELQKKIQLKHDESIRRHMEQi 764
Cdd:pfam17380 443 ERAREMERVRLEEQERQQQVERLRQqEEERKRKKLELEKEKR-----------DRKRAEEQRRKILEKELEERKQAMIE- 510
|
....*....
gi 672062331 765 EQRKEKAAE 773
Cdd:pfam17380 511 EERKRKLLE 519
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
422-713 |
1.17e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 422 AEVLAKKEEL--ADRLEKANEEAIASAIAEEEQLTReieAEENNDINIETDNDSDFSASMGSGSlsfcgmsldwndvlad 499
Cdd:PTZ00121 1524 ADEAKKAEEAkkADEAKKAEEKKKADELKKAEELKK---AEEKKKAEEAKKAEEDKNMALRKAE---------------- 1584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 500 yEARESWRQNTSWGDIVEEEPARLPGhgihmhEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKSlKLQKLLERE 579
Cdd:PTZ00121 1585 -EAKKAEEARIEEVMKLYEEEKKMKA------EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK-KAEELKKAE 1656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 580 KDVRKWKEELldqRRRMMEEKLLHAEfkrevqlqaiVKKAQEEEAKVNEIafINTLEAQNKRHDVLSKLKEYEQRLNELQ 659
Cdd:PTZ00121 1657 EENKIKAAEE---AKKAEEDKKKAEE----------AKKAEEDEKKAAEA--LKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 660 EERQRRQEEK--QARDEAVQERKRALEA----ERQARVEELltkRKEQEARIEQQRQEKE 713
Cdd:PTZ00121 1722 KKAEEENKIKaeEAKKEAEEDKKKAEEAkkdeEEKKKIAHL---KKEEEKKAEEIRKEKE 1778
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
540-768 |
1.67e-06 |
|
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: 51.84 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 540 KRTIAESKKKYEEKHMKAQQLREKLREEKSLK-----LQKLLEREKDVR-----KWKEELldQRRRMMEEKLLHAEFKRE 609
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQaewkeLEKEEEREEDERileylKEKAER--EEEREAEREEIEEEKERE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 610 VQ-LQAIVKKAQEEEAKVNEIAFINTLEAQNKRHdvlsKLKEYEQRLNELQEERQRrqeeKQARDEAVQERKRALEAERQ 688
Cdd:pfam13868 186 IArLRAQQEKAQDEKAERDELRAKLYQEEQERKE----RQKEREEAEKKARQRQEL----QQAREEQIELKERRLAEEAE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 689 ---ARVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLkhDESIRRHMEQIE 765
Cdd:pfam13868 258 reeEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREE--EAERRERIEEER 335
|
...
gi 672062331 766 QRK 768
Cdd:pfam13868 336 QKK 338
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
416-774 |
2.03e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 416 AADWSMAEVLAKKEELADRLEKAnEEAIASAIAEEEQLTREIEAEENNDINIETDN---DSDFSASMGSGSLSFCGMSLD 492
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAEL-EEELEEAQEELEELEEELEQLENELEAAALEErlkEARLLLLIAAALLALLGLGGS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 493 WNDVLAdyeareswrqnTSWGDIVEEEPARLPGHGIHMHEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKSLKL 572
Cdd:COG4717 268 LLSLIL-----------TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 573 QKLLEREKDVRKWKEeLLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEakvneiaFINTLEAQNKRHDVLSKLKEYE 652
Cdd:COG4717 337 EELLELLDRIEELQE-LLREAEELEEELQLEELEQEIAALLAEAGVEDEEE-------LRAALEQAEEYQELKEELEELE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 653 QRLNELqeerqrrqeekqaRDEAVQERKRALEAERQARVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLA 732
Cdd:COG4717 409 EQLEEL-------------LGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELL 475
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 672062331 733 ALTAAQQEAMEELQKKIQLKH--DESIRRHMEQIEQRK-----EKAAEL 774
Cdd:COG4717 476 QELEELKAELRELAEEWAALKlaLELLEEAREEYREERlppvlERASEY 524
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
532-774 |
2.78e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 51.79 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 532 EKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKSlklqKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKrEVQ 611
Cdd:pfam02029 96 EKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEET----EIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAE-EVP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 612 LQAIVKKAQEEEAKVNEIAFINTLEA--QNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERqa 689
Cdd:pfam02029 171 TENFAKEEVKDEKIKKEKKVKYESKVflDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQ-- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 690 RVEELLTKR-------------KEQEARIE-----QQRQEKEKAREDAArerardreerlaaltaaQQEAMEELQKkiQL 751
Cdd:pfam02029 249 KLEELRRRRqekeseefeklrqKQQEAELEleelkKKREERRKLLEEEE-----------------QRRKQEEAER--KL 309
|
250 260
....*....|....*....|...
gi 672062331 752 KHDESIRRHMEQIEQRKEKAAEL 774
Cdd:pfam02029 310 REEEEKRRMKEEIERRRAEAAEK 332
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
534-777 |
2.82e-06 |
|
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: 51.30 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 534 LSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKSLKL----------QKLLEREKDVRKWKEELLDQRRRM----MEE 599
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKallkqlaaleRRIAALARRIRALEQELAALEAELaeleKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 600 KLLHAEFKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERqrrqeekQARDEAVQER 679
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-------RADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 680 KRALEAERQaRVEELLTKRKEQEARIEQQRQEKEKaredaarerardREERLAALTAAQQEAMEELQKKIQlkhdeSIRR 759
Cdd:COG4942 166 RAELEAERA-ELEALLAELEEERAALEALKAERQK------------LLARLEKELAELAAELAELQQEAE-----ELEA 227
|
250
....*....|....*...
gi 672062331 760 HMEQIEQRKEKAAELSSG 777
Cdd:COG4942 228 LIARLEAEAAAAAERTPA 245
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
554-774 |
3.08e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 554 HMKAQQLRE---------KLREEKSLKLQKL------LEREKDVRkwkEELLDQRRRmmeeklLHAEfkREVQLQAIVKK 618
Cdd:COG1196 151 EAKPEERRAiieeaagisKYKERKEEAERKLeateenLERLEDIL---GELERQLEP------LERQ--AEKAERYRELK 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 619 AQEEEAKVNEIAfintleaqNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQaRVEELLTKR 698
Cdd:COG1196 220 EELKELEAELLL--------LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-ELEEAQAEE 290
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672062331 699 KEQEARIEQQRQEKEkaredaarerarDREERLAALTAAQQEAMEELQKKIQ--LKHDESIRRHMEQIEQRKEKAAEL 774
Cdd:COG1196 291 YELLAELARLEQDIA------------RLEERRRELEERLEELEEELAELEEelEELEEELEELEEELEEAEEELEEA 356
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
576-788 |
3.80e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 576 LErEKDVRKWKEELLDQRRRM--MEEKLLHAEFKREvQLQAIVKKAQEEEAKVNEIAFINTL-------EAQNKRHDVLS 646
Cdd:COG4913 218 LE-EPDTFEAADALVEHFDDLerAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEYLraalrlwFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 647 KLKEYEQRLNELqeerQRRQEEKQARDEAVQERKRALEAERQA----RVEELLTKRKEQEARIEQQRQEKEKARED---- 718
Cdd:COG4913 296 ELEELRAELARL----EAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALlaal 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672062331 719 -AARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHASTDYAPKL 788
Cdd:COG4913 372 gLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
544-715 |
4.17e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.96 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 544 AESKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKdvrkwkEELLDQrrrmmEEKLLHAEFKREVQLQAivKKAQEEE 623
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEK------ERLAAQ-----EQKKQAEEAAKQAALKQ--KQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 624 AKVNEIAFINTlEAQNKRHDVLSKLKEYEQRLNElqeerqrrqeEKQARDEAVQERKRALEAERQARVEELLTKRKEQEA 703
Cdd:PRK09510 139 AKAAAAAKAKA-EAEAKRAAAAAKKAAAEAKKKA----------EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA 207
|
170
....*....|..
gi 672062331 704 RIEQQRQEKEKA 715
Cdd:PRK09510 208 KKKAAAEAKKKA 219
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
538-774 |
5.44e-06 |
|
chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 538 SRKRTIAESKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ-LQAIV 616
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEeLESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 617 KKAQEE-EAKVNEIAfintlEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELL 695
Cdd:TIGR02168 375 EELEEQlETLRSKVA-----QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672062331 696 TKRKEQEARIEQQRQEKEKaredaarerardreeRLAALTAAQQEAMEELQKKIQLKHdeSIRRHMEQIEQRKEKAAEL 774
Cdd:TIGR02168 450 EELQEELERLEEALEELRE---------------ELEEAEQALDAAERELAQLQARLD--SLERLQENLEGFSEGVKAL 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
529-773 |
7.63e-06 |
|
chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 529 HMHEKLSSPSRKRT--IAESKKKYEEKHMKAQQLREKLREEKSLklQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEF 606
Cdd:TIGR02168 253 EELEELTAELQELEekLEELRLEVSELEEEIEELQKELYALANE--ISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 607 KREvQLQAIVKKAQEEEAKVNEIafintLEAQNKRHDVL-SKLKEYEQRLNELqeerqrrqeekqarDEAVQERKRALeA 685
Cdd:TIGR02168 331 KLD-ELAEELAELEEKLEELKEE-----LESLEAELEELeAELEELESRLEEL--------------EEQLETLRSKV-A 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 686 ERQARVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIqlKHDESIRRHMEQIE 765
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ--EELERLEEALEELR 467
|
....*...
gi 672062331 766 QRKEKAAE 773
Cdd:TIGR02168 468 EELEEAEQ 475
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
538-714 |
8.09e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 538 SRKRTIAESKKKYEEKHMKAQQLREKLR------EEKSLKLQKLLEREKDV-------------RKWKEELLDQRRRMme 598
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIReleeriEELKKEIEELEEKVKELkelkekaeeyiklSEFYEEYLDELREI-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 599 EKLLhAEFKREVQ-LQAIVKKAQEEEAKVNEIA-----FINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQAR 672
Cdd:PRK03918 313 EKRL-SRLEEEINgIEERIKELEEKEERLEELKkklkeLEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK 391
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 672062331 673 D-EAVQERKRALEAERQ---ARVEELLTKRKEQEARIEQQRQEKEK 714
Cdd:PRK03918 392 ElEELEKAKEEIEEEISkitARIGELKKEIKELKKAIEELKKAKGK 437
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
529-770 |
9.57e-06 |
|
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: 50.45 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 529 HMHEKLSSPSR-KRTIAESKKKYE---EKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHA 604
Cdd:TIGR02169 703 RLDELSQELSDaSRKIGEIEKEIEqleQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 605 EFKREV---QLQAIVKKAQEEEAKVNEI-AFINTLEAQ-NKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQER 679
Cdd:TIGR02169 783 DLEARLshsRIPEIQAELSKLEEEVSRIeARLREIEQKlNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 680 KRALEA---ERQARVEELLTKRKEQEARIEQQR------QEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQ 750
Cdd:TIGR02169 863 KEELEEeleELEAALRDLESRLGDLKKERDELEaqlrelERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
250 260
....*....|....*....|
gi 672062331 751 LKHDESIRRHMEQIEQRKEK 770
Cdd:TIGR02169 943 DEEIPEEELSLEDVQAELQR 962
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
537-767 |
1.04e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 49.46 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 537 PSRKRTIAESKKKYEEKHMKAQQLREKLREEKSLKLQKLlerekdvRKWKEELLDQRRRMMEEKllHAEFKREVQLQAIV 616
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQ-------KELEQRAAAEKAAKQAEQ--AAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 617 KKA-QEEEAKVNEiafintlEAQNKRhdvlsKLKEYEQRLNELQEERQRRQEEKQARDEAV----QERKRALEAERQARV 691
Cdd:TIGR02794 124 AKAkQAAEAKAKA-------EAEAER-----KAKEEAAKQAEEEAKAKAAAEAKKKAEEAKkkaeAEAKAKAEAEAKAKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 692 EELLTKRKEQEARIEQQRQEK---EKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDES-IRRHMEQIEQR 767
Cdd:TIGR02794 192 EEAKAKAEAAKAKAAAEAAAKaeaEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSeVDKYAAIIQQA 271
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
540-706 |
1.08e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.21 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 540 KRTIAESKKKYEEKHMKAQQLREKLrEEKSLKLQKLLereKDVRKWKEELLDQRRRM--MEEKLLHaefKREVQLQAIVK 617
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELEREL-EQKAEEAEALL---KEAEKLKEELEEKKEKLqeEEDKLLE---EAEKEAQQAIK 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 618 KAQEEEAKVneIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRaleaerqARVE----- 692
Cdd:PRK00409 581 EAKKEADEI--IKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDE-------VKYLslgqk 651
|
170
....*....|....*
gi 672062331 693 -ELLTKRKEQEARIE 706
Cdd:PRK00409 652 gEVLSIPDDKEAIVQ 666
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
540-712 |
1.64e-05 |
|
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: 49.18 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 540 KRTIAESKKKYEEKHMKAQQlrEKLREEKslKLQKLLEREKdvRKWKEELLDQRRRMMEEKLLHAEFKREVQLQaivKKA 619
Cdd:pfam15709 346 RRLEVERKRREQEEQRRLQQ--EQLERAE--KMREELELEQ--QRRFEEIRLRKQRLEEERQRQEEEERKQRLQ---LQA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 620 QEEEAKVNEIAFINTLE--AQNKRHDVLSKLKEYEQRLNELQEERQRRQEE--KQARDEAVQERKRALEAERQARVEELL 695
Cdd:pfam15709 417 AQERARQQQEEFRRKLQelQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRlmEMAEEERLEYQRQKQEAEEKARLEAEE 496
|
170 180
....*....|....*....|...
gi 672062331 696 TKRKEQEA------RIEQQRQEK 712
Cdd:pfam15709 497 RRQKEEEAarlaleEAMKQAQEQ 519
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
517-748 |
1.66e-05 |
|
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: 49.18 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 517 EEEPARLPGHGIHMHEKLSSPSRKRTIAEskkKYEEKHMKAQQLREKLREEKSLKlQKLLEREKdvrKWKEEL-LDQRRR 595
Cdd:pfam15709 313 EERSEEDPSKALLEKREQEKASRDRLRAE---RAEMRRLEVERKRREQEEQRRLQ-QEQLERAE---KMREELeLEQQRR 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 596 MMEEKLlhaefkREVQLQAIVKKAQEEEAKvneiafiNTLEAQNKRHDVLSKLKEYEQRLNELQEerqRRQEEKQARDEA 675
Cdd:pfam15709 386 FEEIRL------RKQRLEEERQRQEEEERK-------QRLQLQAAQERARQQQEEFRRKLQELQR---KKQQEEAERAEA 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672062331 676 VQERKRALE---AERQARVEELltkrkEQEARIEQQRQEKEKAREDAARERARDREERLAAlTAAQQEAMEELQKK 748
Cdd:pfam15709 450 EKQRQKELEmqlAEEQKRLMEM-----AEEERLEYQRQKQEAEEKARLEAEERRQKEEEAA-RLALEEAMKQAQEQ 519
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
532-737 |
2.31e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 532 EKLSSPS-RKRTIAESKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREV 610
Cdd:COG4717 56 DELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 611 QLQA----IVKKAQEEEAKVNEIAfintlEAQNKRHDVLSKLKEYEQRLNELQEERQRRqeeKQARDEAVQERKRALEAE 686
Cdd:COG4717 136 ALEAelaeLPERLEELEERLEELR-----ELEEELEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELEELQQR 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 672062331 687 RQARvEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAA 737
Cdd:COG4717 208 LAEL-EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAA 257
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
532-792 |
2.66e-05 |
|
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: 48.58 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 532 EKLSSPSRKRTIAESKKKYE-----EKHMKAQQLREKLREEKSLKLQKLLEREKDV-RKWKEELLDQRRRMMEEKLLHAE 605
Cdd:pfam17380 307 EKAREVERRRKLEEAEKARQaemdrQAAIYAEQERMAMERERELERIRQEERKRELeRIRQEEIAMEISRMRELERLQME 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 606 FKRE-----VQLQAIVK-KAQEEE------AKVNEIAFINTlEAQNKRHDVLSKLKEYEQR-LNELQEERQRRQEE-KQA 671
Cdd:pfam17380 387 RQQKnervrQELEAARKvKILEEErqrkiqQQKVEMEQIRA-EQEEARQREVRRLEEERAReMERVRLEEQERQQQvERL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 672 RDEAVQERKRALEAER----QARVEELLTKRKEQE------ARIEQQRQEK--EKAREDAARERARDREERLAALTAAQQ 739
Cdd:pfam17380 466 RQQEEERKRKKLELEKekrdRKRAEEQRRKILEKEleerkqAMIEEERKRKllEKEMEERQKAIYEEERRREAEEERRKQ 545
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672062331 740 EAMEElQKKIQ------------LKHDESIRRHMEQIEQRKEKAAELSSGRHAST---DYAPKLTPYE 792
Cdd:pfam17380 546 QEMEE-RRRIQeqmrkateersrLEAMEREREMMRQIVESEKARAEYEATTPITTikpIYRPRISEYQ 612
|
|
| ZnF_U1 |
smart00451 |
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ... |
793-825 |
2.68e-05 |
|
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.
Pssm-ID: 197732 [Multi-domain] Cd Length: 35 Bit Score: 42.24 E-value: 2.68e-05
10 20 30
....*....|....*....|....*....|...
gi 672062331 793 RKKQCSLCNVLIASEVYLFSHIKGKKHQQAVRE 825
Cdd:smart00451 2 GGFYCKLCNVTFTDEISVEAHLKGKKHKKNVKK 34
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
545-795 |
2.70e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 545 ESKKKYEEKHMKAQQLREKLREEK---SLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREV-QLQAIVKKAQ 620
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELreiEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLeELEERHELYE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 621 EEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQAR---------- 690
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrel 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 691 ---------------VEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAaltaaqqEAMEELQKKIQLKHDE 755
Cdd:PRK03918 446 teehrkelleeytaeLKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA-------EQLKELEEKLKKYNLE 518
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 672062331 756 SIRRHMEQIEQRKEKAAELSSGRHASTDYAPKLTPYERKK 795
Cdd:PRK03918 519 ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
547-775 |
3.82e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 547 KKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKV 626
Cdd:TIGR00618 657 QERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 627 NEIAFINTL-EAQNKRHDVLSKLKEYEQRLNElqeerqrRQEEKQARDEAVQERKRALEAERQARvEELLTKRKEQEARI 705
Cdd:TIGR00618 737 REDALNQSLkELMHQARTVLKARTEAHFNNNE-------EVTAALQTGAELSHLAAEIQFFNRLR-EEDTHLLKTLEAEI 808
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672062331 706 EQQRQEKEKAREDAARERARDRE---ERLAALTAAQQEAmeelqkKIQLKHDESIRRHMEQIEQRKEKAAELS 775
Cdd:TIGR00618 809 GQEIPSDEDILNLQCETLVQEEEqflSRLEEKSATLGEI------THQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
595-773 |
3.95e-05 |
|
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: 47.61 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 595 RMMEEKLLHAEFKREVQLQAIVKKAQEEEAKvneiafintleAQNKRHDVLSKlkeyEQRLNELQEERQRRQEEKQARDE 674
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIAEKKRIKAEEK-----------EEERRLDEMME----EERERALEEEEEKEEERKEERKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 675 AVQERKRALEAERQARVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTA-AQQEAMEELQKKIQLKH 753
Cdd:pfam13868 74 YRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFnEEQAEWKELEKEEEREE 153
|
170 180
....*....|....*....|
gi 672062331 754 DESIRRHMEQIEQRKEKAAE 773
Cdd:pfam13868 154 DERILEYLKEKAEREEEREA 173
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
556-776 |
4.33e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 556 KAQQLREKLREEKSlklqKLLEREKDVRKWKEELLDQRRRmmEEKLLHA----EFKREVQLQAIVKKAQEEEAKVNEI-A 630
Cdd:PRK02224 409 NAEDFLEELREERD----ELREREAELEATLRTARERVEE--AEALLEAgkcpECGQPVEGSPHVETIEEDRERVEELeA 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 631 FINTLEAQ----NKRHDVLSKLKEYEQR----------LNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLT 696
Cdd:PRK02224 483 ELEDLEEEveevEERLERAEDLVEAEDRierleerredLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 697 KRKE-QEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRhmEQIEQRKEKAAELS 775
Cdd:PRK02224 563 AEEEaEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERR--ERLAEKRERKRELE 640
|
.
gi 672062331 776 S 776
Cdd:PRK02224 641 A 641
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
540-713 |
5.09e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 540 KRTIAESKKKYEEKHMKA--------QQLREKLREEKSLKLQKLLEREKDVRKwKEELLDQRRRMMEekllhaefKREVQ 611
Cdd:PRK12704 41 KRILEEAKKEAEAIKKEAlleakeeiHKLRNEFEKELRERRNELQKLEKRLLQ-KEENLDRKLELLE--------KREEE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 612 LQAIVKKAQEEEAKVneiafintleaQNKRHDVLSKLKEYEQRLNELQEERQRrqeekQARDEAVQERKRALEAERQARV 691
Cdd:PRK12704 112 LEKKEKELEQKQQEL-----------EKKEEELEELIEEQLQELERISGLTAE-----EAKEILLEKVEEEARHEAAVLI 175
|
170 180
....*....|....*....|..
gi 672062331 692 eelltKRKEQEARIEQQRQEKE 713
Cdd:PRK12704 176 -----KEIEEEAKEEADKKAKE 192
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
537-773 |
7.52e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 46.57 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 537 PSRKRTIAE---SKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWkeeLLDQRRRMMEEKLlhAEFKREVQlq 613
Cdd:pfam15558 3 PERDRKIAAlmlARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRL---LLQQSQEQWQAEK--EQRKARLG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 614 aivkkaQEEEAKVnEIAFINTLEAQNKRHDVLSKlKEyEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQArvEE 693
Cdd:pfam15558 76 ------REERRRA-DRREKQVIEKESRWREQAED-QE-NQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQ--NS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 694 LLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQL--KHDESIRRHMEQIEQR---- 767
Cdd:pfam15558 145 LQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELLRRLSLeqSLQRSQENYEQLVEERhrel 224
|
....*.
gi 672062331 768 KEKAAE 773
Cdd:pfam15558 225 REKAQK 230
|
|
| zf-met |
pfam12874 |
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found ... |
797-819 |
7.52e-05 |
|
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.
Pssm-ID: 463736 [Multi-domain] Cd Length: 25 Bit Score: 40.94 E-value: 7.52e-05
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
501-918 |
1.98e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 501 EAR--ESWRQNTswgDIVEEEPARLPGHGIHMHEKLSSPSRKrtiAESKKKYEEKHmKAQQLREKLREEKSLKLQKLLER 578
Cdd:PTZ00121 1241 EAKkaEEERNNE---EIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAEEKK-KADEAKKAEEKKKADEAKKKAEE 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 579 EKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQlqaiVKKAQEEEAKvneiafiNTLEAQNKRHDVLSKLKEYEqrlnel 658
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE----AAKAEAEAAA-------DEAEAAEEKAEAAEKKKEEA------ 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 659 qeerqrrqeeKQARDEA---VQERKRALEAERQA-----RVEEL------------LTKRKEQEARIEQQRQEKEKARED 718
Cdd:PTZ00121 1377 ----------KKKADAAkkkAEEKKKADEAKKKAeedkkKADELkkaaaakkkadeAKKKAEEKKKADEAKKKAEEAKKA 1446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 719 AARERARDREERLAALTAAQQEA--MEELQKKIQ--LKHDESIRRHME---------QIEQRKEKAAELSSGRHASTdyA 785
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEeaKKADEAKKKAEEakkkadeakKAAEAKKKADEAKKAEEAKK--A 1524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 786 PKLTPYERKKQCSlcNVLIASEVYLFSHIKGKKHQQAVRENSSIQGRElSDEEVEHLSLKKYVVDIVIESAAPPEPMKDG 865
Cdd:PTZ00121 1525 DEAKKAEEAKKAD--EAKKAEEKKKADELKKAEELKKAEEKKKAEEAK-KAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 672062331 866 EERQKNKKKAKKIKARMNTRAKEYENSVETKNSGSESPYK-AKLQRLAKDLVKQ 918
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKeAEEKKKAEELKKA 1655
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
533-629 |
2.13e-04 |
|
Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.
Pssm-ID: 459956 [Multi-domain] Cd Length: 136 Bit Score: 42.72 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 533 KLSSPSRKRTIAESKKkyeEKHMKAQQLREKLREEKSLK-LQKLLEREKDVRKWKEELLDQRRRMMEEKLLHA----EFK 607
Cdd:pfam00836 32 KLSLSPKKKDSSLEEI---QKKLEAAEERRKSLEAQKLKqLAEKREKEEEALQKADEENNNFSKMAEEKLKQKmeayKEN 108
|
90 100
....*....|....*....|..
gi 672062331 608 REVQLQAIVKKAQEEEAKVNEI 629
Cdd:pfam00836 109 REAQIAALKEKLKEKEKHVEEV 130
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
497-788 |
2.27e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 45.03 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 497 LADYEARESWRQNTSWGDIVEEEPARLpghgihmHEKLSspsRKRTIAESKKKYEEKHMKAQQ-LREKLREEKSLKLQKL 575
Cdd:pfam15558 81 RADRREKQVIEKESRWREQAEDQENQR-------QEKLE---RARQEAEQRKQCQEQRLKEKEeELQALREQNSLQLQER 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 576 LEREKDVRKWKEELLDQRRRM--MEEKLLHAEFKREVQLQAivkKAQEEEAKvneiafiNTLE-----AQNKRHDVLskl 648
Cdd:pfam15558 151 LEEACHKRQLKEREEQKKVQEnnLSELLNHQARKVLVDCQA---KAEELLRR-------LSLEqslqrSQENYEQLV--- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 649 keyEQRLNELQEerqrrqeeKQARDEA----VQERKRALEAERQARVEELLtkrKEQEARIEQQRQEKEKAREdaarera 724
Cdd:pfam15558 218 ---EERHRELRE--------KAQKEEEqfqrAKWRAEEKEEERQEHKEALA---ELADRKIQQARQVAHKTVQ------- 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672062331 725 rDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHASTDYAPKL 788
Cdd:pfam15558 277 -DKAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKKEQRSEQISREKEATLEEARKT 339
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
543-741 |
2.70e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 543 IAESKKKYEEKHMKAQQLREKLR------EEKSLKLQKLLEREKDVRKWKEELldqrrrmmEEKLLHAEfKREVQLQAIV 616
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDalqaelEELNEEYNELQAELEALQAEIDKL--------QAEIAEAE-AEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 617 KK----AQEEEAKVNEIAFIntLEAQN-----KRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAER 687
Cdd:COG3883 89 GEraraLYRSGGSVSYLDVL--LGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 672062331 688 QARVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEA 741
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
557-758 |
4.49e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.65 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 557 AQQLREKLREEKSLKlQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNeiafintLE 636
Cdd:COG3064 1 AQEALEEKAAEAAAQ-ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAE-------LA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 637 AQNKRhdvlsKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEEllTKRK-EQEARIEQQRQEKEKA 715
Cdd:COG3064 73 AEAAK-----KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEE--AKRKaEEEAKRKAEEERKAAE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 672062331 716 REDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIR 758
Cdd:COG3064 146 AEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAA 188
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
535-774 |
4.84e-04 |
|
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: 44.56 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 535 SSPSRKRTIAESKKKYEEKHmkaqqlreklREEKSLKLQKLLEREKDVR-KWKEELLDQRRRMMEEKLLHAEFKREVQlq 613
Cdd:pfam15709 297 SSPTQTFVVTGNMESEEERS----------EEDPSKALLEKREQEKASRdRLRAERAEMRRLEVERKRREQEEQRRLQ-- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 614 aivKKAQEEEAKVNEiafinTLEAQNKRHDVLSKLKEyeQRLNElqeerqrrQEEKQARDEAVQERKRALEAERqARVEE 693
Cdd:pfam15709 365 ---QEQLERAEKMRE-----ELELEQQRRFEEIRLRK--QRLEE--------ERQRQEEEERKQRLQLQAAQER-ARQQQ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 694 LLTKRKEQEarIEQQRQEKEKAREDAARERARDREERLAA-----LTAAQQEAMEELQKKiqLKHDESIRRHMEQIEQRK 768
Cdd:pfam15709 426 EEFRRKLQE--LQRKKQQEEAERAEAEKQRQKELEMQLAEeqkrlMEMAEEERLEYQRQK--QEAEEKARLEAEERRQKE 501
|
....*.
gi 672062331 769 EKAAEL 774
Cdd:pfam15709 502 EEAARL 507
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
669-796 |
5.22e-04 |
|
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: 44.17 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 669 KQARDEAVQERKRALEAE-RQARVEElltKRKEQEariEQQRQEKEKAREDAARErardreerlAALTAAQQEAMEELQK 747
Cdd:pfam15709 327 KREQEKASRDRLRAERAEmRRLEVER---KRREQE---EQRRLQQEQLERAEKMR---------EELELEQQRRFEEIRL 391
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 672062331 748 KIQLKHDESIRRHMEQIEQRKEKAAELSSGRHASTDYAPKLTPYERKKQ 796
Cdd:pfam15709 392 RKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQ 440
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
539-948 |
5.44e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 539 RKRTIAESKKKYEEKHMKAQQLR---EKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAI 615
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLQTKEqihLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQT 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 616 VKKAQEEEAKVNEI-------AFINTLEAQNKRHDvLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQ 688
Cdd:TIGR00618 537 YAQLETSEEDVYHQltserkqRASLKEQMQEIQQS-FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 689 ARVEELLTKRKEQEARIE----QQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHM--- 761
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRLHlqqcSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtyw 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 762 -EQIEQRKEKAAELSSgrhastdyapKLTPYERKKQcSLCNVLIASevylfshiKGKKHQQAVRENSSIQG-RELSDEEV 839
Cdd:TIGR00618 696 kEMLAQCQTLLRELET----------HIEEYDREFN-EIENASSSL--------GSDLAAREDALNQSLKElMHQARTVL 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 840 EHLSLkkyvVDIVIESAAPPEPMKDGEERQKNKKkakkikarMNTRAKEYENSV-ETKNSGSESPYKAKLQRLAKDLVKQ 918
Cdd:TIGR00618 757 KARTE----AHFNNNEEVTAALQTGAELSHLAAE--------IQFFNRLREEDThLLKTLEAEIGQEIPSDEDILNLQCE 824
|
410 420 430
....*....|....*....|....*....|
gi 672062331 919 LQVQDSGSwVNNKASALDRTLGEIARILEK 948
Cdd:TIGR00618 825 TLVQEEEQ-FLSRLEEKSATLGEITHQLLK 853
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
540-780 |
6.31e-04 |
|
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: 43.75 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 540 KRTIAESKKKYEEKHmkAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLL-HAEFKRE-VQLQAIVK 617
Cdd:pfam13868 31 KKRIKAEEKEEERRL--DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEeYEEKLQErEQMDEIVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 618 KAQEEEakvneiafintleaqnkrhdvlskLKEYEQRLNElqeerqrrQEE-KQARDEAVQERKRALEAERQA------R 690
Cdd:pfam13868 109 RIQEED------------------------QAEAEEKLEK--------QRQlREEIDEFNEEQAEWKELEKEEereedeR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 691 VEELLTKRKEQEARIEQQRQEKEKaredaARERARDREERLAALTAAQQEAMEEL-QKKIQLKHDESIR-RHMEQIEQRK 768
Cdd:pfam13868 157 ILEYLKEKAEREEEREAEREEIEE-----EKEREIARLRAQQEKAQDEKAERDELrAKLYQEEQERKERqKEREEAEKKA 231
|
250
....*....|..
gi 672062331 769 EKAAELSSGRHA 780
Cdd:pfam13868 232 RQRQELQQAREE 243
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
539-704 |
7.06e-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: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 539 RKRTIAESKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREV-QLQAIVK 617
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLeAEREELL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 618 KAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELqeerqrrqeekqardEAVQErkRALE--AERQARVEELL 695
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL---------------GPVNL--LAIEeyEELEERYDFLS 801
|
170
....*....|
gi 672062331 696 TKRKE-QEAR 704
Cdd:COG1196 802 EQREDlEEAR 811
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
669-752 |
7.14e-04 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 43.33 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 669 KQARDEAVQERKRALEAERQarvEELltkrkeQEARIEQQRQEKEKaredaarerardreeRLAALTAAQQEAMEELQKK 748
Cdd:pfam07946 263 KKTREEEIEKIKKAAEEERA---EEA------QEKKEEAKKKEREE---------------KLAKLSPEEQRKYEEKERK 318
|
....
gi 672062331 749 IQLK 752
Cdd:pfam07946 319 KEQR 322
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
540-711 |
1.19e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.05 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 540 KRTIAESKKKYEEKHMKAQQLREKLREEKSL---KLQKLLEREKDVRkwkeELLDQRRRMMEEKLLHAEFKREV-QLQAI 615
Cdd:cd00176 46 EAELAAHEERVEALNELGEQLIEEGHPDAEEiqeRLEELNQRWEELR----ELAEERRQRLEEALDLQQFFRDAdDLEQW 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 616 VKKAQEEEAKVNEIAFINTLEAQNKRHDVL-SKLKEYEQRLNELqeerqrrqeeKQARDEAVQERKRALEAERQARVEEL 694
Cdd:cd00176 122 LEEKEAALASEDLGKDLESVEELLKKHKELeEELEAHEPRLKSL----------NELAEELLEEGHPDADEEIEEKLEEL 191
|
170
....*....|....*..
gi 672062331 695 LTKRKEQEARIEQQRQE 711
Cdd:cd00176 192 NERWEELLELAEERQKK 208
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
578-773 |
1.38e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 578 REKDVRKWKeelldQRRRMM----EEKLlhAEFKREV-QLQAIVKKAQEEEAKVNEIafintLEAQNKRHDVLSKLKEY- 651
Cdd:COG4913 590 HEKDDRRRI-----RSRYVLgfdnRAKL--AALEAELaELEEELAEAEERLEALEAE-----LDALQERREALQRLAEYs 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 652 --EQRLNELQEERQRRQEEKQARD------EAVQERKRALEAERQA---RVEELLTKRKEQEARIEQQRQEKEKAREDAA 720
Cdd:COG4913 658 wdEIDVASAEREIAELEAELERLDassddlAALEEQLEELEAELEEleeELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 672062331 721 RERARDREERLAALTAA-QQEAMEELQKKIQlkhdESIRRHMEQIEQRKEKAAE 773
Cdd:COG4913 738 AAEDLARLELRALLEERfAAALGDAVERELR----ENLEERIDALRARLNRAEE 787
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
543-771 |
1.51e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 543 IAESKKKYEEKHMKAQQLREK-----LREEKSLKLQKLLErekdvrkwkeelLDQRRRMMEEKLLHAEFKREvQLQAIVK 617
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSE------------LESQLAEARAELAEAEARLA-ALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 618 KAQEEEAKVNEIAFINTLEAQnkRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLTK 697
Cdd:COG3206 251 SGPDALPELLQSPVIQQLRAQ--LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAR 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672062331 698 RKEQEARIEQQRQEkekaredaarerardreerLAALTAAQQEaMEELQKKIQLKhdesiRRHMEQIEQRKEKA 771
Cdd:COG3206 329 EASLQAQLAQLEAR-------------------LAELPELEAE-LRRLEREVEVA-----RELYESLLQRLEEA 377
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
559-707 |
1.85e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 559 QLREKLREEKSL-----KLQKLLEREKDVRKWKEELLDQRRRMMEEKLlhAEFKREvqLQAIVKKAQEEEAKVNEIAFIN 633
Cdd:pfam07888 35 RLEECLQERAELlqaqeAANRQREKEKERYKRDREQWERQRRELESRV--AELKEE--LRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672062331 634 TLEAQNKrhDVLSKLK-EYEQRLNELQEERqrrqeekQARDEAVQERKRALEAERQaRVEELLTKRKEQEARIEQ 707
Cdd:pfam07888 111 EELSEEK--DALLAQRaAHEARIRELEEDI-------KTLTQRVLERETELERMKE-RAKKAGAQRKEEEAERKQ 175
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
556-854 |
2.04e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 556 KAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEekllhaefkREVQLQAIVKKAQEEEAKVNeiafintl 635
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ---------LEEELEELNEQLQAAQAELA-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 636 EAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALeAERQARVEELLTKRKEQEARIEQQRQEKEKA 715
Cdd:COG4372 98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI-AEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 716 REDAARerardreerlAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHASTDYAPKLTPYERKK 795
Cdd:COG4372 177 SEAEAE----------QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 672062331 796 QCSLCNVLIASEVYLFSHIKGKKHQQAVRENSSIQGRELSDEEVEHLSLKKYVVDIVIE 854
Cdd:COG4372 247 DKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
532-714 |
2.35e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 532 EKLSSPSRKRTIAESKKKYEEKHMK-AQQLREKLREEKSL--KLQKLLEREKDVRKWK------EELLDQRRRMMEEKLL 602
Cdd:PRK05771 73 REEKKKVSVKSLEELIKDVEEELEKiEKEIKELEEEISELenEIKELEQEIERLEPWGnfdldlSLLLGFKYVSVFVGTV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 603 HAEFKREVQLQAIVKKAQEEEAKVNE--IAFINtleAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQardeaVQERK 680
Cdd:PRK05771 153 PEDKLEELKLESDVENVEYISTDKGYvyVVVVV---LKELSDEVEEELKKLGFERLELEEEGTPSELIRE-----IKEEL 224
|
170 180 190
....*....|....*....|....*....|....*...
gi 672062331 681 RALEAERQARVEELLTKRKEQEARI----EQQRQEKEK 714
Cdd:PRK05771 225 EEIEKERESLLEELKELAKKYLEELlalyEYLEIELER 262
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
571-776 |
3.10e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 571 KLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEIafINTLE-----AQNKRHDVL 645
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEE--IERYEeqreqARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 646 SKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEA--ERQARVEELLTKRKEQEARIEQQRQEKEkaredaarer 723
Cdd:PRK02224 241 EVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEvrDLRERLEELEEERDDLLAEAGLDDADAE---------- 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672062331 724 arDREERLAALTAAQQEAMEELQKK---IQLKHD------ESIRRHMEQIEQRKEKAAELSS 776
Cdd:PRK02224 311 --AVEARREELEDRDEELRDRLEECrvaAQAHNEeaeslrEDADDLEERAEELREEAAELES 370
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
552-714 |
3.13e-03 |
|
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: 40.68 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 552 EKHMKAQQLREKLREEKslklQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREV-QLQAIVKKAQE--EEAKVNE 628
Cdd:COG1579 14 ELDSELDRLEHRLKELP----AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIeEVEARIKKYEEqlGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 629 I--AFINTLEAQNKRHDVLSK-LKEYEQRLNELqeerqrrqeekqardEAVQERKRALEAERQARVEELLTKRKEQEARI 705
Cdd:COG1579 90 EyeALQKEIESLKRRISDLEDeILELMERIEEL---------------EEELAELEAELAELEAELEEKKAELDEELAEL 154
|
....*....
gi 672062331 706 EQQRQEKEK 714
Cdd:COG1579 155 EAELEELEA 163
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
517-694 |
3.24e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 41.37 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 517 EEEPARLPghgiHMHEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKSLKLQKLLErekdvRKWKEELLDQrrrm 596
Cdd:TIGR02794 85 AAEQARQK----ELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE-----RKAKEEAAKQ---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 597 meekllhAEFKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKeyeqrlNELQEERQRRQEEKQARDEAv 676
Cdd:TIGR02794 152 -------AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAK------AEAAKAKAAAEAAAKAEAEA- 217
|
170
....*....|....*...
gi 672062331 677 qERKRALEAERQARVEEL 694
Cdd:TIGR02794 218 -AAAAAAEAERKADEAEL 234
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
607-773 |
4.11e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.33 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 607 KREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRhdvlsKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRA-LEA 685
Cdd:PRK09510 75 KRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKE-----RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAkAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 686 ERQARVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALT--AAQQEAMEELQKKIQLKHDESIRRHMEQ 763
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAkkKAEAEAKKKAAAEAKKKAAAEAKAAAAK 229
|
170
....*....|
gi 672062331 764 IEQRKEKAAE 773
Cdd:PRK09510 230 AAAEAKAAAE 239
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
669-777 |
4.54e-03 |
|
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: 40.64 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 669 KQARDEAVQERKRALeAERQARVEElltkrkEQEARIEQQRQEKEKAredaarerardreerlaaltaaQQEAMEELQKK 748
Cdd:cd16269 195 EKEKEIEAERAKAEA-AEQERKLLE------EQQRELEQKLEDQERS----------------------YEEHLRQLKEK 245
|
90 100 110
....*....|....*....|....*....|
gi 672062331 749 IQLKHDESIRRHMEQIEQR-KEKAAELSSG 777
Cdd:cd16269 246 MEEERENLLKEQERALESKlKEQEALLEEG 275
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
540-708 |
5.09e-03 |
|
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: 40.29 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 540 KRTIAESKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREkdvrkwkEELLDQRRRMMEEKLLHAEFKREvQLQAIVKKA 619
Cdd:COG1579 58 EKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKE-------IESLKRRISDLEDEILELMERIE-ELEEELAEL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 620 QEEeakvneiafintleaqnkrhdvlskLKEYEQRLNELqeerqrrqeeKQARDEAVQErkraLEAERqarvEELLTKRK 699
Cdd:COG1579 130 EAE-------------------------LAELEAELEEK----------KAELDEELAE----LEAEL----EELEAERE 166
|
....*....
gi 672062331 700 EQEARIEQQ 708
Cdd:COG1579 167 ELAAKIPPE 175
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
562-774 |
6.41e-03 |
|
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: 41.21 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 562 EKLREEkslkLQKLLEREKDVRKWKEELLDQRRRMMEEKLlHAEfkrevQLQAIVKKAQEEEAKVnEIAFINTLEAQNKR 641
Cdd:TIGR02169 173 EKALEE----LEEVEENIERLDLIIDEKRQQLERLRRERE-KAE-----RYQALLKEKREYEGYE-LLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 642 HDV-LSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLTKRKEQEARIEQQRQEKEKAREDAA 720
Cdd:TIGR02169 242 IERqLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 672062331 721 RErardrEERLAALTAAQQEAMEELQKKIQlkhDESIRRH--MEQIEQRKEKAAEL 774
Cdd:TIGR02169 322 ER-----LAKLEAEIDKLLAEIEELEREIE---EERKRRDklTEEYAELKEELEDL 369
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
549-793 |
7.12e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 549 KYEEKHMKAQQLREKLREEKSLKLQK----LLEREKDVRKWKEELLDQrrrmmeEKLLHAEFKREVQLQAIVKKAQEEEA 624
Cdd:PRK03918 76 KFEKNGRKYRIVRSFNRGESYLKYLDgsevLEEGDSSVREWVERLIPY------HVFLNAIYIRQGEIDAILESDESREK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 625 KVNEIAFINTLE-AQNKRHDVLSKLKEYEQRLNELQeerqrrqeekqARDEAVQERKRALEAErqarVEELLTKRKEQEA 703
Cdd:PRK03918 150 VVRQILGLDDYEnAYKNLGEVIKEIKRRIERLEKFI-----------KRTENIEELIKEKEKE----LEEVLREINEISS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 704 RIEQQRQEKEKAREDAARERArdreerLAALTAAQQEAMEELQKKIQlKHDESIRRHMEQIEQRKEKAAELSSGRHASTD 783
Cdd:PRK03918 215 ELPELREELEKLEKEVKELEE------LKEEIEELEKELESLEGSKR-KLEEKIRELEERIEELKKEIEELEEKVKELKE 287
|
250
....*....|
gi 672062331 784 YAPKLTPYER 793
Cdd:PRK03918 288 LKEKAEEYIK 297
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
615-714 |
7.83e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 615 IVKKAQ----EEEAKVNEIafINTLEAQ-----NKRHDVLSKLKEYEQRLNELqeerqrrqeekQARDEAVQERKRALEA 685
Cdd:PRK00409 503 IIEEAKkligEDKEKLNEL--IASLEELereleQKAEEAEALLKEAEKLKEEL-----------EEKKEKLQEEEDKLLE 569
|
90 100
....*....|....*....|....*....
gi 672062331 686 ERQARVEELLTKRKEQEARIEQQRQEKEK 714
Cdd:PRK00409 570 EAEKEAQQAIKEAKKEADEIIKELRQLQK 598
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
532-930 |
7.84e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 532 EKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFK--RE 609
Cdd:COG5022 820 IKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISslKL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 610 VQLQ------AIVKKAQEEEAKVNEI--AFINTLEAQNKRHDV-LSKLKEYEQ--RLNELqeerqrrQEEKQARDEAVQE 678
Cdd:COG5022 900 VNLEleseiiELKKSLSSDLIENLEFktELIARLKKLLNNIDLeEGPSIEYVKlpELNKL-------HEVESKLKETSEE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 679 RKRAL----EAERQARVEELLTKRKEQEArieqQRQEKEKAREDAARERARDREERLAALTAAQQEAMEE-LQKKIQLKH 753
Cdd:COG5022 973 YEDLLkkstILVREGNKANSELKNFKKEL----AELSKQYGALQESTKQLKELPVEVAELQSASKIISSEsTELSILKPL 1048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 754 DESIRRHMEQIEQRKEKAAELSSGRHASTDYapKLTPYERKKQCSLCNVLIASEVYLFSHIKGKKhqQAVRENSSIQG-- 831
Cdd:COG5022 1049 QKLKGLLLLENNQLQARYKALKLRRENSLLD--DKQLYQLESTENLLKTINVKDLEVTNRNLVKP--ANVLQFIVAQMik 1124
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 832 RELSDEEVEHLSLKKYVVDIVIESAAPPEPMKDGEERQKNKKKAKKIKARMNTRAKE--YENSVETKNSGSES------- 902
Cdd:COG5022 1125 LNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRlyQSALYDEKSKLSSSevndlkn 1204
|
410 420
....*....|....*....|....*...
gi 672062331 903 PYKAKLQRLAKDLVKQLQVQDSGSWVNN 930
Cdd:COG5022 1205 ELIALFSKIFSGWPRGDKLKKLISEGWV 1232
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
547-714 |
8.36e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 547 KKKYEEKHMKAQQLREKLRE--------EKSLKLQKLLEREK--------DVRKWKEELLDQRRRM-------MEEKL-- 601
Cdd:PRK03918 517 LEELEKKAEEYEKLKEKLIKlkgeikslKKELEKLEELKKKLaelekkldELEEELAELLKELEELgfesveeLEERLke 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 602 LHAEFKREVQLQAIVKKAQEEEAKVNEIAfiNTL-EAQNKRHDVLSKLKEYEQRLNELQEERQrrqeekQARDEAVQERK 680
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKKLE--EELdKAFEELAETEKRLEELRKELEELEKKYS------EEEYEELREEY 668
|
170 180 190
....*....|....*....|....*....|....*..
gi 672062331 681 RALEAE---RQARVEELLTKRKEQEARIEQQRQEKEK 714
Cdd:PRK03918 669 LELSRElagLRAELEELEKRREEIKKTLEKLKEELEE 705
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
572-711 |
8.78e-03 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 38.06 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 572 LQKLLEREKDVRKWKEELLDQRRrmmeekllhAEFKR-EVQLQAIVKKAQEEEAKVNEIAFINTLEAQnkrhdvLSKLKE 650
Cdd:TIGR02473 4 LQKLLDLREKEEEQAKLELAKAQ---------AEFERlETQLQQLIKYREEYEQQALEKVGAGTSALE------LSNYQR 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672062331 651 YEQRLNELQEERQRrqeeKQARDEAVQERKRALEAERQARVE--ELLTKRKEQEARIEQQRQE 711
Cdd:TIGR02473 69 FIRQLDQRIQQQQQ----ELALLQQEVEAKRERLLEARRELKalEKLKEKKQKEYRAEEAKRE 127
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
636-714 |
8.80e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 37.80 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 636 EAQNKRHDVLSKLKEYEQRLnelqeerqrrqeeKQARDEAVQERKRAlEAERQARVEELLTKRKEQEARIEQQ-----RQ 710
Cdd:cd06503 41 EAEKAKEEAEELLAEYEEKL-------------AEARAEAQEIIEEA-RKEAEKIKEEILAEAKEEAERILEQakaeiEQ 106
|
....
gi 672062331 711 EKEK 714
Cdd:cd06503 107 EKEK 110
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
543-755 |
9.12e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 543 IAESKKKYEEKHMKAQQLREKLREEKSlKLQKLLEREKDVRKWKEELLDQRRRMMEEKL-LHAE---FKREVQLQAIVKK 618
Cdd:COG1340 73 VKELKEERDELNEKLNELREELDELRK-ELAELNKAGGSIDKLRKEIERLEWRQQTEVLsPEEEkelVEKIKELEKELEK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 619 AQEEEAKVNEIAFINT--LEAQNKRHDVLSKLKEYEQRLNELQEERQRRqeeKQARDEAVQERKRALEA--ERQARVEEL 694
Cdd:COG1340 152 AKKALEKNEKLKELRAelKELRKEAEEIHKKIKELAEEAQELHEEMIEL---YKEADELRKEADELHKEivEAQEKADEL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672062331 695 ltkRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDE 755
Cdd:COG1340 229 ---HEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTTEE 286
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
543-775 |
9.20e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 543 IAESKKKYEEKHMKAQQLREKLREEKSLKlQKLLEREKDVRKWKEELLDQRRRMMEE-----KLLHAEFKREVQLQAIVK 617
Cdd:COG1340 38 LKELAEKRDELNAQVKELREEAQELREKR-DELNEKVKELKEERDELNEKLNELREEldelrKELAELNKAGGSIDKLRK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 618 KAQEEEAKvneiaFIN---TLEAQNKrhdVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQarVEEL 694
Cdd:COG1340 117 EIERLEWR-----QQTevlSPEEEKE---LVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKK--IKEL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 695 LTKRKEQEARIEQQRQEKEKAREDAARERardreerlAALTAAQQEAMEELQKKIQLKhdESIRRHMEQIEQRKEKAAEL 774
Cdd:COG1340 187 AEEAQELHEEMIELYKEADELRKEADELH--------KEIVEAQEKADELHEEIIELQ--KELRELRKELKKLRKKQRAL 256
|
.
gi 672062331 775 S 775
Cdd:COG1340 257 K 257
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
577-750 |
9.25e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 577 EREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEIAFIntLEAQNKRHDVLSKLKEYEQRLN 656
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL--TGGSRRELLAALLEAEAELEEL 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672062331 657 ELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTA 736
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
170
....*....|....
gi 672062331 737 AQQEaMEELQKKIQ 750
Cdd:COG1196 765 LERE-LERLEREIE 777
|
|
| |
