|
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 ... |
94-191 |
3.11e-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: 186.85 E-value: 3.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 94 KTRHPRKIDLRARYWAFLFDNLRRAVDEIYVTCESDQSVVECKEVLMMLDYYVRDFKALIDWIQLQEKLEKTDAQSRPTS 173
Cdd:pfam16501 1 STGRDKKSELRARYWAFLFDNLQRAVDEIYQTCESDESVVECKEVIMVLDNYTRDFKALIEWFRLKWDYENTPPPQRPTS 80
|
90
....*....|....*...
gi 1958798880 174 LAWEVKKMSPGRHVIQSP 191
Cdd:pfam16501 81 LAWEVRKSSPGKSVNKSP 98
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
546-794 |
9.18e-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: 9.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 546 KRTIAESKKKYEEKHMKAQQLREKLREEkSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKA 625
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 626 QEEEAKVNEIAFINTL-EAQNKRHDVLSKLKEYEQRLNELqeerqrRQEEKQARDEAVQERKRALEAERQARVEELLTKR 704
Cdd:COG1196 331 ELEELEEELEELEEELeEAEEELEEAEAELAEAEEALLEA------EAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 705 KEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQkKIQLKHDESIRRHMEQIEQRKEKAAELSSGR 784
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA-ELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250
....*....|
gi 1958798880 785 HASTDYAPKL 794
Cdd:COG1196 484 EELAEAAARL 493
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
538-924 |
1.13e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.17 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 538 EKLSSPSRKRTIAESKKKYEEKHMKAQQLREK--LREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKRE 615
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAaeAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 616 VqlQAIVKKAQEEEAKVNEiafINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEA------------VQ 683
Cdd:PTZ00121 1393 A--DEAKKKAEEDKKKADE---LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAeeakkaeeakkkAE 1467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 684 ERKRALEAERQA----RVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKH 759
Cdd:PTZ00121 1468 EAKKADEAKKKAeeakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 760 DESIRRHMEQIEQRKEKAAElsSGRHASTDYAPKLTPYERKKQCSlcNVLIASEVYLFSHIKGKKHQQAVR-ENSSIQGR 838
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAE--EAKKAEEDKNMALRKAEEAKKAE--EARIEEVMKLYEEEKKMKAEEAKKaEEAKIKAE 1623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 839 ELSDEEVEHLSLKKYVVDIVIESAAPPEPMKDGEERQKNKKKAKKIKARMNTRAKEYENSVETKNSGSESPYK-AKLQRL 917
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKeAEEAKK 1703
|
....*..
gi 1958798880 918 AKDLVKQ 924
Cdd:PTZ00121 1704 AEELKKK 1710
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
550-779 |
3.74e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.24 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 550 AESKKKYEEKHmKAQQLReKLREEKSLKLQKLLEREKDVRKWKEELLDQ--RRRMMEEKLLHAEFKREVQLQAivKKAQE 627
Cdd:PTZ00121 1542 AEEKKKADELK-KAEELK-KAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEEKKMKAEEA--KKAEE 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 628 EEAKVNEIafiNTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARD--EAVQERKRALE---AERQARVEELLT 702
Cdd:PTZ00121 1618 AKIKAEEL---KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEakKAEEDKKKAEEakkAEEDEKKAAEAL 1694
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798880 703 KRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 779
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
562-779 |
5.40e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 562 KAQQLREKLRE-EKSLKLQKLLEREKDVRKWKEELLDQRRRmmEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEiafint 640
Cdd:COG1196 214 RYRELKEELKElEAELLLLKLRELEAELEELEAELEELEAE--LEELEAELAELEAELEELRLELEELELELEE------ 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 641 leAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQ------ARDEAVQERKRALEAERQARVEELLTKRKEQEARIEQQ 714
Cdd:COG1196 286 --AQAEEYELLAELARLEQDIARLEERRRELEERLEeleeelAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798880 715 RQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 779
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
545-782 |
6.62e-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: 6.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 545 RKRTIAESKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKK 624
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 625 AQEEEAKVNEIAFintLEAQNKRHDVLSKLKEYEQRLNELQEERqrrqeEKQARDEAVQERKRALEAERQARVEELLTKR 704
Cdd:COG1196 341 ELEEELEEAEEEL---EEAEAELAEAEEALLEAEAELAEAEEEL-----EELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798880 705 KEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHD-ESIRRHMEQIEQRKEKAAELSS 782
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELlEEAALLEAALAELLEELAEAAA 491
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
432-776 |
3.18e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 432 AKKEELADRLEK---ANEEAIASAIAEEEQLTREIEA--EENNDINIETDNDSDFSASMGSgslsfcgmslDWNDVLADY 506
Cdd:PRK02224 359 EELREEAAELESeleEAREAVEDRREEIEELEEEIEElrERFGDAPVDLGNAEDFLEELRE----------ERDELRERE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 507 EARESWRQNTSwGDIVEEEPARLPGHGIHMHEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKL--------REEKSLKL 578
Cdd:PRK02224 429 AELEATLRTAR-ERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVeeveerleRAEDLVEA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 579 QKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKR----------EVQLQAIVKKAQEEEAKVNEIAFIN--------T 640
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELReraaeleaeaEEKREAAAEAEEEAEEAREEVAELNsklaelkeR 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 641 LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQ---ERKRALEAERQ-ARVEELLTKRKEQEARIEQQRQ 716
Cdd:PRK02224 588 IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAekrERKRELEAEFDeARIEEAREDKERAEEYLEQVEE 667
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798880 717 EkekaredaarerardreerLAALTaaqqEAMEELQKKI-----QLKHDESIRRHMEQIEQRKEK 776
Cdd:PRK02224 668 K-------------------LDELR----EERDDLQAEIgavenELEELEELRERREALENRVEA 709
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
546-949 |
4.81e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 546 KRTIAESKKKYEEKHmKAQQLREKLREEKslKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLqaiVKKA 625
Cdd:PTZ00121 1469 AKKADEAKKKAEEAK-KADEAKKKAEEAK--KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE---AKKA 1542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 626 qEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELqeerQRRQEEKQARDEAVQERKRALEAERQARVEELltkRK 705
Cdd:PTZ00121 1543 -EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL----RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA---KK 1614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 706 EQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDEsirrhmeqiEQRKEKAAELSSGRH 785
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA---------EEDKKKAEEAKKAEE 1685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 786 ASTDYAPKLTPYERKKQcslcnvlIASEVYLFSHIKGKKHQQAVR--ENSSIQGRELSDEEVEhlslkkyvvdiviESAA 863
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAK-------KAEELKKKEAEEKKKAEELKKaeEENKIKAEEAKKEAEE-------------DKKK 1745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 864 PPEPMKDGEERQKNKKKAKKIKARMNTRAKEYENSVETKNSGSESPYKAKLQRLAKDLVKQLQVQDSGS-----WVNNKA 938
Cdd:PTZ00121 1746 AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGkegnlVINDSK 1825
|
410
....*....|.
gi 1958798880 939 SALDRTLGEIA 949
Cdd:PTZ00121 1826 EMEDSAIKEVA 1836
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
545-779 |
5.48e-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: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 545 RKRTIAESKKKYEEKHMKAQQLREKL------REEKSLKLQKLLEREKD-----VRKWKEE-LLDQRRRMMEEKLLHAEF 612
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELeeqieeREQKRQEEYEEKLQEREqmdeiVERIQEEdQAEAEEKLEKQRQLREEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 613 KREVQLQAIVKKAQEEEAKVNE---IAFINTLEAQNKRHDVLSKLKEY--EQRLNELQEERQRRQEEKQARDEAVQER-K 686
Cdd:pfam13868 133 DEFNEEQAEWKELEKEEEREEDeriLEYLKEKAEREEEREAEREEIEEekEREIARLRAQQEKAQDEKAERDELRAKLyQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 687 RALEAERQARVEELLTKRKEQEARI----EQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKK--IQLKHD 760
Cdd:pfam13868 213 EEQERKERQKEREEAEKKARQRQELqqarEEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRrmKRLEHR 292
|
250
....*....|....*....
gi 1958798880 761 ESIRRHMEQIEQRKEKAAE 779
Cdd:pfam13868 293 RELEKQIEEREEQRAAERE 311
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
544-773 |
8.28e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 8.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 544 SRKRTIAESKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWKEEL--LDQRRRMMEEKLLHAEFKREVQLQAI 621
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELeeAEEELEEAEAELAEAEEALLEAEAEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 622 VKKAQEEEAKVNEIafintLEAQNKRHDVLSKLKEYEQRLNELQEERQRrQEEKQARDEAVQERKRALEAERQARVEELL 701
Cdd:COG1196 375 AEAEEELEELAEEL-----LEALRAAAELAAQLEELEEAEEALLERLER-LEEELEELEEALAELEEEEEEEEEALEEAA 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798880 702 TKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQR 773
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
599-779 |
1.24e-09 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 62.49 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 599 RRRMMEEKLLHAEFKREvqlqAIVKKAQEE-EAKVNEIafinTLEAQNKRHDVLSKL-KEYEQRLNELQEERQRRQEEKQ 676
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAK----RILEEAKKEaEAIKKEA----LLEAKEEIHKLRNEFeKELRERRNELQKLEKRLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 677 A---RDEAVQERKRALEAERQ---ARVEELLTKRKEQEARIEQQRQEKEKaredaarerardreerLAALTA--AQQEAM 748
Cdd:PRK12704 97 NldrKLELLEKREEELEKKEKeleQKQQELEKKEEELEELIEEQLQELER----------------ISGLTAeeAKEILL 160
|
170 180 190
....*....|....*....|....*....|.
gi 1958798880 749 EELQKKIQLKHDESIRRHMEQIEQRKEKAAE 779
Cdd:PRK12704 161 EKVEEEARHEAAVLIKEIEEEAKEEADKKAK 191
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
539-719 |
3.18e-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: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 539 KLSSPSRKRTIAESKKKYEEKHMKAQQLRE----KLREEKSLKLQKL----LEREKDVRKWKEELLDQRRRMMEeklLHA 610
Cdd:pfam17380 405 KILEEERQRKIQQQKVEMEQIRAEQEEARQrevrRLEEERAREMERVrleeQERQQQVERLRQQEEERKRKKLE---LEK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 611 EFKREVQLQAIVKKAQEEEAKVNEIAFIntlEAQNKRHDVLsklKEYEQRLNELQEerqrrqeeKQARDEAVQERKRALE 690
Cdd:pfam17380 482 EKRDRKRAEEQRRKILEKELEERKQAMI---EEERKRKLLE---KEMEERQKAIYE--------EERRREAEEERRKQQE 547
|
170 180
....*....|....*....|....*....
gi 1958798880 691 AERQARVEELLTKRKEQEARIEQQRQEKE 719
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEAMERERE 576
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
546-779 |
5.20e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 546 KRTIAESKKKYEEKHMKAQQLREKLRE-EKSL--KLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEF-KREVQLQAI 621
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEkEKELeeVLREINEISSELPELREELEKLEKEVKELEELKEEIeELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 622 VKKAQEEEAKVNEI-AFINTLEAQnkrhdvLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQE------RKRALEAERQ 694
Cdd:PRK03918 251 EGSKRKLEEKIRELeERIEELKKE------IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDElreiekRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 695 ArVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAaltAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRK 774
Cdd:PRK03918 325 G-IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA---KAKKEELERLKKRLTGLTPEKLEKELEELEKAK 400
|
....*
gi 1958798880 775 EKAAE 779
Cdd:PRK03918 401 EEIEE 405
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
552-779 |
1.03e-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: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 552 SKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ--LQAIVKKAQEEE 629
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEekLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 630 AKVNEIAFINtLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEkQARDEAVQERKRALEAERQARVEELLTKRKEQEA 709
Cdd:TIGR02168 281 EEIEELQKEL-YALANEISRLEQQKQILRERLANLERQLEELEAQ-LEELESKLDELAEELAELEEKLEELKEELESLEA 358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798880 710 RIEQQRQEKEkaredaarerardreeRLAALTAAQQEAMEELQKKI-QLKHD--------ESIRRHMEQIEQRKEKAAE 779
Cdd:TIGR02168 359 ELEELEAELE----------------ELESRLEELEEQLETLRSKVaQLELQiaslnneiERLEARLERLEDRRERLQQ 421
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
545-779 |
1.90e-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: 58.01 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 545 RKRTIAESKK-KYEEKHMK---AQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLL-HAEFKRE-VQL 618
Cdd:pfam13868 24 RDAQIAEKKRiKAEEKEEErrlDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEeYEEKLQErEQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 619 QAIVKKAQEEEAKVNEIAFI---NTLEAQNKRHDVLSKLKEYE-QRLNELQEERQRRQEEKQARDEAVQERKRALEAERQ 694
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEkqrQLREEIDEFNEEQAEWKELEkEEEREEDERILEYLKEKAEREEEREAEREEIEEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 695 ARVEELLtkrkEQEARIEQQRQEKEKaredaarerardreeRLAALTAAQQEA------MEELQKKIQLKHD--ESIRRH 766
Cdd:pfam13868 184 REIARLR----AQQEKAQDEKAERDE---------------LRAKLYQEEQERkerqkeREEAEKKARQRQElqQAREEQ 244
|
250
....*....|...
gi 1958798880 767 MEQIEQRKEKAAE 779
Cdd:pfam13868 245 IELKERRLAEEAE 257
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
418-720 |
1.94e-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: 59.31 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 418 SNVSAADWSMAEVLAKKEELADRLEKANEEaiasaIAEEEQLTREIEAEENNDINIETDNDSDFSAsmgsgslsfcgMSL 497
Cdd:TIGR02169 709 QELSDASRKIGEIEKEIEQLEQEEEKLKER-----LEELEEDLSSLEQEIENVKSELKELEARIEE-----------LEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 498 DWNDV---LADYEARES---WRQNTSWGDIVEEEPARLPGHGIHMHEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLR 571
Cdd:TIGR02169 773 DLHKLeeaLNDLEARLShsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 572 EEK----SLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLlhaefKREVQLQAIVKKAQEEEAKVnEIAFINTLEAQNKR 647
Cdd:TIGR02169 853 EKEienlNGKKEELEEELEELEAALRDLESRLGDLKKERD-----ELEAQLRELERKIEELEAQI-EKKRKRLSELKAKL 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 648 HDVLSKLKEYEQRLNELQEERQRRQEEK--QARDEAVQERKRALE----------AERQARVEELLTK-------RKEQE 708
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEIPEEELSLEdvQAELQRVEEEIRALEpvnmlaiqeyEEVLKRLDELKEKrakleeeRKAIL 1006
|
330
....*....|..
gi 1958798880 709 ARIEQQRQEKEK 720
Cdd:TIGR02169 1007 ERIEEYEKKKRE 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
543-961 |
3.91e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 543 PSRKRTIAESKKK------YEEKHMKAQQLR--EKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEkllhAEFKR 614
Cdd:PTZ00121 1074 PSYKDFDFDAKEDnradeaTEEAFGKAEEAKktETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEE----ARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 615 EVQLQAIVKKAqeEEAKVNEIAfintLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQ 694
Cdd:PTZ00121 1150 DAKRVEIARKA--EDARKAEEA----RKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDA 1223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 695 ARVEELL----TKRKEQEA-RIEQQRQEKEKAREDAARERARDREErlAALTAAQQEAMEELQKKIQLKHDESIRRHME- 768
Cdd:PTZ00121 1224 KKAEAVKkaeeAKKDAEEAkKAEEERNNEEIRKFEEARMAHFARRQ--AAIKAEEARKADELKKAEEKKKADEAKKAEEk 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 769 -QIEQRKEKAAELSSGRHASTDY--------APKLTPYERKKqcslcnvliASEVYLFSHIKGKKHQQAVRENSSIQGRE 839
Cdd:PTZ00121 1302 kKADEAKKKAEEAKKADEAKKKAeeakkkadAAKKKAEEAKK---------AAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 840 LSDEEVEHLSLKKYVvdiviESAAPPEPMKDGEERQKNKKKAKKIKARMNTRAKEYENSVETKNSGSESPYKAKLQRLAK 919
Cdd:PTZ00121 1373 KEEAKKKADAAKKKA-----EEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD 1447
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958798880 920 DLVKQLQVQDSGSWVNNKASAlDRTLGEIARILEKENVADQI 961
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEE-AKKADEAKKKAEEAKKADEA 1488
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
446-961 |
1.28e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 446 EEAIASAIAEEEQLTREIeaeenNDINIETDNDSDFSASMGSGSLSFCGMSLDWNDVLADYEARESWRQNTSWGdivEEE 525
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDI-----IDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFG---KAE 1101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 526 PARLPGHGIHMHEKLSSPSRKRtiAESKKKYEEKHmKAQQLR--EKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMM 603
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKK--AEDARKAEEAR-KAEDARkaEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKA 1178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 604 EEKLLHAEFKR--EVQLQAIVKKAQ-----EEEAKVNEI-AFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEK 675
Cdd:PTZ00121 1179 EAARKAEEVRKaeELRKAEDARKAEaarkaEEERKAEEArKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 676 QARDEAVQERKRALEAERQARVEELLT---KRKEQEARieqQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQ 752
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKaeeKKKADEAK---KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK 1335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 753 KKIQ--LKHDESIRRHMEQIEQRKEKAAELSSGRHASTDYAPKLTPYERKKqcslcnvliASEVYLFSHIKgKKHQQAVR 830
Cdd:PTZ00121 1336 KKAEeaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK---------AEEKKKADEAK-KKAEEDKK 1405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 831 ENSSIQGRELSDEEVEHLSLKKYvvdiviESAAPPEPMKDGEERQknkkkakkikarmntRAKEYENSVETKNSGSESPY 910
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAE------EKKKADEAKKKAEEAK---------------KADEAKKKAEEAKKAEEAKK 1464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1958798880 911 KAKLQRLAKDLVKQLQVQDSGSWVNNKASALDRTLGEIARILEKENVADQI 961
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
544-779 |
2.02e-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: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 544 SRKRTIAESKKKYEEKHMKAQQLREKLREekslKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ------ 617
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAE----LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleeri 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 618 --LQAIVKKAQEEEAKVNEiafiNTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALeAERQA 695
Cdd:TIGR02168 750 aqLSKELTELEAEIEELEE----RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-ANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 696 RVEELLTKRKEQEARIEQQRQEKEKaredaarerARDREERLAALTAAQQEAMEELQKKIQLKHDE--SIRRHMEQIEQR 773
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEE---------LSEDIESLAAEIEELEELIEELESELEALLNEraSLEEALALLRSE 895
|
....*.
gi 1958798880 774 KEKAAE 779
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 ... |
549-779 |
2.86e-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: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 549 IAESKKK----YEEKHMKAQQLREKLREEKSLKLQ--KLLEREKD-----VRKWKEELLDQRRRMMEEKLLHAEFKREVQ 617
Cdd:pfam02463 164 GSRLKRKkkeaLKKLIEETENLAELIIDLEELKLQelKLKEQAKKaleyyQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 618 ------------LQAIVKKAQEEEAKVNEIAFINT--LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQ 683
Cdd:pfam02463 244 ellrdeqeeiesSKQEIEKEEEKLAQVLKENKEEEkeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 684 ERKRALEAERQARVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQ--EAMEELQKKIQLKH-D 760
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERlsSAAKLKEEELELKSeE 403
|
250
....*....|....*....
gi 1958798880 761 ESIRRHMEQIEQRKEKAAE 779
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLK 422
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
428-716 |
5.03e-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: 54.69 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 428 AEVLAKKEELADRLEK--ANEEAIASAIAEEEQLTREIEAEENNDINIETDNDSDFSASMGS--GSLSFCgmsldwNDVL 503
Cdd:TIGR02169 244 RQLASLEEELEKLTEEisELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASleRSIAEK------EREL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 504 ADYEARESwrqntswgdIVEEEPARLpghgihmheklsspsrKRTIAESKKKYEEKHMKAQQLRE---KLREEKSLKLQK 580
Cdd:TIGR02169 318 EDAEERLA---------KLEAEIDKL----------------LAEIEELEREIEEERKRRDKLTEeyaELKEELEDLRAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 581 LLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREV-QLQAIVKKAQEEEAKVNE-----IAFINTLEAQNKrhDVLSKL 654
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREINELKRELdRLQEELQRLSEELADLNAaiagiEAKINELEEEKE--DKALEI 450
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798880 655 KEYEQRLNELqeerqrrqeekQARDEAVQERKRALEAErQARVEELLTKRKEQEARIEQQRQ 716
Cdd:TIGR02169 451 KKQEWKLEQL-----------AADLSKYEQELYDLKEE-YDRVEKELSKLQRELAEAEAQAR 500
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
552-779 |
5.67e-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: 54.36 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 552 SKKKYEEKHMKAQQlrEKLREEKSLKLQKLLEREK--DVRKWKEELLDQRRRM-MEEKLLHAEFKREVQ-LQAIVKKAQE 627
Cdd:pfam17380 285 SERQQQEKFEKMEQ--ERLRQEKEEKAREVERRRKleEAEKARQAEMDRQAAIyAEQERMAMERERELErIRQEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 628 EEAKVNEIAFINT---------LEAQNKRHDVLSKLK-------EYEQRLNELQEERQRRQEEKQARDEAVQERKRALEA 691
Cdd:pfam17380 363 ERIRQEEIAMEISrmrelerlqMERQQKNERVRQELEaarkvkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 692 ERQARVEELLTKRKEQEARIEQQRQ-EKEKAREDAARERARDreerlaaltaaQQEAMEELQKKIQLKHDESIRRHMEQi 770
Cdd:pfam17380 443 ERAREMERVRLEEQERQQQVERLRQqEEERKRKKLELEKEKR-----------DRKRAEEQRRKILEKELEERKQAMIE- 510
|
....*....
gi 1958798880 771 EQRKEKAAE 779
Cdd:pfam17380 511 EERKRKLLE 519
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
428-719 |
1.19e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 428 AEVLAKKEEL--ADRLEKANEEAIASAIAEEEQLTReieAEENNDINIETDNDSDFSASMGSGSlsfcgmsldwndvlad 505
Cdd:PTZ00121 1524 ADEAKKAEEAkkADEAKKAEEKKKADELKKAEELKK---AEEKKKAEEAKKAEEDKNMALRKAE---------------- 1584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 506 yEARESWRQNTSWGDIVEEEPARLPGhgihmhEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKSlKLQKLLERE 585
Cdd:PTZ00121 1585 -EAKKAEEARIEEVMKLYEEEKKMKA------EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK-KAEELKKAE 1656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 586 KDVRKWKEELldqRRRMMEEKLLHAEfkrevqlqaiVKKAQEEEAKVNEIafINTLEAQNKRHDVLSKLKEYEQRLNELQ 665
Cdd:PTZ00121 1657 EENKIKAAEE---AKKAEEDKKKAEE----------AKKAEEDEKKAAEA--LKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 666 EERQRRQEEK--QARDEAVQERKRALEA----ERQARVEELltkRKEQEARIEQQRQEKE 719
Cdd:PTZ00121 1722 KKAEEENKIKaeEAKKEAEEDKKKAEEAkkdeEEKKKIAHL---KKEEEKKAEEIRKEKE 1778
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
546-774 |
1.46e-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: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 546 KRTIAESKKKYEEKHMKAQQLREKLREEKSLK-----LQKLLEREKDVR-----KWKEELldQRRRMMEEKLLHAEFKRE 615
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQaewkeLEKEEEREEDERileylKEKAER--EEEREAEREEIEEEKERE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 616 VQ-LQAIVKKAQEEEAKVNEIAFINTLEAQNKRHdvlsKLKEYEQRLNELQEERQRrqeeKQARDEAVQERKRALEAERQ 694
Cdd:pfam13868 186 IArLRAQQEKAQDEKAERDELRAKLYQEEQERKE----RQKEREEAEKKARQRQEL----QQAREEQIELKERRLAEEAE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 695 ---ARVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLkhDESIRRHMEQIE 771
Cdd:pfam13868 258 reeEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREE--EAERRERIEEER 335
|
...
gi 1958798880 772 QRK 774
Cdd:pfam13868 336 QKK 338
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
422-780 |
2.06e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 422 AADWSMAEVLAKKEELADRLEKAnEEAIASAIAEEEQLTREIEAEENNDINIETDN---DSDFSASMGSGSLSFCGMSLD 498
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAEL-EEELEEAQEELEELEEELEQLENELEAAALEErlkEARLLLLIAAALLALLGLGGS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 499 WNDVLAdyeareswrqnTSWGDIVEEEPARLPGHGIHMHEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKSLKL 578
Cdd:COG4717 268 LLSLIL-----------TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 579 QKLLEREKDVRKWKEeLLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEakvneiaFINTLEAQNKRHDVLSKLKEYE 658
Cdd:COG4717 337 EELLELLDRIEELQE-LLREAEELEEELQLEELEQEIAALLAEAGVEDEEE-------LRAALEQAEEYQELKEELEELE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 659 QRLNELqeerqrrqeekqaRDEAVQERKRALEAERQARVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLA 738
Cdd:COG4717 409 EQLEEL-------------LGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELL 475
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958798880 739 ALTAAQQEAMEELQKKIQLKH--DESIRRHMEQIEQRK-----EKAAEL 780
Cdd:COG4717 476 QELEELKAELRELAEEWAALKlaLELLEEAREEYREERlppvlERASEY 524
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
538-780 |
2.07e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.18 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 538 EKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKSLKLqkllEREKDVRKWKEELLDQRRRMMEEKLLHAEFKrEVQ 617
Cdd:pfam02029 96 EKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIR----EKEYQENKWSTEVRQAEEEGEEEEDKSEEAE-EVP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 618 LQAIVKKAQEEEAKVNEIAFINTLEA--QNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERqa 695
Cdd:pfam02029 171 TENFAKEEVKDEKIKKEKKVKYESKVflDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQ-- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 696 RVEELLTKR-------------KEQEARIE-----QQRQEKEKAREDAArerardreerlaaltaaQQEAMEELQKkiQL 757
Cdd:pfam02029 249 KLEELRRRRqekeseefeklrqKQQEAELEleelkKKREERRKLLEEEE-----------------QRRKQEEAER--KL 309
|
250 260
....*....|....*....|...
gi 1958798880 758 KHDESIRRHMEQIEQRKEKAAEL 780
Cdd:pfam02029 310 REEEEKRRMKEEIERRRAEAAEK 332
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
540-783 |
2.57e-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: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 540 LSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKSLKL----------QKLLEREKDVRKWKEELLDQRRRM----MEE 605
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKallkqlaaleRRIAALARRIRALEQELAALEAELaeleKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 606 KLLHAEFKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERqrrqeekQARDEAVQER 685
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-------RADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 686 KRALEAERQaRVEELLTKRKEQEARIEQQRQEKEKaredaarerardREERLAALTAAQQEAMEELQKKIQlkhdeSIRR 765
Cdd:COG4942 166 RAELEAERA-ELEALLAELEEERAALEALKAERQK------------LLARLEKELAELAAELAELQQEAE-----ELEA 227
|
250
....*....|....*...
gi 1958798880 766 HMEQIEQRKEKAAELSSG 783
Cdd:COG4942 228 LIARLEAEAAAAAERTPA 245
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
560-780 |
2.82e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 560 HMKAQQLRE---------KLREEKSLKLQKL------LEREKDVRkwkEELLDQRRRmmeeklLHAEfkREVQLQAIVKK 624
Cdd:COG1196 151 EAKPEERRAiieeaagisKYKERKEEAERKLeateenLERLEDIL---GELERQLEP------LERQ--AEKAERYRELK 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 625 AQEEEAKVNEIAfintleaqNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQaRVEELLTKR 704
Cdd:COG1196 220 EELKELEAELLL--------LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-ELEEAQAEE 290
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798880 705 KEQEARIEQQRQEKEkaredaarerarDREERLAALTAAQQEAMEELQKKIQ--LKHDESIRRHMEQIEQRKEKAAEL 780
Cdd:COG1196 291 YELLAELARLEQDIA------------RLEERRRELEERLEELEEELAELEEelEELEEELEELEEELEEAEEELEEA 356
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
550-721 |
3.62e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.96 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 550 AESKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKdvrkwkEELLDQrrrmmEEKLLHAEFKREVQLQAivKKAQEEE 629
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEK------ERLAAQ-----EQKKQAEEAAKQAALKQ--KQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 630 AKVNEIAFINTlEAQNKRHDVLSKLKEYEQRLNElqeerqrrqeEKQARDEAVQERKRALEAERQARVEELLTKRKEQEA 709
Cdd:PRK09510 139 AKAAAAAKAKA-EAEAKRAAAAAKKAAAEAKKKA----------EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA 207
|
170
....*....|..
gi 1958798880 710 RIEQQRQEKEKA 721
Cdd:PRK09510 208 KKKAAAEAKKKA 219
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
582-794 |
3.88e-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: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 582 LErEKDVRKWKEELLDQRRRM--MEEKLLHAEFKREvQLQAIVKKAQEEEAKVNEIAFINTL-------EAQNKRHDVLS 652
Cdd:COG4913 218 LE-EPDTFEAADALVEHFDDLerAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEYLraalrlwFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 653 KLKEYEQRLNELqeerQRRQEEKQARDEAVQERKRALEAERQA----RVEELLTKRKEQEARIEQQRQEKEKARED---- 724
Cdd:COG4913 296 ELEELRAELARL----EAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALlaal 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798880 725 -AARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHASTDYAPKL 794
Cdd:COG4913 372 gLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
544-780 |
5.15e-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: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 544 SRKRTIAESKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ-LQAIV 622
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEeLESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 623 KKAQEE-EAKVNEIAfintlEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELL 701
Cdd:TIGR02168 375 EELEEQlETLRSKVA-----QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798880 702 TKRKEQEARIEQQRQEKEKaredaarerardreeRLAALTAAQQEAMEELQKKIQLKHdeSIRRHMEQIEQRKEKAAEL 780
Cdd:TIGR02168 450 EELQEELERLEEALEELRE---------------ELEEAEQALDAAERELAQLQARLD--SLERLQENLEGFSEGVKAL 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
535-779 |
6.99e-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: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 535 HMHEKLSSPSRKRT--IAESKKKYEEKHMKAQQLREKLREEKSLklQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEF 612
Cdd:TIGR02168 253 EELEELTAELQELEekLEELRLEVSELEEEIEELQKELYALANE--ISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 613 KREvQLQAIVKKAQEEEAKVNEIafintLEAQNKRHDVL-SKLKEYEQRLNELqeerqrrqeekqarDEAVQERKRALeA 691
Cdd:TIGR02168 331 KLD-ELAEELAELEEKLEELKEE-----LESLEAELEELeAELEELESRLEEL--------------EEQLETLRSKV-A 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 692 ERQARVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIqlKHDESIRRHMEQIE 771
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ--EELERLEEALEELR 467
|
....*...
gi 1958798880 772 QRKEKAAE 779
Cdd:TIGR02168 468 EELEEAEQ 475
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
544-720 |
7.10e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 544 SRKRTIAESKKKYEEKHMKAQQLREKLR------EEKSLKLQKLLEREKDV-------------RKWKEELLDQRRRMme 604
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIReleeriEELKKEIEELEEKVKELkelkekaeeyiklSEFYEEYLDELREI-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 605 EKLLhAEFKREVQ-LQAIVKKAQEEEAKVNEIA-----FINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQAR 678
Cdd:PRK03918 313 EKRL-SRLEEEINgIEERIKELEEKEERLEELKkklkeLEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK 391
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958798880 679 D-EAVQERKRALEAERQ---ARVEELLTKRKEQEARIEQQRQEKEK 720
Cdd:PRK03918 392 ElEELEKAKEEIEEEISkitARIGELKKEIKELKKAIEELKKAKGK 437
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
535-776 |
8.69e-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: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 535 HMHEKLSSPSR-KRTIAESKKKYE---EKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHA 610
Cdd:TIGR02169 703 RLDELSQELSDaSRKIGEIEKEIEqleQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 611 EFKREV---QLQAIVKKAQEEEAKVNEI-AFINTLEAQ-NKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQER 685
Cdd:TIGR02169 783 DLEARLshsRIPEIQAELSKLEEEVSRIeARLREIEQKlNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 686 KRALEA---ERQARVEELLTKRKEQEARIEQQR------QEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQ 756
Cdd:TIGR02169 863 KEELEEeleELEAALRDLESRLGDLKKERDELEaqlrelERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
250 260
....*....|....*....|
gi 1958798880 757 LKHDESIRRHMEQIEQRKEK 776
Cdd:TIGR02169 943 DEEIPEEELSLEDVQAELQR 962
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
543-773 |
9.20e-06 |
|
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: 9.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 543 PSRKRTIAESKKKYEEKHMKAQQLREKLREEKSLKLQKLlerekdvRKWKEELLDQRRRMMEEKllHAEFKREVQLQAIV 622
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQ-------KELEQRAAAEKAAKQAEQ--AAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 623 KKA-QEEEAKVNEiafintlEAQNKRhdvlsKLKEYEQRLNELQEERQRRQEEKQARDEAV----QERKRALEAERQARV 697
Cdd:TIGR02794 124 AKAkQAAEAKAKA-------EAEAER-----KAKEEAAKQAEEEAKAKAAAEAKKKAEEAKkkaeAEAKAKAEAEAKAKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 698 EELLTKRKEQEARIEQQRQEK---EKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDES-IRRHMEQIEQR 773
Cdd:TIGR02794 192 EEAKAKAEAAKAKAAAEAAAKaeaEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSeVDKYAAIIQQA 271
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
546-712 |
1.10e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.21 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 546 KRTIAESKKKYEEKHMKAQQLREKLrEEKSLKLQKLLereKDVRKWKEELLDQRRRM--MEEKLLHaefKREVQLQAIVK 623
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELEREL-EQKAEEAEALL---KEAEKLKEELEEKKEKLqeEEDKLLE---EAEKEAQQAIK 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 624 KAQEEEAKVneIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRaleaerqARVE----- 698
Cdd:PRK00409 581 EAKKEADEI--IKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDE-------VKYLslgqk 651
|
170
....*....|....*
gi 1958798880 699 -ELLTKRKEQEARIE 712
Cdd:PRK00409 652 gEVLSIPDDKEAIVQ 666
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
523-754 |
1.49e-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: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 523 EEEPARLPGHGIHMHEKLSSPSRKRTIAEskkKYEEKHMKAQQLREKLREEKSLKlQKLLEREKdvrKWKEEL-LDQRRR 601
Cdd:pfam15709 313 EERSEEDPSKALLEKREQEKASRDRLRAE---RAEMRRLEVERKRREQEEQRRLQ-QEQLERAE---KMREELeLEQQRR 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 602 MMEEKLlhaefkREVQLQAIVKKAQEEEAKvneiafiNTLEAQNKRHDVLSKLKEYEQRLNELQEerqRRQEEKQARDEA 681
Cdd:pfam15709 386 FEEIRL------RKQRLEEERQRQEEEERK-------QRLQLQAAQERARQQQEEFRRKLQELQR---KKQQEEAERAEA 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798880 682 VQERKRALE---AERQARVEELltkrkEQEARIEQQRQEKEKAREDAARERARDREERLAAlTAAQQEAMEELQKK 754
Cdd:pfam15709 450 EKQRQKELEmqlAEEQKRLMEM-----AEEERLEYQRQKQEAEEKARLEAEERRQKEEEAA-RLALEEAMKQAQEQ 519
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
538-743 |
2.32e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 538 EKLSSPS-RKRTIAESKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREV 616
Cdd:COG4717 56 DELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 617 QLQA----IVKKAQEEEAKVNEIAfintlEAQNKRHDVLSKLKEYEQRLNELQEERQRRqeeKQARDEAVQERKRALEAE 692
Cdd:COG4717 136 ALEAelaeLPERLEELEERLEELR-----ELEEELEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELEELQQR 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958798880 693 RQARvEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAA 743
Cdd:COG4717 208 LAEL-EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAA 257
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
551-801 |
2.35e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 551 ESKKKYEEKHMKAQQLREKLREEK---SLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREV-QLQAIVKKAQ 626
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELreiEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLeELEERHELYE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 627 EEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQAR---------- 696
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrel 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 697 ---------------VEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAaltaaqqEAMEELQKKIQLKHDE 761
Cdd:PRK03918 446 teehrkelleeytaeLKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA-------EQLKELEEKLKKYNLE 518
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958798880 762 SIRRHMEQIEQRKEKAAELSSGRHASTDYAPKLTPYERKK 801
Cdd:PRK03918 519 ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
538-798 |
2.39e-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: 48.97 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 538 EKLSSPSRKRTIAESKKKYE-----EKHMKAQQLREKLREEKSLKLQKLLEREKDV-RKWKEELLDQRRRMMEEKLLHAE 611
Cdd:pfam17380 307 EKAREVERRRKLEEAEKARQaemdrQAAIYAEQERMAMERERELERIRQEERKRELeRIRQEEIAMEISRMRELERLQME 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 612 FKRE-----VQLQAIVK-KAQEEE------AKVNEIAFINTlEAQNKRHDVLSKLKEYEQR-LNELQEERQRRQEE-KQA 677
Cdd:pfam17380 387 RQQKnervrQELEAARKvKILEEErqrkiqQQKVEMEQIRA-EQEEARQREVRRLEEERAReMERVRLEEQERQQQvERL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 678 RDEAVQERKRALEAER----QARVEELLTKRKEQE------ARIEQQRQEK--EKAREDAARERARDREERLAALTAAQQ 745
Cdd:pfam17380 466 RQQEEERKRKKLELEKekrdRKRAEEQRRKILEKEleerkqAMIEEERKRKllEKEMEERQKAIYEEERRREAEEERRKQ 545
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958798880 746 EAMEElQKKIQ------------LKHDESIRRHMEQIEQRKEKAAELSSGRHAST---DYAPKLTPYE 798
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 ... |
799-831 |
3.03e-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: 3.03e-05
10 20 30
....*....|....*....|....*....|...
gi 1958798880 799 RKKQCSLCNVLIASEVYLFSHIKGKKHQQAVRE 831
Cdd:smart00451 2 GGFYCKLCNVTFTDEISVEAHLKGKKHKKNVKK 34
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
601-779 |
3.63e-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: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 601 RMMEEKLLHAEFKREVQLQAIVKKAQEEEAKvneiafintleAQNKRHDVLSKlkeyEQRLNELQEERQRRQEEKQARDE 680
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIAEKKRIKAEEK-----------EEERRLDEMME----EERERALEEEEEKEEERKEERKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 681 AVQERKRALEAERQARVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTA-AQQEAMEELQKKIQLKH 759
Cdd:pfam13868 74 YRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFnEEQAEWKELEKEEEREE 153
|
170 180
....*....|....*....|
gi 1958798880 760 DESIRRHMEQIEQRKEKAAE 779
Cdd:pfam13868 154 DERILEYLKEKAEREEEREA 173
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
553-781 |
3.91e-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: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 553 KKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKV 632
Cdd:TIGR00618 657 QERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 633 NEIAFINTL-EAQNKRHDVLSKLKEYEQRLNElqeerqrRQEEKQARDEAVQERKRALEAERQARvEELLTKRKEQEARI 711
Cdd:TIGR00618 737 REDALNQSLkELMHQARTVLKARTEAHFNNNE-------EVTAALQTGAELSHLAAEIQFFNRLR-EEDTHLLKTLEAEI 808
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958798880 712 EQQRQEKEKAREDAARERARDRE---ERLAALTAAQQEAmeelqkKIQLKHDESIRRHMEQIEQRKEKAAELS 781
Cdd:TIGR00618 809 GQEIPSDEDILNLQCETLVQEEEqflSRLEEKSATLGEI------THQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
562-782 |
4.21e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 562 KAQQLREKLREEKSlklqKLLEREKDVRKWKEELLDQRRRmmEEKLLHA----EFKREVQLQAIVKKAQEEEAKVNEI-A 636
Cdd:PRK02224 409 NAEDFLEELREERD----ELREREAELEATLRTARERVEE--AEALLEAgkcpECGQPVEGSPHVETIEEDRERVEELeA 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 637 FINTLEAQ----NKRHDVLSKLKEYEQR----------LNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLT 702
Cdd:PRK02224 483 ELEDLEEEveevEERLERAEDLVEAEDRierleerredLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 703 KRKE-QEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRhmEQIEQRKEKAAELS 781
Cdd:PRK02224 563 AEEEaEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERR--ERLAEKRERKRELE 640
|
.
gi 1958798880 782 S 782
Cdd:PRK02224 641 A 641
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
546-719 |
4.77e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 546 KRTIAESKKKYEEKHMKA--------QQLREKLREEKSLKLQKLLEREKDVRKwKEELLDQRRRMMEekllhaefKREVQ 617
Cdd:PRK12704 41 KRILEEAKKEAEAIKKEAlleakeeiHKLRNEFEKELRERRNELQKLEKRLLQ-KEENLDRKLELLE--------KREEE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 618 LQAIVKKAQEEEAKVneiafintleaQNKRHDVLSKLKEYEQRLNELQEERQRrqeekQARDEAVQERKRALEAERQARV 697
Cdd:PRK12704 112 LEKKEKELEQKQQEL-----------EKKEEELEELIEEQLQELERISGLTAE-----EAKEILLEKVEEEARHEAAVLI 175
|
170 180
....*....|....*....|..
gi 1958798880 698 eelltKRKEQEARIEQQRQEKE 719
Cdd:PRK12704 176 -----KEIEEEAKEEADKKAKE 192
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
543-779 |
7.55e-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: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 543 PSRKRTIAE---SKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWkeeLLDQRRRMMEEKLlhAEFKREVQlq 619
Cdd:pfam15558 3 PERDRKIAAlmlARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRL---LLQQSQEQWQAEK--EQRKARLG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 620 aivkkaQEEEAKVnEIAFINTLEAQNKRHDVLSKlKEyEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQArvEE 699
Cdd:pfam15558 76 ------REERRRA-DRREKQVIEKESRWREQAED-QE-NQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQ--NS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 700 LLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQL--KHDESIRRHMEQIEQR---- 773
Cdd:pfam15558 145 LQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELLRRLSLeqSLQRSQENYEQLVEERhrel 224
|
....*.
gi 1958798880 774 KEKAAE 779
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 ... |
803-825 |
8.41e-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: 40.56 E-value: 8.41e-05
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
507-924 |
1.97e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 507 EAR--ESWRQNTswgDIVEEEPARLPGHGIHMHEKLSSPSRKrtiAESKKKYEEKHmKAQQLREKLREEKSLKLQKLLER 584
Cdd:PTZ00121 1241 EAKkaEEERNNE---EIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAEEKK-KADEAKKAEEKKKADEAKKKAEE 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 585 EKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQlqaiVKKAQEEEAKvneiafiNTLEAQNKRHDVLSKLKEYEqrlnel 664
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE----AAKAEAEAAA-------DEAEAAEEKAEAAEKKKEEA------ 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 665 qeerqrrqeeKQARDEA---VQERKRALEAERQA-----RVEEL------------LTKRKEQEARIEQQRQEKEKARED 724
Cdd:PTZ00121 1377 ----------KKKADAAkkkAEEKKKADEAKKKAeedkkKADELkkaaaakkkadeAKKKAEEKKKADEAKKKAEEAKKA 1446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 725 AARERARDREERLAALTAAQQEA--MEELQKKIQ--LKHDESIRRHME---------QIEQRKEKAAELSSGRHASTdyA 791
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEeaKKADEAKKKAEEakkkadeakKAAEAKKKADEAKKAEEAKK--A 1524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 792 PKLTPYERKKQCSlcNVLIASEVYLFSHIKGKKHQQAVRENSSIQGRElSDEEVEHLSLKKYVVDIVIESAAPPEPMKDG 871
Cdd:PTZ00121 1525 DEAKKAEEAKKAD--EAKKAEEKKKADELKKAEELKKAEEKKKAEEAK-KAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1958798880 872 EERQKNKKKAKKIKARMNTRAKEYENSVETKNSGSESPYK-AKLQRLAKDLVKQ 924
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKeAEEKKKAEELKKA 1655
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
539-635 |
1.98e-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: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 539 KLSSPSRKRTIAESKKkyeEKHMKAQQLREKLREEKSLK-LQKLLEREKDVRKWKEELLDQRRRMMEEKLLHA----EFK 613
Cdd:pfam00836 32 KLSLSPKKKDSSLEEI---QKKLEAAEERRKSLEAQKLKqLAEKREKEEEALQKADEENNNFSKMAEEKLKQKmeayKEN 108
|
90 100
....*....|....*....|..
gi 1958798880 614 REVQLQAIVKKAQEEEAKVNEI 635
Cdd:pfam00836 109 REAQIAALKEKLKEKEKHVEEV 130
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
549-747 |
2.09e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 549 IAESKKKYEEKHMKAQQLREKLR------EEKSLKLQKLLEREKDVRKWKEELldqrrrmmEEKLLHAEfKREVQLQAIV 622
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDalqaelEELNEEYNELQAELEALQAEIDKL--------QAEIAEAE-AEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 623 KK----AQEEEAKVNEIAFIntLEAQN-----KRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAER 693
Cdd:COG3883 89 GEraraLYRSGGSVSYLDVL--LGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958798880 694 QARVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEA 747
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
503-794 |
2.26e-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: 45.41 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 503 LADYEARESWRQNTSWGDIVEEEPARLpghgihmHEKLSspsRKRTIAESKKKYEEKHMKAQQ-LREKLREEKSLKLQKL 581
Cdd:pfam15558 81 RADRREKQVIEKESRWREQAEDQENQR-------QEKLE---RARQEAEQRKQCQEQRLKEKEeELQALREQNSLQLQER 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 582 LEREKDVRKWKEELLDQRRRM--MEEKLLHAEFKREVQLQAivkKAQEEEAKvneiafiNTLE-----AQNKRHDVLskl 654
Cdd:pfam15558 151 LEEACHKRQLKEREEQKKVQEnnLSELLNHQARKVLVDCQA---KAEELLRR-------LSLEqslqrSQENYEQLV--- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 655 keyEQRLNELQEerqrrqeeKQARDEA----VQERKRALEAERQARVEELLtkrKEQEARIEQQRQEKEKAREdaarera 730
Cdd:pfam15558 218 ---EERHRELRE--------KAQKEEEqfqrAKWRAEEKEEERQEHKEALA---ELADRKIQQARQVAHKTVQ------- 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958798880 731 rDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHASTDYAPKL 794
Cdd:pfam15558 277 -DKAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKKEQRSEQISREKEATLEEARKT 339
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
563-764 |
3.12e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.03 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 563 AQQLREKLREEKSLKlQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNeiafintLE 642
Cdd:COG3064 1 AQEALEEKAAEAAAQ-ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAE-------LA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 643 AQNKRhdvlsKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEEllTKRK-EQEARIEQQRQEKEKA 721
Cdd:COG3064 73 AEAAK-----KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEE--AKRKaEEEAKRKAEEERKAAE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958798880 722 REDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIR 764
Cdd:COG3064 146 AEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAA 188
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
541-780 |
4.74e-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: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 541 SSPSRKRTIAESKKKYEEKHmkaqqlreklREEKSLKLQKLLEREKDVR-KWKEELLDQRRRMMEEKLLHAEFKREVQlq 619
Cdd:pfam15709 297 SSPTQTFVVTGNMESEEERS----------EEDPSKALLEKREQEKASRdRLRAERAEMRRLEVERKRREQEEQRRLQ-- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 620 aivKKAQEEEAKVNEiafinTLEAQNKRHDVLSKLKEyeQRLNElqeerqrrQEEKQARDEAVQERKRALEAERqARVEE 699
Cdd:pfam15709 365 ---QEQLERAEKMRE-----ELELEQQRRFEEIRLRK--QRLEE--------ERQRQEEEERKQRLQLQAAQER-ARQQQ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 700 LLTKRKEQEarIEQQRQEKEKAREDAARERARDREERLAA-----LTAAQQEAMEELQKKiqLKHDESIRRHMEQIEQRK 774
Cdd:pfam15709 426 EEFRRKLQE--LQRKKQQEEAERAEAEKQRQKELEMQLAEeqkrlMEMAEEERLEYQRQK--QEAEEKARLEAEERRQKE 501
|
....*.
gi 1958798880 775 EKAAEL 780
Cdd:pfam15709 502 EEAARL 507
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
675-802 |
5.03e-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: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 675 KQARDEAVQERKRALEAE-RQARVEElltKRKEQEariEQQRQEKEKAREDAARErardreerlAALTAAQQEAMEELQK 753
Cdd:pfam15709 327 KREQEKASRDRLRAERAEmRRLEVER---KRREQE---EQRRLQQEQLERAEKMR---------EELELEQQRRFEEIRL 391
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958798880 754 KIQLKHDESIRRHMEQIEQRKEKAAELSSGRHASTDYAPKLTPYERKKQ 802
Cdd:pfam15709 392 RKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQ 440
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
546-786 |
5.61e-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: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 546 KRTIAESKKKYEEKHmkAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLL-HAEFKRE-VQLQAIVK 623
Cdd:pfam13868 31 KKRIKAEEKEEERRL--DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEeYEEKLQErEQMDEIVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 624 KAQEEEakvneiafintleaqnkrhdvlskLKEYEQRLNElqeerqrrQEE-KQARDEAVQERKRALEAERQA------R 696
Cdd:pfam13868 109 RIQEED------------------------QAEAEEKLEK--------QRQlREEIDEFNEEQAEWKELEKEEereedeR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 697 VEELLTKRKEQEARIEQQRQEKEKaredaARERARDREERLAALTAAQQEAMEEL-QKKIQLKHDESIR-RHMEQIEQRK 774
Cdd:pfam13868 157 ILEYLKEKAEREEEREAEREEIEE-----EKEREIARLRAQQEKAQDEKAERDELrAKLYQEEQERKERqKEREEAEKKA 231
|
250
....*....|..
gi 1958798880 775 EKAAELSSGRHA 786
Cdd:pfam13868 232 RQRQELQQAREE 243
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
545-954 |
5.61e-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: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 545 RKRTIAESKKKYEEKHMKAQQLR---EKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAI 621
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLQTKEqihLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQT 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 622 VKKAQEEEAKVNEI-------AFINTLEAQNKRHDvLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQ 694
Cdd:TIGR00618 537 YAQLETSEEDVYHQltserkqRASLKEQMQEIQQS-FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 695 ARVEELLTKRKEQEARIE----QQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHM--- 767
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRLHlqqcSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtyw 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 768 -EQIEQRKEKAAELSSgrhastdyapKLTPYERKKQcSLCNVLIASevylfshiKGKKHQQAVRENSSIQG-RELSDEEV 845
Cdd:TIGR00618 696 kEMLAQCQTLLRELET----------HIEEYDREFN-EIENASSSL--------GSDLAAREDALNQSLKElMHQARTVL 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 846 EHLSLkkyvVDIVIESAAPPEPMKDGEERQKNKKkakkikarMNTRAKEYENSV-ETKNSGSESPYKAKLQRLAKDLVKQ 924
Cdd:TIGR00618 757 KARTE----AHFNNNEEVTAALQTGAELSHLAAE--------IQFFNRLREEDThLLKTLEAEIGQEIPSDEDILNLQCE 824
|
410 420 430
....*....|....*....|....*....|
gi 1958798880 925 LQVQDSGSwVNNKASALDRTLGEIARILEK 954
Cdd:TIGR00618 825 TLVQEEEQ-FLSRLEEKSATLGEITHQLLK 853
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
545-710 |
6.69e-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: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 545 RKRTIAESKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREV-QLQAIVK 623
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLeAEREELL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 624 KAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELqeerqrrqeekqardEAVQErkRALE--AERQARVEELL 701
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL---------------GPVNL--LAIEeyEELEERYDFLS 801
|
170
....*....|
gi 1958798880 702 TKRKE-QEAR 710
Cdd:COG1196 802 EQREDlEEAR 811
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
675-758 |
7.18e-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: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 675 KQARDEAVQERKRALEAERQarvEELltkrkeQEARIEQQRQEKEKaredaarerardreeRLAALTAAQQEAMEELQKK 754
Cdd:pfam07946 263 KKTREEEIEKIKKAAEEERA---EEA------QEKKEEAKKKEREE---------------KLAKLSPEEQRKYEEKERK 318
|
....
gi 1958798880 755 IQLK 758
Cdd:pfam07946 319 KEQR 322
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
546-717 |
1.24e-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: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 546 KRTIAESKKKYEEKHMKAQQLREKLREEKSL---KLQKLLEREKDVRkwkeELLDQRRRMMEEKLLHAEFKREV-QLQAI 621
Cdd:cd00176 46 EAELAAHEERVEALNELGEQLIEEGHPDAEEiqeRLEELNQRWEELR----ELAEERRQRLEEALDLQQFFRDAdDLEQW 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 622 VKKAQEEEAKVNEIAFINTLEAQNKRHDVL-SKLKEYEQRLNELqeerqrrqeeKQARDEAVQERKRALEAERQARVEEL 700
Cdd:cd00176 122 LEEKEAALASEDLGKDLESVEELLKKHKELeEELEAHEPRLKSL----------NELAEELLEEGHPDADEEIEEKLEEL 191
|
170
....*....|....*..
gi 1958798880 701 LTKRKEQEARIEQQRQE 717
Cdd:cd00176 192 NERWEELLELAEERQKK 208
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
549-777 |
1.34e-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: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 549 IAESKKKYEEKHMKAQQLREK-----LREEKSLKLQKLLErekdvrkwkeelLDQRRRMMEEKLLHAEFKREvQLQAIVK 623
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSE------------LESQLAEARAELAEAEARLA-ALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 624 KAQEEEAKVNEIAFINTLEAQnkRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLTK 703
Cdd:COG3206 251 SGPDALPELLQSPVIQQLRAQ--LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAR 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958798880 704 RKEQEARIEQQRQEkekaredaarerardreerLAALTAAQQEaMEELQKKIQLKhdesiRRHMEQIEQRKEKA 777
Cdd:COG3206 329 EASLQAQLAQLEAR-------------------LAELPELEAE-LRRLEREVEVA-----RELYESLLQRLEEA 377
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
584-779 |
1.37e-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: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 584 REKDVRKWKeelldQRRRMM----EEKLlhAEFKREV-QLQAIVKKAQEEEAKVNEIafintLEAQNKRHDVLSKLKEY- 657
Cdd:COG4913 590 HEKDDRRRI-----RSRYVLgfdnRAKL--AALEAELaELEEELAEAEERLEALEAE-----LDALQERREALQRLAEYs 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 658 --EQRLNELQEERQRRQEEKQARD------EAVQERKRALEAERQA---RVEELLTKRKEQEARIEQQRQEKEKAREDAA 726
Cdd:COG4913 658 wdEIDVASAEREIAELEAELERLDassddlAALEEQLEELEAELEEleeELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958798880 727 RERARDREERLAALTAA-QQEAMEELQKKIQlkhdESIRRHMEQIEQRKEKAAE 779
Cdd:COG4913 738 AAEDLARLELRALLEERfAAALGDAVERELR----ENLEERIDALRARLNRAEE 787
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
565-713 |
1.61e-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: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 565 QLREKLREEKSL-----KLQKLLEREKDVRKWKEELLDQRRRMMEEKLlhAEFKREvqLQAIVKKAQEEEAKVNEIAFIN 639
Cdd:pfam07888 35 RLEECLQERAELlqaqeAANRQREKEKERYKRDREQWERQRRELESRV--AELKEE--LRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958798880 640 TLEAQNKrhDVLSKLK-EYEQRLNELQEERqrrqeekQARDEAVQERKRALEAERQaRVEELLTKRKEQEARIEQ 713
Cdd:pfam07888 111 EELSEEK--DALLAQRaAHEARIRELEEDI-------KTLTQRVLERETELERMKE-RAKKAGAQRKEEEAERKQ 175
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
562-860 |
1.75e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 562 KAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEekllhaefkREVQLQAIVKKAQEEEAKVNeiafintl 641
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ---------LEEELEELNEQLQAAQAELA-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 642 EAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALeAERQARVEELLTKRKEQEARIEQQRQEKEKA 721
Cdd:COG4372 98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI-AEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 722 REDAARerardreerlAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHASTDYAPKLTPYERKK 801
Cdd:COG4372 177 SEAEAE----------QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798880 802 QCSLCNVLIASEVYLFSHIKGKKHQQAVRENSSIQGRELSDEEVEHLSLKKYVVDIVIE 860
Cdd:COG4372 247 DKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
538-720 |
2.36e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 538 EKLSSPSRKRTIAESKKKYEEKHMK-AQQLREKLREEKSL--KLQKLLEREKDVRKWK------EELLDQRRRMMEEKLL 608
Cdd:PRK05771 73 REEKKKVSVKSLEELIKDVEEELEKiEKEIKELEEEISELenEIKELEQEIERLEPWGnfdldlSLLLGFKYVSVFVGTV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 609 HAEFKREVQLQAIVKKAQEEEAKVNE--IAFINtleAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQardeaVQERK 686
Cdd:PRK05771 153 PEDKLEELKLESDVENVEYISTDKGYvyVVVVV---LKELSDEVEEELKKLGFERLELEEEGTPSELIRE-----IKEEL 224
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958798880 687 RALEAERQARVEELLTKRKEQEARI----EQQRQEKEK 720
Cdd:PRK05771 225 EEIEKERESLLEELKELAKKYLEELlalyEYLEIELER 262
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
523-700 |
2.57e-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: 41.75 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 523 EEEPARLPghgiHMHEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKSLKLQKLLErekdvRKWKEELLDQrrrm 602
Cdd:TIGR02794 85 AAEQARQK----ELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE-----RKAKEEAAKQ---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 603 meekllhAEFKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKeyeqrlNELQEERQRRQEEKQARDEAv 682
Cdd:TIGR02794 152 -------AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAK------AEAAKAKAAAEAAAKAEAEA- 217
|
170
....*....|....*...
gi 1958798880 683 qERKRALEAERQARVEEL 700
Cdd:TIGR02794 218 -AAAAAAEAERKADEAEL 234
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
577-782 |
2.65e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 577 KLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEIafINTLE-----AQNKRHDVL 651
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEE--IERYEeqreqARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 652 SKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEA--ERQARVEELLTKRKEQEARIEQQRQEKEkaredaarer 729
Cdd:PRK02224 241 EVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEvrDLRERLEELEEERDDLLAEAGLDDADAE---------- 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798880 730 arDREERLAALTAAQQEAMEELQKK---IQLKHD------ESIRRHMEQIEQRKEKAAELSS 782
Cdd:PRK02224 311 --AVEARREELEDRDEELRDRLEECrvaAQAHNEeaeslrEDADDLEERAEELREEAAELES 370
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
558-720 |
2.74e-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: 41.06 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 558 EKHMKAQQLREKLREEKslklQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREV-QLQAIVKKAQE--EEAKVNE 634
Cdd:COG1579 14 ELDSELDRLEHRLKELP----AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIeEVEARIKKYEEqlGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 635 I--AFINTLEAQNKRHDVLSK-LKEYEQRLNELqeerqrrqeekqardEAVQERKRALEAERQARVEELLTKRKEQEARI 711
Cdd:COG1579 90 EyeALQKEIESLKRRISDLEDeILELMERIEEL---------------EEELAELEAELAELEAELEEKKAELDEELAEL 154
|
....*....
gi 1958798880 712 EQQRQEKEK 720
Cdd:COG1579 155 EAELEELEA 163
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
613-779 |
3.63e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.33 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 613 KREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRhdvlsKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRA-LEA 691
Cdd:PRK09510 75 KRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKE-----RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAkAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 692 ERQARVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALT--AAQQEAMEELQKKIQLKHDESIRRHMEQ 769
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAkkKAEAEAKKKAAAEAKKKAAAEAKAAAAK 229
|
170
....*....|
gi 1958798880 770 IEQRKEKAAE 779
Cdd:PRK09510 230 AAAEAKAAAE 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
546-714 |
4.38e-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: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 546 KRTIAESKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREkdvrkwkEELLDQRRRMMEEKLLHAEFKREvQLQAIVKKA 625
Cdd:COG1579 58 EKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKE-------IESLKRRISDLEDEILELMERIE-ELEEELAEL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 626 QEEeakvneiafintleaqnkrhdvlskLKEYEQRLNELqeerqrrqeeKQARDEAVQErkraLEAERqarvEELLTKRK 705
Cdd:COG1579 130 EAE-------------------------LAELEAELEEK----------KAELDEELAE----LEAEL----EELEAERE 166
|
....*....
gi 1958798880 706 EQEARIEQQ 714
Cdd:COG1579 167 ELAAKIPPE 175
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
675-783 |
4.48e-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: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 675 KQARDEAVQERKRALeAERQARVEElltkrkEQEARIEQQRQEKEKAredaarerardreerlaaltaaQQEAMEELQKK 754
Cdd:cd16269 195 EKEKEIEAERAKAEA-AEQERKLLE------EQQRELEQKLEDQERS----------------------YEEHLRQLKEK 245
|
90 100 110
....*....|....*....|....*....|
gi 1958798880 755 IQLKHDESIRRHMEQIEQR-KEKAAELSSG 783
Cdd:cd16269 246 MEEERENLLKEQERALESKlKEQEALLEEG 275
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
568-780 |
5.68e-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: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 568 EKLREEkslkLQKLLEREKDVRKWKEELLDQRRRMMEEKLlHAEfkrevQLQAIVKKAQEEEAKVnEIAFINTLEAQNKR 647
Cdd:TIGR02169 173 EKALEE----LEEVEENIERLDLIIDEKRQQLERLRRERE-KAE-----RYQALLKEKREYEGYE-LLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 648 HDV-LSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLTKRKEQEARIEQQRQEKEKAREDAA 726
Cdd:TIGR02169 242 IERqLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798880 727 RErardrEERLAALTAAQQEAMEELQKKIQlkhDESIRRH--MEQIEQRKEKAAEL 780
Cdd:TIGR02169 322 ER-----LAKLEAEIDKLLAEIEELEREIE---EERKRRDklTEEYAELKEELEDL 369
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
555-799 |
6.25e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 555 KYEEKHMKAQQLREKLREEKSLKLQK----LLEREKDVRKWKEELLDQrrrmmeEKLLHAEFKREVQLQAIVKKAQEEEA 630
Cdd:PRK03918 76 KFEKNGRKYRIVRSFNRGESYLKYLDgsevLEEGDSSVREWVERLIPY------HVFLNAIYIRQGEIDAILESDESREK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 631 KVNEIAFINTLE-AQNKRHDVLSKLKEYEQRLNELQeerqrrqeekqARDEAVQERKRALEAErqarVEELLTKRKEQEA 709
Cdd:PRK03918 150 VVRQILGLDDYEnAYKNLGEVIKEIKRRIERLEKFI-----------KRTENIEELIKEKEKE----LEEVLREINEISS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 710 RIEQQRQEKEKAREDAARERArdreerLAALTAAQQEAMEELQKKIQlKHDESIRRHMEQIEQRKEKAAELSSGRHASTD 789
Cdd:PRK03918 215 ELPELREELEKLEKEVKELEE------LKEEIEELEKELESLEGSKR-KLEEKIRELEERIEELKKEIEELEEKVKELKE 287
|
250
....*....|
gi 1958798880 790 YAPKLTPYER 799
Cdd:PRK03918 288 LKEKAEEYIK 297
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
538-936 |
7.55e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 538 EKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKSLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFK--RE 615
Cdd:COG5022 820 IKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISslKL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 616 VQLQ------AIVKKAQEEEAKVNEI--AFINTLEAQNKRHDV-LSKLKEYEQ--RLNELqeerqrrQEEKQARDEAVQE 684
Cdd:COG5022 900 VNLEleseiiELKKSLSSDLIENLEFktELIARLKKLLNNIDLeEGPSIEYVKlpELNKL-------HEVESKLKETSEE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 685 RKRAL----EAERQARVEELLTKRKEQEArieqQRQEKEKAREDAARERARDREERLAALTAAQQEAMEE-LQKKIQLKH 759
Cdd:COG5022 973 YEDLLkkstILVREGNKANSELKNFKKEL----AELSKQYGALQESTKQLKELPVEVAELQSASKIISSEsTELSILKPL 1048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 760 DESIRRHMEQIEQRKEKAAELSSGRHASTDYapKLTPYERKKQCSLCNVLIASEVYLFSHIKGKKhqQAVRENSSIQG-- 837
Cdd:COG5022 1049 QKLKGLLLLENNQLQARYKALKLRRENSLLD--DKQLYQLESTENLLKTINVKDLEVTNRNLVKP--ANVLQFIVAQMik 1124
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 838 RELSDEEVEHLSLKKYVVDIVIESAAPPEPMKDGEERQKNKKKAKKIKARMNTRAKE--YENSVETKNSGSES------- 908
Cdd:COG5022 1125 LNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRlyQSALYDEKSKLSSSevndlkn 1204
|
410 420
....*....|....*....|....*...
gi 1958798880 909 PYKAKLQRLAKDLVKQLQVQDSGSWVNN 936
Cdd:COG5022 1205 ELIALFSKIFSGWPRGDKLKKLISEGWV 1232
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
621-720 |
7.80e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 621 IVKKAQ----EEEAKVNEIafINTLEAQ-----NKRHDVLSKLKEYEQRLNELqeerqrrqeekQARDEAVQERKRALEA 691
Cdd:PRK00409 503 IIEEAKkligEDKEKLNEL--IASLEELereleQKAEEAEALLKEAEKLKEEL-----------EEKKEKLQEEEDKLLE 569
|
90 100
....*....|....*....|....*....
gi 1958798880 692 ERQARVEELLTKRKEQEARIEQQRQEKEK 720
Cdd:PRK00409 570 EAEKEAQQAIKEAKKEADEIIKELRQLQK 598
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
553-720 |
7.85e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 553 KKKYEEKHMKAQQLREKLRE--------EKSLKLQKLLEREK--------DVRKWKEELLDQRRRM-------MEEKL-- 607
Cdd:PRK03918 517 LEELEKKAEEYEKLKEKLIKlkgeikslKKELEKLEELKKKLaelekkldELEEELAELLKELEELgfesveeLEERLke 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 608 LHAEFKREVQLQAIVKKAQEEEAKVNEIAfiNTL-EAQNKRHDVLSKLKEYEQRLNELQEERQrrqeekQARDEAVQERK 686
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKKLE--EELdKAFEELAETEKRLEELRKELEELEKKYS------EEEYEELREEY 668
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958798880 687 RALEAE---RQARVEELLTKRKEQEARIEQQRQEKEK 720
Cdd:PRK03918 669 LELSRElagLRAELEELEKRREEIKKTLEKLKEELEE 705
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
642-720 |
8.59e-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: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 642 EAQNKRHDVLSKLKEYEQRLnelqeerqrrqeeKQARDEAVQERKRAlEAERQARVEELLTKRKEQEARIEQQ-----RQ 716
Cdd:cd06503 41 EAEKAKEEAEELLAEYEEKL-------------AEARAEAQEIIEEA-RKEAEKIKEEILAEAKEEAERILEQakaeiEQ 106
|
....
gi 1958798880 717 EKEK 720
Cdd:cd06503 107 EKEK 110
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
549-781 |
8.62e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 549 IAESKKKYEEKHMKAQQLREKLREEKSLKlQKLLEREKDVRKWKEELLDQRRRMMEE-----KLLHAEFKREVQLQAIVK 623
Cdd:COG1340 38 LKELAEKRDELNAQVKELREEAQELREKR-DELNEKVKELKEERDELNEKLNELREEldelrKELAELNKAGGSIDKLRK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 624 KAQEEEAKvneiaFIN---TLEAQNKrhdVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQarVEEL 700
Cdd:COG1340 117 EIERLEWR-----QQTevlSPEEEKE---LVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKK--IKEL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 701 LTKRKEQEARIEQQRQEKEKAREDAARERardreerlAALTAAQQEAMEELQKKIQLKhdESIRRHMEQIEQRKEKAAEL 780
Cdd:COG1340 187 AEEAQELHEEMIELYKEADELRKEADELH--------KEIVEAQEKADELHEEIIELQ--KELRELRKELKKLRKKQRAL 256
|
.
gi 1958798880 781 S 781
Cdd:COG1340 257 K 257
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
549-761 |
8.62e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 549 IAESKKKYEEKHMKAQQLREKLREEKSlKLQKLLEREKDVRKWKEELLDQRRRMMEEKL-LHAE---FKREVQLQAIVKK 624
Cdd:COG1340 73 VKELKEERDELNEKLNELREELDELRK-ELAELNKAGGSIDKLRKEIERLEWRQQTEVLsPEEEkelVEKIKELEKELEK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 625 AQEEEAKVNEIAFINT--LEAQNKRHDVLSKLKEYEQRLNELQEERQRRqeeKQARDEAVQERKRALEA--ERQARVEEL 700
Cdd:COG1340 152 AKKALEKNEKLKELRAelKELRKEAEEIHKKIKELAEEAQELHEEMIEL---YKEADELRKEADELHKEivEAQEKADEL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958798880 701 ltkRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDE 761
Cdd:COG1340 229 ---HEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTTEE 286
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
593-756 |
8.91e-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: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 593 EELLDQRRRMMEEKLL--HAEFKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLnelqeerqr 670
Cdd:COG1196 624 GRTLVAARLEAALRRAvtLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE--------- 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 671 rqeEKQARDEAVQERKRALEAERQARVEELLTKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEE 750
Cdd:COG1196 695 ---LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
....*.
gi 1958798880 751 LQKKIQ 756
Cdd:COG1196 772 LEREIE 777
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
578-717 |
9.08e-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: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798880 578 LQKLLEREKDVRKWKEELLDQRRrmmeekllhAEFKR-EVQLQAIVKKAQEEEAKVNEIAFINTLEAQnkrhdvLSKLKE 656
Cdd:TIGR02473 4 LQKLLDLREKEEEQAKLELAKAQ---------AEFERlETQLQQLIKYREEYEQQALEKVGAGTSALE------LSNYQR 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958798880 657 YEQRLNELQEERQRrqeeKQARDEAVQERKRALEAERQARVE--ELLTKRKEQEARIEQQRQE 717
Cdd:TIGR02473 69 FIRQLDQRIQQQQQ----ELALLQQEVEAKRERLLEARRELKalEKLKEKKQKEYRAEEAKRE 127
|
|
| |
