|
Name |
Accession |
Description |
Interval |
E-value |
| SCAPER_N |
pfam16501 |
S phase cyclin A-associated protein in the endoplasmic reticulum; SCAPER_N is a short highly ... |
88-185 |
3.28e-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: 3.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 88 KTRHPRKIDLRARYWAFLFDNLRRAVDEIYVTCESDQSVVECKEVLMMLDYYVRDFKALIDWIQLQEKLEKTDAQSRPTS 167
Cdd:pfam16501 1 STGRDKKSELRARYWAFLFDNLQRAVDEIYQTCESDESVVECKEVIMVLDNYTRDFKALIEWFRLKWDYENTPPPQRPTS 80
|
90
....*....|....*...
gi 124486797 168 LAWEVKKMSPGRHVIQSP 185
Cdd:pfam16501 81 LAWEVRKSSPGKSVNKSP 98
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
536-784 |
7.30e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 7.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 536 KRTIAESKKKYEEKHMKAQQLREKLREEkTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKA 615
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 616 QEEEAKVNEIAFINTL-EAQNKRHDVLSKLKEYEQRLNELqeerqrRQEEKQARDEAVQERKRALEAERQARVEELLMKR 694
Cdd:COG1196 331 ELEELEEELEELEEELeEAEEELEEAEAELAEAEEALLEA------EAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 695 KEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQkKIQLKHDESIRRHMEQIEQRKEKAAELSSGR 774
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA-ELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250
....*....|
gi 124486797 775 HASTDYAPKL 784
Cdd:COG1196 484 EELAEAAARL 493
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
536-910 |
1.35e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.78 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 536 KRTIAESKKKYEEKHMKAQQLREKLREEKT---LKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ----L 608
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKaaeAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEekkkA 1393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 609 QAIVKKAQEEEAKVNEiafINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEA------------VQERK 676
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADE---LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAeeakkaeeakkkAEEAK 1470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 677 RALEAERQA----RVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDES 752
Cdd:PTZ00121 1471 KADEAKKKAeeakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 753 IRRHMEQIEQRKEKAAElsSGRHASTDYAPKLTPYERKKQCSlcNVLIASEVYLFSHIKGKKHQQAVR-ENSSIQGRELS 831
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAE--EAKKAEEDKNMALRKAEEAKKAE--EARIEEVMKLYEEEKKMKAEEAKKaEEAKIKAEELK 1626
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486797 832 DEEVEhlslKKYVVDIVIESAappEPVKDGEERQKNKKKAKKIKARMNIRAKEYENLVETKNSGSESPYKAKLQRLTKD 910
Cdd:PTZ00121 1627 KAEEE----KKKVEQLKKKEA---EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
540-769 |
2.52e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 540 AESKKKYEEKHmKAQQLReKLREEKTLKLQKLLEREKDVRKWKEELLDQ--RRRMMEEKLLHAEFKREVQLQAivKKAQE 617
Cdd:PTZ00121 1542 AEEKKKADELK-KAEELK-KAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEEKKMKAEEA--KKAEE 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 618 EEAKVNEIafiNTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARD--EAVQERKRALE---AERQARVEELLM 692
Cdd:PTZ00121 1618 AKIKAEEL---KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEakKAEEDKKKAEEakkAEEDEKKAAEAL 1694
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124486797 693 KRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 769
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
552-769 |
7.71e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 7.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 552 KAQQLREKLRE-EKTLKLQKLLEREKDVRKWKEELLDQRRRmmEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEiafint 630
Cdd:COG1196 214 RYRELKEELKElEAELLLLKLRELEAELEELEAELEELEAE--LEELEAELAELEAELEELRLELEELELELEE------ 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 631 leAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQ------ARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQ 704
Cdd:COG1196 286 --AQAEEYELLAELARLEQDIARLEERRRELEERLEeleeelAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486797 705 RQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 769
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
536-939 |
1.11e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 536 KRTIAESKKKYEEKHmKAQQLREKLREEKtlKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLqaiVKKA 615
Cdd:PTZ00121 1469 AKKADEAKKKAEEAK-KADEAKKKAEEAK--KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE---AKKA 1542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 616 qEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELqeerQRRQEEKQARDEAVQERKRALEAERQARVEELlmkRK 695
Cdd:PTZ00121 1543 -EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL----RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA---KK 1614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 696 EQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDEsirrhmeqiEQRKEKAAELSSGRH 775
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA---------EEDKKKAEEAKKAEE 1685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 776 ASTDYAPKLTPYERKKQcslcnvlIASEVYLFSHIKGKKHQQAVR--ENSSIQGRELSDEEVEhlslkkyvvdiviESAA 853
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAK-------KAEELKKKEAEEKKKAEELKKaeEENKIKAEEAKKEAEE-------------DKKK 1745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 854 PPEPVKDGEERQKNKKKAKKIKARMNIRAKEYENLVETKNSGSESPYKAKLQRLTKDLVKQLQVQDSGS-----WVNNKA 928
Cdd:PTZ00121 1746 AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGkegnlVINDSK 1825
|
410
....*....|.
gi 124486797 929 SALDRTLGEIA 939
Cdd:PTZ00121 1826 EMEDSAIKEVA 1836
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
535-772 |
1.89e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 535 RKRTIAESKKKYEEKHMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKK 614
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 615 AQEEEAKVNEIAFintLEAQNKRHDVLSKLKEYEQRLNELQEERqrrqeEKQARDEAVQERKRALEAERQARVEELLMKR 694
Cdd:COG1196 341 ELEEELEEAEEEL---EEAEAELAEAEEALLEAEAELAEAEEEL-----EELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486797 695 KEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHD-ESIRRHMEQIEQRKEKAAELSS 772
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELlEEAALLEAALAELLEELAEAAA 491
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
535-769 |
2.16e-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: 63.78 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 535 RKRTIAESKKKYEEKHMK----AQQLREKLREEKTLKLQKLLEREKD-------VRKWKEE-LLDQRRRMMEEKLLHAEF 602
Cdd:pfam13868 53 RERALEEEEEKEEERKEErkryRQELEEQIEEREQKRQEEYEEKLQEreqmdeiVERIQEEdQAEAEEKLEKQRQLREEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 603 KREVQLQAIVKKAQEEEAKVNE---IAFINTLEAQNKRHDVLSKLKEY--EQRLNELQEERQRRQEEKQARDEAVQER-K 676
Cdd:pfam13868 133 DEFNEEQAEWKELEKEEEREEDeriLEYLKEKAEREEEREAEREEIEEekEREIARLRAQQEKAQDEKAERDELRAKLyQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 677 RALEAERQARVEELLMKRKEQEARI----EQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKK--IQLKHD 750
Cdd:pfam13868 213 EEQERKERQKEREEAEKKARQRQELqqarEEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRrmKRLEHR 292
|
250
....*....|....*....
gi 124486797 751 ESIRRHMEQIEQRKEKAAE 769
Cdd:pfam13868 293 RELEKQIEEREEQRAAERE 311
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
422-766 |
4.58e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 422 AKKEELADRLEK---ANEEAIASAIAEEEQLTREIEA--EENNDINIETDNDSDFSASMGSgslsfcgvslDWNDVLADY 496
Cdd:PRK02224 359 EELREEAAELESeleEAREAVEDRREEIEELEEEIEElrERFGDAPVDLGNAEDFLEELRE----------ERDELRERE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 497 EARESWRQNTSwGDIVEEEPARLPGHGIHMHEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKL--------REEKTLKL 568
Cdd:PRK02224 429 AELEATLRTAR-ERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVeeveerleRAEDLVEA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 569 QKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKR----------EVQLQAIVKKAQEEEAKVNEIAFIN--------T 630
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELReraaeleaeaEEKREAAAEAEEEAEEAREEVAELNsklaelkeR 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 631 LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQ---ERKRALEAERQ-ARVEELLMKRKEQEARIEQQRQ 706
Cdd:PRK02224 588 IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAekrERKRELEAEFDeARIEEAREDKERAEEYLEQVEE 667
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486797 707 EkekaredaarerardreerLAALTaaqqEAMEELQKKI-----QLKHDESIRRHMEQIEQRKEK 766
Cdd:PRK02224 668 K-------------------LDELR----EERDDLQAEIgavenELEELEELRERREALENRVEA 709
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
529-709 |
7.99e-10 |
|
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: 63.60 E-value: 7.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 529 KLSSPSRKRTIAESKKKYEEKHMKAQQLRE----KLREEKTLKLQKL----LEREKDVRKWKEELLDQRRRMMEeklLHA 600
Cdd:pfam17380 405 KILEEERQRKIQQQKVEMEQIRAEQEEARQrevrRLEEERAREMERVrleeQERQQQVERLRQQEEERKRKKLE---LEK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 601 EFKREVQLQAIVKKAQEEEAKVNEIAFIntlEAQNKRHDVLsklKEYEQRLNELQEerqrrqeeKQARDEAVQERKRALE 680
Cdd:pfam17380 482 EKRDRKRAEEQRRKILEKELEERKQAMI---EEERKRKLLE---KEMEERQKAIYE--------EERRREAEEERRKQQE 547
|
170 180
....*....|....*....|....*....
gi 124486797 681 AERQARVEELLMKRKEQEARIEQQRQEKE 709
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEAMERERE 576
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
534-763 |
1.82e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 534 SRKRTIAESKKKYEEKHMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEEL--LDQRRRMMEEKLLHAEFKREVQLQAI 611
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELeeAEEELEEAEAELAEAEEALLEAEAEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 612 VKKAQEEEAKVNEIafintLEAQNKRHDVLSKLKEYEQRLNELQEERQRrQEEKQARDEAVQERKRALEAERQARVEELL 691
Cdd:COG1196 375 AEAEEELEELAEEL-----LEALRAAAELAAQLEELEEAEEALLERLER-LEEELEELEEALAELEEEEEEEEEALEEAA 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486797 692 MKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQR 763
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
536-769 |
5.33e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 536 KRTIAESKKKYEEKHMKAQQLREKLRE---EKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEF-KREVQLQAI 611
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEkekELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIeELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 612 VKKAQEEEAKVNEI-AFINTLEAQnkrhdvLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQE------RKRALEAERQ 684
Cdd:PRK03918 251 EGSKRKLEEKIRELeERIEELKKE------IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDElreiekRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 685 ArVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAaltAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRK 764
Cdd:PRK03918 325 G-IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA---KAKKEELERLKKRLTGLTPEKLEKELEELEKAK 400
|
....*
gi 124486797 765 EKAAE 769
Cdd:PRK03918 401 EEIEE 405
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
528-770 |
2.01e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 58.73 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 528 EKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKTLKLqkllEREKDVRKWKEELLDQRRRMMEEKLLHAEFKrEVQ 607
Cdd:pfam02029 96 EKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIR----EKEYQENKWSTEVRQAEEEGEEEEDKSEEAE-EVP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 608 LQAIVKKAQEEEAKVNEIAFINTLEA--QNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERqa 685
Cdd:pfam02029 171 TENFAKEEVKDEKIKKEKKVKYESKVflDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQ-- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 686 RVEELLMKRKEQEAR-IEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKkiQLKHDESIRRHMEQIEQRK 764
Cdd:pfam02029 249 KLEELRRRRQEKESEeFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAER--KLREEEEKRRMKEEIERRR 326
|
....*.
gi 124486797 765 EKAAEL 770
Cdd:pfam02029 327 AEAAEK 332
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
542-769 |
4.06e-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: 58.14 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 542 SKKKYEEKHMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ--LQAIVKKAQEEE 619
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEekLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 620 AKVNEI--------AFINTLEAQ-----NKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERqAR 686
Cdd:TIGR02168 281 EEIEELqkelyalaNEISRLEQQkqilrERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE-AE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 687 VEELLMKRKEQEARIEQQRQEKEKaredaarerardreerLAALTAAQQEAMEELQKKIQlkhdeSIRRHMEQIEQRKEK 766
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLET----------------LRSKVAQLELQIASLNNEIE-----RLEARLERLEDRRER 418
|
...
gi 124486797 767 AAE 769
Cdd:TIGR02168 419 LQQ 421
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
408-710 |
4.08e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 408 SNVSAADWSMAEVLAKKEELADRLEKANEEAIASAiAEEEQLTREIEAEEnndinietDNDSDFSASMGSGSLSFCGVSL 487
Cdd:TIGR02169 709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE-EDLSSLEQEIENVK--------SELKELEARIEELEEDLHKLEE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 488 DWNDVLADYeARESWRQNTSWGDIVEEEPARLPGHGIHMHEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEK--- 564
Cdd:TIGR02169 780 ALNDLEARL-SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEien 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 565 -TLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLlhaefKREVQLQAIVKKAQEEEAKVnEIAFINTLEAQNKRHDVLSK 643
Cdd:TIGR02169 859 lNGKKEELEEELEELEAALRDLESRLGDLKKERD-----ELEAQLRELERKIEELEAQI-EKKRKRLSELKAKLEALEEE 932
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 644 LKEYEQRLNELQEERQRRQEEK--QARDEAVQERKRALE----------AERQARVEELLMK-------RKEQEARIEQQ 704
Cdd:TIGR02169 933 LSEIEDPKGEDEEIPEEELSLEdvQAELQRVEEEIRALEpvnmlaiqeyEEVLKRLDELKEKrakleeeRKAILERIEEY 1012
|
....*.
gi 124486797 705 RQEKEK 710
Cdd:TIGR02169 1013 EKKKRE 1018
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
542-769 |
1.62e-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: 55.90 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 542 SKKKYEEKHMKAQQlrEKLREEKTLKLQKLLEREK--DVRKWKEELLDQRRRM-MEEKLLHAEFKREVQ-LQAIVKKAQE 617
Cdd:pfam17380 285 SERQQQEKFEKMEQ--ERLRQEKEEKAREVERRRKleEAEKARQAEMDRQAAIyAEQERMAMERERELErIRQEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 618 EEAKVNEIAFINT---------LEAQNKRHDVLSKLK-------EYEQRLNELQEERQRRQEEKQARDEAVQERKRALEA 681
Cdd:pfam17380 363 ERIRQEEIAMEISrmrelerlqMERQQKNERVRQELEaarkvkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 682 ERQ---ARVEELLMKRKEQEARIEQQRQE-------KEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDE 751
Cdd:pfam17380 443 ERAremERVRLEEQERQQQVERLRQQEEErkrkkleLEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEM 522
|
250
....*....|....*...
gi 124486797 752 SIRRHMEQIEQRKEKAAE 769
Cdd:pfam17380 523 EERQKAIYEEERRREAEE 540
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
536-914 |
2.01e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 536 KRTIAESKKKYEEKhmKAQQLREKLREEKTLKLQKLLEREK---DVRKWKEEL---LDQRRRMMEEKLLHAEF-KREVQL 608
Cdd:PTZ00121 1277 ARKADELKKAEEKK--KADEAKKAEEKKKADEAKKKAEEAKkadEAKKKAEEAkkkADAAKKKAEEAKKAAEAaKAEAEA 1354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 609 QAIVKKAQEEEAKVNEIafinTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQA--- 685
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEK----KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAeek 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 686 -RVEELlmKRKEQEAR----IEQQRQEKEKAREDAARERARDREERLAAlTAAQQEAMEELQKK---IQLKHDEsirrhM 757
Cdd:PTZ00121 1431 kKADEA--KKKAEEAKkadeAKKKAEEAKKAEEAKKKAEEAKKADEAKK-KAEEAKKADEAKKKaeeAKKKADE-----A 1502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 758 EQIEQRKEKAAELSSGRHASTdyAPKLTPYERKKQCSlcNVLIASEVYLFSHIKGKKHQQAVRENSSIQGRElSDEEVEH 837
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKK--ADEAKKAEEAKKAD--EAKKAEEKKKADELKKAEELKKAEEKKKAEEAK-KAEEDKN 1577
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124486797 838 LSLKKYVVDIVIESAAPPEPVKDGEERQKNKKKAKKIKARMNIRAKEYENLVETKNSGSESPYKAKLQRLTKDLVKQ 914
Cdd:PTZ00121 1578 MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
536-769 |
2.72e-07 |
|
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: 54.15 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 536 KRTIAESKKKYEEKHmkAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLL-HAEFKRE-VQLQAIVK 613
Cdd:pfam13868 31 KKRIKAEEKEEERRL--DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEeYEEKLQErEQMDEIVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 614 KAQ-EEEAKV--NEIAFINTLEAQNKRHDVLSKLKEYE-QRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEE 689
Cdd:pfam13868 109 RIQeEDQAEAeeKLEKQRQLREEIDEFNEEQAEWKELEkEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 690 LLmkrkEQEARIEQQRQEKEKaredaarerardreeRLAALTAAQQEA------MEELQKKIQLKHD--ESIRRHMEQIE 761
Cdd:pfam13868 189 LR----AQQEKAQDEKAERDE---------------LRAKLYQEEQERkerqkeREEAEKKARQRQElqQAREEQIELKE 249
|
....*...
gi 124486797 762 QRKEKAAE 769
Cdd:pfam13868 250 RRLAEEAE 257
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
534-769 |
3.56e-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: 55.06 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 534 SRKRTIAESKKKYEEKhmkAQQLREKLREEKTLKlQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ------ 607
Cdd:TIGR02168 674 ERRREIEELEEKIEEL---EEKIAELEKALAELR-KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleeri 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 608 --LQAIVKKAQEEEAKVNEiafiNTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALeAERQA 685
Cdd:TIGR02168 750 aqLSKELTELEAEIEELEE----RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-ANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 686 RVEELLMKRKEQEARIEQQRQEKEKaredaarerARDREERLAALTAAQQEAMEELQKKIQLKHDE--SIRRHMEQIEQR 763
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEE---------LSEDIESLAAEIEELEELIEELESELEALLNEraSLEEALALLRSE 895
|
....*.
gi 124486797 764 KEKAAE 769
Cdd:TIGR02168 896 LEELSE 901
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
536-764 |
5.01e-07 |
|
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: 53.38 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 536 KRTIAESKKKYEEKHMKAQQLREKLREEKTLK-----LQKLLEREKDVR-----KWKEELldQRRRMMEEKLLHAEFKRE 605
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQaewkeLEKEEEREEDERileylKEKAER--EEEREAEREEIEEEKERE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 606 VQ-LQAIVKKAQEEEAKVNEIAFINTLEAQNKRHdvlsKLKEYEQRLNELQEERQRrqeeKQARDEAVQERKRALEAERQ 684
Cdd:pfam13868 186 IArLRAQQEKAQDEKAERDELRAKLYQEEQERKE----RQKEREEAEKKARQRQEL----QQAREEQIELKERRLAEEAE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 685 -ARVEELLMKRKEQEA-RIEQQRQEKEKAREDAARERARDREERLAAL-TAAQQEAMEELQKKIQLkhDESIRRHMEQIE 761
Cdd:pfam13868 258 rEEEEFERMLRKQAEDeEIEQEEAEKRRMKRLEHRRELEKQIEEREEQrAAEREEELEEGERLREE--EAERRERIEEER 335
|
...
gi 124486797 762 QRK 764
Cdd:pfam13868 336 QKK 338
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
539-769 |
6.17e-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: 54.21 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 539 IAESKKK----YEEKHMKAQQLREKLREEKTLKLQ--KLLEREKD-----VRKWKEELLDQRRRMMEEKLLHAEFKREVQ 607
Cdd:pfam02463 164 GSRLKRKkkeaLKKLIEETENLAELIIDLEELKLQelKLKEQAKKaleyyQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 608 ------------LQAIVKKAQEEEAKVNEIAFINT--LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQ 673
Cdd:pfam02463 244 ellrdeqeeiesSKQEIEKEEEKLAQVLKENKEEEkeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 674 ERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQ--EAMEELQKKIQLKH-D 750
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERlsSAAKLKEEELELKSeE 403
|
250
....*....|....*....
gi 124486797 751 ESIRRHMEQIEQRKEKAAE 769
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLK 422
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
542-769 |
8.70e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.24 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 542 SKKKYEEKHMKAQQ-LREKLREEKTLKLQKLLErekdvrkWKEELLDQRRrmmeekllhaEFKREVqlqaivkKAQEEEa 620
Cdd:PRK12704 29 AEAKIKEAEEEAKRiLEEAKKEAEAIKKEALLE-------AKEEIHKLRN----------EFEKEL-------RERRNE- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 621 kvneiafintLEAQNKRhdvlskLKEYEQRLNElqeerqrrqeekqaRDEAVQERKRALEAERQ---ARVEELLMKRKEQ 697
Cdd:PRK12704 84 ----------LQKLEKR------LLQKEENLDR--------------KLELLEKREEELEKKEKeleQKQQELEKKEEEL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486797 698 EARIEQQRQEKEKaredaarerardreerLAALTA--AQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 769
Cdd:PRK12704 134 EELIEEQLQELER----------------ISGLTAeeAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAK 191
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
533-928 |
9.78e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 9.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 533 PSRKRTIAESKKK------YEEKHMKAQQLR--EKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEkllhAEFKR 604
Cdd:PTZ00121 1074 PSYKDFDFDAKEDnradeaTEEAFGKAEEAKktETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEE----ARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 605 EVQLQAIVKKAqeEEAKVNEIAfintLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQ 684
Cdd:PTZ00121 1150 DAKRVEIARKA--EDARKAEEA----RKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDA 1223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 685 ARVEELL----MKRKEQEAR-IEQQRQEKEKAREDAARERARDREErlAALTAAQQEAMEELQKKIQLKHDESIRRHME- 758
Cdd:PTZ00121 1224 KKAEAVKkaeeAKKDAEEAKkAEEERNNEEIRKFEEARMAHFARRQ--AAIKAEEARKADELKKAEEKKKADEAKKAEEk 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 759 -QIEQRKEKAAELSSGRHASTDY--------APKLTPYERKKqcslcnvliASEVYLFSHIKGKKHQQAVRENSSIQGRE 829
Cdd:PTZ00121 1302 kKADEAKKKAEEAKKADEAKKKAeeakkkadAAKKKAEEAKK---------AAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 830 LSDEEVEHLSLKKYVvdiviESAAPPEPVKDGEERQKNKKKAKKIKARMNIRAKEYENLVETKNSGSESPYKAKLQRLTK 909
Cdd:PTZ00121 1373 KEEAKKKADAAKKKA-----EEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD 1447
|
410
....*....|....*....
gi 124486797 910 DLVKQLQVQDSGSWVNNKA 928
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKA 1466
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
418-709 |
1.23e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 418 AEVLAKKEEL--ADRLEKANEEAIASAIAEEEQLTReieAEENNDINIETDNDSDFSASMGSGSlsfcgvsldwndvlad 495
Cdd:PTZ00121 1524 ADEAKKAEEAkkADEAKKAEEKKKADELKKAEELKK---AEEKKKAEEAKKAEEDKNMALRKAE---------------- 1584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 496 yEARESWRQNTSWGDIVEEEPARLPGhgihmhEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKTlKLQKLLERE 575
Cdd:PTZ00121 1585 -EAKKAEEARIEEVMKLYEEEKKMKA------EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK-KAEELKKAE 1656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 576 KDVRKWKEELldqRRRMMEEKLLHAEfkrevqlqaiVKKAQEEEAKVNEIafINTLEAQNKRHDVLSKLKEYEQRLNELQ 655
Cdd:PTZ00121 1657 EENKIKAAEE---AKKAEEDKKKAEE----------AKKAEEDEKKAAEA--LKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 656 EERQRRQEEK--QARDEAVQERKRALEA----ERQARVEELlmkRKEQEARIEQQRQEKE 709
Cdd:PTZ00121 1722 KKAEEENKIKaeEAKKEAEEDKKKAEEAkkdeEEKKKIAHL---KKEEEKKAEEIRKEKE 1778
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
527-788 |
1.46e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.82 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 527 HEKLSSpSRKRT---IAESKKKYEEKHMKAQQLR---EKLREEKTLKLqkllEREKDVRKWKEELLDQRRrmmeEKLLHA 600
Cdd:pfam17380 339 QERMAM-ERERElerIRQEERKRELERIRQEEIAmeiSRMRELERLQM----ERQQKNERVRQELEAARK----VKILEE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 601 EFKREVQLQAIVK---KAQEEEAKVNEIafiNTLEAQNKRHDVLSKLKEYE--QRLNELQEERQRRQEEKQARDEavQER 675
Cdd:pfam17380 410 ERQRKIQQQKVEMeqiRAEQEEARQREV---RRLEEERAREMERVRLEEQErqQQVERLRQQEEERKRKKLELEK--EKR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 676 KRALEAERQARVEELLMKRKEQeARIEQQRQEK--EKAREDAARERARDREERLAALTAAQQEAMEElQKKIQ------- 746
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQ-AMIEEERKRKllEKEMEERQKAIYEEERRREAEEERRKQQEMEE-RRRIQeqmrkat 562
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 124486797 747 -----LKHDESIRRHMEQIEQRKEKAAELSSGRHAST---DYAPKLTPYE 788
Cdd:pfam17380 563 eersrLEAMEREREMMRQIVESEKARAEYEATTPITTikpIYRPRISEYQ 612
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
418-706 |
1.95e-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: 52.76 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 418 AEVLAKKEELADRLEK--ANEEAIASAIAEEEQLTREIEAEENNDINIETDNDSDFSASMGS--GSLSFCgvsldwNDVL 493
Cdd:TIGR02169 244 RQLASLEEELEKLTEEisELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASleRSIAEK------EREL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 494 ADYEARESwrqntswgdIVEEEPARLpghgihmheklsspsrKRTIAESKKKYEEKHMKAQQLRE---KLREEKTLKLQK 570
Cdd:TIGR02169 318 EDAEERLA---------KLEAEIDKL----------------LAEIEELEREIEEERKRRDKLTEeyaELKEELEDLRAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 571 LLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREV-QLQAIVKKAQEEEAKVNE-----IAFINTLEAQNKrhDVLSKL 644
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREINELKRELdRLQEELQRLSEELADLNAaiagiEAKINELEEEKE--DKALEI 450
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486797 645 KEYEQRLNELqeerqrrqeekQARDEAVQERKRALEAErQARVEELLMKRKEQEARIEQQRQ 706
Cdd:TIGR02169 451 KKQEWKLEQL-----------AADLSKYEQELYDLKEE-YDRVEKELSKLQRELAEAEAQAR 500
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
513-744 |
2.66e-06 |
|
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: 51.88 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 513 EEEPARLPGHGIHMHEKLSSPSRKRTIAEskkKYEEKHMKAQQLREKLREEKTLKlQKLLEREKdvrKWKEEL-LDQRRR 591
Cdd:pfam15709 313 EERSEEDPSKALLEKREQEKASRDRLRAE---RAEMRRLEVERKRREQEEQRRLQ-QEQLERAE---KMREELeLEQQRR 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 592 MMEEKLlhaefkREVQLQAIVKKAQEEEAKvneiafiNTLEAQNKRHDVLSKLKEYEQRLNELQEerqRRQEEKQARDEA 671
Cdd:pfam15709 386 FEEIRL------RKQRLEEERQRQEEEERK-------QRLQLQAAQERARQQQEEFRRKLQELQR---KKQQEEAERAEA 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486797 672 VQERKRALEaERQARVEELLMKRKEQEaRIEQQRQEKEKAREDAARERARDREERLAAlTAAQQEAMEELQKK 744
Cdd:pfam15709 450 EKQRQKELE-MQLAEEQKRLMEMAEEE-RLEYQRQKQEAEEKARLEAEERRQKEEEAA-RLALEEAMKQAQEQ 519
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
550-770 |
2.70e-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: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 550 HMKAQQLRE-----------KLREEKTLKlqKL------LEREKDVRkwkEELLDQRRRmmeeklLHAEfkREVQLQAIV 612
Cdd:COG1196 151 EAKPEERRAiieeaagiskyKERKEEAER--KLeateenLERLEDIL---GELERQLEP------LERQ--AEKAERYRE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 613 KKAQEEEAKVNEIAfintleaqNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQaRVEELLM 692
Cdd:COG1196 218 LKEELKELEAELLL--------LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-ELEEAQA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 693 KRKEQEARIEQQRQEKEkaredaarerarDREERLAALTAAQQEAMEELQKKIQ--LKHDESIRRHMEQIEQRKEKAAEL 770
Cdd:COG1196 289 EEYELLAELARLEQDIA------------RLEERRRELEERLEELEEELAELEEelEELEEELEELEEELEEAEEELEEA 356
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
412-770 |
3.38e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 412 AADWSMAEVLAKKEELADRLEKAnEEAIASAIAEEEQLTREIEAEENNDINIETDN---DSDFSASMGSGSLSFCGVSLD 488
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAEL-EEELEEAQEELEELEEELEQLENELEAAALEErlkEARLLLLIAAALLALLGLGGS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 489 WNDVLAdyeareswrqnTSWGDIVEEEPARLPGHGIHMHEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKTLKL 568
Cdd:COG4717 268 LLSLIL-----------TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 569 QKLLEREKDVRKWKEeLLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEakvneiaFINTLEAQNKRHDVLSKLKEYE 648
Cdd:COG4717 337 EELLELLDRIEELQE-LLREAEELEEELQLEELEQEIAALLAEAGVEDEEE-------LRAALEQAEEYQELKEELEELE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 649 QRLNELqeerqrrqeekqaRDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLA 728
Cdd:COG4717 409 EQLEEL-------------LGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELL 475
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 124486797 729 ALTAAQQEAMEELQKKIQLKH--DESIRRHMEQIEQRK-----EKAAEL 770
Cdd:COG4717 476 QELEELKAELRELAEEWAALKlaLELLEEAREEYREERlppvlERASEY 524
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
540-711 |
3.49e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.96 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 540 AESKKKYEEKHMKAQQLREKLREEKTLKLQKLLEREKdvrkwkEELLDQrrrmmEEKLLHAEFKREVQLQAivKKAQEEE 619
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEK------ERLAAQ-----EQKKQAEEAAKQAALKQ--KQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 620 AKVNEIAFINTlEAQNKRHDVLSKLKEYEQRLNElqeerqrrqeEKQARDEAVQERKRALEAERQARVEELLMKRKEQEA 699
Cdd:PRK09510 139 AKAAAAAKAKA-EAEAKRAAAAAKKAAAEAKKKA----------EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA 207
|
170
....*....|..
gi 124486797 700 RIEQQRQEKEKA 711
Cdd:PRK09510 208 KKKAAAEAKKKA 219
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
536-710 |
3.95e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.37 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 536 KRTIAESKKKYEEKHMKAQQLREKLrEEKTLKLQKLLereKDVRKWKEELLDQRRRM--MEEKLLHaefKREVQLQAIVK 613
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELEREL-EQKAEEAEALL---KEAEKLKEELEEKKEKLqeEEDKLLE---EAEKEAQQAIK 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 614 KAQEEEAKVneIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKR-------------ALE 680
Cdd:PRK00409 581 EAKKEADEI--IKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEvkylslgqkgevlSIP 658
|
170 180 190
....*....|....*....|....*....|
gi 124486797 681 AERQARVEELLMKRKEQEARIEQQRQEKEK 710
Cdd:PRK00409 659 DDKEAIVQAGIMKMKVPLSDLEKIQKPKKK 688
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
572-784 |
4.02e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 572 LErEKDVRKWKEELLDQRRRM--MEEKLLHAEFKREvQLQAIVKKAQEEEAKVNEIAFINTL-------EAQNKRHDVLS 642
Cdd:COG4913 218 LE-EPDTFEAADALVEHFDDLerAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEYLraalrlwFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 643 KLKEYEQRLNELqeerQRRQEEKQARDEAVQERKRALEAERQA----RVEEL--LMKRKEQE-ARIEQQRQEKEKAREDA 715
Cdd:COG4913 296 ELEELRAELARL----EAELERLEARLDALREELDELEAQIRGnggdRLEQLerEIERLERElEERERRRARLEALLAAL 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486797 716 ARERARDREERLAALTAAQQ--EAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHASTDYAPKL 784
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAAllEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
536-773 |
5.36e-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: 50.53 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 536 KRTIAESKKKYEEKHMKAQQLREKLREEKtlklQKLLEREKDVRKWKEELLDQRRRM----MEEKLLHAEFKREVQLQAI 611
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALE----RRIAALARRIRALEQELAALEAELaeleKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 612 VKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERqrrqeekQARDEAVQERKRALEAERQaRVEELL 691
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-------RADLAELAALRAELEAERA-ELEALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 692 MKRKEQEARIEQQRQEKEKaredaarerardREERLAALTAAQQEAMEELQKKIQlkhdeSIRRHMEQIEQRKEKAAELS 771
Cdd:COG4942 181 AELEEERAALEALKAERQK------------LLARLEKELAELAAELAELQQEAE-----ELEALIARLEAEAAAAAERT 243
|
..
gi 124486797 772 SG 773
Cdd:COG4942 244 PA 245
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
534-770 |
7.11e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 534 SRKRTIAESKKKYEEKHMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ-LQAIV 612
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEeLESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 613 KKAQEE-EAKVNEIAfintlEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELL 691
Cdd:TIGR02168 375 EELEEQlETLRSKVA-----QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486797 692 MKRKEQEARIEQQRQEKEKaredaarerardreeRLAALTAAQQEAMEELQKKIQLKHdeSIRRHMEQIEQRKEKAAEL 770
Cdd:TIGR02168 450 EELQEELERLEEALEELRE---------------ELEEAEQALDAAERELAQLQARLD--SLERLQENLEGFSEGVKAL 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
535-769 |
7.74e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 535 RKRTIAESKKKYEEKHMKAQ-QLREKLREEKTLKLQKLlEREKDVRKWKEELLDQRRRM--MEEKLLHAEFKREvQLQAI 611
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTaELQELEEKLEELRLEVS-ELEEEIEELQKELYALANEIsrLEQQKQILRERLA-NLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 612 VKKAQEE----EAKVNEIAFIntLEAQNKRHDVLSK-LKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALeAERQAR 686
Cdd:TIGR02168 318 LEELEAQleelESKLDELAEE--LAELEEKLEELKEeLESLEAELEELEAELEELESRLEELEEQLETLRSKV-AQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 687 VEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIqlKHDESIRRHMEQIEQRKEK 766
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ--EELERLEEALEELREELEE 472
|
...
gi 124486797 767 AAE 769
Cdd:TIGR02168 473 AEQ 475
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
533-763 |
9.87e-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: 9.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 533 PSRKRTIAESKKKYEEKHMKAQQLREKLREEKTLKLQKLlerekdvRKWKEELLDQRRRMMEEKllHAEFKREVQLQAIV 612
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQ-------KELEQRAAAEKAAKQAEQ--AAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 613 KKA-QEEEAKVNEiafintlEAQNKRhdvlsKLKEYEQRLNELQEERQRRQEEKQARDEAV----QERKRALEAERQARV 687
Cdd:TIGR02794 124 AKAkQAAEAKAKA-------EAEAER-----KAKEEAAKQAEEEAKAKAAAEAKKKAEEAKkkaeAEAKAKAEAEAKAKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 688 EELLMKRKEQEARIEQQRQEK---EKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDES-IRRHMEQIEQR 763
Cdd:TIGR02794 192 EEAKAKAEAAKAKAAAEAAAKaeaEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSeVDKYAAIIQQA 271
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
540-792 |
2.03e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 540 AESKKKYEE--KHMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQE 617
Cdd:PTZ00121 1202 AEAARKAEEerKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 618 EEAKVNEIAFINTLEA--QNKRHDVLSKLKEYEQRLNELQEERQRRQEE----------KQARDEA--VQERKRALEAER 683
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKaeEKKKADEAKKKAEEAKKADEAKKKAEEAKKKadaakkkaeeAKKAAEAakAEAEAAADEAEA 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 684 QARVEELLMKRKEQEAR----IEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQ--LKHDESIRRHM 757
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKkadaAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEekKKADEAKKKAE 1441
|
250 260 270
....*....|....*....|....*....|....*..
gi 124486797 758 E--QIEQRKEKAAELSSGRHASTDYAPKLTPYERKKQ 792
Cdd:PTZ00121 1442 EakKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
559-774 |
2.23e-05 |
|
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: 49.20 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 559 KLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKllhAEFKREVQLQAIVKKAQEEEAKVNEIAF--------INT 630
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA---KKALEYYQLKEKLELEEEYLLYLDYLKLneeridllQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 631 LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAE-----RQARVEELLMKRKEQEARIEQQR 705
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEElkselLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486797 706 QEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLkhdESIRRHMEQIEQRKEKAAELSSGR 774
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK---LEQLEEELLAKKKLESERLSSAAK 391
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
534-710 |
2.41e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 534 SRKRTIAESKKKYEEKHMKAQQLREKLR------EEKTLKLQKLLEREKDV-------------RKWKEELLDQRRRMme 594
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIReleeriEELKKEIEELEEKVKELkelkekaeeyiklSEFYEEYLDELREI-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 595 EKLLHaefKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHdvLSKLKEYEQRLNELQEERQRRQEEKQAR-DEAVQ 673
Cdd:PRK03918 313 EKRLS---RLEEEINGIEERIKELEEKEERLEELKKKLKELEKR--LEELEERHELYEEAKAKKEELERLKKRLtGLTPE 387
|
170 180 190
....*....|....*....|....*....|....*....
gi 124486797 674 ERKRALEAERQAR--VEELLMKRKEQEARIEQQRQEKEK 710
Cdd:PRK03918 388 KLEKELEELEKAKeeIEEEISKITARIGELKKEIKELKK 426
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
533-769 |
2.55e-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: 48.11 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 533 PSRKRTIAE---SKKKYEEKHMKAQQLREKLREEKTLKLQKLLEREKDVRKWkeeLLDQRRRMMEEKLlhAEFKREVQlq 609
Cdd:pfam15558 3 PERDRKIAAlmlARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRL---LLQQSQEQWQAEK--EQRKARLG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 610 aivkkaQEEEAKVnEIAFINTLEAQNKRHDVLSKlKEyEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQArvEE 689
Cdd:pfam15558 76 ------REERRRA-DRREKQVIEKESRWREQAED-QE-NQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQ--NS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 690 LLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQL--KHDESIRRHMEQIEQR---- 763
Cdd:pfam15558 145 LQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELLRRLSLeqSLQRSQENYEQLVEERhrel 224
|
....*.
gi 124486797 764 KEKAAE 769
Cdd:pfam15558 225 REKAQK 230
|
|
| ZnF_U1 |
smart00451 |
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ... |
789-821 |
2.86e-05 |
|
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.
Pssm-ID: 197732 [Multi-domain] Cd Length: 35 Bit Score: 42.24 E-value: 2.86e-05
10 20 30
....*....|....*....|....*....|...
gi 124486797 789 RKKQCSLCNVLIASEVYLFSHIKGKKHQQAVRE 821
Cdd:smart00451 2 GGFYCKLCNVTFTDEISVEAHLKGKKHKKNVKK 34
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
591-769 |
3.00e-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: 47.99 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 591 RMMEEKLLHAEFKREVQLQAIVKKAQEEEAKvneiafintleAQNKRHDVLSKlkeyEQRLNELQEERQRRQEEKQARDE 670
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIAEKKRIKAEEK-----------EEERRLDEMME----EERERALEEEEEKEEERKEERKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 671 AVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTA-AQQEAMEELQKKIQLKH 749
Cdd:pfam13868 74 YRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFnEEQAEWKELEKEEEREE 153
|
170 180
....*....|....*....|
gi 124486797 750 DESIRRHMEQIEQRKEKAAE 769
Cdd:pfam13868 154 DERILEYLKEKAEREEEREA 173
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
436-951 |
3.69e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 436 EEAIASAIAEEEQLTREIeaeenNDINIETDNDSDFSASMGSGSLSFCGVSLDWNDVLADYEARESWRQNTSWGdivEEE 515
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDI-----IDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFG---KAE 1101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 516 PARLPGHGIHMHEKLSSPSRKRtiAESKKKYEEKHmKAQQLR--EKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMM 593
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKK--AEDARKAEEAR-KAEDARkaEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKA 1178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 594 EEKLLHAEFKR--EVQLQAIVKKAQ-----EEEAKVNEI-AFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEK 665
Cdd:PTZ00121 1179 EAARKAEEVRKaeELRKAEDARKAEaarkaEEERKAEEArKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 666 QARDEAVQERKRALEAERQARVEELLM---KRKEQEARieqQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQ 742
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKaeeKKKADEAK---KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK 1335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 743 KKIQ--LKHDESIRRHMEQIEQRKEKAAELSSGRHASTDYAPKLTPYERKKqcslcnvliASEVYLFSHIKgKKHQQAVR 820
Cdd:PTZ00121 1336 KKAEeaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK---------AEEKKKADEAK-KKAEEDKK 1405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 821 ENSSIQGRELSDEEVEHLSLKKyvvdiviesaappEPVKDGEErqknkkkaKKIKARMNIRAKEYENLVETKNSGSESPY 900
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKA-------------EEKKKADE--------AKKKAEEAKKADEAKKKAEEAKKAEEAKK 1464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 124486797 901 KAKLQRLTKDLVKQLQVQDSGSWVNNKASALDRTLGEIARILEKENVPDQI 951
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
541-791 |
7.06e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 541 ESKKKYEEKHMKAQQLREKLREEKT---LKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREV-QLQAIVKKAQ 616
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELReieKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLeELEERHELYE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 617 EEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQAR---------- 686
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrel 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 687 ---------------VEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAaltaaqqEAMEELQKKIQLKHDE 751
Cdd:PRK03918 446 teehrkelleeytaeLKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA-------EQLKELEEKLKKYNLE 518
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 124486797 752 SIRRHMEQIEQRKEKAAELSSGRHASTDYAPKLTPYERKK 791
Cdd:PRK03918 519 ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
|
|
| zf-met |
pfam12874 |
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found ... |
793-815 |
7.88e-05 |
|
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.
Pssm-ID: 463736 [Multi-domain] Cd Length: 25 Bit Score: 40.94 E-value: 7.88e-05
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
529-625 |
8.52e-05 |
|
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: 43.88 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 529 KLSSPSRKRTIAESKKkyeEKHMKAQQLREKLREEKTLK-LQKLLEREKDVRKWKEELLDQRRRMMEEKLLHA----EFK 603
Cdd:pfam00836 32 KLSLSPKKKDSSLEEI---QKKLEAAEERRKSLEAQKLKqLAEKREKEEEALQKADEENNNFSKMAEEKLKQKmeayKEN 108
|
90 100
....*....|....*....|..
gi 124486797 604 REVQLQAIVKKAQEEEAKVNEI 625
Cdd:pfam00836 109 REAQIAALKEKLKEKEKHVEEV 130
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
543-771 |
1.46e-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: 46.50 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 543 KKKYEEKHMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKV 622
Cdd:TIGR00618 657 QERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 623 NEIAFINTL-EAQNKRHDVLSKLKEYEQRLNElqeerqrRQEEKQARDEAVQERKRALEAERQARvEELLMKRKEQEARI 701
Cdd:TIGR00618 737 REDALNQSLkELMHQARTVLKARTEAHFNNNE-------EVTAALQTGAELSHLAAEIQFFNRLR-EEDTHLLKTLEAEI 808
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486797 702 EQQRQEKEKAREDAARERARDRE---ERLAALTAAQQEAmeelqkKIQLKHDESIRRHMEQIEQRKEKAAELS 771
Cdd:TIGR00618 809 GQEIPSDEDILNLQCETLVQEEEqflSRLEEKSATLGEI------THQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
493-784 |
2.00e-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: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 493 LADYEARESWRQNTSWGDIVEEEPARLpghgihmHEKLSspsRKRTIAESKKKYEEKHMKAQQ-LREKLREEKTLKLQKL 571
Cdd:pfam15558 81 RADRREKQVIEKESRWREQAEDQENQR-------QEKLE---RARQEAEQRKQCQEQRLKEKEeELQALREQNSLQLQER 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 572 LEREKDVRKWKEELLDQRRRM--MEEKLLHAEFKREVQLQAivkKAQEEEAKvneiafiNTLE-----AQNKRHDVLskl 644
Cdd:pfam15558 151 LEEACHKRQLKEREEQKKVQEnnLSELLNHQARKVLVDCQA---KAEELLRR-------LSLEqslqrSQENYEQLV--- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 645 keyEQRLNELQEerqrrqeekQARDEAVQERK---RALEAERQaRVEELLMKRKEQEARIEQQRQEKEKAREdaarerar 721
Cdd:pfam15558 218 ---EERHRELRE---------KAQKEEEQFQRakwRAEEKEEE-RQEHKEALAELADRKIQQARQVAHKTVQ-------- 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486797 722 DREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHASTDYAPKL 784
Cdd:pfam15558 277 DKAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKKEQRSEQISREKEATLEEARKT 339
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
553-754 |
2.33e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.42 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 553 AQQLREKLREEKTLKlQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNeiafintLE 632
Cdd:COG3064 1 AQEALEEKAAEAAAQ-ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAE-------LA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 633 AQNKRhdvlsKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLmKRKEQEARIEQQRQEKEKAR 712
Cdd:COG3064 73 AEAAK-----KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAK-RKAEEEAKRKAEEERKAAEA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 124486797 713 EDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIR 754
Cdd:COG3064 147 EAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAA 188
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
552-772 |
3.01e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 552 KAQQLREKLREEKtlklQKLLEREKDVRKWKEELLDQRRRmmEEKLLHA----EFKREVQLQAIVKKAQEEEAKVNEI-A 626
Cdd:PRK02224 409 NAEDFLEELREER----DELREREAELEATLRTARERVEE--AEALLEAgkcpECGQPVEGSPHVETIEEDRERVEELeA 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 627 FINTLEAQ----NKRHDVLSKLKEYEQR----------LNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLM 692
Cdd:PRK02224 483 ELEDLEEEveevEERLERAEDLVEAEDRierleerredLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 693 KRKE-QEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRhmEQIEQRKEKAAELS 771
Cdd:PRK02224 563 AEEEaEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERR--ERLAEKRERKRELE 640
|
.
gi 124486797 772 S 772
Cdd:PRK02224 641 A 641
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
528-710 |
3.46e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 528 EKLSSPS-RKRTIAESKKKYEEKHMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMmeekllhaefKREV 606
Cdd:COG4717 56 DELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----------EKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 607 QLQAIVKKAQEEEAKVNEIAfintleaqnkrhDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQAR 686
Cdd:COG4717 126 QLLPLYQELEALEAELAELP------------ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE 193
|
170 180
....*....|....*....|....
gi 124486797 687 VEELLMKRKEQEARIEQQRQEKEK 710
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEE 217
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
533-770 |
3.48e-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: 44.94 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 533 PSRKRTIAESKKKYEEKHMKAQQLREKLREEKTLklQKLLEREkdvRKWKEEllDQRRRMMEEKLLHAEFKREvQLQaiv 612
Cdd:pfam15709 311 SEEERSEEDPSKALLEKREQEKASRDRLRAERAE--MRRLEVE---RKRREQ--EEQRRLQQEQLERAEKMRE-ELE--- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 613 kkaQEEEAKVNEIafinTLEAQnkrhdvlsKLKEYEQRlnelqeerqrrqeekQARDEAVQERKRALEAERqARVEELLM 692
Cdd:pfam15709 380 ---LEQQRRFEEI----RLRKQ--------RLEEERQR---------------QEEEERKQRLQLQAAQER-ARQQQEEF 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 693 KRKEQEarIEQQRQEKEKAREDAARERARDREERLAA-----LTAAQQEAMEELQKKiqLKHDESIRRHMEQIEQRKEKA 767
Cdd:pfam15709 429 RRKLQE--LQRKKQQEEAERAEAEKQRQKELEMQLAEeqkrlMEMAEEERLEYQRQK--QEAEEKARLEAEERRQKEEEA 504
|
...
gi 124486797 768 AEL 770
Cdd:pfam15709 505 ARL 507
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
488-712 |
3.78e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 488 DWNDVLADYEARESWRQNTSW--GDIVEEEPARLPGHGIHMHEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKT 565
Cdd:pfam02029 95 DEKESVAERKENNEEEENSSWekEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENF 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 566 LKLQKLLEREKDVRKWKEE---LLDQRRRMMEEKLLHAEF---------KREVQLQAIVKKAQEEEAKVNEIAfiNTLEA 633
Cdd:pfam02029 175 AKEEVKDEKIKKEKKVKYEskvFLDQKRGHPEVKSQNGEEevtklkvttKRRQGGLSQSQEREEEAEVFLEAE--QKLEE 252
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486797 634 QNKRHDVLSKlKEYEQRLNELQEERQRRQEEKQARdeavQERKRALEAERQARVEEllmkRKEQEARIEQqrqEKEKAR 712
Cdd:pfam02029 253 LRRRRQEKES-EEFEKLRQKQQEAELELEELKKKR----EERRKLLEEEEQRRKQE----EAERKLREEE---EKRRMK 319
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
665-792 |
4.17e-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: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 665 KQARDEAVQERKRALEAE-RQARVEEllmKRKEQEariEQQRQEKEKAREDAARErardreerlAALTAAQQEAMEELQK 743
Cdd:pfam15709 327 KREQEKASRDRLRAERAEmRRLEVER---KRREQE---EQRRLQQEQLERAEKMR---------EELELEQQRRFEEIRL 391
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 124486797 744 KIQLKHDESIRRHMEQIEQRKEKAAELSSGRHASTDYAPKLTPYERKKQ 792
Cdd:pfam15709 392 RKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQ 440
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
665-748 |
5.15e-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: 43.71 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 665 KQARDEAVQERKRALEAERQarvEELLMKRKEQEarieqqRQEKEKaredaarerardreeRLAALTAAQQEAMEELQKK 744
Cdd:pfam07946 263 KKTREEEIEKIKKAAEEERA---EEAQEKKEEAK------KKEREE---------------KLAKLSPEEQRKYEEKERK 318
|
....
gi 124486797 745 IQLK 748
Cdd:pfam07946 319 KEQR 322
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
539-737 |
7.49e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 539 IAESKKKYEEKHMKAQQLREKLR------EEKTLKLQKLLEREKDVRKWKEELldqrrrmmEEKLLHAEfKREVQLQAIV 612
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDalqaelEELNEEYNELQAELEALQAEIDKL--------QAEIAEAE-AEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 613 KK----AQEEEAKVNEIAFIntLEAQN-----KRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAER 683
Cdd:COG3883 89 GEraraLYRSGGSVSYLDVL--LGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 124486797 684 QARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEA 737
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
497-770 |
9.38e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.32 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 497 EARESWRQntswgdivEEEPARLPGHGIHMHEKLSSPSRKRTIAESKKKYEEKHMKAQQLReKLREEKTLKLQKLLEREK 576
Cdd:pfam02029 17 EERRRQKE--------EEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTA-KREERRQKRLQEALERQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 577 D----VRKWKEELLDQRRRMMEEKLLHAEFKREVQlqaivkkAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLN 652
Cdd:pfam02029 88 EfdptIADEKESVAERKENNEEEENSSWEKEEKRD-------SRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 653 ELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTA 732
Cdd:pfam02029 161 DKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEA 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 124486797 733 AQQEAMEELQKKIQLKHDESIRRHMEQIEQRK-EKAAEL 770
Cdd:pfam02029 241 EVFLEAEQKLEELRRRRQEKESEEFEKLRQKQqEAELEL 279
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
513-690 |
9.96e-04 |
|
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: 42.91 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 513 EEEPARLPghgiHMHEKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKTLKLQKLLErekdvRKWKEELLDQrrrm 592
Cdd:TIGR02794 85 AAEQARQK----ELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE-----RKAKEEAAKQ---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 593 meekllhAEFKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKeyeqrlNELQEERQRRQEEKQARDEAv 672
Cdd:TIGR02794 152 -------AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAK------AEAAKAKAAAEAAAKAEAEA- 217
|
170
....*....|....*...
gi 124486797 673 qERKRALEAERQARVEEL 690
Cdd:TIGR02794 218 -AAAAAAEAERKADEAEL 234
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
528-926 |
1.09e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.53 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 528 EKLSSPSRKRTIAESKKKYEEKHMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFK--RE 605
Cdd:COG5022 820 IKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISslKL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 606 VQLQ------AIVKKAQEEEAKVNEI--AFINTLEAQNKRHDV-LSKLKEYEQ--RLNELqeerqrrQEEKQARDEAVQE 674
Cdd:COG5022 900 VNLEleseiiELKKSLSSDLIENLEFktELIARLKKLLNNIDLeEGPSIEYVKlpELNKL-------HEVESKLKETSEE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 675 RKRAL----EAERQARVEELLMKRKEQEArieqQRQEKEKAREDAARERARDREERLAALTAAQQEAMEE-LQKKIQLKH 749
Cdd:COG5022 973 YEDLLkkstILVREGNKANSELKNFKKEL----AELSKQYGALQESTKQLKELPVEVAELQSASKIISSEsTELSILKPL 1048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 750 DESIRRHMEQIEQRKEKAAELSSGRHASTDYapKLTPYERKKQCSLCNVLIASEVYLFSHIKGKKhqQAVRENSSIQG-- 827
Cdd:COG5022 1049 QKLKGLLLLENNQLQARYKALKLRRENSLLD--DKQLYQLESTENLLKTINVKDLEVTNRNLVKP--ANVLQFIVAQMik 1124
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 828 RELSDEEVEHLSLKKYVVDIVIESAAPPEPVKDGEERQKNKKKAKKIKARMNIRAKE--YENLVETKNSGSES------- 898
Cdd:COG5022 1125 LNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRlyQSALYDEKSKLSSSevndlkn 1204
|
410 420
....*....|....*....|....*...
gi 124486797 899 PYKAKLQRLTKDLVKQLQVQDSGSWVNN 926
Cdd:COG5022 1205 ELIALFSKIFSGWPRGDKLKKLISEGWV 1232
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
567-772 |
1.45e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 567 KLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEIafINTLE-----AQNKRHDVL 641
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEE--IERYEeqreqARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 642 SKLKEYEQRLNE----------LQEERQRRQEEKQARDEAVQERKRA---LEAERQARVEELLMKRKEQEArIEQQRQEK 708
Cdd:PRK02224 241 EVLEEHEERREEletleaeiedLRETIAETEREREELAEEVRDLRERleeLEEERDDLLAEAGLDDADAEA-VEARREEL 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486797 709 EKAREDAARErardreerLAALTAAQQEAMEELQKkiqlkHDESIRRHMEQIEQRKEKAAELSS 772
Cdd:PRK02224 320 EDRDEELRDR--------LEECRVAAQAHNEEAES-----LREDADDLEERAEELREEAAELES 370
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
535-770 |
1.56e-03 |
|
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: 43.03 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 535 RKRTIAESKKKYEEKHMKAQQLR---EKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAI 611
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLQTKEqihLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQT 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 612 VKKAQEEEAKVNEI-------AFINTLEAQNKRHDvLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQ 684
Cdd:TIGR00618 537 YAQLETSEEDVYHQltserkqRASLKEQMQEIQQS-FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 685 ARVEELLMKRKEQEARIE----QQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHM--- 757
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRLHlqqcSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtyw 695
|
250
....*....|....
gi 124486797 758 -EQIEQRKEKAAEL 770
Cdd:TIGR00618 696 kEMLAQCQTLLREL 709
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
539-767 |
2.16e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 539 IAESKKKYEEKHMKAQQLREK-----LREEKTLKLQKLLErekdvrkwkeelLDQRRRMMEEKLLHAEFKREvQLQAIVK 613
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSE------------LESQLAEARAELAEAEARLA-ALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 614 KAQEEEAKVNEIAFINTLEAQnkRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMK 693
Cdd:COG3206 251 SGPDALPELLQSPVIQQLRAQ--LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAR 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486797 694 RKEQEARIEQQRQEkekaredaarerardreerLAALTAAQQEaMEELQKKIQLKhdesiRRHMEQIEQRKEKA 767
Cdd:COG3206 329 EASLQAQLAQLEAR-------------------LAELPELEAE-LRRLEREVEVA-----RELYESLLQRLEEA 377
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
555-703 |
2.27e-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: 42.19 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 555 QLREKLREEKTL-----KLQKLLEREKDVRKWKEELLDQRRRMMEEKLlhAEFKREvqLQAIVKKAQEEEAKVNEIAFIN 629
Cdd:pfam07888 35 RLEECLQERAELlqaqeAANRQREKEKERYKRDREQWERQRRELESRV--AELKEE--LRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486797 630 TLEAQNKrhDVLSKLK-EYEQRLNELQEERqrrqeekQARDEAVQERKRALEAERQaRVEELLMKRKEQEARIEQ 703
Cdd:pfam07888 111 EELSEEK--DALLAQRaAHEARIRELEEDI-------KTLTQRVLERETELERMKE-RAKKAGAQRKEEEAERKQ 175
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
547-710 |
2.64e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 547 EEKHMKAQQLREKLREEktlkLQKLLEREKDVRKwKEELLDQRRRMMEEKLLHAEFKREVQLQAivkkaqeeeakvnEIA 626
Cdd:COG4913 287 QRRLELLEAELEELRAE----LARLEAELERLEA-RLDALREELDELEAQIRGNGGDRLEQLER-------------EIE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 627 fintlEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERqARVEELLMKRKEQEARIEQQRQ 706
Cdd:COG4913 349 -----RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL-EALEEALAEAEAALRDLRRELR 422
|
....
gi 124486797 707 EKEK 710
Cdd:COG4913 423 ELEA 426
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
536-707 |
3.12e-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: 40.51 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 536 KRTIAESKKKYEEKHMKAQQLREKLREEKTL---KLQKLLEREKDVRkwkeELLDQRRRMMEEKLLHAEFKREV-QLQAI 611
Cdd:cd00176 46 EAELAAHEERVEALNELGEQLIEEGHPDAEEiqeRLEELNQRWEELR----ELAEERRQRLEEALDLQQFFRDAdDLEQW 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 612 VKKAQEEEAKVNEIAFINTLEAQNKRHDVL-SKLKEYEQRLNELqeerqrrqeeKQARDEAVQERKRALEAERQARVEEL 690
Cdd:cd00176 122 LEEKEAALASEDLGKDLESVEELLKKHKELeEELEAHEPRLKSL----------NELAEELLEEGHPDADEEIEEKLEEL 191
|
170
....*....|....*..
gi 124486797 691 LMKRKEQEARIEQQRQE 707
Cdd:cd00176 192 NERWEELLELAEERQKK 208
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
535-654 |
3.37e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 535 RKRTIAESKKKYEEKHMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREV-QLQAIVK 613
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLeAEREELL 738
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 124486797 614 KAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNEL 654
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
644-770 |
3.72e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 644 LKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEaERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDR 723
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAE-EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 124486797 724 EERLAALTAAQQEAMEELQKKIQ--LKHDESIRRHMEQIEQRKEKAAEL 770
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEelEERLEELRELEEELEELEAELAEL 175
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
669-773 |
3.76e-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: 41.02 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 669 DEAVQERKRALEAER-QARVEELLMKR-KEQEARIEQQRQEKEKAredaarerardreerlaaltaaQQEAMEELQKKIQ 746
Cdd:cd16269 190 DQALTEKEKEIEAERaKAEAAEQERKLlEEQQRELEQKLEDQERS----------------------YEEHLRQLKEKME 247
|
90 100
....*....|....*....|....*...
gi 124486797 747 LKHDESIRRHMEQIEQR-KEKAAELSSG 773
Cdd:cd16269 248 EERENLLKEQERALESKlKEQEALLEEG 275
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
603-769 |
4.10e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.33 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 603 KREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRhdvlsKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRA-LEA 681
Cdd:PRK09510 75 KRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKE-----RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAkAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 682 ERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALT--AAQQEAMEELQKKIQLKHDESIRRHMEQ 759
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAkkKAEAEAKKKAAAEAKKKAAAEAKAAAAK 229
|
170
....*....|
gi 124486797 760 IEQRKEKAAE 769
Cdd:PRK09510 230 AAAEAKAAAE 239
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
552-850 |
4.58e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 552 KAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEekllhaefkREVQLQAIVKKAQEEEAKVNeiafintl 631
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ---------LEEELEELNEQLQAAQAELA-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 632 EAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALeAERQARVEELLMKRKEQEARIEQQRQEKEKA 711
Cdd:COG4372 98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI-AEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 712 REDAARerardreerlAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHASTDYAPKLTPYERKK 791
Cdd:COG4372 177 SEAEAE----------QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 124486797 792 QCSLCNVLIASEVYLFSHIKGKKHQQAVRENSSIQGRELSDEEVEHLSLKKYVVDIVIE 850
Cdd:COG4372 247 DKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
558-770 |
6.13e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 558 EKLREEktlkLQKLLEREKDVRKWKEELLDQRRRMMEEKLlHAEfkrevQLQAIVKKAQEEEAKVnEIAFINTLEAQNKR 637
Cdd:TIGR02169 173 EKALEE----LEEVEENIERLDLIIDEKRQQLERLRRERE-KAE-----RYQALLKEKREYEGYE-LLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 638 HDV-LSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAA 716
Cdd:TIGR02169 242 IERqLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 124486797 717 RErardrEERLAALTAAQQEAMEELQKKIQlkhDESIRRH--MEQIEQRKEKAAEL 770
Cdd:TIGR02169 322 ER-----LAKLEAEIDKLLAEIEELEREIE---EERKRRDklTEEYAELKEELEDL 369
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
583-746 |
7.10e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 583 EELLDQRRRMMEEKLL--HAEFKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLnelqeerqr 660
Cdd:COG1196 624 GRTLVAARLEAALRRAvtLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE--------- 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 661 rqeEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEE 740
Cdd:COG1196 695 ---LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
....*.
gi 124486797 741 LQKKIQ 746
Cdd:COG1196 772 LEREIE 777
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
539-771 |
7.76e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 539 IAESKKKYEEKHMKAQQLREKLREEKTLKlQKLLEREKDVRKWKEELLDQRRRMMEE-----KLLHAEFKREVQLQAIVK 613
Cdd:COG1340 38 LKELAEKRDELNAQVKELREEAQELREKR-DELNEKVKELKEERDELNEKLNELREEldelrKELAELNKAGGSIDKLRK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 614 KAQEEEAKvneiaFIN---TLEAQNKrhdVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQarVEEL 690
Cdd:COG1340 117 EIERLEWR-----QQTevlSPEEEKE---LVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKK--IKEL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 691 LMKRKEQEARIEQQRQEKEKAREDAARERardreerlAALTAAQQEAMEELQKKIQLKhdESIRRHMEQIEQRKEKAAEL 770
Cdd:COG1340 187 AEEAQELHEEMIELYKEADELRKEADELH--------KEIVEAQEKADELHEEIIELQ--KELRELRKELKKLRKKQRAL 256
|
.
gi 124486797 771 S 771
Cdd:COG1340 257 K 257
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
568-707 |
8.51e-03 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 38.06 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 568 LQKLLEREKDVRKWKEELLDQRRrmmeekllhAEFKR-EVQLQAIVKKAQEEEAKVNEIAFINTLEAQnkrhdvLSKLKE 646
Cdd:TIGR02473 4 LQKLLDLREKEEEQAKLELAKAQ---------AEFERlETQLQQLIKYREEYEQQALEKVGAGTSALE------LSNYQR 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486797 647 YEQRLNELQEERQRrqeeKQARDEAVQERKRALEAERQARVE--ELLMKRKEQEARIEQQRQE 707
Cdd:TIGR02473 69 FIRQLDQRIQQQQQ----ELALLQQEVEAKRERLLEARRELKalEKLKEKKQKEYRAEEAKRE 127
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
545-789 |
8.62e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 545 KYEEKHMKAQQLREKLREEKTLKLQK----LLEREKDVRKWKEELLDQrrrmmeEKLLHAEFKREVQLQAIVKKAQEEEA 620
Cdd:PRK03918 76 KFEKNGRKYRIVRSFNRGESYLKYLDgsevLEEGDSSVREWVERLIPY------HVFLNAIYIRQGEIDAILESDESREK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 621 KVNEIAFINTLE-AQNKRHDVLSKLKEYEQRLNELQeerqrrqeekqARDEAVQERKRALEAErqarVEELLMKRKEQEA 699
Cdd:PRK03918 150 VVRQILGLDDYEnAYKNLGEVIKEIKRRIERLEKFI-----------KRTENIEELIKEKEKE----LEEVLREINEISS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 700 RIEQQRQEKEKAREDAARERArdreerLAALTAAQQEAMEELQKKIQlKHDESIRRHMEQIEQRKEKAAELSSGRHASTD 779
Cdd:PRK03918 215 ELPELREELEKLEKEVKELEE------LKEEIEELEKELESLEGSKR-KLEEKIRELEERIEELKKEIEELEEKVKELKE 287
|
250
....*....|
gi 124486797 780 YAPKLTPYER 789
Cdd:PRK03918 288 LKEKAEEYIK 297
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
574-769 |
9.29e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 574 REKDVRKWKeelldQRRRMM----EEKLlhAEFKREV-QLQAIVKKAQEEEAKVNEIafintLEAQNKRHDVLSKLKEY- 647
Cdd:COG4913 590 HEKDDRRRI-----RSRYVLgfdnRAKL--AALEAELaELEEELAEAEERLEALEAE-----LDALQERREALQRLAEYs 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 648 --EQRLNELQEERQRRQEEKQARD------EAVQERKRALEAERQA---RVEELLMKRKEQEARIEQQRQEKEKAREDAA 716
Cdd:COG4913 658 wdEIDVASAEREIAELEAELERLDassddlAALEEQLEELEAELEEleeELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 124486797 717 RERARDREERLAALTAA-QQEAMEELQKKIQlkhdESIRRHMEQIEQRKEKAAE 769
Cdd:COG4913 738 AAEDLARLELRALLEERfAAALGDAVERELR----ENLEERIDALRARLNRAEE 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
528-710 |
9.71e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 528 EKLSSPSRKRTIAESKKKYEEKHMK--AQQLREKLREEKTLKlQKLLEREKDVRKWKEEL-----LDQRRRMMEEKLLHA 600
Cdd:PRK03918 490 KKESELIKLKELAEQLKELEEKLKKynLEELEKKAEEYEKLK-EKLIKLKGEIKSLKKELekleeLKKKLAELEKKLDEL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 601 EFKREVQLQAIVKKA----QEEEAKVNEI--AFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQE 674
Cdd:PRK03918 569 EEELAELLKELEELGfesvEELEERLKELepFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 124486797 675 ----------------RKRALEAERQ-----ARVEELLMKRKEQEARIEQQRQEKEK 710
Cdd:PRK03918 649 leelekkyseeeyeelREEYLELSRElaglrAELEELEKRREEIKKTLEKLKEELEE 705
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
536-654 |
9.78e-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: 39.52 E-value: 9.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 536 KRTIAESKKKYEEKHMKAQQLREKLREEKTLKLQKLLEREkdvrkwkEELLDQRRRMMEEKLLHAEFKREvQLQAIVKKA 615
Cdd:COG1579 58 EKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKE-------IESLKRRISDLEDEILELMERIE-ELEEELAEL 129
|
90 100 110
....*....|....*....|....*....|....*....
gi 124486797 616 QEEEAKVNEiafinTLEAQNKRHDvlSKLKEYEQRLNEL 654
Cdd:COG1579 130 EAELAELEA-----ELEEKKAELD--EELAELEAELEEL 161
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
539-751 |
9.84e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 539 IAESKKKYEEKHMKAQQLREKLREEKTlKLQKLLEREKDVRKWKEELLDQRRRMMEEKL-LHAE---FKREVQLQAIVKK 614
Cdd:COG1340 73 VKELKEERDELNEKLNELREELDELRK-ELAELNKAGGSIDKLRKEIERLEWRQQTEVLsPEEEkelVEKIKELEKELEK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486797 615 AQEEEAKVNEIAFINT--LEAQNKRHDVLSKLKEYEQRLNELQEERQRRqeeKQARDEAVQERKRALEA--ERQARVEEL 690
Cdd:COG1340 152 AKKALEKNEKLKELRAelKELRKEAEEIHKKIKELAEEAQELHEEMIEL---YKEADELRKEADELHKEivEAQEKADEL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486797 691 lmkRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDE 751
Cdd:COG1340 229 ---HEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTTEE 286
|
|
| |
