|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-394 |
7.92e-15 |
|
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: 79.72 E-value: 7.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 53 QEAALQATQNRLEEAQGKLRRLQEDFVYNLQVLEERDRELERYDIEFTQARRREEAQQAEASELKIEVAKLKQELTREAR 132
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 133 HMEELRHQHKLMLQEHRLELERVHsdknsELNHQREQYENLKWKLERKLKELDGELALQRQVHKTLEEIYSLLSEVFLNV 212
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLE-----EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 213 CYRLVALQARgCARIPVMPVMLALTERRTPWDSSLPVDVMKQEWVWLDSSTELLQEFE---SEAQRREHEFQLRADDLSN 289
Cdd:TIGR02168 823 RERLESLERR-IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLnerASLEEALALLRSELEELSE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 290 TVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHAR-ELQDLEAMK----------DARIKDLEKKL 358
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALEnkieddeeeaRRRLKRLENKI 981
|
330 340 350
....*....|....*....|....*....|....*....
gi 1958663236 359 HS---VQLAkkkAEETFRRKHEELDRQAREKDTVLAAVK 394
Cdd:TIGR02168 982 KElgpVNLA---AIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
29-651 |
4.39e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 29 RELSELLAQKEEEWRALQAHRAQLQEAALQAtqnRLEEAQGKLRRLQEDfvynlqvLEERDRELERYDIEFTQARRREEA 108
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEA---ELEELEAELEELEAE-------LAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 109 QQAEASELKIEVAKLKQELtreaRHMEELRHQhklmLQEHRLELERVHSDKNSELNHQREQYENLkwklERKLKELDGEL 188
Cdd:COG1196 286 AQAEEYELLAELARLEQDI----ARLEERRRE----LEERLEELEEELAELEEELEELEEELEEL----EEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 189 ALQRQVHKTLEEIYSLLSEVFLNVCYRLVALQARgcaripvmpvmlALTERRTpwdsslpvdvmkqewvwldssTELLQE 268
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEE------------LLEALRA---------------------AAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 269 FESEAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAmKD 348
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA-AL 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 349 ARIKDLEKKLHSVQLAKKKAEEtfrrKHEELDRQAREKDTVLAAVKGAHAEQLQTLDAKVLELQFRCETLEGQLRRAEWR 428
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEA----DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 429 QAEDSKERNSLTDKEFGDRSTCVLS-MYWHSVITSVPSGLPSRFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEE 507
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 508 MKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGLDWQRRCDDIECNQIQRSETLIQGLTKARDQVAAKLQETER 587
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958663236 588 ALHKQETLLKAVSLERDQAMETLRTHGLLPGQEAQVPPQPHEGEIRTDSPSSEIQRLQEQNAGL 651
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
35-428 |
7.86e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.49 E-value: 7.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 35 LAQKEEEWRALQAHRAQLqEAALQATQNRLEEAQGKLRRL--QEDFVYNLQVLEERDRELERYDIEFTQARRREEAQQae 112
Cdd:COG4717 83 AEEKEEEYAELQEELEEL-EEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEELR-- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 113 asELKIEVAKLKQELTREARHMEELRHQHKLMLQEHRLELERVHSDKNSELNHQREQYENLKWKLERKLKELDgELALQR 192
Cdd:COG4717 160 --ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE-QLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 193 QVHKTLEEIYSLLSEVFLN--VCYRLVALQARGCARIPVMPVMLALTErrtpwdsslpvdVMKQEWVWLDSSTELLQEFE 270
Cdd:COG4717 237 EAAALEERLKEARLLLLIAaaLLALLGLGGSLLSLILTIAGVLFLVLG------------LLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 271 SEAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEhiELERKLQDHARELQDLEAMKDAR 350
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL--EEELQLEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 351 -IKDLEKKLHSVQlAKKKAEETFRRKHEELDRQAREKDTVLAAV-KGAHAEQLQTLDAKVLELQFRCETLEGQLRRAEWR 428
Cdd:COG4717 383 dEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALdEEELEEELEELEEELEELEEELEELREELAELEAE 461
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
32-814 |
6.92e-12 |
|
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: 70.09 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 32 SELLAQKEEEWRALqahraqLQEAA--------LQATQNRLEEAQGKLRRLQEdfvynlqVLEERDRELERYDIeftQAR 103
Cdd:TIGR02168 147 SEIIEAKPEERRAI------FEEAAgiskykerRKETERKLERTRENLDRLED-------ILNELERQLKSLER---QAE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 104 RREEAQ--QAEASELKIEVAKL--------KQELTREARHMEELRHQHKLMLQEHRLELERV---HSDKNSELNHQREQY 170
Cdd:TIGR02168 211 KAERYKelKAELRELELALLVLrleelreeLEELQEELKEAEEELEELTAELQELEEKLEELrleVSELEEEIEELQKEL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 171 ENLKwkleRKLKELDGELALQRQVHKTLEEIYSLLSEVFLNVCYRLVALQARgcaripvmpvmLALTERRtpwdsslpVD 250
Cdd:TIGR02168 291 YALA----NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE-----------LAELEEK--------LE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 251 VMKQEwvwLDSSTELLQEFESEAQ---RREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHI 327
Cdd:TIGR02168 348 ELKEE---LESLEAELEELEAELEeleSRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 328 ELERKLQDHARELQDLE-AMKDARIKDLEKKLHSVQLAKKKAEETFRRKHEELD------RQAREKDTVLAAVKGAHaEQ 400
Cdd:TIGR02168 425 ELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDaaerelAQLQARLDSLERLQENL-EG 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 401 LQTLDAKVLELQFRCETLEGQLR-----RAEWRQA--------------EDS----KERNSLTDKEFGDRSTCVLSMYWH 457
Cdd:TIGR02168 504 FSEGVKALLKNQSGLSGILGVLSelisvDEGYEAAieaalggrlqavvvENLnaakKAIAFLKQNELGRVTFLPLDSIKG 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 458 SVITSVPSGLPSRFREDAAALKAAWDAQ-------------------------------------------------IAQ 488
Cdd:TIGR02168 584 TEIQGNDREILKNIEGFLGVAKDLVKFDpklrkalsyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvITG 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 489 MSKEAVSKDL-----------QIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGLDWQRrcddiE 557
Cdd:TIGR02168 664 GSAKTNSSILerrreieeleeKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-----L 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 558 CNQIQRSETLIQGLTKARDQVAAKLQETERALHKQETLLKAVSLERDQAMETLRThgllpgQEAQVppqpHEGEIRTDSP 637
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ------LKEEL----KALREALDEL 808
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 638 SSEIQRLQEQNAGLRNAVSQMRKEMEMLSGHLPFAQ------SEERSNANPEPKAGEDSAPpdyvlALEAEMQNLKHELK 711
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEeqieelSEDIESLAAEIEELEELIE-----ELESELEALLNERA 883
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 712 ALEEQLQGTGEPVKTSMATADpHHGAHNSAEAADAAPADQTLITLALRKLGDRVHLLNLLvTQLKKKLRQKPLELVAVQQ 791
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELR-ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ-ERLSEEYSLTLEEAEALEN 961
|
890 900
....*....|....*....|...
gi 1958663236 792 EIPSEVDQVHLEVLELQKQVAEL 814
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENKIKEL 984
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
28-426 |
7.25e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.71 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 28 ERELSELLAQKEEEWRALQAHRAQLQ--EAALQATQNRLEEAQGKLRRLQED---------FVYNLQVLEER--DRELER 94
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEekEERLEELKKKLKELEKRLEELEERhelyeeakaKKEELERLKKRltGLTPEK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 95 YDIEFTQARRREEAQQAEASELKIEVAKLKQELTREARHMEELRHQH-------KLMLQEHRLELERVHSDKNSELNHQR 167
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEHRKELLEEYTAELKRIEKEL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 168 EQYENLKWKLERKLKELDGELALQRQV---HKTLEEIYSLLSEvfLNVcYRLVALQArgcaripvmpvmlALTERRTPWD 244
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELiklKELAEQLKELEEK--LKK-YNLEELEK-------------KAEEYEKLKE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 245 SSLPVdvmKQEWVWLDSSTELLQEFESEAQRREHEFQLRADDLSNtvLTHELK------VKLLNKELQALKEAGAQATEs 318
Cdd:PRK03918 533 KLIKL---KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAE--LLKELEelgfesVEELEERLKELEPFYNEYLE- 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 319 LQKAESEHIELERKLQDHARELQDLEAM---KDARIKDLEKKLHsvQLAKKKAEETFRRKHEELDRQAREKDTVLAAVKG 395
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEElaeTEKRLEELRKELE--ELEKKYSEEEYEELREEYLELSRELAGLRAELEE 684
|
410 420 430
....*....|....*....|....*....|.
gi 1958663236 396 AHaEQLQTLDAKVLELQFRCETLEGQLRRAE 426
Cdd:PRK03918 685 LE-KRREEIKKTLEKLKEELEEREKAKKELE 714
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
28-665 |
1.63e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 28 ERELSELLAQKE--EEWRALQAhraQLQEAALQATQNRLEEAQGKLRRLQEDFVYNLQVLEERDRELERYDIEFTQARRR 105
Cdd:COG1196 199 ERQLEPLERQAEkaERYRELKE---ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 106 EEAQQAEASELKIEVAKLKQELTREARhmeELRHQhKLMLQEHRLELERVHSDKNSELNHQREQYENLKwKLERKLKELD 185
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQ---DIARL-EERRRELEERLEELEEELAELEEELEELEEELE-ELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 186 GELALQRQVHKTLEEIYSLLSEVFLNVCYRLVALQARgcaripvmpvmlALTERRTpwdsslpvdvmkqewvwldssTEL 265
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE------------LLEALRA---------------------AAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 266 LQEFESEAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEA 345
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 346 mKDARIKDLEKKLHSVQLAKKKAEEtfrrKHEELDRQAREKDTVLAAVKGAHAEQLQTLDAKVLELQFRCETLEGQLRRA 425
Cdd:COG1196 478 -ALAELLEELAEAAARLLLLLEAEA----DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 426 EWRQAEDSKERNSLTDKEFGDRSTCVLsmywhsvitSVPSGLPSRFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQE 505
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPL---------DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 506 EEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGLDWQRRCDDIECNQIQRSETLIQGLTKARDQVAAKLQET 585
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 586 ERALHKQETLLKAVSLERDQAMETLRTHGLLPGQEAQVPPQPHEGEIRTDSPSSEIQRLQEqnagLRNAVSQMRKEMEML 665
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE----LERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
267-882 |
6.09e-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: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 267 QEFESEAQRREHEFQLraddlsntvltheLKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEA- 345
Cdd:COG1196 216 RELKEELKELEAELLL-------------LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELe 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 346 --MKDARIKDLEKKLHSVQLAKKKAEETFRRKHEELDRQAREKDtVLAAVKGAHAEQLQTLDAKVLELQFRCETLEGQLR 423
Cdd:COG1196 283 leEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA-ELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 424 RAEWRQAEDSKERNSLTDKEFGDRSTcvlsmywhsvitsvpsglpsrfREDAAALKAAWDAQIAQMSKEAVSKDLQIQAL 503
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEE----------------------LLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 504 QEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLgldwqrrcddiecnqIQRSETLIQGLTKARDQVAAKLQ 583
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL---------------LELLAELLEEAALLEAALAELLE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 584 ETERALHKQETLLKAVSLERDQAMETLRTHGLlpgqEAQVPPQPHEGEIRTDSPSSEIQRLQEQNAGLRNAV----SQMR 659
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLL----AGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVveddEVAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 660 KEMEMLSGHLPFAQSEERSNANPEPKAGEDSAPPDYVLALEAEMQNLKHELKALEEQLQGTGepVKTSMATADPHHGAHN 739
Cdd:COG1196 561 AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL--LGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 740 SAEAADAApadqtlitLALRKLGDRVHLLNLLVTQLKKKLRQKPLELVAVQQEIPSEVDQVHLEVLELQKQVAELRKHLK 819
Cdd:COG1196 639 AVTLAGRL--------REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958663236 820 MTQPQGEPSYIKQLQREGLAD---WHPMGMEDQTESPTFLQEGAQPPQTTSVSHLQRKLKDAARKI 882
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEaerEELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
53-547 |
7.98e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 66.68 E-value: 7.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 53 QEAALQATQNRLEEAQGKLRRLQEDFVynlqvlEERDRELERYDIEFTQARRREEAQQAEASELKIEVAKLKQELTREAR 132
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKI------EELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 133 HMEELRHQHKLMLQEHR------LELERVHSDKNSELNHQREQYENLK----WKLERKLKELDGE---LALQRQVHKTLE 199
Cdd:pfam15921 392 ELSLEKEQNKRLWDRDTgnsitiDHLRRELDDRNMEVQRLEALLKAMKsecqGQMERQMAAIQGKnesLEKVSSLTAQLE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 200 EIYSLLSEVFLNVCYRLVALQArgcARIPVMPVMLALTERRTPwdsslpVDVMKQEWVWLDSSTEL-LQEFESEAQRREH 278
Cdd:pfam15921 472 STKEMLRKVVEELTAKKMTLES---SERTVSDLTASLQEKERA------IEATNAEITKLRSRVDLkLQELQHLKNEGDH 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 279 --EFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAM---KDARIKD 353
Cdd:pfam15921 543 lrNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILkdkKDAKIRE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 354 LEKKLHSVQLAKKKAEETFRRKHEELDRQAREKDTVLAAVKGAHAEqLQTL--DAKVLELQFRCET---------LEGQL 422
Cdd:pfam15921 623 LEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNE-LNSLseDYEVLKRNFRNKSeemetttnkLKMQL 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 423 RRAewrQAEDSKERNSLTDKEFGDRSTCVLSMYWHSVITSVPSGLPS-----RFREDAAALKAAWDAQIAQmSKEAVSKD 497
Cdd:pfam15921 702 KSA---QSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDAlqskiQFLEEAMTNANKEKHFLKE-EKNKLSQE 777
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958663236 498 L------------QIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGL 547
Cdd:pfam15921 778 LstvateknkmagELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKL 839
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
28-725 |
2.83e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 28 ERELSELLAQKEEEWRALQAHRAQlqeaalqaTQNRLEEAqgklRRLQEDFVYNLQVLEERDRELErydieftQARRREE 107
Cdd:PTZ00121 1114 ARKAEEAKKKAEDARKAEEARKAE--------DARKAEEA----RKAEDAKRVEIARKAEDARKAE-------EARKAED 1174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 108 AQQAEASELKIEVAKLKQ-ELTREARHMEELRHQHklmlQEHRLELERVHSDKnselnhqrEQYENLKWKLERKLKELDG 186
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEElRKAEDARKAEAARKAE----EERKAEEARKAEDA--------KKAEAVKKAEEAKKDAEEA 1242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 187 ELALQRQVHKTLEEIYSLLSEVFLNVCYRLVALQARGCARIPVMPVMLALTERRTPwDSSLPVDVMKQEWVWLDSSTELL 266
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKA-EEKKKADEAKKKAEEAKKADEAK 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 267 QEFEsEAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQ-----DHARELQ 341
Cdd:PTZ00121 1322 KKAE-EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEekkkaDEAKKKA 1400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 342 DLEAMKDARIKDLEKKLHSVQLAKKKAEEtfRRKHEELDRQAREKDTVLAAVKGAH-AEQLQTLDAKVLELQfrcETLEG 420
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEE--KKKADEAKKKAEEAKKADEAKKKAEeAKKAEEAKKKAEEAK---KADEA 1475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 421 QLRRAEWRQAEDSKERNSLTDKEfgdrstcvlsmywhsvitsvpsglPSRFREDAAALKAAWDAQIAQMSKEAvskdlqi 500
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKK------------------------ADEAKKAAEAKKKADEAKKAEEAKKA------- 1524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 501 QALQEEEMKLKAQVAKSQQDIdRYKQQLSLAVEREQSLEREQVQlgldWQRRCDDIECNQIQRSETLIQgLTKARDQVAA 580
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEK-KKADELKKAEELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKK-AEEARIEEVM 1598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 581 KLQETERALHKQEtlLKAVSLERDQAMETLRTHgllpgQEAQVPPQPHEGEIRTDSPSSEIQRLQEQNAGLRNAVSQMRK 660
Cdd:PTZ00121 1599 KLYEEEKKMKAEE--AKKAEEAKIKAEELKKAE-----EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958663236 661 EMEMLSGHLPFAQSEERSNANPEPKAGEDSAPPDYVLALEAEMQNLKHELKALEEQLQGTGEPVK 725
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
28-718 |
2.92e-09 |
|
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: 61.61 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 28 ERELSELLAQKEEEWRALQAHRAQLQE------AALQATQNRLEEAQGKLRRLQEDFVYNLQVLEERDRELERYDIEFTQ 101
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEeieelqKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 102 ARRREEAQQAEASELKIEVAKLKQELTREARHMEELrHQHKLMLQEHRLELERVHSDKNSELNHQREQYENLKWKLERkl 181
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEEL-ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER-- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 182 keldgelaLQRQVHKTLEEIYSLLSEVFLNvcyRLVALQARGCARIPvmpvMLALTERRtpwdsslpVDVMKQEWVWLDS 261
Cdd:TIGR02168 412 --------LEDRRERLQQEIEELLKKLEEA---ELKELQAELEELEE----ELEELQEE--------LERLEEALEELRE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 262 STELLQEFESEAQRREHEFQLRADDLSNTVLTHE---LKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHAR 338
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQ 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 339 EL--QDLEAMKDArIKDLEKK---------LHSVQLAKKKAEETFRRKHEELDRQ-AREKDTVLAAVKGAHAEQLQTL-- 404
Cdd:TIGR02168 549 AVvvENLNAAKKA-IAFLKQNelgrvtflpLDSIKGTEIQGNDREILKNIEGFLGvAKDLVKFDPKLRKALSYLLGGVlv 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 405 ---------DAKVLELQFRCETLEGQLRRAEWRQAEDSKERNsltdkefgdrstcvlsmywhsvitsvpSGLPSRFREda 475
Cdd:TIGR02168 628 vddldnaleLAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTN---------------------------SSILERRRE-- 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 476 aalKAAWDAQIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGLDWQRRCDD 555
Cdd:TIGR02168 679 ---IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 556 IECNQIQRSETLIQgLTKARDQVAAKLQETERALHKQETLLKAVSLERDQAMETLRTHGLLPGQEAQVPPQPHEGEIRTD 635
Cdd:TIGR02168 756 LTELEAEIEELEER-LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 636 SPSSEIQRLQEQNAGLRNAVSQMRKEMEMLSghLPFAQSEERSNANPEPKAGEDSAppdyVLALEAEMQNLKHELKALEE 715
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELE--ELIEELESELEALLNERASLEEA----LALLRSELEELSEELRELES 908
|
...
gi 1958663236 716 QLQ 718
Cdd:TIGR02168 909 KRS 911
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-211 |
1.14e-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: 59.69 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 30 ELSELLAQKEEEWRALQAHRAQLQEaALQATQNRLEEAQGKLRRLQEDFVYNLQVLEERDRELERYDIEFTQARRREEAQ 109
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 110 QAEASELKIEVAKLKQ---ELTREARHMEELRHQHKLMLQEHRLELE------RVHSDKNSELNHQREQYENLKWKLERK 180
Cdd:TIGR02168 851 SEDIESLAAEIEELEElieELESELEALLNERASLEEALALLRSELEelseelRELESKRSELRRELEELREKLAQLELR 930
|
170 180 190
....*....|....*....|....*....|.
gi 1958663236 181 LKELDGELAlqrQVHKTLEEIYSLLSEVFLN 211
Cdd:TIGR02168 931 LEGLEVRID---NLQERLSEEYSLTLEEAEA 958
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-722 |
4.92e-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: 57.37 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 30 ELSELLAQKEEEWRALQAHRAQLQEAALQAtQNRLEEAQGKLRRLQEDFVYNLQVLEERDRELERYDIEftQARRREEAQ 109
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETL-RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE--IEELLKKLE 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 110 QAEASELKIEVAKLKQELTREARHMEELRHQHKLmLQEHRLELERVHSDKNSELNHQREQYENLKWKLERKLKELDGELA 189
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEE-LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 190 LQrQVHKTLEEIYSLLSEvFLNVC--YRLvALQARGCARIPvMPVMLALTERRTPWDSSLPVDVMKQEWVWLDSSTE-LL 266
Cdd:TIGR02168 511 LL-KNQSGLSGILGVLSE-LISVDegYEA-AIEAALGGRLQ-AVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGtEI 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 267 QEFESEAQRREHEFQLRADDLsntVLTHELKVKLLNKELqalkeAGAQATESLQKAesehIELERKLQDHAR--ELQDLE 344
Cdd:TIGR02168 587 QGNDREILKNIEGFLGVAKDL---VKFDPKLRKALSYLL-----GGVLVVDDLDNA----LELAKKLRPGYRivTLDGDL 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 345 AMKDARIKDLEKKLHSVQLAKKKAEETFRRKHEELDRQAREKDTVLAAVKGAH---AEQLQTLDAKVLELQFRCETLEGQ 421
Cdd:TIGR02168 655 VRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELeelEEELEQLRKELEELSRQISALRKD 734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 422 LRRAEWR--QAEDSKERNSLTDKEFGDRSTCVLSMYWHSvitsvpsglpSRFREDAAALKAAWDAQIAQMSKEAVSKDLQ 499
Cdd:TIGR02168 735 LARLEAEveQLEERIAQLSKELTELEAEIEELEERLEEA----------EEELAEAEAEIEELEAQIEQLKEELKALREA 804
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 500 IQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGLdwqrrcddiecnQIQRSETLIQGLTKARDQVA 579
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE------------DIESLAAEIEELEELIEELE 872
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 580 AKLQETERALHKQETLLKAVSLERDQAMETLRTHgllpgqeaqvppqphegeirtdspSSEIQRLQEQNAGLRNAVSQMR 659
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELREL------------------------ESKRSELRRELEELREKLAQLE 928
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958663236 660 KEMEMLSGHLpfAQSEERSNANPEPKAGEDSAPPDyvlALEAEMQNLKHELKALEEQLQGTGE 722
Cdd:TIGR02168 929 LRLEGLEVRI--DNLQERLSEEYSLTLEEAEALEN---KIEDDEEEARRRLKRLENKIKELGP 986
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
28-436 |
1.78e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 28 ERELSELLAQKEEEWRALQAHRAQLQEAalqatQNRLEEAQGKLRRLQEDfvynLQVLEERDRELErydieftqarrree 107
Cdd:PRK03918 216 LPELREELEKLEKEVKELEELKEEIEEL-----EKELESLEGSKRKLEEK----IRELEERIEELK-------------- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 108 aqqAEASELKIEVAKLK--QELTREARHMEELRHQHKLMLQEHRLELERVHSDKNS--ELNHQREQYENLKWKLERKLKE 183
Cdd:PRK03918 273 ---KEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGieERIKELEEKEERLEELKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 184 LDGELALQRQVHKTLEEIYSLLSEvflnvcyrlvalqargcaripvmpvMLALTERRTPwdssLPVDVMKQEWVWLDSST 263
Cdd:PRK03918 350 LEKRLEELEERHELYEEAKAKKEE-------------------------LERLKKRLTG----LTPEKLEKELEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 264 ELLQEFESEAQRREHEFQLRADDLSNTV----------------LTHELKVKLLNK---ELQALKEAGAQATESLQKAES 324
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgreLTEEHRKELLEEytaELKRIEKELKEIEEKERKLRK 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 325 EHIELERKLQDHaRELQDLEAMKDaRIKDLEKKLHSVQLAK-KKAEETFRRKHEELDRQAREKDTVLAAVKGAHA--EQL 401
Cdd:PRK03918 481 ELRELEKVLKKE-SELIKLKELAE-QLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkKKL 558
|
410 420 430
....*....|....*....|....*....|....*
gi 1958663236 402 QTLDAKVLELQFRCETLEGQLRRAEWRQAEDSKER 436
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
28-608 |
3.12e-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: 54.68 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 28 ERELSELLAQKEEEWRALQAHRAQLQEAALQATQNRLEEAQGKLRRLQEDfvynlqvLEERDRELERYDIEFTQARRREE 107
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE-------LERLEEALEELREELEEAEQALD 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 108 AQQAEASELKIEVAKLKqelTREARHMEELRHQHKLMLQEHRLELervHSDKNSELNHQREQYEnlkwklerKLKELDGE 187
Cdd:TIGR02168 479 AAERELAQLQARLDSLE---RLQENLEGFSEGVKALLKNQSGLSG---ILGVLSELISVDEGYE--------AAIEAALG 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 188 LALQRQVHKTLE---EIYSLLSEVFLNVCYRLV-------ALQARGCARIPVMPVMLALTERRTPWDSSLPVDVmkQEWV 257
Cdd:TIGR02168 545 GRLQAVVVENLNaakKAIAFLKQNELGRVTFLPldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAL--SYLL 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 258 WLDSSTELLQefESEAQRREHEFQLR------------------ADDLSNTVLTHELKVKLLNKELQALKEAGAQATESL 319
Cdd:TIGR02168 623 GGVLVVDDLD--NALELAKKLRPGYRivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEEKIAELEKAL 700
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 320 QKAESEHIELERKLQDHARELQDLEamkdARIKDLEKKLHSVQLAKKKAEETFRRKHEELDRQAREKDTVLAAV------ 393
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELS----RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaeee 776
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 394 KGAHAEQLQTLDAKVLELQFRCETLEGQLRRAewrQAEDSKERNSLTDKEFGDRSTcvlsmywhsvitsvpsglpSRFRE 473
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDEL---RAELTLLNEEAANLRERLESL-------------------ERRIA 834
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 474 DAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQvqlgldwqrrc 553
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL----------- 903
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958663236 554 DDIEcNQIQRSETLIQGLTKARDQVAAKLQETE-RALHKQETLLKAVSLERDQAME 608
Cdd:TIGR02168 904 RELE-SKRSELRRELEELREKLAQLELRLEGLEvRIDNLQERLSEEYSLTLEEAEA 958
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
69-877 |
1.19e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 69 GKLRRLQEDFVYNLQVLEERDRELERYDIEFTQArrrEEAQQAEASelKIEVAKLKQELTR---EARHMEELRHQHKLML 145
Cdd:PTZ00121 1067 GQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKA---EEAKKTETG--KAEEARKAEEAKKkaeDARKAEEARKAEDARK 1141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 146 QEhrlELERVHSDKNSELNHQREqyENLKWKLERKLKEldgelALQRQVHKTLEEIYSllsevflnvcyrlvALQARGCA 225
Cdd:PTZ00121 1142 AE---EARKAEDAKRVEIARKAE--DARKAEEARKAED-----AKKAEAARKAEEVRK--------------AEELRKAE 1197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 226 RIPVMPVMLALTERRTPWDSSLPVDVMKQEWVwldSSTELLQEFESEAQRREHE-FQLRADDLSNTVLTHELKVKLLNKE 304
Cdd:PTZ00121 1198 DARKAEAARKAEEERKAEEARKAEDAKKAEAV---KKAEEAKKDAEEAKKAEEErNNEEIRKFEEARMAHFARRQAAIKA 1274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 305 LQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAMKDARIKDLEKKLHSVQLAKKKAEETFRRKHEELDRQAR 384
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA 1354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 385 EKDTVLAAVKGAHAEQLQTLDA--KVLELQFRCETLEgQLRRAEWRQAEDSKERNSLTDKEFGDRSTcvlsmywhsviTS 462
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAkkKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKAAAAKKKA-----------DE 1422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 463 VPSGLPSRFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVErEQSLEREQ 542
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE-EAKKKADE 1501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 543 VQLGLDWQRRCDDI-ECNQIQRSETLIQGLTKARDQVAAKLQETERA--LHKQETLLKAVSL---------ERDQAMETL 610
Cdd:PTZ00121 1502 AKKAAEAKKKADEAkKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdeLKKAEELKKAEEKkkaeeakkaEEDKNMALR 1581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 611 RTHGLLPGQEAQVPPQPHEGEIRTDSPSSEIQRLQEQnaglRNAVSQMRKEMEM--LSGHLPFAQSEERSNANPEPKAGE 688
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA----KIKAEELKKAEEEkkKVEQLKKKEAEEKKKAEELKKAEE 1657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 689 DSAPPDYVLALEAEMQNLK-HELKALEEQLQGTGEPVKTSMATAdphhgahnsaeaadaapadqtlitlalRKlgdrvhl 767
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKaEEAKKAEEDEKKAAEALKKEAEEA---------------------------KK------- 1703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 768 lnllVTQLKKKL---RQKPLELVAVQQEIPSEVDQVHLEVLELQKQVAELRKHlkmtqpQGEPSYIKQLQREGladwHPM 844
Cdd:PTZ00121 1704 ----AEELKKKEaeeKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD------EEEKKKIAHLKKEE----EKK 1769
|
810 820 830
....*....|....*....|....*....|...
gi 1958663236 845 GMEDQTESPTFLQEGAQPPQTTSVSHLQRKLKD 877
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
33-200 |
3.16e-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: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 33 ELLAQKEEEWRALQAHRAQLQE--AALQATQNRLEEAQGKLRRLQEDF---------VYNLQVLEERDRELERYDIEFTQ 101
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEErlEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 102 ARRREEAQQAEASELKIEVAKLKQELTREARHMEELRHQhklmLQEHRLELERVHSDKNSELNhqreqyenlkWKLERKL 181
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----LDELQDRLEAAEDLARLELR----------ALLEERF 755
|
170
....*....|....*....
gi 1958663236 182 KELDGElALQRQVHKTLEE 200
Cdd:COG4913 756 AAALGD-AVERELRENLEE 773
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
28-432 |
5.35e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 28 ERELSELLAQKEEEWRALQAHRAQLQEAALQATQ-------NRLEEAQGKLRRLQEDfvynlqvLEERDRELERYDIEFT 100
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAqirgnggDRLEQLEREIERLERE-------LEERERRRARLEALLA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 101 QARRREEAQQAEASELKIEVAKLKQELTREARHMEELRHQHKLMLQEHRLELERVHSDKNSeLNHQR----EQYENLKWK 176
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS-LERRKsnipARLLALRDA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 177 LERKLKELDGEL------------------ALQRQVHK---TL---EEIYSLLSEVflnvcyrLVALQARGCARIPVMPV 232
Cdd:COG4913 449 LAEALGLDEAELpfvgelievrpeeerwrgAIERVLGGfalTLlvpPEHYAAALRW-------VNRLHLRGRLVYERVRT 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 233 MLALTERRTPWDSSLP--VDVMKQEW-VWLDSstELLQEF-----ESEAQRREHEFQL-----------------RADDL 287
Cdd:COG4913 522 GLPDPERPRLDPDSLAgkLDFKPHPFrAWLEA--ELGRRFdyvcvDSPEELRRHPRAItragqvkgngtrhekddRRRIR 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 288 SNTVL--THELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAMKD-----ARIKDLEKKLHS 360
Cdd:COG4913 600 SRYVLgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaeREIAELEAELER 679
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958663236 361 VQLAK---KKAEETFRRKHEELDRQAREKDTVlaavkgahAEQLQTLDAKVLELQFRCETLEGQLRRAEWRQAED 432
Cdd:COG4913 680 LDASSddlAALEEQLEELEAELEELEEELDEL--------KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
29-593 |
5.85e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 29 RELSELLAQKEEEWRALqahRAQLQEaaLQATQNRLEEAQGKLRRLQEdfvyNLQVLEERDRELERydieftqarRREEa 108
Cdd:PRK03918 210 NEISSELPELREELEKL---EKEVKE--LEELKEEIEELEKELESLEG----SKRKLEEKIRELEE---------RIEE- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 109 QQAEASELKIEVAKLK--QELTREARHMEELRHQHKLMLQEHRLELERVHSDKNS--ELNHQREQYENLKWKLERKLKEL 184
Cdd:PRK03918 271 LKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGieERIKELEEKEERLEELKKKLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 185 DGELALQRQVHKTLEEIYSLLSEvflnvcyrlvalqargcaripvmpvMLALTERRTPwdssLPVDVMKQEWVWLDSSTE 264
Cdd:PRK03918 351 EKRLEELEERHELYEEAKAKKEE-------------------------LERLKKRLTG----LTPEKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 265 LLQEFESEAQRREHEFQLRADDLSNTV----------------LTHELKVKLLNK---ELQALKEAGAQATESLQKAESE 325
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgreLTEEHRKELLEEytaELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 326 HIELERKLQDHaRELQDLEAMKDaRIKDLEKKLHSVQLAK-KKAEETFRRKHEELDRQAREKDTVLAAVKgahaeqlqtl 404
Cdd:PRK03918 482 LRELEKVLKKE-SELIKLKELAE-QLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLKKELE---------- 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 405 daKVLELQFRCETLEGQLRRAEWRQAEDSKERNSLTDKEFGDrstcvlsmywhsvitsvpsgLPSRFREdaaalkaawDA 484
Cdd:PRK03918 550 --KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE--------------------LEERLKE---------LE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 485 QIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGLDWQRRCDDIECNQIQRS 564
Cdd:PRK03918 599 PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGL 678
|
570 580
....*....|....*....|....*....
gi 1958663236 565 ETLIQGLTKARDQVAAKLQETERALHKQE 593
Cdd:PRK03918 679 RAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-429 |
6.63e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 86 EERDRELERYDIEFTQARRREEAQQAEASELKIEVAKLKQEltREarhmeelrhqHKLMLQEHRLELERVH-SDKNSELN 164
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE--RE----------KAERYQALLKEKREYEgYELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 165 HQREQYENLKWKLERKLKELDGELALQRQVHKTLEEIYSLLSEVFLNVCYRLVALQARGCARIPVMPVMLALTERRtpwd 244
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERS---- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 245 sslpVDVMKQEwvwLDSSTELLQEFESE--AQRREHE--------FQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQ 314
Cdd:TIGR02169 310 ----IAEKERE---LEDAEERLAKLEAEidKLLAEIEelereieeERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 315 ATESLQKAESEHIELERKLQDHARE---LQDLEAMKDARIKDLEKKLHSVQLAKKKAEETFRRKHEELdRQAREKDTVLA 391
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKREldrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI-KKQEWKLEQLA 461
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958663236 392 AVKGAHAEQLQTLDAKVLELQFRCETLEGQLRRAEWRQ 429
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
330-606 |
1.32e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 330 ERKLqDHARE----LQDLEAMKDARIKDLEKKlhsvqlaKKKAEetfrrKHEELDRQAREKDTVLAAVKGAHAE-QLQTL 404
Cdd:COG1196 178 ERKL-EATEEnlerLEDILGELERQLEPLERQ-------AEKAE-----RYRELKEELKELEAELLLLKLRELEaELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 405 DAKVLELQFRCETLEGQLRRAEwrqaedskernsltdkefgdrstcvlsmywhsvitsvpsglpsrfredaaalkaawdA 484
Cdd:COG1196 245 EAELEELEAELEELEAELAELE---------------------------------------------------------A 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 485 QIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLgldwQRRCDDIEcNQIQRS 564
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL----EEELEELE-EELEEL 342
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958663236 565 ETLIQGLTKARDQVAAKLQETERALHKQETLLKAVSLERDQA 606
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-442 |
1.73e-05 |
|
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: 49.30 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 101 QARRREEAQQ--AEASELKIEVAKLKQELTREARHMEELRHQHKLMLQEHRlELERVHSDKNSELNHQREQYENlkwkLE 178
Cdd:TIGR02169 669 SRSEPAELQRlrERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG-EIEKEIEQLEQEEEKLKERLEE----LE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 179 RKLKELDGELALQRQVHKTLEEIYSLLSEVFLNVCYRLVALQAR-GCARIP-VMPVMLALTERRTPWDSSLpvDVMKQEW 256
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPeIQAELSKLEEEVSRIEARL--REIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 257 VWLDSSTELLQEFESEAQRREHEFQLRADDLsntvlthELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDH 336
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSI-------EKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 337 ARELQDLEAMKDARIKDLEKKLHSVQLAKKKAEETFRRKHEELDRQAREKDTVLAAVkgahaeQLQTLDAKVLELQFRCE 416
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL------SLEDVQAELQRVEEEIR 968
|
330 340
....*....|....*....|....*.
gi 1958663236 417 TLEGQLRRAEWRQAEDSKERNSLTDK 442
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLDELKEK 994
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
28-154 |
1.75e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.70 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 28 ERELSELLAQKEEEWRALQAHraqlQEAALQATQNRLEEAQGKLRRLQEdFVYNLQ-VLEERDRELERYDIEFTQARRRE 106
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEH----EERELTEEEEEIRRLEEQVERLEA-EVEELEaELEEKDERIERLERELSEARSEE 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958663236 107 EAQ---QAEASELKIEVAKLKQELTREARHMEELRHQHKLMLQEHRLELER 154
Cdd:COG2433 458 RREirkDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSG 508
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
29-181 |
3.17e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 29 RELSELLAQKEEEWRALQAHRAQLQEAA---------------LQATQNRLEEAQGKLRRLQEDfvynLQVLEERDRELE 93
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidVASAEREIAELEAELERLDAS----SDDLAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 94 RYDIEFTQARRREEAQQAEASELKIEVAKLKQELTREARHMEEL----RHQHKLMLQEHRLEL--ERVHSDKNSELNHQR 167
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAedlaRLELRALLEERFAAAlgDAVERELRENLEERI 775
|
170
....*....|....
gi 1958663236 168 EQYENLKWKLERKL 181
Cdd:COG4913 776 DALRARLNRAEEEL 789
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
97-449 |
3.64e-05 |
|
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: 48.14 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 97 IEFTQARRREEAQQ-AEASELKIEVAKLKQELTREARHMEELRhqhkLMLQEHRLELERVHSDKNSELNHQ--------R 167
Cdd:TIGR02169 148 ISMSPVERRKIIDEiAGVAEFDRKKEKALEELEEVEENIERLD----LIIDEKRQQLERLRREREKAERYQallkekreY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 168 EQYENLKWK--LERKLKELDGELALQRQVhktLEEIYSLLSEVFLnvcyRLVALQARgcaripvmpvmlalterrtpwds 245
Cdd:TIGR02169 224 EGYELLKEKeaLERQKEAIERQLASLEEE---LEKLTEEISELEK----RLEEIEQL----------------------- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 246 slpvdvmkqewvwLDSSTELLQEFESEAQRReheFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESE 325
Cdd:TIGR02169 274 -------------LEELNKKIKDLGEEEQLR---VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 326 HIELERKLQDHARELQDLEAMKDARIKDLEKKLHSVQLAKKKAEETFR-------------RKHEELDRQAREKDTVLAA 392
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDelkdyrekleklkREINELKRELDRLQEELQR 417
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 393 VKGAHAE---QLQTLDAKVLELQFRCETLEGQLRRAEWRQAEDSKERNSLTDKEFGDRST 449
Cdd:TIGR02169 418 LSEELADlnaAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
27-200 |
4.07e-05 |
|
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: 47.07 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 27 SERELSELLAQKEEEWRALQAHRAQLQEAA--LQATQNRLEEAQGKLRRLQEDfvynlqvLEERDRELERYDIEFTQARR 104
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLkqLAALERRIAALARRIRALEQE-------LAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 105 REEAQQAEASELKIEVAKLKQ--------------ELTREARHMEELRHQHKLMLQEHRLELERVhSDKNSELNHQREQY 170
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAEL-AALRAELEAERAEL 176
|
170 180 190
....*....|....*....|....*....|
gi 1958663236 171 ENLKWKLERKLKELDGELALQRQVHKTLEE 200
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEK 206
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
297-661 |
5.35e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 297 KVKLLNKELQALKEAG---AQATESLQKAESEHIELERKLQDHARELQDLEAMKDARIKDLEKKLHSVQLAKKKAE-ETF 372
Cdd:COG4717 72 ELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERlEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 373 RRKHEELDRQAREKDTVLAAVKGAHAE--------------QLQTLDAKVLELQFRCETLEGQLRRAEWRQAEDSKERNS 438
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEEleelleqlslateeELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 439 LTDKEFGDR----------------STCVLSMYWHSVITSVPS---------GLPSRFREDAAALKAAWDAQIAQMSKEA 493
Cdd:COG4717 232 LENELEAAAleerlkearlllliaaALLALLGLGGSLLSLILTiagvlflvlGLLALLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 494 VSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLgldwqrrcdDIECNQIQRSETLIQGLTK 573
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL---------QLEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 574 ARDQVAAKLQETERAlHKQETLLKAVSLERDQAMETLRtHGLLPGQEAQVPPQPHEGEIRTDSPSSEIQRLQEQNAGLRN 653
Cdd:COG4717 383 DEEELRAALEQAEEY-QELKEELEELEEQLEELLGELE-ELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
....*...
gi 1958663236 654 AVSQMRKE 661
Cdd:COG4717 461 ELEQLEED 468
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-194 |
5.60e-05 |
|
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: 47.37 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 39 EEEWRALQAHrAQLQEAALQATQNRLEEAQGKLRRLQedfvYNLQVLEERDRELERYDIEfTQARRREEAQQAEasELKI 118
Cdd:TIGR02169 790 HSRIPEIQAE-LSKLEEEVSRIEARLREIEQKLNRLT----LEKEYLEKEIQELQEQRID-LKEQIKSIEKEIE--NLNG 861
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958663236 119 EVAKLKQELTREARHMEELRHQHKlMLQEHRLELErvhsdknSELNHQREQYENLKWKLERKlKELDGELALQRQV 194
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLG-DLKKERDELE-------AQLRELERKIEELEAQIEKK-RKRLSELKAKLEA 928
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
301-442 |
1.28e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 301 LNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEamkdARIKDLEKKLHSVQLAK-----KKAEETFRRK 375
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE----ARIKKYEEQLGNVRNNKeyealQKEIESLKRR 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958663236 376 HEELDRQAREKDTVLAAVKGAHAEQLQTLDAKVLELQFRCETLEGQLRRAEWRQAEDSKERNSLTDK 442
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
35-207 |
1.37e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 35 LAQKEEEWRALQAHRAQLQE------AALQATQNRLEEAQGKLRRLQEDFVYNLQVLEERDRELERYDIEFTQARRREEA 108
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAeidkllAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 109 QQAEASELKIEVAKLKQELTREARHMEELRHQhklmLQEHRLELERVHSDKNsELNHQREQYENLKWKLERKLKELDGEL 188
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEE----LADLNAAIAGIEAKIN-ELEEEKEDKALEIKKQEWKLEQLAADL 464
|
170
....*....|....*....
gi 1958663236 189 ALQRQVHKTLEEIYSLLSE 207
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEK 483
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
101-207 |
1.55e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 101 QARRREEAQQAEA-SELKIEVAKLKQELTREARHME-ELRHQ-HKLMLQEHRLE--LERVhSDKNSELNHQREQYENLKW 175
Cdd:PRK12704 46 EAKKEAEAIKKEAlLEAKEEIHKLRNEFEKELRERRnELQKLeKRLLQKEENLDrkLELL-EKREEELEKKEKELEQKQQ 124
|
90 100 110
....*....|....*....|....*....|..
gi 1958663236 176 KLERKLKELDgelALQRQVHKTLEEIYSLLSE 207
Cdd:PRK12704 125 ELEKKEEELE---ELIEEQLQELERISGLTAE 153
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-349 |
1.86e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 28 ERELSELLAQKEEEWRALQAHRAQLQEAA----------------LQATQNRLEEAQGKLRRLQEDFVYNLQvleerdRE 91
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIERQLASLEeeleklteeiselekrLEEIEQLLEELNKKIKDLGEEEQLRVK------EK 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 92 LERYDIEFTQARRREEAQQAEASELKIEVAKLKQELTREARHMEELRHQhklmLQEHRLELERVhsdkNSELNHQREQYE 171
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE----IEEERKRRDKL----TEEYAELKEELE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 172 nlkwKLERKLKELDGELALQRQVHKTLEEIYSllsevflnvcyrlvalqargcaripvmpvmlALTERRTPWDSSLpvDV 251
Cdd:TIGR02169 368 ----DLRAELEEVDKEFAETRDELKDYREKLE-------------------------------KLKREINELKREL--DR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 252 MKQEWVWLDSSTELLQEFESEAQRREHEFQLRADDLsntvlthELKVKLLNKELQALKEAGAQATESLQKAESEHIELER 331
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK-------ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
330
....*....|....*...
gi 1958663236 332 KLQDHARELQDLEAMKDA 349
Cdd:TIGR02169 484 ELSKLQRELAEAEAQARA 501
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
32-453 |
2.02e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 32 SELLAQKEEEWRALQAHRAQLQEAALQATQNR-LEEAQGKLRRLQEdfVYNLQVLEERDRELERYDIEFTQARRREEAQ- 109
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKAEEKKkADEAKKKAEEAKK--ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKk 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 110 ------QAEASELKIEVAKLKQELTR----------EARHMEELRHQHKLMLQEHRL---ELERVHSDKNSELNHQREQY 170
Cdd:PTZ00121 1478 kaeeakKADEAKKKAEEAKKKADEAKkaaeakkkadEAKKAEEAKKADEAKKAEEAKkadEAKKAEEKKKADELKKAEEL 1557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 171 ---ENLKWKLERKLKELDGELALQR-QVHKTLEEIYSLLSEVFLNVCYRLVALQARGC--ARIPVMPVMLALTERRtpwd 244
Cdd:PTZ00121 1558 kkaEEKKKAEEAKKAEEDKNMALRKaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAeeAKIKAEELKKAEEEKK---- 1633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 245 sslpvdvmkqewvwldsSTELLQEFESEAQRREHefQLRADDLSNTVLTHELKVKLLN-----KELQALKEAGAQATESL 319
Cdd:PTZ00121 1634 -----------------KVEQLKKKEAEEKKKAE--ELKKAEEENKIKAAEEAKKAEEdkkkaEEAKKAEEDEKKAAEAL 1694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 320 QKAESEHIELERKLQDHARELQDLEAMKdariKDLEKKLHSVQLAKKKAEETfRRKHEELDRQAREKDTV--LAAVKGAH 397
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELK----KAEEENKIKAEEAKKEAEED-KKKAEEAKKDEEEKKKIahLKKEEEKK 1769
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958663236 398 AEQLQTLDAKVLELQFRCEtlEGQLRRAEWRQAEDSKErNSLTDKEFGDRSTCVLS 453
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEE--DEKRRMEVDKKIKDIFD-NFANIIEGGKEGNLVIN 1822
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
29-232 |
2.21e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 29 RELSELLAQKEEEWRALQAHRAQLQEAALQATQNRLEEAQGKLRRLQEDfvynlqvLEERDRELERYDIEFTQARRREEA 108
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAE-------LARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 109 QQAEASELK-IEVAKLKQELTREARHMEELRHQHK-LMLQEHRLELERVHSDKN-----SELNHQREQYENLKWKLERKL 181
Cdd:COG4913 328 LEAQIRGNGgDRLEQLEREIERLERELEERERRRArLEALLAALGLPLPASAEEfaalrAEAAALLEALEEELEALEEAL 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958663236 182 KELDGEL-ALQRQVHKTLEEIYSLLSEVFlNVCYRLVALQARGCARIPVMPV 232
Cdd:COG4913 408 AEAEAALrDLRRELRELEAEIASLERRKS-NIPARLLALRDALAEALGLDEA 458
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
619-715 |
3.22e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 619 QEAQVPPQPHEGEIRtdSPSSEIQRLQEQNAGLRNAVSQMRKEMEMLSGHLPFAQSEERSNANPEPKagedsappdyVLA 698
Cdd:COG2433 402 EHEERELTEEEEEIR--RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDRE----------ISR 469
|
90
....*....|....*..
gi 1958663236 699 LEAEMQNLKHELKALEE 715
Cdd:COG2433 470 LDREIERLERELEEERE 486
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
28-434 |
3.35e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 28 ERELSELLAQKEEEWRALQAHRAqlqEAALQATQNRLEEAQGKLRRLQEDfvynlqvLEERDRELERYDIEFTQARRREE 107
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAA---EEKAEAAEKKKEEAKKKADAAKKK-------AEEKKKADEAKKKAEEDKKKADE 1409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 108 AQQAEASELKIEVAKLKQELTR----------EARHMEELRHQHKLMLQEHRLELERVHSDKNSELNHQREQ---YENLK 174
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKkadeakkkaeEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakkADEAK 1489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 175 WKLERKLKELDgELALQRQVHKTLEEIYSLLSevflnvcyRLVALQARGCARIPVMPVMLALTERRTPWDSSLPVDVMKQ 254
Cdd:PTZ00121 1490 KKAEEAKKKAD-EAKKAAEAKKKADEAKKAEE--------AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 255 EWVWLDSSTELLQEFESEAQRREHEF-QLRADDLSNTVLTHELKVKLLNKELQALKEAGAQAtESLQKAESEHIELERKL 333
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-EELKKAEEEKKKVEQLK 1639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 334 QDHARELQDLEAMKDArikDLEKKLHSVQLAKK------------KAEETFRRKHEELDRQAREKDTVlAAVKGAHAEQL 401
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKA---EEENKIKAAEEAKKaeedkkkaeeakKAEEDEKKAAEALKKEAEEAKKA-EELKKKEAEEK 1715
|
410 420 430
....*....|....*....|....*....|....*
gi 1958663236 402 QTLDAKVLELQFRCETLEGQLRRAEW--RQAEDSK 434
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKKEAEEdkKKAEEAK 1750
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
303-380 |
3.72e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.97 E-value: 3.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958663236 303 KELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAMKdARIKDLEKKLHSVQLAKKKAEETFRRKHEELD 380
Cdd:pfam13851 47 KLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLK-ARLKVLEKELKDLKWEHEVLEQRFEKVERERD 123
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
63-433 |
4.11e-04 |
|
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: 44.58 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 63 RLEEAQGKLRRLQedfvynlqvleERDRELERYDIEFTQARRREEAQQAEASELKIEVAKLKQELTRearhmeELRHQHK 142
Cdd:pfam02463 170 KKKEALKKLIEET-----------ENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEY------LLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 143 LMLQEHRLELERVHSDKNSELNHQREQYENLKWKLERKLKELDGELALQRQVHKTLEEIYSLLSEVFLNvcyrlvalqar 222
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE----------- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 223 gcaripvmpvmlALTERRTPWDSSLPVDVMKQEWVWLDSSTELLQEFESEAQRREHEFQLRADDLSNTVLTHELKVKLLN 302
Cdd:pfam02463 302 ------------LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 303 KELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAMKDaRIKDLEKKLHSVQLAKKKAEETFRRKHEELDRQ 382
Cdd:pfam02463 370 QLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELAR-QLEDLLKEEKKEELEILEEEEESIELKQGKLTE 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958663236 383 AREKDTVLAAVKGAHAEQLQTLDAKVLELQFRCETLEGQLRRAEWRQAEDS 433
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERS 499
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
271-439 |
6.81e-04 |
|
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: 43.21 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 271 SEAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAMKDAR 350
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 351 IKDLEKKLHSVQLAKKKAEETFRRKHEELDRQAReKDTVLAAVKGAHAEQLQTLDAKVLELQFRCETLEGQLRRAEWRQA 430
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVR-RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
....*....
gi 1958663236 431 EDSKERNSL 439
Cdd:COG4942 182 ELEEERAAL 190
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
32-431 |
7.50e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 32 SELLAQKEEEWRALQAHRAQLQEAALQATQnrLEEAQGKLRRLQEDFVYNLQVLEERDRELERYDIEFTQARRREEAQQA 111
Cdd:pfam15921 440 SECQGQMERQMAAIQGKNESLEKVSSLTAQ--LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNA 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 112 EASELKIEVAKLKQELTREARHMEELRHqhkLMLQEHRLELERVHSDKNSELnhQREQYENLKWKLERKLKELDGELALQ 191
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEGDHLRN---VQTECEALKLQMAEKDKVIEI--LRQQIENMTQLVGQHGRTAGAMQVEK 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 192 RQVHKTLEEIYSLLSEVFL---NVCYRLVALQARgCARIPVMPVML--ALTER-RTPWDSSLPVDVMKQEwvwLDSSTEL 265
Cdd:pfam15921 593 AQLEKEINDRRLELQEFKIlkdKKDAKIRELEAR-VSDLELEKVKLvnAGSERlRAVKDIKQERDQLLNE---VKTSRNE 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 266 LQEFESEAQRREHEFQLRADDLSNTvlTHELKVKLlnKELQALKEAGAQATESLQKAESEHIELerklqdhARELQDLEA 345
Cdd:pfam15921 669 LNSLSEDYEVLKRNFRNKSEEMETT--TNKLKMQL--KSAQSELEQTRNTLKSMEGSDGHAMKV-------AMGMQKQIT 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 346 MKDARIKDLEKKLHSVQLAKKKAEETFRRKHEELDRQAREKDTVlAAVKGAHAEQLQTLDAKVLELQFRCETLEGQLRRA 425
Cdd:pfam15921 738 AKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTV-ATEKNKMAGELEVLRSQERRLKEKVANMEVALDKA 816
|
....*.
gi 1958663236 426 EWRQAE 431
Cdd:pfam15921 817 SLQFAE 822
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
28-370 |
7.82e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 28 ERELSELLAQKEEEWRALQAHRAQLQEAALQATQnrLEEAQGKLRRLQEDF-VYNLQVLEERDRELERYDIEFTQARRRE 106
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQ--AKEGLSALNRLLPRLnLLADETLADRVEEIREQLDEAEEAKRFV 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 107 EAQQAEASELKIEVAKLKQeltrEARHMEELRHQHKLMlqEHRLELERVHSDKNSELNHQREQ--YEN----------LK 174
Cdd:PRK04863 914 QQHGNALAQLEPIVSVLQS----DPEQFEQLKQDYQQA--QQTQRDAKQQAFALTEVVQRRAHfsYEDaaemlaknsdLN 987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 175 WKLERKLKELDGELALQRQVHKTLEEIYSLLSEVFLNvcyrlvalqargcaripvmpvmlalterrtpwdsslpvdvmkq 254
Cdd:PRK04863 988 EKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLAS------------------------------------------- 1024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 255 ewvwLDSSTELLQEFESEAQRREHEFQLRADdlSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQ 334
Cdd:PRK04863 1025 ----LKSSYDAKRQMLQELKQELQDLGVPAD--SGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLR 1098
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958663236 335 DHARELQDLE------------AMKDARIKDLEKKLHSVQLAKKKAEE 370
Cdd:PRK04863 1099 KLERDYHEMReqvvnakagwcaVLRLVKDNGVERRLHRRELAYLSADE 1146
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
485-663 |
8.03e-04 |
|
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: 43.21 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 485 QIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGLDWQRRCDDI-------- 556
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellraly 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 557 ---------------ECNQIQRSETLIQGLTKARDQVAAKLQETERALHKQETLLKAVSLERDQAMETLRT-HGLLPGQE 620
Cdd:COG4942 115 rlgrqpplalllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEeRAALEALK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958663236 621 AQVPPQPHEGEIRTDSPSSEIQRLQEQNAGLRNAVSQMRKEME 663
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
259-540 |
1.03e-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: 43.13 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 259 LDSSTELLQEFESEAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHAR 338
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 339 ELQ--------------DLEAMK----------------------DARIKDLEKKLHSVQLAKKKAEETFRRKHEEL--- 379
Cdd:TIGR02169 766 RIEeleedlhkleealnDLEARLshsripeiqaelskleeevsriEARLREIEQKLNRLTLEKEYLEKEIQELQEQRidl 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 380 -DRQAREKDTV--LAAVKGAHAEQLQTLDAKVLELQFRCETLEGQLRRAEWRQAEDSKERNSLTDKEFGDRSTCVLSMYW 456
Cdd:TIGR02169 846 kEQIKSIEKEIenLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 457 HSVITSVPSGLPSRFREDAAALKAAWDAQIAQMSKEAVSKDlqIQALQEEEMKLKAQVAKSQQDIDRYKQQLS-LAVERE 535
Cdd:TIGR02169 926 LEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEE--IRALEPVNMLAIQEYEEVLKRLDELKEKRAkLEEERK 1003
|
....*
gi 1958663236 536 QSLER 540
Cdd:TIGR02169 1004 AILER 1008
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
33-589 |
2.47e-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: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 33 ELLAQKEEEWRALQAHRAQLQEAALQATQNRLEEAQGKLRRLQedfvynlQVLEERDRELERYDIEFTQARRREEAQQAE 112
Cdd:COG4913 252 ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLE-------AELEELRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 113 ASELK--------IEVAKLKQELTREARHMEELRHQHK-LMLQEHRLELERVHSDKN-----SELNHQREQYENLKWKLE 178
Cdd:COG4913 325 LDELEaqirgnggDRLEQLEREIERLERELEERERRRArLEALLAALGLPLPASAEEfaalrAEAAALLEALEEELEALE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 179 RKLKELDGEL-ALQRQVHKTLEEIYSLLSEVFlNVCYRLVALQARGCARIPVMPvmlalterrtpwdSSLP-----VDVM 252
Cdd:COG4913 405 EALAEAEAALrDLRRELRELEAEIASLERRKS-NIPARLLALRDALAEALGLDE-------------AELPfvgelIEVR 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 253 KQEWVWLDS--------STELLQEFESEAQRREHefqLRADDLSNTVLTHELKVKLLNKELQALKEAGAqaTESLQKAES 324
Cdd:COG4913 471 PEEERWRGAiervlggfALTLLVPPEHYAAALRW---VNRLHLRGRLVYERVRTGLPDPERPRLDPDSL--AGKLDFKPH 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 325 EHIE-LERKLQ--------DHARELQD------LEAM----KDARIKDLEKKLHSVQLAKKKAeetfRRKHEELDRQARE 385
Cdd:COG4913 546 PFRAwLEAELGrrfdyvcvDSPEELRRhpraitRAGQvkgnGTRHEKDDRRRIRSRYVLGFDN----RAKLAALEAELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 386 kdtvLAAVKGAHAEQLQTLDAKVLELQFRCETLEgQLRRAEWRQAEDSKERNSLTDKEfGDRSTCVLSMYWHSVITSvps 465
Cdd:COG4913 622 ----LEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVASAEREIAELE-AELERLDASSDDLAALEE--- 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 466 glpsrfredaaalkaawdaQIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREqvQL 545
Cdd:COG4913 693 -------------------QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LL 751
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1958663236 546 GLDWQRRCDDiecnqiQRSETLIQGLTKARDQVAAKLQETERAL 589
Cdd:COG4913 752 EERFAAALGD------AVERELRENLEERIDALRARLNRAEEEL 789
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
86-201 |
2.69e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 86 EERDRELERYDIEFTQARRREEAQQAEASELKIEVAKLKQELTREARHMEELRHQHKLMLQEHRLE---------LERVH 156
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREirkdreisrLDREI 474
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958663236 157 SDKNSELNHQREQYENLKWKLER--KLKELD--GELALQRQVHK-TLEEI 201
Cdd:COG2433 475 ERLERELEEERERIEELKRKLERlkELWKLEhsGELVPVKVVEKfTKEAI 524
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
28-544 |
2.71e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 28 ERELSELLAQKEEEWRALQAHRAQLQEAALQAtQNRLEEAQG--KLRRLQEDFVYNLQVLEERDRELERYDiEFTQARRR 105
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADEAKKAEEKKKADEA-KKKAEEAKKadEAKKKAEEAKKKADAAKKKAEEAKKAA-EAAKAEAE 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 106 EEAQQAEASELKIEVAKLKQELTREA-----RHMEELRHQHKLmlqEHRLELERVHSDKNSELNHQREQYENLKWKLERK 180
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKadaakKKAEEKKKADEA---KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 181 LKEldGELALQRQVHKTLEEIYSLLSEVFLNVCYRLVALQARGCaripvmpvmlalTERRTPWDSSLPVDVMKQEWVWLD 260
Cdd:PTZ00121 1431 KKA--DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA------------DEAKKKAEEAKKADEAKKKAEEAK 1496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 261 SSTELLQEFESEAQR----REHEFQLRADDLSNT---VLTHELKVKLLNKELQALKEAG-AQATESLQKAESEHIELERK 332
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKadeaKKAEEAKKADEAKKAeeaKKADEAKKAEEKKKADELKKAEeLKKAEEKKKAEEAKKAEEDK 1576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 333 lQDHARELQDLEAMKDARIKDLEKKLHSVQLAK----KKAEETfRRKHEELdRQAREKDTVLAAVKGAHAEQLQTLDakv 408
Cdd:PTZ00121 1577 -NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaeeaKKAEEA-KIKAEEL-KKAEEEKKKVEQLKKKEAEEKKKAE--- 1650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 409 lelQFRCETLEGQLRRAEW-RQAEDSKERNSLTDKEFGDRstcvlsmywhsvitsvpsglpsRFREDAAALKAAWDAQIA 487
Cdd:PTZ00121 1651 ---ELKKAEEENKIKAAEEaKKAEEDKKKAEEAKKAEEDE----------------------KKAAEALKKEAEEAKKAE 1705
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 488 QMSK---EAVSKDLQIQAlQEEEMKLKAQVAKSQQDIDRYKQQlSLAVEREqslEREQVQ 544
Cdd:PTZ00121 1706 ELKKkeaEEKKKAEELKK-AEEENKIKAEEAKKEAEEDKKKAE-EAKKDEE---EKKKIA 1760
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
8-201 |
3.59e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 8 FQPCRPILQSSTVTMLPPCSERELSELLAQKEEEWRALQAHRAQLQEAALQATQNRLEEAQGKLRRLQEDFVYNLQVLEE 87
Cdd:COG1196 576 FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEG 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 88 RDRELERY-------DIEFTQARRREEAQQAEASELKIEVAKLKQELTREARHMEELRHQHKLMLQEHRLELERVHSDKN 160
Cdd:COG1196 656 GSAGGSLTggsrrelLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958663236 161 SELNHQREQYENLKWKLERKLKELDGELALQRQVHKTLEEI 201
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
27-184 |
4.27e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 39.50 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 27 SERELSELLAQKEEEWRALQAHRAQLQEaALQATQNRLEEAQGKLRRLQEDfvynLQVLEE--RDRELerydieftqarr 104
Cdd:pfam15619 54 TESELPQLIARHNEEVRVLRERLRRLQE-KERDLERKLKEKEAELLRLRDQ----LKRLEKlsEDKNL------------ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 105 reeaqqAEASELKIEVAKLKQELTREARHMEELRHQHKLMLQEHRLEL---ERVHSDKNSELNHQREQYENLKWKLERKL 181
Cdd:pfam15619 117 ------AEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLaaeKKKHKEAQEEVKILQEEIERLQQKLKEKE 190
|
...
gi 1958663236 182 KEL 184
Cdd:pfam15619 191 REL 193
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
29-429 |
4.83e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 29 RELSELLAQKEEEWRALQAhRAQLQEAALQATQNRLEEAQGKLRRLQEDFVYNLQVLEERDRELERYDIEFTQARRREEA 108
Cdd:PRK02224 282 RDLRERLEELEEERDDLLA-EAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 109 QQAEASELKIEVAKLKQELTREARHMEELRHQhklmLQEHRLELERVHSDKNsELNHQREQYENLKWKLERKLKELDGEL 188
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEELEEE----IEELRERFGDAPVDLG-NAEDFLEELREERDELREREAELEATL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 189 alqRQVHKTLEEIYSLLSEVFLNVCYRLVALQARGCARIPVMPVMLALTERRTpwDSSLPVDVMKQEWVWLDSSTELLQE 268
Cdd:PRK02224 436 ---RTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELE--DLEEEVEEVEERLERAEDLVEAEDR 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 269 FESEAQRREHEFQLRADDlSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIE-------LERKLQDHARELQ 341
Cdd:PRK02224 511 IERLEERREDLEELIAER-RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEareevaeLNSKLAELKERIE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 342 DLEAMKDA-------------------------------------RIKDLEKKLHSVQLA-----KKKAEETFRRKHEEL 379
Cdd:PRK02224 590 SLERIRTLlaaiadaedeierlrekrealaelnderrerlaekreRKRELEAEFDEARIEearedKERAEEYLEQVEEKL 669
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958663236 380 DRQAREKDTVLAAVKGAHAE--QLQTLDAKVLELQFRCETLE-------------GQLrRAEWRQ 429
Cdd:PRK02224 670 DELREERDDLQAEIGAVENEleELEELRERREALENRVEALEalydeaeelesmyGDL-RAELRQ 733
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
27-193 |
5.14e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 27 SERELSELLAQKEEEWRALQAHRAQLQE--AALQATQNRLEEAQGKLRRLQEDFVYNLQVLEERDRELERYDIEFTQARR 104
Cdd:pfam05557 25 HKRARIELEKKASALKRQLDRESDRNQElqKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADARE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 105 REEAQQAEASELKIEVAKLKQELTREARHMEELRHQHKLMLQehrlelervhsdKNSELNHQREQYENLKWKL---ERKL 181
Cdd:pfam05557 105 VISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKA------------KASEAEQLRQNLEKQQSSLaeaEQRI 172
|
170
....*....|..
gi 1958663236 182 KELDGELALQRQ 193
Cdd:pfam05557 173 KELEFEIQSQEQ 184
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
485-611 |
6.33e-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: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 485 QIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAV-ERE-QSLEREQVQLGLdwqrrcddiecnQIQ 562
Cdd:COG1579 39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnNKEyEALQKEIESLKR------------RIS 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958663236 563 RSETLIQGLTKARDQVAAKLQETERALHKQETLLKAVSLERDQAMETLR 611
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
266-378 |
6.59e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 38.76 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 266 LQEFESEAQRREHEFQLRaddlsntvlthelkVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDlea 345
Cdd:pfam08614 62 LREELAELYRSRGELAQR--------------LVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELRE--- 124
|
90 100 110
....*....|....*....|....*....|...
gi 1958663236 346 mKDARIKDLEKKLHSVQLAKKKAEETFRRKHEE 378
Cdd:pfam08614 125 -KRKLNQDLQDELVALQLQLNMAEEKLRKLEKE 156
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
50-200 |
8.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 50 AQLQEAALQATQNRLEEAQGKLRRLQEDfvynlqvLEERDRELERYDIEFTQARRREEAQQAEASELKIEVAKLKQELTR 129
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAE-------LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 130 EARHM-----------------------------EELRHQHKLMLQEHRLELERVHSDKnSELNHQREQYENLKWKLERK 180
Cdd:COG3883 91 RARALyrsggsvsyldvllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAKK-AELEAKLAELEALKAELEAA 169
|
170 180
....*....|....*....|
gi 1958663236 181 LKELDGELALQRQVHKTLEE 200
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSA 189
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
29-154 |
9.05e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 39.65 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 29 RELSELLAQKEEEWRALQAHRAQLQeaALQATQNRLEEAQGKLRRLQEDfvynlqvLEERDRELERYD----------IE 98
Cdd:COG1566 79 TDLQAALAQAEAQLAAAEAQLARLE--AELGAEAEIAAAEAQLAAAQAQ-------LDLAQRELERYQalykkgavsqQE 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958663236 99 FTQARRREEAQQAEASELKIEVAKLKQELTREARhMEELRHQH---KLMLQEHRLELER 154
Cdd:COG1566 150 LDEARAALDAAQAQLEAAQAQLAQAQAGLREEEE-LAAAQAQVaqaEAALAQAELNLAR 207
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
30-380 |
9.47e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 30 ELSELLAQKEEEWRALQAhRAQLQEAALQATQNRLEEAQGKLRRLQEDFvynlqvleerdrELERYDIEFTQARRREEAQ 109
Cdd:pfam01576 233 ELRAQLAKKEEELQAALA-RLEEETAQKNNALKKIRELEAQISELQEDL------------ESERAARNKAEKQRRDLGE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 110 QAEASELKIE------------VAKLKQELTREARHMEELRHQHKLMLQEHRLElervHSDKNSELNHQREQYENLKWKL 177
Cdd:pfam01576 300 ELEALKTELEdtldttaaqqelRSKREQEVTELKKALEEETRSHEAQLQEMRQK----HTQALEELTEQLEQAKRNKANL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 178 ERKLKELDGElalqrqvHKTLEEIYSLLSEVFLNVCYRLVALQARgcaripVMPVMLALTE-RRTPWDSSLPVDVMKQEw 256
Cdd:pfam01576 376 EKAKQALESE-------NAELQAELRTLQQAKQDSEHKRKKLEGQ------LQELQARLSEsERQRAELAEKLSKLQSE- 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 257 vwLDSSTELLQEFESEAQRREHEFQLRADDLSNT--VLTHELKVKL-LNKELQALKEAGAQATESLQKAESEHIELERKL 333
Cdd:pfam01576 442 --LESVSSLLNEAEGKNIKLSKDVSSLESQLQDTqeLLQEETRQKLnLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQL 519
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958663236 334 QDHARELQD-----------LEAMKDAR------IKDLEKKLHSVQLAKKKAEETFRRKHEELD 380
Cdd:pfam01576 520 STLQAQLSDmkkkleedagtLEALEEGKkrlqreLEALTQQLEEKAAAYDKLEKTKNRLQQELD 583
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
34-154 |
9.66e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 39.69 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 34 LLAQKEEEWRALQAHRAQLQEAALQATQNRLEEAQGKLRRLQEDFVYNLQVLEER--------DRELERYDIEFTQARRR 105
Cdd:PRK12705 31 LAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERlvqkeeqlDARAEKLDNLENQLEER 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958663236 106 EEAQQAEASELKIEVAKLKQELTR-------EARHM----------EELRHQHKLMLQEHRLELER 154
Cdd:PRK12705 111 EKALSARELELEELEKQLDNELYRvagltpeQARKLllklldaeleEEKAQRVKKIEEEADLEAER 176
|
|
| BBP1_C |
pfam15272 |
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ... |
259-388 |
9.92e-03 |
|
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole body component, carries coiled-coils that are necessary for the localization of BBP1 to the spindle pole body (SPB). Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge
Pssm-ID: 405864 [Multi-domain] Cd Length: 183 Bit Score: 38.53 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663236 259 LDSSTELLQEFESEAQRREHEFQLRADDLSNTVLthELKVKLLNKELQALKEAGA-----QATESLQKAESEHIELERKL 333
Cdd:pfam15272 13 LDKNNRALHLLNKDVRERDEHYQLQETSYKKKYL--QTRNELINELKQSKKLYDNyyklySKYQQLKKISNESLDLQSTI 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958663236 334 QDHARELQDLEAMKDARIKDLEKKLHSVQLAKKKAEETFRR-------KHEELDRQAREKDT 388
Cdd:pfam15272 91 TNLESQLVDQAIDKDREIHNLNEKILSLELRNQELETKREIdkmkyesRIDELERQLKEQEY 152
|
|
| |
