|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-370 |
2.00e-14 |
|
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: 78.17 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 53 QEAALQATQNRLEEAQGKLRRLQEDFVYNLQVLEERDRELERYDIEFTQARRREEAQQAEASELKIEVAKLKQELTREAR 132
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 133 HMEELRHQHKLMLQEHRLELERVHsdknsELNHQREQYENLKWKLERKLKELDGELALQRQVHKTLEEIYSLLSEVFLNV 212
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLE-----EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 213 CYRLVALQARgCARIPVMPVMLALTERRTPWDSSLPVDVMKQEWVWLDSSTELLQEFE---SEAQRREHEFQLRADDLSN 289
Cdd:TIGR02168 823 RERLESLERR-IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLnerASLEEALALLRSELEELSE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 290 TVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHAR-ELQDLEAMKDARIKDLEKKLHSVQLAKKKA 368
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
..
gi 1958663244 369 EE 370
Cdd:TIGR02168 982 KE 983
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
29-619 |
1.08e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.74 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 29 RELSELLAQKEEEWRALQAHRAQLQEAALQAtqnRLEEAQGKLRRLQEDfvynlqvLEERDRELERYDIEFTQARRREEA 108
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEA---ELEELEAELEELEAE-------LAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 109 QQAEASELKIEVAKLKQELTREARHMEELRhQHKLMLQEHRLELERVHSDKNSELNHQREQYENLKWKLERKLKELDGEL 188
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELE-ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 189 ALQRQVHKTLEEIYSLLSEvflnvcyRLVALQARGCARIPVMPVMLALTERRTpwDSSLPVDVMKQEWVWLDSSTELLQE 268
Cdd:COG1196 365 EALLEAEAELAEAEEELEE-------LAEELLEALRAAAELAAQLEELEEAEE--ALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 269 FESEAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAMKD 348
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 349 ARIKDLEKKLHSVQLAKKKAEETFRRKFREDAAALKAAWDAQIAQMSKEAVSKDLQ--IQALQEEEMKLKAQVAKSQQDI 426
Cdd:COG1196 516 LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgrATFLPLDKIRARAALAAALARG 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 427 DRYKQQLSLAVEREQSLEREQVQ----LGLDWQRRCDDIECNQIQRSETLIQGLTKARDQVAAKLQETERALHKQETLLK 502
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLgdtlLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 503 AVSLERDQAMETLRTHGLlpgqeaqvppQPHEGEIRTDSPSSEIQRLQEQNAGLRNAVSQMRKEMEMLSGHLPFAQSEEr 582
Cdd:COG1196 676 EAEAELEELAERLAEEEL----------ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE- 744
|
570 580 590
....*....|....*....|....*....|....*...
gi 1958663244 583 snANPEPKAGEDSAPPDYVLA-LEAEMQNLKHELKALE 619
Cdd:COG1196 745 --EELLEEEALEELPEPPDLEeLERELERLEREIEALG 780
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
35-456 |
9.55e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.11 E-value: 9.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 35 LAQKEEEWRALQAHRAQLqEAALQATQNRLEEAQGKLRRL--QEDFVYNLQVLEERDRELERYDIEFTQARRREEAQQae 112
Cdd:COG4717 83 AEEKEEEYAELQEELEEL-EEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEELR-- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 113 asELKIEVAKLKQELTREARHMEELRHQHKLM----LQEHRLELERVHSDKNsELNHQREQYENLKWKLERKLKELDGEL 188
Cdd:COG4717 160 --ELEEELEELEAELAELQEELEELLEQLSLAteeeLQDLAEELEELQQRLA-ELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 189 ALQRQVHKTLEEIYSLLSEVFLNVcyrLVALQARGCARIPVMPVMLALTerrtpwdsslpVDVMKQEWVWLDSSTELLQE 268
Cdd:COG4717 237 EAAALEERLKEARLLLLIAAALLA---LLGLGGSLLSLILTIAGVLFLV-----------LGLLALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 269 FESEAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEhiELERKLQDHARELQDLEAMKD 348
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL--EEELQLEELEQEIAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 349 AR-IKDLEKKLHSVQLAKKKAEEtfRRKFREDAAALKAAWDAQIAQMSKEAVSKDLQ-----IQALQEEEMKLKAQVAKS 422
Cdd:COG4717 381 VEdEEELRAALEQAEEYQELKEE--LEELEEQLEELLGELEELLEALDEEELEEELEeleeeLEELEEELEELREELAEL 458
|
410 420 430
....*....|....*....|....*....|....*.
gi 1958663244 423 QQDIDRYK--QQLSLAVEREQSLEREQVQLGLDWQR 456
Cdd:COG4717 459 EAELEQLEedGELAELLQELEELKAELRELAEEWAA 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
255-787 |
6.55e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 255 EWVWLDSSTELLQEFESEAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQ 334
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 335 DHARELQDLE---AMKDARIKDLEKKLHSVQLAKKKAEETfrrkfREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEE 411
Cdd:COG1196 313 ELEERLEELEeelAELEEELEELEEELEELEEELEEAEEE-----LEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 412 EMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGLDWQRRCDDIE----------------CNQIQRSETLIQG 475
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEeeeealeeaaeeeaelEEEEEALLELLAE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 476 LTKARDQVAAKLQETERALHKQETLLKAVSLERDQAMETLRTHGLLPGQEAQVPPQPHEGEIRTDSPSSEIQRLQEQNAG 555
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 556 LRNAV----SQMRKEMEMLSGHLP----FAQSEERSNANPEPKAGEDSAPPDYVLALEAEMQNLKHELKALEEQLQGTge 627
Cdd:COG1196 548 LQNIVveddEVAAAAIEYLKAAKAgratFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR-- 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 628 pvktSMATADPHHGAHNSAEAADAApadqtlitLALRKLGDRVHLLNLLVTQLKKKLRQKPLELVAVQQEIPSEVDQVHL 707
Cdd:COG1196 626 ----TLVAARLEAALRRAVTLAGRL--------REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 708 EVLELQKQVAELRKHLKMTQPQGEPSYIKQLQREGLAD---WHPMGMEDQTESPTFLQEGAQPPQTTSVSHLQRKLKDAA 784
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEaerEELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
...
gi 1958663244 785 RKI 787
Cdd:COG1196 774 REI 776
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
28-445 |
1.29e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 28 ERELSELLAQKEEEWRALQAHRAQLQ--EAALQATQNRLEEAQGKLRRLQED---------FVYNLQVLEER--DRELER 94
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEekEERLEELKKKLKELEKRLEELEERhelyeeakaKKEELERLKKRltGLTPEK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 95 YDIEFTQARRREEAQQAEASELKIEVAKLKQELTREARHMEELRHQH-------KLMLQEHRLELERVHSDKNSELNHQR 167
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEHRKELLEEYTAELKRIEKEL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 168 EQYENLKWKLERKLKELDGELALQRQV---HKTLEEIYSLLSEvfLNVcYRLVALQArgcaripvmpvmlALTERRTPWD 244
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELiklKELAEQLKELEEK--LKK-YNLEELEK-------------KAEEYEKLKE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 245 SSLPVdvmKQEWVWLDSSTELLQEFESEAQRREHEFQLRADDLSNtvLTHELK------VKLLNKELQALKEAGAQATEs 318
Cdd:PRK03918 533 KLIKL---KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAE--LLKELEelgfesVEELEERLKELEPFYNEYLE- 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 319 LQKAESEHIELERKLQDHARELQDLEAM---KDARIKDLEKKLHsvQLAKKKAEETFRRKFREdaaalkaawdaqIAQMS 395
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEElaeTEKRLEELRKELE--ELEKKYSEEEYEELREE------------YLELS 672
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1958663244 396 KEAVSKDLQIQALQeeemKLKAQVAKSQQDIDRYKQQLSLAVEREQSLER 445
Cdd:PRK03918 673 RELAGLRAELEELE----KRREEIKKTLEKLKEELEEREKAKKELEKLEK 718
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
28-623 |
3.94e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 28 ERELSELLAQKE--EEWRALQAhraQLQEAALQATQNRLEEAQGKLRRLQEDFVYNLQVLEERDRELERYDIEFTQARRR 105
Cdd:COG1196 199 ERQLEPLERQAEkaERYRELKE---ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 106 EEAQQAEASELKIEVAKLKQELTREARhmeELRHQhKLMLQEHRLELERVHSDKNSELNHQREQYENLKwKLERKLKELD 185
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQ---DIARL-EERRRELEERLEELEEELAELEEELEELEEELE-ELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 186 GELALQRQVHKTLEEIYSLLSEVFLNVCYRLVALQARgcaripvmpvmlALTERRTpwdsslpvdvmkqewvwldssTEL 265
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE------------LLEALRA---------------------AAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 266 LQEFESEAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEA 345
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 346 mKDARIKDLEKKLHSVQLAKKKAEETFRRKFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEEM--KLKAQVAKSQ 423
Cdd:COG1196 478 -ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaaALQNIVVEDD 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 424 QD----IDRYKQQ-------LSLAVEREQSLEREQVQLGLDWQRRcDDIECNQIQRSE--TLIQGLTKARDQVAAKLQET 490
Cdd:COG1196 557 EVaaaaIEYLKAAkagratfLPLDKIRARAALAAALARGAIGAAV-DLVASDLREADAryYVLGDTLLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 491 ERALHKQETLLKAVSLERDQAMETLRTHGLLPGQEAQvppqphEGEIRTDSPSSEIQRLQEQNAGLRNAVSQMRKEMEML 570
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA------ALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958663244 571 SGHLPFAQSEERSNAN---------------PEPKAGEDSAPPDYVLALEAEMQNLKHELKALEEQLQ 623
Cdd:COG1196 710 AEAEEERLEEELEEEAleeqleaereelleeLLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
28-451 |
4.75e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 28 ERELSELLAQKEEEWRALQAHRAQLQEAALQAtQNRLEEAQGKLRRLQEDfvynLQVLEERDRELERYDIEFTQARRREE 107
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLER----LERLEEELEELEEALAELEEEEEEEE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 108 AQQAEASELKIEVAKLKQELTREARHMEELRHQHKLMLQEHRLELERVHSDKNSELNHQREQYENLKWKLERKLKE---- 183
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrg 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 184 LDGELALQRQVHKTLEEIYSLLSEVFLNVCYRLVALQARGCARipvmpvmlALTERRTPWDSSLPVDVMKQewvwLDSST 263
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIE--------YLKAAKAGRATFLPLDKIRA----RAALA 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 264 ELLQEFESEAQRREHEFQLRADDLSNTVLTHELKVKLL--------NKELQALKEAGAQATESLQKAESEHIELERKLQD 335
Cdd:COG1196 590 AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLvaarleaaLRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 336 HARELQDLEAMKDARIKDLEKKLHSVQLAKKKAEETFRRKFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEEMKL 415
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
410 420 430
....*....|....*....|....*....|....*.
gi 1958663244 416 KAQVAKSQQDIDRYKQQlslavEREQSLEREQVQLG 451
Cdd:COG1196 750 EEALEELPEPPDLEELE-----RELERLEREIEALG 780
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
32-447 |
4.98e-11 |
|
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: 67.00 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 32 SELLAQKEEEWRALqahraqLQEAA--------LQATQNRLEEAQGKLRRLQEdfvynlqVLEERDRELERYDIeftQAR 103
Cdd:TIGR02168 147 SEIIEAKPEERRAI------FEEAAgiskykerRKETERKLERTRENLDRLED-------ILNELERQLKSLER---QAE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 104 RREEAQQAEASELKIEVAKLKQELTREARHMEELRHQHKlmlqehrlelervhsdknsELNHQREQYENLKWKLERKLKE 183
Cdd:TIGR02168 211 KAERYKELKAELRELELALLVLRLEELREELEELQEELK-------------------EAEEELEELTAELQELEEKLEE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 184 LDGElalQRQVHKTLEEIYSLLsevflnvcYRLVALQARgcaripvmpvmlalterrtpwdsslpVDVMKQEwvwLDSST 263
Cdd:TIGR02168 272 LRLE---VSELEEEIEELQKEL--------YALANEISR--------------------------LEQQKQI---LRERL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 264 ELLQEFESEAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDL 343
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 344 E---AMKDARIKDLEKKLHSVQLAKKKAEETFRRKFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEEMKLKAQVA 420
Cdd:TIGR02168 392 ElqiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
410 420
....*....|....*....|....*..
gi 1958663244 421 KSQQDIDRYKQQLSLAVEREQSLEREQ 447
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQ 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
36-722 |
3.78e-10 |
|
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: 64.31 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 36 AQKEEEWRALqahRAQLQEAALQATQNRLEEAQGKLRRLQEDFVYNLQVLEERDRELERYDIEFTQAR-------RREEA 108
Cdd:TIGR02168 209 AEKAERYKEL---KAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRlevseleEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 109 QQAEASELKIEVAKLKQELTREARHMEELrHQHKLMLQEHRLELERVHSDKNSELNHQREQYENLKWKLERKLKELDGEL 188
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANL-ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 189 ALQRQvhktLEEIYSLLSEVFLNVCYRLVALQARGC---ARIPVMPVMLALTERRtpwdsslpVDVMKQEWVWLDSSTEL 265
Cdd:TIGR02168 365 AELEE----LESRLEELEEQLETLRSKVAQLELQIAslnNEIERLEARLERLEDR--------RERLQQEIEELLKKLEE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 266 LQEFESEAQRREHEFQLraDDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEA 345
Cdd:TIGR02168 433 AELKELQAELEELEEEL--EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 346 MKDAR-----IKDLEKKLHSVQLAKKKAEETFRRKFREDAAALKAAWDAQIAQMSKEA-----------VSKDLQIQALQ 409
Cdd:TIGR02168 511 LLKNQsglsgILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNelgrvtflpldSIKGTEIQGND 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 410 EEEMKLKAQVAKSQQDIDRYKQQLSLAVE----------------REQSLEREQ---VQLGLDWQRRCDDIEcNQIQRSE 470
Cdd:TIGR02168 591 REILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvddldnalELAKKLRPGyriVTLDGDLVRPGGVIT-GGSAKTN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 471 TLIQGLTKARDQVAAKLQETERALHKQETLLKAVSLERDQAMETLRthgLLPGQEAQVPPQPHEGEIRTDSPSSEIQRLQ 550
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE---QLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 551 EQNAGLRNAVSQMRKEMEmlsghlpfAQSEERSNANPEPKAGEDSappdyVLALEAEMQNLKHELKALEEQLQGTGEPVK 630
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIE--------ELEERLEEAEEELAEAEAE-----IEELEAQIEQLKEELKALREALDELRAELT 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 631 -TSMATADPHHGAHNSAEAADAAPADQTLITLALRKLGDRVHLLNLLVTQLKKKLRQKPLELVAVQQEIPSEVDQVHLEV 709
Cdd:TIGR02168 814 lLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
730
....*....|...
gi 1958663244 710 LELQKQVAELRKH 722
Cdd:TIGR02168 894 SELEELSEELREL 906
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
28-494 |
4.90e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 4.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 28 ERELSELLAQKEE---EWRALQAHRAQLQEAALQATQNRLEEAQGKLRRLQEDfvynlqvLEERDRELERYDIEFTQARR 104
Cdd:COG4913 301 RAELARLEAELERleaRLDALREELDELEAQIRGNGGDRLEQLEREIERLERE-------LEERERRRARLEALLAALGL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 105 REEAQQAEASELKIEVAKLKQELTREARHMEELRHQHKLMLQEHRLELERVHSDKNSeLNHQR----EQYENLKWKLERK 180
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS-LERRKsnipARLLALRDALAEA 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 181 LKELDGEL------------------ALQRQVHK---TL---EEIYSLLSEVflnvcyrLVALQARGCARIPVMPVMLAL 236
Cdd:COG4913 453 LGLDEAELpfvgelievrpeeerwrgAIERVLGGfalTLlvpPEHYAAALRW-------VNRLHLRGRLVYERVRTGLPD 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 237 TERRTPWDSSLP--VDVMKQEW-VWLDSstELLQEF-----ESEAQRREHEFQL-----------------RADDLSNTV 291
Cdd:COG4913 526 PERPRLDPDSLAgkLDFKPHPFrAWLEA--ELGRRFdyvcvDSPEELRRHPRAItragqvkgngtrhekddRRRIRSRYV 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 292 L--THELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAMKD-----ARIKDLEKKLHSVQLA 364
Cdd:COG4913 604 LgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaeREIAELEAELERLDAS 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 365 KKKAEEtfrrkfredaaalkaaWDAQIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLE 444
Cdd:COG4913 684 SDDLAA----------------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1958663244 445 REqvQLGLDWQRRCDDiecnqiQRSETLIQGLTKARDQVAAKLQETERAL 494
Cdd:COG4913 748 RA--LLEERFAAALGD------AVERELRENLEERIDALRARLNRAEEEL 789
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-211 |
5.61e-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: 60.46 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 30 ELSELLAQKEEEWRALQAHRAQLQEaALQATQNRLEEAQGKLRRLQEDFVYNLQVLEERDRELERYDIEFTQARRREEAQ 109
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 110 QAEASELKIEVAKLKQ---ELTREARHMEELRHQHKLMLQEHRLELE------RVHSDKNSELNHQREQYENLKWKLERK 180
Cdd:TIGR02168 851 SEDIESLAAEIEELEElieELESELEALLNERASLEEALALLRSELEelseelRELESKRSELRRELEELREKLAQLELR 930
|
170 180 190
....*....|....*....|....*....|.
gi 1958663244 181 LKELDGELAlqrQVHKTLEEIYSLLSEVFLN 211
Cdd:TIGR02168 931 LEGLEVRID---NLQERLSEEYSLTLEEAEA 958
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
29-627 |
1.02e-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: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 29 RELSELLAQKEEEWRALQAHRAQL--QEAALQATQNRLEE----AQGKLRRLQEDFVYNLQVLEERD-----RELERYDI 97
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLelQIASLNNEIERLEArlerLEDRRERLQQEIEELLKKLEEAElkelqAELEELEE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 98 EFTQARRREEAQQAEASELKIEVAKLKQELTREARHMEELRhQHKLMLQEHRLELERVHSDKNSELNHQRE--QYENLKW 175
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ-ARLDSLERLQENLEGFSEGVKALLKNQSGlsGILGVLS 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 176 KL------ERKLKELDGELALQRQVHKTLE---EIYSLLSEVFLNVCYRLV-------ALQARGCARIPVMPVMLALTER 239
Cdd:TIGR02168 527 ELisvdegYEAAIEAALGGRLQAVVVENLNaakKAIAFLKQNELGRVTFLPldsikgtEIQGNDREILKNIEGFLGVAKD 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 240 RTPWDSSLPVDVmkQEWVWLDSSTELLQEfeSEAQRREHEFQLR------------------ADDLSNTVLTHELKVKLL 301
Cdd:TIGR02168 607 LVKFDPKLRKAL--SYLLGGVLVVDDLDN--ALELAKKLRPGYRivtldgdlvrpggvitggSAKTNSSILERRREIEEL 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 302 NKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAMKDARIKDLEKKLHSVQ------------LAKKKAE 369
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleeriaqlskeLTELEAE 762
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 370 ETFRRKFREDAAALKAAWD-------AQIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQS 442
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEaeieeleAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 443 LEREQVQLGLdwqrrcddiecnQIQRSETLIQGLTKARDQVAAKLQETERALHKQETLLKAVSLERDQAMETLRTHgllp 522
Cdd:TIGR02168 843 LEEQIEELSE------------DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL---- 906
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 523 gqeaqvppqphegeirtdspSSEIQRLQEQNAGLRNAVSQMRKEMEMLSGHLpfAQSEERSNANPEPKAGEDSAPPDyvl 602
Cdd:TIGR02168 907 --------------------ESKRSELRRELEELREKLAQLELRLEGLEVRI--DNLQERLSEEYSLTLEEAEALEN--- 961
|
650 660
....*....|....*....|....*
gi 1958663244 603 ALEAEMQNLKHELKALEEQLQGTGE 627
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENKIKELGP 986
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
259-536 |
3.11e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 259 LDSSTELLQEFESEAQRREHEFQLRADDLSNtvlthelKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHAR 338
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASR-------KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 339 ELQDLEAmkdaRIKDLEKKLHSVQLAKKKAEETFRRKFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEEMKLKAQ 418
Cdd:TIGR02169 759 ELKELEA----RIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 419 VAKSQQDIDRYKQQLSlavEREQSLEREQVQLGlDWQRRCDDIECNQIQRSETLIqGLTKARDQVAAKLQETERALHKQE 498
Cdd:TIGR02169 835 IQELQEQRIDLKEQIK---SIEKEIENLNGKKE-ELEEELEELEAALRDLESRLG-DLKKERDELEAQLRELERKIEELE 909
|
250 260 270
....*....|....*....|....*....|....*...
gi 1958663244 499 TllkAVSLERDQAMETLRTHGLLPGQEAQVPPQPHEGE 536
Cdd:TIGR02169 910 A---QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
337-624 |
3.59e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 337 ARELQDLEAMKDARIKDLEKKLHSVQLAKKKAEETFRRKFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEEMKLK 416
Cdd:COG1196 215 YRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 417 AQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLgldwQRRCDDIEcNQIQRSETLIQGLTKARDQVAAKLQETERALHK 496
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAEL----EEELEELE-EELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 497 QETLLKAVSLERDQAMETLRTHgllpgqeaqvppqphegEIRTDSPSSEIQRLQEQNAGLRNAVSQMRKEMEMLsghlpf 576
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEA-----------------LRAAAELAAQLEELEEAEEALLERLERLEEELEEL------ 426
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958663244 577 AQSEERSNANPEPKAGEDSAPPDYVLALEAEMQNLKHELKALEEQLQG 624
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
273-622 |
6.24e-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: 56.99 E-value: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 273 AQRREHEFQLRA--DDLSN-TVLTHELKVKLLNKELQAlkeagaqateslQKAEsEHIELERKLQDHARELQDLeamkda 349
Cdd:TIGR02168 172 ERRKETERKLERtrENLDRlEDILNELERQLKSLERQA------------EKAE-RYKELKAELRELELALLVL------ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 350 RIKDLEKKLHSVQLAKKKAEETfrrkfREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRY 429
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEE-----LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 430 KQQLSLAverEQSLEREQVQLGLDWQRRCDDIEcnQIQRSETLIQGLTKARDQVAAKLQETERALHKQETLLKavslERD 509
Cdd:TIGR02168 308 RERLANL---ERQLEELEAQLEELESKLDELAE--ELAELEEKLEELKEELESLEAELEELEAELEELESRLE----ELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 510 QAMETLRthgllpgqeaqvppqphegeirtdspsSEIQRLQEQNAGLRNAVSQMRKEMEMLSGHLPfAQSEERSNANPEP 589
Cdd:TIGR02168 379 EQLETLR---------------------------SKVAQLELQIASLNNEIERLEARLERLEDRRE-RLQQEIEELLKKL 430
|
330 340 350
....*....|....*....|....*....|...
gi 1958663244 590 KAGEDSAPPDYVLALEAEMQNLKHELKALEEQL 622
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEAL 463
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
36-630 |
1.56e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 36 AQKEEEWRalQAHRAQLQEAALQATQNRLEEaqgKLRRLQEdfvynLQVLEERDRELERYDIEftQARRREEAQQAEASE 115
Cdd:PTZ00121 1163 ARKAEEAR--KAEDAKKAEAARKAEEVRKAE---ELRKAED-----ARKAEAARKAEEERKAE--EARKAEDAKKAEAVK 1230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 116 lKIEVAKLKQELTREA---------RHMEELRHQHKLMLQEHRLELERVHSDKNSELNHQREQYENLKWKLERKLKELDG 186
Cdd:PTZ00121 1231 -KAEEAKKDAEEAKKAeeernneeiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK 1309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 187 ELALQR---QVHKTLEEIYSLLSEVflnvcyRLVALQARGCARIPVMPVMLALTERRTPWDSSLPVDVMKQEWVwlDSST 263
Cdd:PTZ00121 1310 KAEEAKkadEAKKKAEEAKKKADAA------KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK--KKAD 1381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 264 ELLQEFES-----EAQRREHEFQLRADDLSNTVL----THELKVKLLNK----ELQALKEAGAQATESLQKAESEhiele 330
Cdd:PTZ00121 1382 AAKKKAEEkkkadEAKKKAEEDKKKADELKKAAAakkkADEAKKKAEEKkkadEAKKKAEEAKKADEAKKKAEEA----- 1456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 331 RKLQDHARELQDLEAMKDARIKDLEKKlhSVQLAKKKAEETfRRKFREDAAALKAAWDAQIAQMSKEAVSKDlqiqALQE 410
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAK--KADEAKKKAEEA-KKKADEAKKAAEAKKKADEAKKAEEAKKAD----EAKK 1529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 411 EEMKLKAQVAKSQQDIdRYKQQLSLAVEREQSLEREQVQlgldWQRRCDDIECNQIQRSETLIQgLTKARDQVAAKLQET 490
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEK-KKADELKKAEELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKK-AEEARIEEVMKLYEE 1603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 491 ERALHKQEtlLKAVSLERDQAMETLRTHgllpgQEAQVPPQPHEGEIRTDSPSSEIQRLQEQNAGLRNAVSQMRKEMEML 570
Cdd:PTZ00121 1604 EKKMKAEE--AKKAEEAKIKAEELKKAE-----EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK 1676
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 571 SGHLPFAQSEERSNANPEPKAGEDSAPPDYVLALEAEMQNLKHELKALEEQLQGTGEPVK 630
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-445 |
4.30e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 101 QARRREEAQQ--AEASELKIEVAKLKQELTREARHMEELRHQHKLMLQEHRlELERVHSDKNSELNHQREQYENlkwkLE 178
Cdd:TIGR02169 669 SRSEPAELQRlrERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG-EIEKEIEQLEQEEEKLKERLEE----LE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 179 RKLKELDGELALQRQVHKTLEEIYSLLSEVFLNVCYRLVALQAR-GCARIP-VMPVMLALTERRTPWDSSLpvDVMKQEW 256
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPeIQAELSKLEEEVSRIEARL--REIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 257 VWLDSSTELLQEFESEAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDH 336
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 337 ARELQDLEA---MKDARIKDLEKKLHsvqlAKKKAEETFRRKFREDAAALKAAWDAQIAQMSKEAVSKDlqIQALQEEEM 413
Cdd:TIGR02169 902 ERKIEELEAqieKKRKRLSELKAKLE----ALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEE--IRALEPVNM 975
|
330 340 350
....*....|....*....|....*....|...
gi 1958663244 414 KLKAQVAKSQQDIDRYKQQLS-LAVEREQSLER 445
Cdd:TIGR02169 976 LAIQEYEEVLKRLDELKEKRAkLEEERKAILER 1008
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
53-557 |
7.73e-07 |
|
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: 53.58 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 53 QEAALQATQNRLEEAQGKLRRLQEDFVynlqvlEERDRELERYDIEFTQARRREEAQQAEASELKIEVAKLKQELTREAR 132
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKI------EELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 133 HMEELRHQHKLMLQEHR------LELERVHSDKNSELNHQREQYENLK----WKLERKLKELDGE---LALQRQVHKTLE 199
Cdd:pfam15921 392 ELSLEKEQNKRLWDRDTgnsitiDHLRRELDDRNMEVQRLEALLKAMKsecqGQMERQMAAIQGKnesLEKVSSLTAQLE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 200 EIYSLLSEVFLNVCYRLVALQArgcARIPVMPVMLALTERRTPwdsslpVDVMKQEWVWLDSSTEL-LQEFESEAQRREH 278
Cdd:pfam15921 472 STKEMLRKVVEELTAKKMTLES---SERTVSDLTASLQEKERA------IEATNAEITKLRSRVDLkLQELQHLKNEGDH 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 279 --EFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAM---KDARIKD 353
Cdd:pfam15921 543 lrNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILkdkKDAKIRE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 354 LEKKLHSVQLAKKKAEETFRRKFRedaaaLKAAWDAQIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQL 433
Cdd:pfam15921 623 LEARVSDLELEKVKLVNAGSERLR-----AVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKL 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 434 SLAVEREQSlEREQVQLGLDWQRRCDDiecNQIQRSETLIQGLTKARDQVAA---KLQETERAL---HKQETLLKAVSLE 507
Cdd:pfam15921 698 KMQLKSAQS-ELEQTRNTLKSMEGSDG---HAMKVAMGMQKQITAKRGQIDAlqsKIQFLEEAMtnaNKEKHFLKEEKNK 773
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958663244 508 RDQAMETLRTHG--------LLPGQEAQVPPQPHEGEIRTDSPSSE-------IQRLQEQNAGLR 557
Cdd:pfam15921 774 LSQELSTVATEKnkmageleVLRSQERRLKEKVANMEVALDKASLQfaecqdiIQRQEQESVRLK 838
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
29-378 |
1.03e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 29 RELSELLAQKEEEWRALqahRAQLQEaaLQATQNRLEEAQGKLRRLQEdfvyNLQVLEERDRELERydieftqarRREEa 108
Cdd:PRK03918 210 NEISSELPELREELEKL---EKEVKE--LEELKEEIEELEKELESLEG----SKRKLEEKIRELEE---------RIEE- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 109 QQAEASELKIEVAKLK--QELTREARHMEELRHQHKLMLQEHRLELERVHSDKNS--ELNHQREQYENLKWKLERKLKEL 184
Cdd:PRK03918 271 LKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGieERIKELEEKEERLEELKKKLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 185 DGELALQRQVHKTLEEIYSLLSEvflnvcyrlvalqargcaripvmpvMLALTERRTPwdssLPVDVMKQEWVWLDSSTE 264
Cdd:PRK03918 351 EKRLEELEERHELYEEAKAKKEE-------------------------LERLKKRLTG----LTPEKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 265 LLQEFESEAQRREHEFQLRADDLSNTV----------------LTHELKVKLLNK---ELQALKEAGAQATESLQKAESE 325
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgreLTEEHRKELLEEytaELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958663244 326 HIELERKLQDHaRELQDLEAMKDaRIKDLEKKLHSVQLAKKKAEETFRRKFRE 378
Cdd:PRK03918 482 LRELEKVLKKE-SELIKLKELAE-QLKELEEKLKKYNLEELEKKAEEYEKLKE 532
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-446 |
1.83e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 86 EERDRELERYDIEFTQARRREEAQQAEASELKIEVAKLKQEltREarhmeelrhqHKLMLQEHRLELERVH-SDKNSELN 164
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE--RE----------KAERYQALLKEKREYEgYELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 165 HQREQYENLKWKLERKLKELDGELALQRQVHKTLEEIYSLLSEVFLNVCYRLVALQARGCARIPVMPVMLALTERrtpwd 244
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLER----- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 245 sslpvdvmkqewvwldSSTELLQEFEsEAQRREHEFQLRADDLsntvlthELKVKLLNKELQALKEAGAQATESLQKAES 324
Cdd:TIGR02169 309 ----------------SIAEKERELE-DAEERLAKLEAEIDKL-------LAEIEELEREIEEERKRRDKLTEEYAELKE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 325 EHIELERKLQDHARELQDL-EAMKDAR--IKDLEKKLHSVQLAKKKAEETFRRKF--REDAAALKAAWDAQIAQMSKEAV 399
Cdd:TIGR02169 365 ELEDLRAELEEVDKEFAETrDELKDYRekLEKLKREINELKRELDRLQEELQRLSeeLADLNAAIAGIEAKINELEEEKE 444
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958663244 400 SKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSlAVEREQS-LERE 446
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD-RVEKELSkLQRE 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
30-498 |
5.86e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 30 ELSELLAQKEEEWRALQAHRAQLqEAALQATQNRLEEAQGKLRRLQEDF--VYNLQVLEERDRELER---------YDIE 98
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKL-EEKIRELEERIEELKKEIEELEEKVkeLKELKEKAEEYIKLSEfyeeyldelREIE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 99 FTQARRREEAQQ-----AEASELKIEVAKLKQELTREARHMEELRHQHKL--MLQEHRLELERVHSDKN----SELNHQR 167
Cdd:PRK03918 314 KRLSRLEEEINGieeriKELEEKEERLEELKKKLKELEKRLEELEERHELyeEAKAKKEELERLKKRLTgltpEKLEKEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 168 EQYENLKWKLERKLKELDGELALQRQVHKTLEEIYSLLSEvflnvcyrlvalqARGcaRIPVMPVMLALTERRtpwdssl 247
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK-------------AKG--KCPVCGRELTEEHRK------- 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 248 pvDVMKQEWVWLDSSTELLQEFESeaqrREHEFQLRADDLSNTVLTHE--LKVKLLNKELQALKEA-GAQATESLQKAES 324
Cdd:PRK03918 452 --ELLEEYTAELKRIEKELKEIEE----KERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKlKKYNLEELEKKAE 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 325 EHIELERKLQDHARELQDLEamKDA-RIKDLEKKLHSVQLAKKKAEE---TFRRKFREDAAALKAAWDAQIAQMSK---- 396
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLK--KELeKLEELKKKLAELEKKLDELEEelaELLKELEELGFESVEELEERLKELEPfyne 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 397 --EAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGLDWQRRCDDIECNQIQRSETLIQ 474
Cdd:PRK03918 604 ylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELE 683
|
490 500
....*....|....*....|....
gi 1958663244 475 GLTKARDQVAAKLQETERALHKQE 498
Cdd:PRK03918 684 ELEKRREEIKKTLEKLKEELEERE 707
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
28-154 |
1.30e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.09 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 28 ERELSELLAQKEEEWRALQAHraqlQEAALQATQNRLEEAQGKLRRLQEdFVYNLQ-VLEERDRELERYDIEFTQARRRE 106
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEH----EERELTEEEEEIRRLEEQVERLEA-EVEELEaELEEKDERIERLERELSEARSEE 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958663244 107 EAQ---QAEASELKIEVAKLKQELTREARHMEELRHQHKLMLQEHRLELER 154
Cdd:COG2433 458 RREirkDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSG 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-194 |
2.80e-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: 48.53 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 28 ERELSELLAQ-KEEEWRALQAHrAQLQEAALQATQNRLEEAQGKLRRLQedfvYNLQVLEERDRELERYDIEfTQARRRE 106
Cdd:TIGR02169 778 EEALNDLEARlSHSRIPEIQAE-LSKLEEEVSRIEARLREIEQKLNRLT----LEKEYLEKEIQELQEQRID-LKEQIKS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 107 EAQQAEasELKIEVAKLKQELTREARHMEELRHQHKlMLQEHRLELErvhsdknSELNHQREQYENLKWKLERKlKELDG 186
Cdd:TIGR02169 852 IEKEIE--NLNGKKEELEEELEELEAALRDLESRLG-DLKKERDELE-------AQLRELERKIEELEAQIEKK-RKRLS 920
|
....*...
gi 1958663244 187 ELALQRQV 194
Cdd:TIGR02169 921 ELKAKLEA 928
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
27-200 |
3.47e-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: 47.45 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 27 SERELSELLAQKEEEWRALQAHRAQLQEAA--LQATQNRLEEAQGKLRRLQEDfvynlqvLEERDRELERYDIEFTQARR 104
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLkqLAALERRIAALARRIRALEQE-------LAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 105 REEAQQAEASELKIEVAKLKQ--------------ELTREARHMEELRHQHKLMLQEHRLELERVhSDKNSELNHQREQY 170
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAEL-AALRAELEAERAEL 176
|
170 180 190
....*....|....*....|....*....|
gi 1958663244 171 ENLKWKLERKLKELDGELALQRQVHKTLEE 200
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEK 206
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
301-489 |
6.08e-05 |
|
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: 45.69 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 301 LNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEamkdARIKDLEKKLHSVQLAKkkaeetfrrkfreda 380
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE----ARIKKYEEQLGNVRNNK--------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 381 aalkaawdaQIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSlavEREQSLEREQVQLgldwqrrcdd 460
Cdd:COG1579 90 ---------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA---ELEAELEEKKAEL---------- 147
|
170 180
....*....|....*....|....*....
gi 1958663244 461 ieCNQIQRSETLIQGLTKARDQVAAKLQE 489
Cdd:COG1579 148 --DEELAELEAELEELEAEREELAAKIPP 174
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-349 |
8.51e-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: 46.60 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 28 ERELSELLAQKEEEWRALQAHRAQLQEAA----------------LQATQNRLEEAQGKLRRLQEDFVYNLQvleerdRE 91
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIERQLASLEeeleklteeiselekrLEEIEQLLEELNKKIKDLGEEEQLRVK------EK 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 92 LERYDIEFTQARRREEAQQAEASELKIEVAKLKQELTREARHMEELRHQhklmLQEHRLELERVhsdkNSELNHQREQYE 171
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE----IEEERKRRDKL----TEEYAELKEELE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 172 nlkwKLERKLKELDGELALQRQVHKTLEEIYSllsevflnvcyrlvalqargcaripvmpvmlALTERRTPWDSSLpvDV 251
Cdd:TIGR02169 368 ----DLRAELEEVDKEFAETRDELKDYREKLE-------------------------------KLKREINELKREL--DR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 252 MKQEWVWLDSSTELLQEFESEAQRREHEFQLRADDLsntvlthELKVKLLNKELQALKEAGAQATESLQKAESEHIELER 331
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK-------ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
330
....*....|....*...
gi 1958663244 332 KLQDHARELQDLEAMKDA 349
Cdd:TIGR02169 484 ELSKLQRELAEAEAQARA 501
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
101-207 |
1.01e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 101 QARRREEAQQAEA-SELKIEVAKLKQELTREARHME-ELRHQ-HKLMLQEHRLE--LERVhSDKNSELNHQREQYENLKW 175
Cdd:PRK12704 46 EAKKEAEAIKKEAlLEAKEEIHKLRNEFEKELRERRnELQKLeKRLLQKEENLDrkLELL-EKREEELEKKEKELEQKQQ 124
|
90 100 110
....*....|....*....|....*....|..
gi 1958663244 176 KLERKLKELDGELALQRQVhktLEEIYSLLSE 207
Cdd:PRK12704 125 ELEKKEEELEELIEEQLQE---LERISGLTAE 153
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
271-450 |
1.23e-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: 45.53 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 271 SEAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAMKDAR 350
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 351 IKDLEKKLHSVQLAKKKAEETF-----------------------RRKFREDAAALKAAWDAQIAQMSKEAVSKDLQIQA 407
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALllspedfldavrrlqylkylapaRREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958663244 408 LQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQL 450
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
97-516 |
2.16e-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: 45.44 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 97 IEFTQARRREEAQQ-AEASELKIEVAKLKQELTREARHMEELRhqhkLMLQEHRLELERVHSDKNSELNHQ--------R 167
Cdd:TIGR02169 148 ISMSPVERRKIIDEiAGVAEFDRKKEKALEELEEVEENIERLD----LIIDEKRQQLERLRREREKAERYQallkekreY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 168 EQYENLKWK--LERKLKELDGELALQRQVhktLEEIYSLLSEVFLnvcyRLVALQARgcaripvmpvmlalterrtpwds 245
Cdd:TIGR02169 224 EGYELLKEKeaLERQKEAIERQLASLEEE---LEKLTEEISELEK----RLEEIEQL----------------------- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 246 slpvdvmkqewvwLDSSTELLQEFESEAQRReheFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESE 325
Cdd:TIGR02169 274 -------------LEELNKKIKDLGEEEQLR---VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 326 HIELERKLQDHARELQDLEAMKDARIKDLEKKLHSVQLAKKKAEETFRRkfredaaalKAAWDAQIAQMSKEAVSKDLQI 405
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE---------LKDYREKLEKLKREINELKREL 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 406 QALQEEEMKLKAQVAKSQQDIDRYKQQLSlaverEQSLEREQVQLGLDWQRrcddiecnqiQRSETLIQGLTKARDQ--- 482
Cdd:TIGR02169 409 DRLQEELQRLSEELADLNAAIAGIEAKIN-----ELEEEKEDKALEIKKQE----------WKLEQLAADLSKYEQElyd 473
|
410 420 430
....*....|....*....|....*....|....
gi 1958663244 483 VAAKLQETERALHKQETLLKAVSLERDQAMETLR 516
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
524-620 |
2.46e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 524 QEAQVPPQPHEGEIRtdSPSSEIQRLQEQNAGLRNAVSQMRKEMEMLSGHLPFAQSEERSNANPEPKagedsappdyVLA 603
Cdd:COG2433 402 EHEERELTEEEEEIR--RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDRE----------ISR 469
|
90
....*....|....*..
gi 1958663244 604 LEAEMQNLKHELKALEE 620
Cdd:COG2433 470 LDREIERLERELEEERE 486
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
264-574 |
2.66e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 264 ELLQEFESEAQRREHEFQLRADDLSNtvLTHEL-KVKLLNKELQALKEAGAQATESLQKAESEHIELERKLqdhaRELQD 342
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPE--LREELeKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI----RELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 343 LEAMKDARIKDLEKKLHSVQLAKKKAEETFR-RKFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEEMKLKaQVAK 421
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKlSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 422 SQQDIDRYKQQLSLAVEREQSLEREQVQLgldwQRRCDDIECNQIQRSETLIQGLTKARDQVAAKLQETERALHKqetlL 501
Cdd:PRK03918 346 KLKELEKRLEELEERHELYEEAKAKKEEL----ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE----L 417
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958663244 502 KAVSLERDQAMETLR-THGLLP--GQEAQvppQPHEGEIrTDSPSSEIQRLQEQNAGLRNAVSQMRKEMEMLSGHL 574
Cdd:PRK03918 418 KKEIKELKKAIEELKkAKGKCPvcGRELT---EEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL 489
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
32-513 |
3.01e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 32 SELLAQKEEEWRALQAHRAQLQEAALQATQNR-LEEAQGKLRRLQEdfVYNLQVLEERDRELERYDIEFTQARRREEAQQ 110
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKAEEKKkADEAKKKAEEAKK--ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 111 AEASELKIEVAKLKQELTREARHMEELRHQHKLMLQEHRLELERVHSDKNSELNHQREQYENLKWKLERKLKELDGELAL 190
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 191 QRQVHKTLEEIYSLLSEVFLNVCYRlvALQARGCARIPVMPVMLALTERRTpwdsslpvdvMKQEwvwlDSSTELLQEFE 270
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRK--AEEAKKAEEARIEEVMKLYEEEKK----------MKAE----EAKKAEEAKIK 1621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 271 SEAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQalkEAGAQATESLQKAESEhielERKLQDHARELQDLEAMKDAR 350
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE---ENKIKAAEEAKKAEED----KKKAEEAKKAEEDEKKAAEAL 1694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 351 IKDLEKKLHSVQLAKKKAEEtfrRKFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQ-EEEMKLKAQVAKSQQDIDRY 429
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEE---KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKkDEEEKKKIAHLKKEEEKKAE 1771
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 430 KQQLSLAVEREQSLEREQVQLGLDWQRRCDDIECNqiqrSETLIQGlTKARDQVAAKLQETERALHKQETLLKAVSLERD 509
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDN----FANIIEG-GKEGNLVINDSKEMEDSAIKEVADSKNMQLEEA 1846
|
....
gi 1958663244 510 QAME 513
Cdd:PTZ00121 1847 DAFE 1850
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
82-724 |
4.01e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 82 LQVLEERDRELERYDIEFTQARRREEAQQAEASELKIEVAKLKQELTREARHMEElrhQHKLMLQEHRLELErVHSDKNS 161
Cdd:TIGR00618 228 LKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEET---QERINRARKAAPLA-AHIKAVT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 162 ELNHQREQ-YENLKWKLERKLKELDGELALQRQVHKTLEEIYSLlsEVFLNVCYRLVALQARGCARIPVMPVMLALTERR 240
Cdd:TIGR00618 304 QIEQQAQRiHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL--QTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 241 TPWDSSLPVDVMKQEwvwlDSSTELLQEFESEAQRrehEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQ 320
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQ----SLCKELDILQREQATI---DTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 321 KAESEHI-ELERKLQDHARELQDLEamkdaRIKDLEKKLHSVQLAKKKAEETFRRKFREdaaalKAAWDAQIAQMSKEAV 399
Cdd:TIGR00618 455 KLEKIHLqESAQSLKEREQQLQTKE-----QIHLQETRKKAVVLARLLELQEEPCPLCG-----SCIHPNPARQDIDNPG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 400 SKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGLDWQRRCDDIE--CNQIQRSETLIQGLT 477
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPnlQNITVRLQDLTEKLS 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 478 KARDQVAAKLQETER----ALHKQETLLKAVSLERDQAMETLRTHGLLPgQEAQVPPQPHEGEIRTDSPSSEIQRLQEQN 553
Cdd:TIGR00618 605 EAEDMLACEQHALLRklqpEQDLQDVRLHLQQCSQELALKLTALHALQL-TLTQERVREHALSIRVLPKELLASRQLALQ 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 554 AgLRNAVSQMRKEMEMLSGHLPFAQSEERSNANPEPKAGEDSappdyvLALEAEMQNLKHELKALEEQLQGTGEPVKTSM 633
Cdd:TIGR00618 684 K-MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIE------NASSSLGSDLAAREDALNQSLKELMHQARTVL 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 634 ATADPHHgAHNSAEAADAAPADQTLITLA------LRKLGDRVHLLNLLVTQLKKKLRQKPLELVAVQQEIPSEVDQVHL 707
Cdd:TIGR00618 757 KARTEAH-FNNNEEVTAALQTGAELSHLAaeiqffNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLS 835
|
650
....*....|....*..
gi 1958663244 708 EVLELQKQVAELRKHLK 724
Cdd:TIGR00618 836 RLEEKSATLGEITHQLL 852
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
32-452 |
4.02e-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: 44.72 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 32 SELLAQKEEEWRALQAHRAQLQEAALQATQnrLEEAQGKLRRLQEDFVYNLQVLEERDRELERYDIEFTQARRREEAQQA 111
Cdd:pfam15921 440 SECQGQMERQMAAIQGKNESLEKVSSLTAQ--LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNA 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 112 EASELKIEVAKLKQELTREARHMEELRHqhkLMLQEHRLELERVHSDKNSELnhQREQYENLKWKLERKLKELDGELALQ 191
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEGDHLRN---VQTECEALKLQMAEKDKVIEI--LRQQIENMTQLVGQHGRTAGAMQVEK 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 192 RQVHKTLEEIYSLLSEVFL---NVCYRLVALQARgCARIPVMPVML--ALTER-RTPWDSSLPVDVMKQEwvwLDSSTEL 265
Cdd:pfam15921 593 AQLEKEINDRRLELQEFKIlkdKKDAKIRELEAR-VSDLELEKVKLvnAGSERlRAVKDIKQERDQLLNE---VKTSRNE 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 266 LQEFESEAQRREHEFQLRADDLSNTvlTHELKVKLlnKELQALKEAGAQATESLQKAESEHIELerklqdhARELQDLEA 345
Cdd:pfam15921 669 LNSLSEDYEVLKRNFRNKSEEMETT--TNKLKMQL--KSAQSELEQTRNTLKSMEGSDGHAMKV-------AMGMQKQIT 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 346 MKDARIKDLEKKLHSVQLAKKKA--EETFRRKFREDAAALKAAWDAQIAQMSKEavskdlqIQALQEEEMKLKAQVAKSQ 423
Cdd:pfam15921 738 AKRGQIDALQSKIQFLEEAMTNAnkEKHFLKEEKNKLSQELSTVATEKNKMAGE-------LEVLRSQERRLKEKVANME 810
|
410 420
....*....|....*....|....*....
gi 1958663244 424 QDIDRYKQQLSLAVEREQSLEREQVQLGL 452
Cdd:pfam15921 811 VALDKASLQFAECQDIIQRQEQESVRLKL 839
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
816-1040 |
4.05e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.78 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 816 TPCPGPPTSEP---QDPREVPERPLDRGPPLGQLQPHSTTQDPRHTKRKcvseyagknqPHSAQVVNKNSTPQGHKAG-- 890
Cdd:PHA03307 183 ARAPSSPPAEPppsTPPAAASPRPPRRSSPISASASSPAPAPGRSAADD----------AGASSSDSSSSESSGCGWGpe 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 891 -MASRPVQKQHRIPTETWKSVYQKENRTPKLPQAQEVPEESDH------HTHRSSSLASSSLLDTWRlLDLGSSLSGVPS 963
Cdd:PHA03307 253 nECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSpspspsSPGSGPAPSSPRASSSSS-SSRESSSSSTSS 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958663244 964 QDNSAAECPAPLGPSCfqkvSRSPVP--TQRVSRSPVPTQRAFAVKGLKMEAQPKASHPRPSKSHPAKPANCQPQRHPR 1040
Cdd:PHA03307 332 SSESSRGAAVSPGPSP----SRSPSPsrPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGR 406
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
28-370 |
4.80e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 28 ERELSELLAQKEEEWRALQAHRAQLQEAALQATQnrLEEAQGKLRRLQEDF-VYNLQVLEERDRELERYDIEFTQARRRE 106
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQ--AKEGLSALNRLLPRLnLLADETLADRVEEIREQLDEAEEAKRFV 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 107 EAQQAEASELKIEVAKLKQeltrEARHMEELRHQHKLMlqEHRLELERVHSDKNSELNHQREQ--YEN----------LK 174
Cdd:PRK04863 914 QQHGNALAQLEPIVSVLQS----DPEQFEQLKQDYQQA--QQTQRDAKQQAFALTEVVQRRAHfsYEDaaemlaknsdLN 987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 175 WKLERKLKELDGELALQRQVHKTLEEIYSLLSEVFLNvcyrlvalqargcaripvmpvmlalterrtpwdsslpvdvmkq 254
Cdd:PRK04863 988 EKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLAS------------------------------------------- 1024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 255 ewvwLDSSTELLQEFESEAQRREHEFQLRADdlSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQ 334
Cdd:PRK04863 1025 ----LKSSYDAKRQMLQELKQELQDLGVPAD--SGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLR 1098
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958663244 335 DHARELQDLE------------AMKDARIKDLEKKLHSVQLAKKKAEE 370
Cdd:PRK04863 1099 KLERDYHEMReqvvnakagwcaVLRLVKDNGVERRLHRRELAYLSADE 1146
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
30-516 |
5.24e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 30 ELSELLAQKEEEWRALQAH---RAQLQEAALQATQNRLEEAQGKLRRLQED--------------FVYNLQVLEERDREL 92
Cdd:pfam12128 287 ELNQLLRTLDDQWKEKRDElngELSAADAAVAKDRSELEALEDQHGAFLDAdietaaadqeqlpsWQSELENLEERLKAL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 93 ERYDIEFTQARRREEAQQAEASELKIEVAKLKQELTREAR---------HME----ELRHQHKLMLQEHRLELERVHS-- 157
Cdd:pfam12128 367 TGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARdrqlavaedDLQalesELREQLEAGKLEFNEEEYRLKSrl 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 158 ---------------------DKNSELNHQREQYENLKWKLERKLKEL-------DGELALQRQVHKTLEEIYSLLSEV- 208
Cdd:pfam12128 447 gelklrlnqatatpelllqleNFDERIERAREEQEAANAEVERLQSELrqarkrrDQASEALRQASRRLEERQSALDELe 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 209 ------------FLNvcyRLVALQARGCARIpVMPVMLALTERRTPWDSSLPVDVMKQEWVWLD-------SSTELLQEF 269
Cdd:pfam12128 527 lqlfpqagtllhFLR---KEAPDWEQSIGKV-ISPELLHRTDLDPEVWDGSVGGELNLYGVKLDlkridvpEWAASEEEL 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 270 ESEAQRREHEFQL---RADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLeam 346
Cdd:pfam12128 603 RERLDKAEEALQSareKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDS--- 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 347 KDARIKDLEKKLHSVQLAKKKAEETFRRKFREDAAALKAAWDA-------QIAQMS----KEAVSKDLQIQALQEE-EMK 414
Cdd:pfam12128 680 ANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVvegaldaQLALLKaaiaARRSGAKAELKALETWyKRD 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 415 LKA------QVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGLDWQRRCDdiecNQIQRSETLIQGLTKARDQVAAKLQ 488
Cdd:pfam12128 760 LASlgvdpdVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRP----RLATQLSNIERAISELQQQLARLIA 835
|
570 580
....*....|....*....|....*...
gi 1958663244 489 ETERALHKQETLLKAVSLERDQAMETLR 516
Cdd:pfam12128 836 DTKLRRAKLEMERKASEKQQVRLSENLR 863
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
298-449 |
6.08e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 298 VKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAmkdarikdlekklhSVQLAKKKAEETFRRKFR 377
Cdd:COG1842 25 EKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEE--------------KARLALEKGREDLAREAL 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958663244 378 EdaaalkaawdaQIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLE-REQVQ 449
Cdd:COG1842 91 E-----------RKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKaQEKVN 152
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
63-450 |
6.29e-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: 43.81 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 63 RLEEAQGKLRRLQedfvynlqvleERDRELERYDIEFTQARRREEAQQAEASELKIEVAKLKQELTRearhmeELRHQHK 142
Cdd:pfam02463 170 KKKEALKKLIEET-----------ENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEY------LLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 143 LMLQEHRLELERVHSDKNSELNHQREQYENLKWKLERKLKELDGELALQRQVHKTLEEIYSLLSEVFLNvcyrlvalqar 222
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE----------- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 223 gcaripvmpvmlALTERRTPWDSSLPVDVMKQEWVWLDSSTELLQEFESEAQRREHEFQLRADDLSNTVLTHELKVKLLN 302
Cdd:pfam02463 302 ------------LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 303 KELQALKEAGAQATESLQKAESEH---IELERKLQDHARELQDLEAMKDARIKDLEKKLHSVQLAKKKAEETFRRKFRED 379
Cdd:pfam02463 370 QLEEELLAKKKLESERLSSAAKLKeeeLELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEE 449
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958663244 380 AAALKAAWDAQIAQMSKEAVSKDLqIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQL 450
Cdd:pfam02463 450 KEELEKQELKLLKDELELKKSEDL-LKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDG 519
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
28-498 |
7.06e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 28 ERELSELLAQKEEEWRALQAHRAqlqEAALQATQNRLEEAQGKLRRLQEDfvynlqvLEERDRELERYDIEFTQARRREE 107
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAA---EEKAEAAEKKKEEAKKKADAAKKK-------AEEKKKADEAKKKAEEDKKKADE 1409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 108 AQQAEASELKIEVAKLKQELTR----------EARHMEELRHQHKLMLQEHRLELERVHSDKNSELNHQREQ---YENLK 174
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKkadeakkkaeEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakkADEAK 1489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 175 WKLERKLKELDgELALQRQVHKTLEEIYSLLSevflnvcyRLVALQARGCARIPVMPVMLALTERRTPWDSSLPVDVMKQ 254
Cdd:PTZ00121 1490 KKAEEAKKKAD-EAKKAAEAKKKADEAKKAEE--------AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 255 EWVWLDSSTELLQEFESEAQRREHEF-QLRADDLSNTVLTHELKVKLLNKELQALKEAGAQAtESLQKAESEHIELERKL 333
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-EELKKAEEEKKKVEQLK 1639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 334 QDHARELQDLEAMKDArikDLEKKLHSVQLAKKkaEETFRRKFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEEM 413
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKA---EEENKIKAAEEAKK--AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 414 KLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVqlgldwqrRCDDIECNQIQRsetliqgLTKARDQVAAKLQETERA 493
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA--------KKDEEEKKKIAH-------LKKEEEKKAEEIRKEKEA 1779
|
....*
gi 1958663244 494 LHKQE 498
Cdd:PTZ00121 1780 VIEEE 1784
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
390-568 |
7.09e-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: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 390 QIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGLDWQRRCDDI-------- 461
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellraly 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 462 ---------------ECNQIQRSETLIQGLTKARDQVAAKLQETERALHKQETLLKAVSLERDQAMETLRT-HGLLPGQE 525
Cdd:COG4942 115 rlgrqpplalllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEeRAALEALK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958663244 526 AQVPPQPHEGEIRTDSPSSEIQRLQEQNAGLRNAVSQMRKEME 568
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
30-418 |
7.23e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 30 ELSELLAQKEEEWRALQAHRAQLQEAALQATQ--NRLEEAQGKLRRLqedfvynLQVLEERDRELERYDIEFTQARRREE 107
Cdd:pfam05483 395 EMTKFKNNKEVELEELKKILAEDEKLLDEKKQfeKIAEELKGKEQEL-------IFLLQAREKEIHDLEIQLTAIKTSEE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 108 AQQAEASELKIEVAKLKQELTREARHMEELRHQHKLMLQEHrlelervhSDKNSELNHQREQYENLKWKLERKLKELDG- 186
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEA--------SDMTLELKKHQEDIINCKKQEERMLKQIENl 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 187 ---ELALQRQVHKTLEEIYSLLSEVflnvcyrlvalqargcaripvmPVMLALTERRTPWDSSLPVDVMKQEWVWLDSST 263
Cdd:pfam05483 540 eekEMNLRDELESVREEFIQKGDEV----------------------KCKLDKSEENARSIEYEVLKKEKQMKILENKCN 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 264 ELLQEFES------EAQRREHEFQLRADDLSNTVLTHELKVKLLNKELQALKEAGAQATESLQK-------AESEHIELE 330
Cdd:pfam05483 598 NLKKQIENknknieELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKeiedkkiSEEKLLEEV 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 331 RKLQDHARELQDLEAMKDARIKD--------LEKKLHSVQ--LAKKKAEETFRRKFREDAAALKAAWDAQIAQMSKEAVS 400
Cdd:pfam05483 678 EKAKAIADEAVKLQKEIDKRCQHkiaemvalMEKHKHQYDkiIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLS 757
|
410
....*....|....*...
gi 1958663244 401 KDLQIQALQEEEMKLKAQ 418
Cdd:pfam05483 758 LKKQLEIEKEEKEKLKME 775
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
29-637 |
1.12e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 29 RELSELLAQKEEEWRALQAhraqlQEAALQATQNRLEEAQGKLRRLQEDfvynLQVLEERDRELERYDIEFTQARRREEA 108
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKE-----KEKELEEVLREINEISSELPELREE----LEKLEKEVKELEELKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 109 QQAEASELKIEVAKLKQELTREARHMEELRHQHKlmlqehRLELERVHSDKNSELNHQREQYENLKWKLERKLKELDGEL 188
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVK------ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 189 alqRQVHKTLEEIYSLLSEVflnvcyrlvalqargcaripvmpvmlalterrtpwdsslpvdvmkqewvwldsstELLQE 268
Cdd:PRK03918 324 ---NGIEERIKELEEKEERL-------------------------------------------------------EELKK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 269 FESEAQRREHEFQLRADDLSntvlthelKVKLLNKELQALKEAgaQATESLQKAESEHIELERKLQDHARELQDLEAMK- 347
Cdd:PRK03918 346 KLKELEKRLEELEERHELYE--------EAKAKKEELERLKKR--LTGLTPEKLEKELEELEKAKEEIEEEISKITARIg 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 348 --DARIKDLEKKLHSVQLAKKKAEETFRRKFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKsQQD 425
Cdd:PRK03918 416 elKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESE 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 426 IDRYKQQLSLAVEREQSLEREQVQ-LGLDWQ------RRCDDIECNQIQRSETL--IQGLTKARDQVAAKLQETERALHK 496
Cdd:PRK03918 495 LIKLKELAEQLKELEEKLKKYNLEeLEKKAEeyeklkEKLIKLKGEIKSLKKELekLEELKKKLAELEKKLDELEEELAE 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 497 QETLLKAVSLERDQAMEtLRTHGLLPgqeaqvppqPHEGEIRTDSPSSEIQRLQEQNAGLRNAVSQMRKEMEMLSGHLPF 576
Cdd:PRK03918 575 LLKELEELGFESVEELE-ERLKELEP---------FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958663244 577 AQS---EERSNANPEPKAGedsappdyvlaLEAEMQNLKHELKALEEQLQGTGEPVKTSMATAD 637
Cdd:PRK03918 645 LRKeleELEKKYSEEEYEE-----------LREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
29-504 |
1.25e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 29 RELSELLAQKEEEWRALQAHRAQLQeaALQATQNRLE----EAQGKLRRLQEDFVYnLQVLEERDRELE--------RYD 96
Cdd:PRK01156 221 ERLSIEYNNAMDDYNNLKSALNELS--SLEDMKNRYEseikTAESDLSMELEKNNY-YKELEERHMKIIndpvyknrNYI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 97 IEFTQARRREEAQQAEASELKIEVAKLkQELTREARHMEELRHQHKLM------LQEHRLELERVHSDKNSELNhqreQY 170
Cdd:PRK01156 298 NDYFKYKNDIENKKQILSNIDAEINKY-HAIIKKLSVLQKDYNDYIKKksryddLNNQILELEGYEMDYNSYLK----SI 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 171 ENLKWKLERKLKELDGELALQRQVHK----TLEEIYSLLSEV---FLNVCYRLVALQAR-------------------GC 224
Cdd:PRK01156 373 ESLKKKIEEYSKNIERMSAFISEILKiqeiDPDAIKKELNEInvkLQDISSKVSSLNQRiralrenldelsrnmemlnGQ 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 225 ARIPVMPVMLA------LTERRTPWDSSLPVDV--MKQEWVWLDSSTELLQEFESEAQRREHEFQLRADDLSNTvLTHEL 296
Cdd:PRK01156 453 SVCPVCGTTLGeeksnhIINHYNEKKSRLEEKIreIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIES-ARADL 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 297 KvKLLNKElQALKEAGAQATESLQKAESEHIE-LERKLQDH-----ARELQDLEAM------KDARIKDLEKKLHSVQLA 364
Cdd:PRK01156 532 E-DIKIKI-NELKDKHDKYEEIKNRYKSLKLEdLDSKRTSWlnalaVISLIDIETNrsrsneIKKQLNDLESRLQEIEIG 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 365 KKKAEETFRRKFREdaaalKAAWDAQIAQMSKEAVSKDLQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLE 444
Cdd:PRK01156 610 FPDDKSYIDKSIRE-----IENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLK 684
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 445 REQVQLgldwqrrcDDIECNQiQRSETLIQGLTKARDQVAAKLQETERALHKQETLLKAV 504
Cdd:PRK01156 685 KSRKAL--------DDAKANR-ARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
39-582 |
1.28e-03 |
|
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: 42.80 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 39 EEEWRALQAHRAQLQEAALQATQNRLEeaqgklrrlqedfvynlQVLEERDRELERYDIEFTQARrreeaQQAEASELKI 118
Cdd:pfam15921 244 EDQLEALKSESQNKIELLLQQHQDRIE-----------------QLISEHEVEITGLTEKASSAR-----SQANSIQSQL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 119 EVAKlkqeltrearhmEELRHQHKlMLQEHRLELERVHSDKNSELNHQREQYENLKWKLERKLKELDGELALQRqvhkTL 198
Cdd:pfam15921 302 EIIQ------------EQARNQNS-MYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEAR----TE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 199 EEIYSLLSEVFLNVCYRLVA-LQARGcaripvMPVMLALTERRTPWD----SSLPVDVMKQEwvwLDSST-------ELL 266
Cdd:pfam15921 365 RDQFSQESGNLDDQLQKLLAdLHKRE------KELSLEKEQNKRLWDrdtgNSITIDHLRRE---LDDRNmevqrleALL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 267 QEFESEAQrREHEFQLRADDLSNTVLThelKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAM 346
Cdd:pfam15921 436 KAMKSECQ-GQMERQMAAIQGKNESLE---KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 347 KDARIKDLEK-------KLHSVQLAKKKAEETFRRKFREDAAALKAAWDAQIAQMSKEAVSKDLQI--------QALQEE 411
Cdd:pfam15921 512 IEATNAEITKlrsrvdlKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLvgqhgrtaGAMQVE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 412 EMKLKAQVAKSQQDIDRYK-------QQLSLAVEREQSLEREQVQL---GLDWQRRCDDIE------CNQIQRSETLIQG 475
Cdd:pfam15921 592 KAQLEKEINDRRLELQEFKilkdkkdAKIRELEARVSDLELEKVKLvnaGSERLRAVKDIKqerdqlLNEVKTSRNELNS 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 476 LTKA----RDQVAAKLQETERALHKQETLLKAVSLERDQAMETLRT------HGLLPGQEAQVPPQPHEGEIrtDSPSSE 545
Cdd:pfam15921 672 LSEDyevlKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmegsdgHAMKVAMGMQKQITAKRGQI--DALQSK 749
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1958663244 546 IQRLQ--------------EQNAGLRNAVSQMRKEMEMLSGHLPFAQSEER 582
Cdd:pfam15921 750 IQFLEeamtnankekhflkEEKNKLSQELSTVATEKNKMAGELEVLRSQER 800
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
303-363 |
1.66e-03 |
|
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: 41.05 E-value: 1.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958663244 303 KELQALKEAGAQATESLQKAESEHIELERKLQDHARELQDLEAMKdARIKDLEKKLHSVQL 363
Cdd:pfam13851 47 KLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLK-ARLKVLEKELKDLKW 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
328-631 |
1.89e-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: 42.36 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 328 ELERKLQDHARELQDLE---AMKDARIKDLEKKLHSVQLAKKKAEEtFR--RKFREDAAALKAAWDAQIAQMSKEAVSKd 402
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEeniERLDLIIDEKRQQLERLRREREKAER-YQalLKEKREYEGYELLKEKEALERQKEAIER- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 403 lQIQALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSL-EREQVQLgldwQRRCDDIEcNQIQRSETLIQGLTKARD 481
Cdd:TIGR02169 245 -QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRV----KEKIGELE-AEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 482 QVAAKLQETERALHKqeTLLKAVSLERDQAMETLRthgllpgqEAQVPPQPHEGEIRTDSPSSEIQRLQEQNAGLRNAVS 561
Cdd:TIGR02169 319 DAEERLAKLEAEIDK--LLAEIEELEREIEEERKR--------RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 562 QMRKEMEMLS-------------GHLPFAQSEERSNANPEPKAGEDSappdyVLALEAEMQNLKHELKALEEQLQGTGEP 628
Cdd:TIGR02169 389 DYREKLEKLKreinelkreldrlQEELQRLSEELADLNAAIAGIEAK-----INELEEEKEDKALEIKKQEWKLEQLAAD 463
|
...
gi 1958663244 629 VKT 631
Cdd:TIGR02169 464 LSK 466
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
86-201 |
2.09e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 86 EERDRELERYDIEFTQARRREEAQQAEASELKIEVAKLKQELTREARHMEELRHQHKLMLQEHRLE---------LERVH 156
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREirkdreisrLDREI 474
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958663244 157 SDKNSELNHQREQYENLKWKLER--KLKELD--GELALQRQVHK-TLEEI 201
Cdd:COG2433 475 ERLERELEEERERIEELKRKLERlkELWKLEhsGELVPVKVVEKfTKEAI 524
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
270-510 |
3.20e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 270 ESEAQRREHEFQLRADDLSNTVLTHELKVKllNKELQALKEAGAQATESlQKAESEHIELERKLQDHARELQDLEAMKDA 349
Cdd:PTZ00121 1057 EGKAEAKAHVGQDEGLKPSYKDFDFDAKED--NRADEATEEAFGKAEEA-KKTETGKAEEARKAEEAKKKAEDARKAEEA 1133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 350 RIKDLEKKLHSVqlakKKAEETFRRKFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEEMKlKAQVAKSQQDIDRY 429
Cdd:PTZ00121 1134 RKAEDARKAEEA----RKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELR-KAEDARKAEAARKA 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 430 KQQLSLAVEREQSLER--------EQVQLGLDWQRRCDDIECNQIQRSETLIQGLTKARDQVAAKLQETERA--LHKQET 499
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKkaeavkkaEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdeLKKAEE 1288
|
250
....*....|.
gi 1958663244 500 LLKAVSLERDQ 510
Cdd:PTZ00121 1289 KKKADEAKKAE 1299
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
27-184 |
3.36e-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: 39.89 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 27 SERELSELLAQKEEEWRALQAHRAQLQEaALQATQNRLEEAQGKLRRLQEDfvynLQVLEE--RDRELerydieftqarr 104
Cdd:pfam15619 54 TESELPQLIARHNEEVRVLRERLRRLQE-KERDLERKLKEKEAELLRLRDQ----LKRLEKlsEDKNL------------ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 105 reeaqqAEASELKIEVAKLKQELTREARHMEELRHQHKLMLQEHRLEL---ERVHSDKNSELNHQREQYENLKWKLERKL 181
Cdd:pfam15619 117 ------AEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLaaeKKKHKEAQEEVKILQEEIERLQQKLKEKE 190
|
...
gi 1958663244 182 KEL 184
Cdd:pfam15619 191 REL 193
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
27-193 |
3.97e-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: 41.26 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 27 SERELSELLAQKEEEWRALQAHRAQLQE--AALQATQNRLEEAQGKLRRLQEDFVYNLQVLEERDRELERYDIEFTQARR 104
Cdd:pfam05557 25 HKRARIELEKKASALKRQLDRESDRNQElqKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADARE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 105 REEAQQAEASELKIEVAKLKQELTREARHMEELRHQHKLMLQehrlelervhsdKNSELNHQREQYENLKWKL---ERKL 181
Cdd:pfam05557 105 VISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKA------------KASEAEQLRQNLEKQQSSLaeaEQRI 172
|
170
....*....|..
gi 1958663244 182 KELDGELALQRQ 193
Cdd:pfam05557 173 KELEFEIQSQEQ 184
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
330-496 |
4.97e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 330 ERKLQDHARELQ----DLEAMKDArIKDLEKKLHSVQLAKKKAEEtFRRKFREDAAALKAAWDAQIAQMSKEavskdlqI 405
Cdd:COG4913 220 EPDTFEAADALVehfdDLERAHEA-LEDAREQIELLEPIRELAER-YAAARERLAELEYLRAALRLWFAQRR-------L 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 406 QALQEEEMKLKAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGLDwqrrcddiecnQIQRSETLIQGLTKARDQVAA 485
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD-----------RLEQLEREIERLERELEERER 359
|
170
....*....|.
gi 1958663244 486 KLQETERALHK 496
Cdd:COG4913 360 RRARLEALLAA 370
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
106-491 |
5.20e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 106 EEAQQAEASELKIEVAKLKQELTREARHMEELrhqhKLMLQEHRlelervhsDKNSELNHQRE-QYENLKWKLERK---L 181
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLIQITEKENKMKDL----TFLLEESR--------DKANQLEEKTKlQDENLKELIEKKdhlT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 182 KEL-DGELALQRQV--HKTLEEIYSLLSEvflNVCYRLVALQARgcaripvmpvMLALTERRTPwdSSLPVDVMKQEWVW 258
Cdd:pfam05483 296 KELeDIKMSLQRSMstQKALEEDLQIATK---TICQLTEEKEAQ----------MEELNKAKAA--HSFVVTEFEATTCS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 259 LDsstELLQEFESEAQRREHEFQLRADDLSNTVLTHELKVKLLNK---ELQALKEAGAQaTESLQKAESEHIELERKLQD 335
Cdd:pfam05483 361 LE---ELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNkevELEELKKILAE-DEKLLDEKKQFEKIAEELKG 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 336 HARELQDLEAMKDARIKDLEkklhsVQLAKKKAEETFRRKFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEEMKL 415
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLE-----IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDM 511
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958663244 416 KAQVAKSQQDIDRYKQQLSLAVEREQSLEREQVQLGldwqrrcddiecnqiQRSETLIQGLTKARDQVAAKLQETE 491
Cdd:pfam05483 512 TLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR---------------DELESVREEFIQKGDEVKCKLDKSE 572
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
34-511 |
5.51e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 34 LLAQKEEEWRALQAHRAQLQEAALQATQNRLEEAqgklrrlqedfvynlqvLEERDRELERYDIEFTQAR-RREEAQ--- 109
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESE-----------------LAELDEEIERYEEQREQAReTRDEADevl 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 110 ------QAEASELKIEVAKLKQELTREARHMEELRHQhklmLQEHRLELERVHSDKNSELNhqreqyenlkwklERKLKE 183
Cdd:PRK02224 244 eeheerREELETLEAEIEDLRETIAETEREREELAEE----VRDLRERLEELEEERDDLLA-------------EAGLDD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 184 LDGELALQRQ--VHKTLEEIYSLLSEVflnvcyRLVALQARGCAripvmpvmlalterrtpwdsslpvdvmkqewvwlDS 261
Cdd:PRK02224 307 ADAEAVEARReeLEDRDEELRDRLEEC------RVAAQAHNEEA----------------------------------ES 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 262 STELLQEFESEAQRREHEFQLRADDLSNT---VLTHELKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLqDHAR 338
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAreaVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREER-DELR 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 339 ElqdleamkdaRIKDLEKKLHSVQLAKKKAEEtfrrkFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEEMKLKAQ 418
Cdd:PRK02224 426 E----------REAELEATLRTARERVEEAEA-----LLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 419 VAKSQQDIDRYKQQLSLAVEREQSLEREQvqlglDWQRRCDDIEcNQIQRSETLIQGLTKARDQVAAKLQETERALHK-- 496
Cdd:PRK02224 491 VEEVEERLERAEDLVEAEDRIERLEERRE-----DLEELIAERR-ETIEEKRERAEELRERAAELEAEAEEKREAAAEae 564
|
490
....*....|....*...
gi 1958663244 497 ---QETLLKAVSLERDQA 511
Cdd:PRK02224 565 eeaEEAREEVAELNSKLA 582
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
27-448 |
6.15e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 27 SERELSELLAQKEEEWRALQAHRAQLQeaalQATQNRLEEAQGKLRRLQEDFvYNLQVLEERDRELERYDIEFTQARRRE 106
Cdd:TIGR00618 418 AFRDLQGQLAHAKKQQELQQRYAELCA----AAITCTAQCEKLEKIHLQESA-QSLKEREQQLQTKEQIHLQETRKKAVV 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 107 EAQQAEASELKIEVAKLKQELTREARHMEELRHQHKLMLQ--EHRLELERVHSDKNSELNHQREQYENLKWKLERklkEL 184
Cdd:TIGR00618 493 LARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRgeQTYAQLETSEEDVYHQLTSERKQRASLKEQMQE---IQ 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 185 DGELALQRQVHKTLEEIYSLLSEVFLNVCYRLVALQARGCARIPVMPVMLALTERRTPWDSSLPVDVMKQEWVWLDSS-- 262
Cdd:TIGR00618 570 QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAlh 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 263 ---TELLQEFESEAQRREHEFQLRADDlsntvlthelKVKLLNKELQALKEAGAQATESLQKAESEHIELERKLQDHARE 339
Cdd:TIGR00618 650 alqLTLTQERVREHALSIRVLPKELLA----------SRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 340 LQDLEAMKDARIKDLEKKLHSVQLAKKKAEETFRRKFREDAAALKAAWDAQIAQMSKEAVSKDL------QIQALQEEEM 413
Cdd:TIGR00618 720 FNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLaaeiqfFNRLREEDTH 799
|
410 420 430
....*....|....*....|....*....|....*
gi 1958663244 414 KLKAQVAKSQQDIDRYKQQLSLAVEREQSlEREQV 448
Cdd:TIGR00618 800 LLKTLEAEIGQEIPSDEDILNLQCETLVQ-EEEQF 833
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
50-200 |
6.48e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 50 AQLQEAALQATQNRLEEAQGKLRRLQEDfvynlqvLEERDRELERYDIEFTQARRREEAQQAEASELKIEVAKLKQELTR 129
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAE-------LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 130 EARHM-----------------------------EELRHQHKLMLQEHRLELERVHSDKnSELNHQREQYENLKWKLERK 180
Cdd:COG3883 91 RARALyrsggsvsyldvllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAKK-AELEAKLAELEALKAELEAA 169
|
170 180
....*....|....*....|
gi 1958663244 181 LKELDGELALQRQVHKTLEE 200
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSA 189
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
34-154 |
6.78e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 34 LLAQKEEEWRALQAHRAQLQEAALQATQNRLEEAQGKLRRLQEDFVYNLQVLEER--------DRELERYDIEFTQARRR 105
Cdd:PRK12705 31 LAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERlvqkeeqlDARAEKLDNLENQLEER 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958663244 106 EEAQQAEASELKIEVAKLKQELTR-------EARHM----------EELRHQHKLMLQEHRLELER 154
Cdd:PRK12705 111 EKALSARELELEELEKQLDNELYRvagltpeQARKLllklldaeleEEKAQRVKKIEEEADLEAER 176
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
29-154 |
7.07e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.03 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 29 RELSELLAQKEEEWRALQAHRAQLQeaALQATQNRLEEAQGKLRRLQEDfvynlqvLEERDRELERYD----------IE 98
Cdd:COG1566 79 TDLQAALAQAEAQLAAAEAQLARLE--AELGAEAEIAAAEAQLAAAQAQ-------LDLAQRELERYQalykkgavsqQE 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958663244 99 FTQARRREEAQQAEASELKIEVAKLKQELTREARhMEELRHQH---KLMLQEHRLELER 154
Cdd:COG1566 150 LDEARAALDAAQAQLEAAQAQLAQAQAGLREEEE-LAAAQAQVaqaEAALAQAELNLAR 207
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
297-638 |
7.90e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 297 KVKLLNKELQALKEAG----------AQATESLQKAESEHIELERKLQDHARELQDLEAMKDA-----RIKDLEKKLHSV 361
Cdd:COG4717 65 KPELNLKELKELEEELkeaeekeeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 362 QLAKKKAEEtfRRKFREDAAALKAAWDAQIAQMSKEAVSKDLQIQALQEEEMK-LKAQVAKSQQDIDRYKQQLSLAVERE 440
Cdd:COG4717 145 PERLEELEE--RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 441 QSLEREQVQLGLDWQRRCDdieCNQIQRSETLIQGLTKARDQVAAKLQETERALHKQETLLKAVSLERDQAMETLRTHGL 520
Cdd:COG4717 223 EELEEELEQLENELEAAAL---EERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 521 LPGQEAQVPPQPHEGEIRTDSPSSEIQRLQ----EQNAGLRNAVSQMRK------EMEMLSGHLPFAQSEERSNANPEPK 590
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGlppdLSPEELLELLDRIEElqellrEAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958663244 591 AGEDSAPPDYVLALEAEMQNLKHELKALEEQLQGTGEPVKTSMATADP 638
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
30-187 |
8.88e-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: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 30 ELSELLAQKEEEWRALQAhRAQLQEAALQATQNRLEEAQGKLRRLQEDFvynlqvleerdrELERYDIEFTQARRREEAQ 109
Cdd:pfam01576 233 ELRAQLAKKEEELQAALA-RLEEETAQKNNALKKIRELEAQISELQEDL------------ESERAARNKAEKQRRDLGE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 110 QAEASELKIE------------VAKLKQELTREARHMEELRHQHKLMLQEHRLElervHSDKNSELNHQREQYENLKWKL 177
Cdd:pfam01576 300 ELEALKTELEdtldttaaqqelRSKREQEVTELKKALEEETRSHEAQLQEMRQK----HTQALEELTEQLEQAKRNKANL 375
|
170
....*....|
gi 1958663244 178 ERKLKELDGE 187
Cdd:pfam01576 376 EKAKQALESE 385
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
29-208 |
9.09e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 29 RELSELLAQKEEEWRAL--QAHRAQLQEAALQATQNRLEEAQGKL----RRLQEDFVYNLQVLEERDRELERYDIEFTQA 102
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLkkELEKLEELKKKLAELEKKLDELEEELaellKELEELGFESVEELEERLKELEPFYNEYLEL 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 103 -------RRREEAQQAEASELKIEVAKLKQELTREARHMEELRHQHKLMLQEHRLELERVHSDKNSELNHQREQYENLKW 175
Cdd:PRK03918 608 kdaekelEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEK 687
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958663244 176 KLE---RKLKELDGELALQRQVHKTLEEIYSLLSEV 208
Cdd:PRK03918 688 RREeikKTLEKLKEELEEREKAKKELEKLEKALERV 723
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
57-188 |
9.10e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958663244 57 LQATQNRLEEAQGKLRRLQEDFVYNLQVLEERDRELErydIEFTQARRREEAQQAEASELKIEVAKLKQELTREARHMEE 136
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE---LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1958663244 137 LRHQHKlMLQEHRLELERVHSD---KNSELNHQREQYENLKWKLERKLKELDGEL 188
Cdd:TIGR04523 494 KEKELK-KLNEEKKELEEKVKDltkKISSLKEKIEKLESEKKEKESKISDLEDEL 547
|
|
| |
