|
Name |
Accession |
Description |
Interval |
E-value |
| CNH |
smart00036 |
Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2; |
941-1222 |
8.10e-81 |
|
Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2;
Pssm-ID: 214481 Cd Length: 302 Bit Score: 267.29 E-value: 8.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 941 NNLKIFKAHTIE-DWILFATQTGLFFTSIS-QPRNPTRIAGPSSVTSLEVMSEINCVAMITNSNRQLALIPLDSLTL--- 1015
Cdd:smart00036 1 NTAKWNHPITCDgKWLLVGTEEGLYVLNISdQPGTLEKLIGRRSVTQIWVLEENNVLLMISGKKPQLYSHPLSALVEkke 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 1016 AMQSTHPSIRAEVLPEFGHVH-TIRYHQQDGQRFLLVSDDTQLHIRKYNsTRDVFAHFAKLV----------VPEPVSFI 1084
Cdd:smart00036 81 ALGSARLVIRKNVLTKIPDVKgCHLCAVVNGKRSLFLCVALQSSVVLLQ-WYNPLKKFKLFKskflfplispVPVFVELV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 1085 ESTP--AGFIFASDT-FYYVPLDHQSpsDVSARKLMPPRRSDY----PVSAHAITANEILLAYQNHGIFVNLYG-EQSRN 1156
Cdd:smart00036 160 SSSFerPGICIGSDKgGGDVVQFHES--LVSKEDLSLPFLSEEtslkPISVVQVPRDEVLLCYDEFGVFVNLYGkRRSRN 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17536671 1157 QIIEWEKMPIEFAYTSPLLYIVHDDSIEIVQISKSSKETVLAEREviaCVNAHIV--QSDGVLISVSS 1222
Cdd:smart00036 238 PILHWEFMPESFAYHSPYLLAFHDNGIEIRSIKTGELLQELADRE---TRKIRLLgsSDRKILLSSSP 302
|
|
| CNH |
pfam00780 |
CNH domain; Domain found in NIK1-like kinase, mouse citron and yeast ROM1, ROM2. Unpublished ... |
952-1207 |
1.26e-71 |
|
CNH domain; Domain found in NIK1-like kinase, mouse citron and yeast ROM1, ROM2. Unpublished observations.
Pssm-ID: 459938 Cd Length: 261 Bit Score: 239.84 E-value: 1.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 952 EDWILFATQTGLFFTSISQPRNPTRIAGPSSVTSLEVMSEINCVAMITNSNRQLALIPLDSLTLAMQSTHPSIRAEVLPE 1031
Cdd:pfam00780 2 GQNLLLGTEEGLYVLNRSGPREPVRIIDKKRVTQLAVLEEFNLLLLLSGKDKRLYVYPLSALDSREENDRKDAAKNKLPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 1032 FGHVHTIRYHQQDGQRFLLVSDDTQLHIRKYNST-RDVFAHFAKLVVPEPVSFIESTPAGFIFASDTFYY-VPLDHQSPS 1109
Cdd:pfam00780 82 TKGCHFFKVGRHSNGRFLVVAVKRTIKLLEWYEPlLDKFRKFKEFYLPSPPVSIELLKSKLCVGCAKGFEiVSLDSKATE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 1110 DV-SARKLMPPRRSDYPVSAHAITANEILLAYQNHGIFVNLYGEQSRNQIIEWEKMPIEFAYTSPLLYIVHDDSIEIVQI 1188
Cdd:pfam00780 162 SLlTSLLFANRQENLKPLAVVRLDRSEFLLCYNEFGVYVNLQGRRSRPWEIEWEGAPEAVAYLYPYLLAFHDNFIEIRDV 241
|
250
....*....|....*....
gi 17536671 1189 SKSSKETVLAEREVIACVN 1207
Cdd:pfam00780 242 ETGELVQEIAGRKIRFLNS 260
|
|
| CRIK |
cd20814 |
protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) ... |
737-794 |
3.07e-23 |
|
protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) and similar proteins; CRIK, also called serine/threonine-protein kinase 21, is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger (C1 domain), and a pleckstrin homology (PH) domain, in addition to other motifs. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410364 Cd Length: 56 Bit Score: 93.85 E-value: 3.07e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 17536671 737 HDIPHKWLEFRHYSvlSMKCSLCFVGITFFTKANKCSHCDVRVHASCAPRVNNTCGIP 794
Cdd:cd20814 1 HNIPHRFTTGLNMR--ATKCAVCLDGVPFGRQASKCSECGIVCHPKCSSSLPNTCGLP 56
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
91-699 |
1.97e-19 |
|
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: 95.12 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 91 RRDVTLLEDDLKQKESQIRilqnrclRLETEKQKMQDTISgYQEDLKENEI-----RIENLNSRLHKLEDELSAKTHEIF 165
Cdd:TIGR02168 185 RENLDRLEDILNELERQLK-------SLERQAEKAERYKE-LKAELRELELallvlRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 166 SIGEELKNKTMKLNEKNSQF---QTKLAEISSENRNLERKVQKFREELIVKDQRSLEVHQDQENTQKVLKEVKQLSDRLd 242
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 243 yltpkRKDVSRIKERDDFLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLH 322
Cdd:TIGR02168 336 -----AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 323 AENMKLTRQKADIRCDLLEARRN-LKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSR 401
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 402 VAGYEVLRRDHE----AVKNELAKAEEKLNKMGA------------------------HLVMADKQS--SHFKTLKETAE 451
Cdd:TIGR02168 491 LDSLERLQENLEgfseGVKALLKNQSGLSGILGVlselisvdegyeaaieaalggrlqAVVVENLNAakKAIAFLKQNEL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 452 GsrRRAIeqCNEMVARIRGLEASLENQRKVEQELEMVKAENVRQAKKIE----------FMKEEIQ-------ETHLDYR 514
Cdd:TIGR02168 571 G--RVTF--LPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvLVVDDLDnalelakKLRPGYR 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 515 ---EELSKLAKGG----GSHEADSQ---RDSELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAEAIE 584
Cdd:TIGR02168 647 ivtLDGDLVRPGGvitgGSAKTNSSileRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 585 KIEEFKRNWHSSREAGE-------RLQLEAKENEEKVLKVEEELQEKRLEVLEKEELVNYLQSQINTKQtkqpklSRRST 657
Cdd:TIGR02168 727 QISALRKDLARLEAEVEqleeriaQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK------EELKA 800
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 17536671 658 LMSTISEVDtSTYVREVEEVRALEEQREELQAYLAEKRKMAD 699
Cdd:TIGR02168 801 LREALDELR-AELTLLNEEAANLRERLESLERRIAATERRLE 841
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
97-700 |
4.83e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.38 E-value: 4.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 97 LEDDLKQKESQIRILQNRCLRLETEKQkmqdtisgyQEDLKENEIRIENLNSRLHKLEDELsaktheifsigEELKNKTM 176
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEEL---------EAELEELEAELEELEAELAELEAEL-----------EELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 177 KLNEKNSQFQTKLAEISSENRNLERKVQKFREELIVKDQRSLEVHQDQENTQKVLKEVKQLSDRLdyltpkRKDVSRIKE 256
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL------EEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 257 RddflqfsAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLHAENMKLTRQKADIR 336
Cdd:COG1196 352 E-------LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 337 CDLLEARRNLKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEE---REEQIDELKSRVAGYEVLRRDHE 413
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAlaeLLEELAEAAARLLLLLEAEADYE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 414 AVKNELAKAEEKLNKMGAHLVMADKQSSHFK--TLKETAEGSRRRAIEQCNEMVAR--IRGLEASLENQRKVEQELEMVK 489
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAyeAALEAALAAALQNIVVEDDEVAAaaIEYLKAAKAGRATFLPLDKIRA 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 490 AENVRQAKKIEFMKEEIQETHLDYREELSKLAKGGGSHEADSQRDSELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVL 569
Cdd:COG1196 585 RAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 570 EENVKLRKGMAEAIEKIEEFKRNWHSSREAGERLQLEAKENEEKVLKVEEELQEKRLEVLEKEELVNYLQSQINTKQTKQ 649
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 17536671 650 PKLSRRSTLmstisevdtstyvREVEEVRALEEQREELQAYlaeKRKMADL 700
Cdd:COG1196 745 EELLEEEAL-------------EELPEPPDLEELERELERL---EREIEAL 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
28-590 |
9.90e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 89.35 E-value: 9.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 28 VIDLNNESQEDLKtRLLEAENIIQDLRSERDALHESLVDKAGLNESVIIERSNKVSTQETRIyrrdvtlleDDLKQKESQ 107
Cdd:PRK03918 170 VIKEIKRRIERLE-KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---------KELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 108 IRILQNRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEdELSAKTHEIFSIGEELKNKTMKLNE---KNSQ 184
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREiekRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 185 FQTKLAEISSENRNLERKVQKFRE--ELIVKDQRSLEVhqdQENTQKVLKEVKQLSDRLDYLTPKRKDVS--RIKERDDF 260
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEElkKKLKELEKRLEE---LEERHELYEEAKAKKEELERLKKRLTGLTpeKLEKELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 261 LQFSAKIIEETMSELKLKNARLERELSEK----EELVK-----------VTKEELQELQKTVTQAMGDSEQATKYLHAEN 325
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELkkaiEELKKakgkcpvcgreLTEEHRKELLEEYTAELKRIEKELKEIEEKE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 326 MKLTRQKADIRCDLLEARRNLKgfDEKREELEKQRDEALEDVrRITELKKNVEiELRSLKLLAEEREEQIDELKSRVAGY 405
Cdd:PRK03918 476 RKLRKELRELEKVLKKESELIK--LKELAEQLKELEEKLKKY-NLEELEKKAE-EYEKLKEKLIKLKGEIKSLKKELEKL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 406 EVLRRDHEAVKNELAKAEEKLNKMGAHLvmadkQSSHFKTLKETAE--GSRRRAIEQCNEMVARIRGLEASLENQRKVEQ 483
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKEL-----EELGFESVEELEErlKELEPFYNEYLELKDAEKELEREEKELKKLEE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 484 ELEMVKAENVRQAKKIEFMKEEI--------QETHLDYREELSKLAKgggsheADSQRDSELRSAKKTIQEVKADNKKLQ 555
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELeelekkysEEEYEELREEYLELSR------ELAGLRAELEELEKRREEIKKTLEKLK 700
|
570 580 590
....*....|....*....|....*....|....*
gi 17536671 556 QILEEvRQNQSKVLEENVKLRKGMAEAIEKIEEFK 590
Cdd:PRK03918 701 EELEE-REKAKKELEKLEKALERVEELREKVKKYK 734
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
108-704 |
2.11e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 88.20 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 108 IRILQNRCLRLETE---KQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIFSIgEELKNKTMKLNEKNSQ 184
Cdd:PRK03918 171 IKEIKRRIERLEKFikrTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 185 FQTKLAEISSENRNLERKVQKFREELIVKDQRSLEVHQDQENTQKVLKEVKQLSDRLDYLTPKRKDVSRIKERddflqfs 264
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE------- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 265 AKIIEETMSELKLKNARLErELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYlhaenmkltrqKADIRCdllearR 344
Cdd:PRK03918 323 INGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKEELERL-----------KKRLTG------L 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 345 NLKGFDEKREELEKQRDEALEDVRRITElkknveiELRSLKLLAEEREEQIDELKSRVAGYEVLRR--DHEAVKNELAKA 422
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITA-------RIGELKKEIKELKKAIEELKKAKGKCPVCGRelTEEHRKELLEEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 423 EEKLNKMGahlvmadkqsshfKTLKETAEGSRrraieqcnEMVARIRGLEASLENQRKVEQELEMVKAENVRQAKKIEFM 502
Cdd:PRK03918 458 TAELKRIE-------------KELKEIEEKER--------KLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYN 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 503 KEEIQETHLDYREELSKLAKGGGsheadsqrdsELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVLEENVKLR------ 576
Cdd:PRK03918 517 LEELEKKAEEYEKLKEKLIKLKG----------EIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfes 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 577 -KGMAEAIEKIEEFKRNWHSSREAGERLQ-----LEAKENEEKVLKVEEELQEKRLEVLEKEelVNYLQSQINTKQTKqp 650
Cdd:PRK03918 587 vEELEERLKELEPFYNEYLELKDAEKELEreekeLKKLEEELDKAFEELAETEKRLEELRKE--LEELEKKYSEEEYE-- 662
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 17536671 651 KLSRRSTLMStisevdtSTYVREVEEVRALEEQREELQAYLAE-KRKMADLQKSR 704
Cdd:PRK03918 663 ELREEYLELS-------RELAGLRAELEELEKRREEIKKTLEKlKEELEEREKAK 710
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
50-705 |
2.16e-17 |
|
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: 88.20 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 50 IQDLRSERDALHESLvdkaGLNESVIIERSNKVSTQETRiyrRDVTLLEDDLKQKESQIR--ILQNRCLRLETEKQKMQD 127
Cdd:TIGR02169 172 KEKALEELEEVEENI----ERLDLIIDEKRQQLERLRRE---REKAERYQALLKEKREYEgyELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 128 TISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIFSIGEELKNktmklneknsQFQTKLAEISSENRNLERKVQKFR 207
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL----------RVKEKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 208 EELivkDQRSLEVHQDQENTQKVLKEVKQLSDRLdylTPKRKDVSRIKERDDFLQFSAKIIEETMSELKLKNARLERELS 287
Cdd:TIGR02169 315 REL---EDAEERLAKLEAEIDKLLAEIEELEREI---EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 288 EKEELVKVTKEELQELQKTVTQAMGDSEQATKYLHAENMKLTRQKADI---RCDLLEARRNLKGFDEKREELEKQRDEAL 364
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKInelEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 365 EDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRVAGY----EVLRRDHEAVKN---ELAKAEEK------------ 425
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGraveEVLKASIQGVHGtvaQLGSVGERyataievaagnr 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 426 -------------------------------LNKMGAH------------------LVMADKQ-SSHFK------TLKET 449
Cdd:TIGR02169 549 lnnvvveddavakeaiellkrrkagratflpLNKMRDErrdlsilsedgvigfavdLVEFDPKyEPAFKyvfgdtLVVED 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 450 AEGSRRRAI------------EQCNEMVARIRGLEASLENQRKVEQELEMVKAEnvrqakkIEFMKEEIqETHLDYREEL 517
Cdd:TIGR02169 629 IEAARRLMGkyrmvtlegelfEKSGAMTGGSRAPRGGILFSRSEPAELQRLRER-------LEGLKREL-SSLQSELRRI 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 518 SKLAKGGGSHEADSQRdsELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAEAIEKIEEFKRNWHSSR 597
Cdd:TIGR02169 701 ENRLDELSQELSDASR--KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 598 EAGERL-------QLEAKENEEKVLKVEEELQEKRLEVLEKEE-----LVNYLQSQINTKQTKQPKL-SRRSTLMSTISE 664
Cdd:TIGR02169 779 EALNDLearlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLnrltlEKEYLEKEIQELQEQRIDLkEQIKSIEKEIEN 858
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 17536671 665 VDTstyvreveEVRALEEQREELQAYLAEKRK-MADLQKSRS 705
Cdd:TIGR02169 859 LNG--------KKEELEEELEELEAALRDLESrLGDLKKERD 892
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
36-653 |
6.57e-17 |
|
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: 86.23 E-value: 6.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 36 QEDLKTRLLEAENIiQDLRSERDALHESLVDKAGLNESVIIERSNKVSTQETRIYR--RDVTLLEDDLKQKESQIRILQN 113
Cdd:TIGR04523 46 KNELKNKEKELKNL-DKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKlnSDLSKINSEIKNDKEQKNKLEV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 114 RCLRLETEKQKMQDTISGYQEDL--KENEI------------RIENLNSRLHKLEDELSAKTHEIFSIGEELKNKTMKL- 178
Cdd:TIGR04523 125 ELNKLEKQKKENKKNIDKFLTEIkkKEKELeklnnkyndlkkQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLs 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 179 -----NEKNSQFQTKLAEISSENRNLERKVQKFREELIVKDQRSLEVHQDQENT-QKVLKEVKQLSDrldyltpKRKDVS 252
Cdd:TIGR04523 205 nlkkkIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLkDEQNKIKKQLSE-------KQKELE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 253 RIKerddflqfsaKIIEETMSELKLKNARLERELSEKEE-LVKVTKEELQELQKTVTQA---MGDSEQATKYLHAENMKL 328
Cdd:TIGR04523 278 QNN----------KKIKELEKQLNQLKSEISDLNNQKEQdWNKELKSELKNQEKKLEEIqnqISQNNKIISQLNEQISQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 329 TRQKADIRCDLLEARRNLKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRvagYEVL 408
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQE---KELL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 409 RRDHEAVKNELAKAEEKLNKMgahlvmaDKQSSHFKTLKETAEGSRRRAIEQCNEMVARIRGLEASLENQRK----VEQE 484
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDL-------TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKelksKEKE 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 485 LEMVKAENVRQAKKIEFMKEEIQEThLDYREELSKLAKgggsheadsQRDSELRSAKKTIQEVKADNKKLQqiLEEVRQN 564
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSL-KEKIEKLESEKK---------EKESKISDLEDELNKDDFELKKEN--LEKEIDE 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 565 QSKvleenvklrkgmaeaieKIEEFKRNWHSSREAGERLQLEAKEneekvlkVEEELQEKRLEVLEKEELVNYLQSQINT 644
Cdd:TIGR04523 566 KNK-----------------EIEELKQTQKSLKKKQEEKQELIDQ-------KEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
....*....
gi 17536671 645 KQTKQPKLS 653
Cdd:TIGR04523 622 AKKENEKLS 630
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
80-586 |
2.32e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 84.73 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 80 NKVSTQETRIYR--RDVTLLEDDLKQKESQIRILQNRCLRLET----------EKQKMQDTISGYQEDLKENEIRIENLN 147
Cdd:PRK03918 193 ELIKEKEKELEEvlREINEISSELPELREELEKLEKEVKELEElkeeieelekELESLEGSKRKLEEKIRELEERIEELK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 148 SRLHKLEDelsaKTHEIFSIgEELKNKTMKLNEKNSQFQTKLAEISSENRNLERKVQKFREELivkdqrslevhQDQENT 227
Cdd:PRK03918 273 KEIEELEE----KVKELKEL-KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI-----------KELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 228 QKVLKEVKQLSDRLdyltpkRKDVSRIKERDDFLQfSAKIIEETMSELKLKNARLERELSEKE-ELVKVTKEELQELQKT 306
Cdd:PRK03918 337 EERLEELKKKLKEL------EKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 307 VTQAMGDSEQATKYLHAENMKLtrQKADIRC---------------------DLLEARRNLKGFDEKREELEKQRDE--- 362
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIEEL--KKAKGKCpvcgrelteehrkelleeytaELKRIEKELKEIEEKERKLRKELRElek 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 363 ALEDVRRITELK------KNVEIELRSLKL--------LAEEREEQIDELKSRVAGYEVLRRDHEAVKNELAKAEEKLNK 428
Cdd:PRK03918 488 VLKKESELIKLKelaeqlKELEEKLKKYNLeelekkaeEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 429 MGAHLVMADKQSSH--FKTLKETAE--GSRRRAIEQCNEMVARIRGLEASLENQRKVEQELEMVKAENVRQAKKIEFMKE 504
Cdd:PRK03918 568 LEEELAELLKELEElgFESVEELEErlKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 505 EIQETHLDYREE-----------LSKLAKG--GGSHEADSQRDS------ELRSAKKTIQEVKADNKKLQQILEEVRQNQ 565
Cdd:PRK03918 648 ELEELEKKYSEEeyeelreeyleLSRELAGlrAELEELEKRREEikktleKLKEELEEREKAKKELEKLEKALERVEELR 727
|
570 580
....*....|....*....|.
gi 17536671 566 SKVLEENVKLRKGMAEAIEKI 586
Cdd:PRK03918 728 EKVKKYKALLKERALSKVGEI 748
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
34-699 |
4.78e-16 |
|
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: 83.96 E-value: 4.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 34 ESQEDLKTRLLEAENIIQDLRSERDALHESLVDKAGLNESvIIERSNKVSTQETRIYRRDVTLLEDDLKQKESQIRILQN 113
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE-LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 114 RCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHE---IFSIGEELKNKTMKLNEKNSQFQTKLA 190
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEledLRAELEEVDKEFAETRDELKDYREKLE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 191 EISSENRNLERKVQKFREELIVKDQRSLEVHQD----QENTQKVLKEVKQLSDRLDYLTPKRKDVS--RIKERDDFLQFS 264
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAiagiEAKINELEEEKEDKALEIKKQEWKLEQLAadLSKYEQELYDLK 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 265 AKI--IEETMSELKLKNARLERELSEKE-------------------------ELVKVtKEELQ---------ELQKTVT 308
Cdd:TIGR02169 476 EEYdrVEKELSKLQRELAEAEAQARASEervrggraveevlkasiqgvhgtvaQLGSV-GERYAtaievaagnRLNNVVV 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 309 QAMGDSEQATKYLHAEN------MKLTRQKADIRCDLLEARR-------NLKGFDEKREELEKQ--RD----EALEDVRR 369
Cdd:TIGR02169 555 EDDAVAKEAIELLKRRKagratfLPLNKMRDERRDLSILSEDgvigfavDLVEFDPKYEPAFKYvfGDtlvvEDIEAARR 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 370 ITELKKNVEIE----------------LRSLKLLAEEREEQIDELKSRVAGyevLRRDHEAVKNELAKAEEKLNKMGAHL 433
Cdd:TIGR02169 635 LMGKYRMVTLEgelfeksgamtggsraPRGGILFSRSEPAELQRLRERLEG---LKRELSSLQSELRRIENRLDELSQEL 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 434 VMADKQSSHFKTLKETAEGSRRRAIEQcnemvarirgLEASLENQRKVEQELEMVKAENVRQAKKIEFMKEEIQEthldY 513
Cdd:TIGR02169 712 SDASRKIGEIEKEIEQLEQEEEKLKER----------LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK----L 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 514 REELSKLAkgggsheaDSQRDSELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAEAIEKIEEFKRNW 593
Cdd:TIGR02169 778 EEALNDLE--------ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 594 HSSREAGE--RLQLEAKENEEKVLKVEEELQEKRLEVLEKE------------ELVNYLQSQINTKQTKQPKL-SRRSTL 658
Cdd:TIGR02169 850 KSIEKEIEnlNGKKEELEEELEELEAALRDLESRLGDLKKErdeleaqlreleRKIEELEAQIEKKRKRLSELkAKLEAL 929
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 17536671 659 MSTISEVDTSTY--VREVEEVRALEEQREELQAYLAEKRKMAD 699
Cdd:TIGR02169 930 EEELSEIEDPKGedEEIPEEELSLEDVQAELQRVEEEIRALEP 972
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
90-697 |
5.15e-16 |
|
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: 83.95 E-value: 5.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 90 YRRDVTLLEDDLKQKESQIRILQNRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIfsigE 169
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL----E 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 170 ELKNKTMKLNEKNSQFQTKLAEISSENRNLERKVQKFREELIVKDQRSLEVHQDQENTQK----VLKEVKQLSDRLDYLt 245
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaqLELQIASLNNEIERL- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 246 pkRKDVSRIKERDDFLQFSAKIIEETMSELKLKnaRLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLHAEN 325
Cdd:TIGR02168 406 --EARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 326 MKLTRQKAdiRCDLLEA-RRNLKGFDEKREELEKQRDEALEDVRRITEL-------KKNVEIELRS-LKLLAEEREEQ-- 394
Cdd:TIGR02168 482 RELAQLQA--RLDSLERlQENLEGFSEGVKALLKNQSGLSGILGVLSELisvdegyEAAIEAALGGrLQAVVVENLNAak 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 395 --IDELK------------SRVAGYEVLRRDHEAVKN---------ELAKAEEKLNK----MGAHLVMAD--------KQ 439
Cdd:TIGR02168 560 kaIAFLKqnelgrvtflplDSIKGTEIQGNDREILKNiegflgvakDLVKFDPKLRKalsyLLGGVLVVDdldnalelAK 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 440 SSHFKTLKETAEG---------------------SRRRAIEQCNEMVARIRGLEASLENQRK-VEQELEMVKaENVRQAK 497
Cdd:TIGR02168 640 KLRPGYRIVTLDGdlvrpggvitggsaktnssilERRREIEELEEKIEELEEKIAELEKALAeLRKELEELE-EELEQLR 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 498 KIEfmkEEIQETHLDYREELSKLAKGGGSHEADSQR-DSELRSAKKTIQEVKADNKKLQQILEEVRQNQSKV-------L 569
Cdd:TIGR02168 719 KEL---EELSRQISALRKDLARLEAEVEQLEERIAQlSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqieqlK 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 570 EENVKLRKGMAEAIEKIEEFKRNWHSSREAGERLQLEAKENEEKVLKVEEELQEKRLEVLEKEELVNYLQSQINTKQTKQ 649
Cdd:TIGR02168 796 EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 17536671 650 PKLSRRSTLMSTISEVDTSTYVREVEEVRALEEQREELQAYLAEKRKM 697
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
36-706 |
6.00e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.45 E-value: 6.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 36 QEDLKTRLLE-AENIIQDLRSERDALHEslvdKAGLNESVIIERSNKVSTQETRIyrrdvTLLEDDLKQKESQIRILQNR 114
Cdd:COG1196 219 KEELKELEAElLLLKLRELEAELEELEA----ELEELEAELEELEAELAELEAEL-----EELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 115 CLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIfsigEELKNKTMKLNEKNSQFQTKLAEISS 194
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL----EELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 195 ENRNLERKVQKFREELIVKDQRSLEVHQDQENTQKVLKEVKQLSDRLdyltpkrkdvsrikerddflqfsakiiEETMSE 274
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL---------------------------LERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 275 LKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKyLHAENMKLTRQKADIRCDLLEARRNLKGFDEKRE 354
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE-LLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 355 ELEKQRDEALEDVRRITELKKNVEIElRSLKLLAEEREEQIDELKSRVAGYEVLRRDHEAVKNELAKAEEKLNKMGAhlv 434
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLA-GAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGR--- 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 435 madkqsSHFKTLKETAEGSRRRAIEQCNEMVARIRGLEASLENQRKVEQELEMVKAENVRQAKKIEFMKEEIQETHLDYR 514
Cdd:COG1196 574 ------ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 515 EElskLAKGGGSHEADSQRDSELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAEAIEKIEEfkrnwh 594
Cdd:COG1196 648 EV---TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE------ 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 595 ssreagERLQLEAKENEEKVLKVEEELQEKRLEVLEKEELVNYLQSQINTKQTKQpKLSRRSTLMSTISEVDtstyvrev 674
Cdd:COG1196 719 ------EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER-ELERLEREIEALGPVN-------- 783
|
650 660 670
....*....|....*....|....*....|....
gi 17536671 675 eeVRALEEQREELQ--AYLAEKRkmADLQKSRST 706
Cdd:COG1196 784 --LLAIEEYEELEEryDFLSEQR--EDLEEARET 813
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
117-707 |
1.05e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.88 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 117 RLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIFSIGEELKNKTMKLNEKNSQFQtKLAEISSEN 196
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD-EAKKKAEEA 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 197 RNLERKVQKFREELIVKDQRSLEVHQDQENTQKVLKEVKQLSDRLDYLTPKRKDVSRIKERDDFLQFSAKiieetmseLK 276
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK--------KK 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 277 LKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLHAENMKltrQKADIRCDLLEARrnlKGFDEKR--E 354
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK---KKAEEAKKADEAK---KKAEEAKkaE 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 355 ELEKQRDEAledvRRITELKKNVEIELRS--LKLLAEEREEQIDELKSRVAG---YEVLRRDHEAVK-NELAKAEEKLNK 428
Cdd:PTZ00121 1461 EAKKKAEEA----KKADEAKKKAEEAKKAdeAKKKAEEAKKKADEAKKAAEAkkkADEAKKAEEAKKaDEAKKAEEAKKA 1536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 429 MGAHLVMADKQSSHFKTLKETAEGSRRRAIEQcnemvarirgleaslenQRKVEQELEMV--KAENVRQAKKiefmkEEI 506
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEE-----------------AKKAEEDKNMAlrKAEEAKKAEE-----ARI 1594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 507 QETHLDYREELSKLAKGGGSHEADSQRDSELRSA---KKTIQEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAEAI 583
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAeeeKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 584 EKIEEFKRNWHSSREAGERLQLEAKENEEKVLKVEEELQEKR-LEVLEKEELVNYLQSQINTKQTKQPKlsrrstlmsti 662
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKkAEELKKAEEENKIKAEEAKKEAEEDK----------- 1743
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 17536671 663 sevdtstyvREVEEVRALEEQREELQAYLAEKRKMADLQKSRSTA 707
Cdd:PTZ00121 1744 ---------KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
169-564 |
1.46e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 82.41 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 169 EELKNKTMKLNEKNSQFQTKLAEISSENRNLERKVQKFREELIVKDQrslEVHQDQENTQKVLKEVKQLSDRLDyltpkr 248
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR---QISALRKDLARLEAEVEQLEERIA------ 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 249 kdvsrikerddflqfsakIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLHAENMKL 328
Cdd:TIGR02168 751 ------------------QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 329 TRQKADIRcdllEARRNLKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRVAGYEV- 407
Cdd:TIGR02168 813 TLLNEEAA----NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEa 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 408 ---LRRDHEAVKNELAKAEEKLNKMGAHLVMADKQSSHFKTLKETAEGSRRRAIEQCNEmvarirGLEASLENQRKVEQE 484
Cdd:TIGR02168 889 lalLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE------EYSLTLEEAEALENK 962
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 485 LEMVKAENVRQAKKIEFMKEEIQETHLDYREELSKLAKgggSHEADSQRDSELRSAKKTIQEVKAD-----NKKLQQILE 559
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKE---RYDFLTAQKEDLTEAKETLEEAIEEidreaRERFKDTFD 1039
|
....*
gi 17536671 560 EVRQN 564
Cdd:TIGR02168 1040 QVNEN 1044
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
166-703 |
2.00e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.11 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 166 SIGEELKNKTMKLNEKNSQFQTKLAEISSENRNLERK---VQKFREELIVKDQRSLEVHQDQENTQKVLKEVKQLSDRLD 242
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKaedARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKA 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 243 YLTPKRKDVSRIKERDDFLQF-SAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYL 321
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKAEEVrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 322 HAENMKLTRQKADIRCDLLEARRNLKGFDEKR--EELEKQrdealEDVRRITELKKNVEI-ELRSLKLLAEEREEQiDEL 398
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARkaDELKKA-----EEKKKADEAKKAEEKkKADEAKKKAEEAKKA-DEA 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 399 KSRVagyEVLRRDHEAVKNelaKAEEKLNKMGAHLVMADKQSSHFKTLKETAEGSRRRAieqcnemvarirgleaslENQ 478
Cdd:PTZ00121 1321 KKKA---EEAKKKADAAKK---KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK------------------EEA 1376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 479 RKVEQELEMvKAENVRQAKKIEFMKEEIQEThldyREELSKLAKGGGSHEADSQRDSELRSA----KKTIQEVKADnkKL 554
Cdd:PTZ00121 1377 KKKADAAKK-KAEEKKKADEAKKKAEEDKKK----ADELKKAAAAKKKADEAKKKAEEKKKAdeakKKAEEAKKAD--EA 1449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 555 QQILEEVRQnqskvlEENVKLRkgmAEAIEKIEEFKRNWHSSREAgERLQLEAKENEEKVLKVEEELQEKRlevleKEEL 634
Cdd:PTZ00121 1450 KKKAEEAKK------AEEAKKK---AEEAKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAAEAKK-----KADE 1514
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17536671 635 VNYLQSQINTKQTKQPKLSRRSTLMSTISEVDTSTYVREVEEVRALEEQREELQAYLAEKRKMADLQKS 703
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
29-425 |
1.26e-14 |
|
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: 78.91 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 29 IDLNNESQEDLKTRLLEAENIIQDLRSERDALHESLVDKAglNEsviIERSNKVSTQetriyrrdvtlLEDDLKQKESQI 108
Cdd:TIGR04523 234 IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ--KE---LEQNNKKIKE-----------LEKQLNQLKSEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 109 RILQNrclrletekQKMQDTISGYQEDLK--------------ENEIRIENLNSRLHKLEDELSAKTHEIFSIGEELKNK 174
Cdd:TIGR04523 298 SDLNN---------QKEQDWNKELKSELKnqekkleeiqnqisQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 175 TMKLNEKNSQFQTKLAEI---SSENRNLERKVQKFREELIVKDQRsleVHQDQENTQKVLKEVKQL-----------SDR 240
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIknlESQINDLESKIQNQEKLNQQKDEQ---IKKLQQEKELLEKEIERLketiiknnseiKDL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 241 LDYLTPKRKDVSRIKERDDFLQFSAKIIEETMSELKLKNARLERELSEKE-ELVKVTKE--ELQELQKTVTQAMGDSEQA 317
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEkELKKLNEEkkELEEKVKDLTKKISSLKEK 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 318 TKYLHAENMKLTRQKADIRCDLLEarrnlKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDE 397
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELNK-----DDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
410 420
....*....|....*....|....*...
gi 17536671 398 LKSRVAGYEVLRrdhEAVKNELAKAEEK 425
Cdd:TIGR04523 601 LIKEIEEKEKKI---SSLEKELEKAKKE 625
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
152-604 |
2.02e-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: 78.56 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 152 KLEDELSAKTHEIFSIGEELKNKTmKLNEKNSQFQTKLAEIsseNRNLERkVQKFREELivkdQRSLEVHQDQ-ENTQKV 230
Cdd:TIGR02168 145 KISEIIEAKPEERRAIFEEAAGIS-KYKERRKETERKLERT---RENLDR-LEDILNEL----ERQLKSLERQaEKAERY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 231 LKEVKQLSD-RLDYLtpkrkdVSRIKERDDFLQFSAKIIEETMSELKlknaRLERELSEKEELVKVTKEELQELQKTVTQ 309
Cdd:TIGR02168 216 KELKAELRElELALL------VLRLEELREELEELQEELKEAEEELE----ELTAELQELEEKLEELRLEVSELEEEIEE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 310 AMGDSEQATKYLHaenmKLTRQKADIRCDLLEARRNLKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAE 389
Cdd:TIGR02168 286 LQKELYALANEIS----RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 390 EREEQIDELKSRVAGyevLRRDHEAVKNELAKAEEKLNKMGAHLVMADKQsshfktlKETAEGSRRRAIEQcnemvarIR 469
Cdd:TIGR02168 362 ELEAELEELESRLEE---LEEQLETLRSKVAQLELQIASLNNEIERLEAR-------LERLEDRRERLQQE-------IE 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 470 GLEASLENQRKVEQElemvkaenvRQAKKIEFMKEEIQETHLDYREELSKLAkgggshEADSQRDSELRSAKKTIQEVKA 549
Cdd:TIGR02168 425 ELLKKLEEAELKELQ---------AELEELEEELEELQEELERLEEALEELR------EELEEAEQALDAAERELAQLQA 489
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 550 DNKKLQQILEEVRQNQ---SKVLEENVKLRKGMAEAIEKIeEFKRNWHSSREA--GERLQ 604
Cdd:TIGR02168 490 RLDSLERLQENLEGFSegvKALLKNQSGLSGILGVLSELI-SVDEGYEAAIEAalGGRLQ 548
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
29-588 |
5.09e-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: 77.40 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 29 IDLNNESQEDLKTRLLEAENIIQDLRSERDALHESLVDKAGLNEsviiERSNKVSTQETRI--YRRDVTLLEDDLKQKES 106
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE----ELESRLEELEEQLetLRSKVAQLELQIASLNN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 107 QIRILQNRCLRLETEKQKMQDTISGYQEDLKENEI-----RIENLNSRLHKLEDELSAKTHEIFSIGEELKNKTMKLNEK 181
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAELkelqaELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 182 NSQFQTKLAEISSENRNLERKVQKFREELIVKDQRS------------LEVHQDQE-----------------NTQKVLK 232
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgilgvlselISVDEGYEaaieaalggrlqavvveNLNAAKK 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 233 EVKQLS------------DRLDYLTPKRKDVSRIKERDDFLQfSAKIIEETMSELKL----------------------- 277
Cdd:TIGR02168 561 AIAFLKqnelgrvtflplDSIKGTEIQGNDREILKNIEGFLG-VAKDLVKFDPKLRKalsyllggvlvvddldnalelak 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 278 -----------------------------KNARLER--ELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLHaenm 326
Cdd:TIGR02168 640 klrpgyrivtldgdlvrpggvitggsaktNSSILERrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELE---- 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 327 KLTRQKADIRCDLLEARRNLKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRVAGYE 406
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK 795
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 407 ----VLRRDHEAVKNELAKAEEKLNKMGAHLVMADKQSSHFKTLKETAEGSRRRAIEQCNEMVARIRGLEASLENQRKVE 482
Cdd:TIGR02168 796 eelkALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 483 QELEMVKAENVRQAKKIEFMKEEIQETHLDYREELSKLakgggSHEADSQRDsELRSAKKTIQEVKAdnkKLQQILEEVR 562
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELRELESKRSEL-----RRELEELRE-KLAQLELRLEGLEV---RIDNLQERLS 946
|
650 660
....*....|....*....|....*.
gi 17536671 563 QNQSKVLEENVKLRKGMAEAIEKIEE 588
Cdd:TIGR02168 947 EEYSLTLEEAEALENKIEDDEEEARR 972
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
116-503 |
1.31e-13 |
|
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: 75.87 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 116 LRLETEKQKMQDTISGYQEDLKeneiRIENLNSRLHKLEDELSAKTHEIFSIGEELKNKTMKLNEKNSQFQTKLAEISSE 195
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELR----RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 196 NRNLERKVQKFREELivkDQRSLEVHQDQEntqkvlkEVKQLSDRLDYltpkrkdvSRIKERDDFLQFsakiIEETMSEL 275
Cdd:TIGR02169 753 IENVKSELKELEARI---EELEEDLHKLEE-------ALNDLEARLSH--------SRIPEIQAELSK----LEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 276 KLKNARLERELSEKEELVKVTKEELQELQktvtQAMGDSEQATKYLHAENMKLTRQKADIRCDLLEARRNLKGFDEKREE 355
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQ----EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 356 LEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRVAGYE-VLRRDHEAVKNELA--KAEEKLNKMGAH 432
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEdPKGEDEEIPEEELSleDVQAELQRVEEE 966
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17536671 433 LvmadkqsshfktlkETAEGSRRRAIEQCNEMVARIRGLE---ASLENQRKVEQELemvkAENVRQAKKIEFMK 503
Cdd:TIGR02169 967 I--------------RALEPVNMLAIQEYEEVLKRLDELKekrAKLEEERKAILER----IEEYEKKKREVFME 1022
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
101-730 |
4.80e-13 |
|
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: 74.24 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 101 LKQKESQIRILQNRCLRLETEKQKmqdtisgyqEDLKENEIRIENLNSRLHKLEDELSAKTHEIFSIGEELKNKTMKLNE 180
Cdd:pfam02463 178 LIEETENLAELIIDLEELKLQELK---------LKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 181 KNSQFQTKLAEISSENRNLERKVQKFREEL-IVKDQRSLEVHQDQENTQKVLKEVKQLSDRLDYLTPKRKDVSRIKERDD 259
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEkEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 260 FLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLHAENMKLTRQKADIRCDL 339
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 340 LEARRNLKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRVAGYE----VLRRDHEAV 415
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKetqlVKLQEQLEL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 416 KNELAKAEEKLNKMGAHLVMAD--------------KQSSHFKTLKETAEGSRRRAIE------------QCNEMVARIR 469
Cdd:pfam02463 489 LLSRQKLEERSQKESKARSGLKvllalikdgvggriISAHGRLGDLGVAVENYKVAIStavivevsatadEVEERQKLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 470 GLEASLENQRKVEQELEMVKAENVRQAKKIEF--MKEEIQETHLDYREELSKLAKGGGSHEADSQRDSELRSAKKTIQEV 547
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLPLKSIAVLEIDpiLNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGL 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 548 KADNKKLQQILEEVRQNQSKVLEENVKLRKGMAEAIEKIEEFKRNWHSSREAGERLQLEAKENEEKVLKVEEELQEKRLE 627
Cdd:pfam02463 649 RKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQ 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 628 VLE---KEELVNYLQSQINTKQTKQPKLSRRSTLMSTISEVDTSTYVREVEEVRAlEEQREELQAYLAEKRKMADLQKSR 704
Cdd:pfam02463 729 EAQdkiNEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKT-EKLKVEEEKEEKLKAQEEELRALE 807
|
650 660
....*....|....*....|....*.
gi 17536671 705 STANTTTLITSTTATEVSKSACELSY 730
Cdd:pfam02463 808 EELKEEAELLEEEQLLIEQEEKIKEE 833
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-693 |
8.78e-13 |
|
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: 73.17 E-value: 8.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 27 QVIDLNNESQEDLKTRLLEAENIIQDLRSERDALHESLVDKAGLNESVIIERSNKvsTQETRIYRRDVTLLEDDLKQKES 106
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL--EQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 107 QIRILQNRCLRLETEKQKMQDTISGYQED-------LKENEIRIENLNSRLHKLEDELSAKTHEIFSIGEELK--NKTMK 177
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEElesleaeLEELEAELEELESRLEELEEQLETLRSKVAQLELQIAslNNEIE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 178 LNEK-----NSQFQTKLAEISSENRNLER-KVQKFREELIVKDQRSLEVHQDQENTQKVLKEVKQLSDRLDY-LTPKRKD 250
Cdd:TIGR02168 404 RLEArlerlEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQaLDAAERE 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 251 VSRIKERDDFLQF---SAKIIEETMSELKLKNARLERELSEKEELVKVTKE-------ELQE-LQKTVTQAMGDSEQATK 319
Cdd:TIGR02168 484 LAQLQARLDSLERlqeNLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyeaaieaALGGrLQAVVVENLNAAKKAIA 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 320 YLHAEN------MKLTRQK-ADIRCDLLEARRNLKGFDEKREELEKQR--------------------DEALEDVRRITE 372
Cdd:TIGR02168 564 FLKQNElgrvtfLPLDSIKgTEIQGNDREILKNIEGFLGVAKDLVKFDpklrkalsyllggvlvvddlDNALELAKKLRP 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 373 LKKNV---------------------------EIELRSLKLLAEEREEQIDELKSRVAgyeVLRRDHEAVKNELAKAEEK 425
Cdd:TIGR02168 644 GYRIVtldgdlvrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEKALA---ELRKELEELEEELEQLRKE 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 426 LNKMGAHLVMADKQSSHFKTLKETAEGSRRRAIEQCNEMVARIRGLEASLEnqrKVEQELEMVKAENVRQAKKIEFMKEE 505
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE---EAEEELAEAEAEIEELEAQIEQLKEE 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 506 IQ---ETHLDYREELSKLAKGGGSHEADSQR-DSELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAE 581
Cdd:TIGR02168 798 LKalrEALDELRAELTLLNEEAANLRERLESlERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 582 AIEKIEEFKRNWHSSREAGERLQLEAKENEEKVLKVEEELQEKRLEVLEKEELVNYLQSQINTKQtkqpklSRRSTLMST 661
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ------ERLSEEYSL 951
|
730 740 750
....*....|....*....|....*....|..
gi 17536671 662 ISEVDTSTYVREVEEVRALEEQREELQAYLAE 693
Cdd:TIGR02168 952 TLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
37-517 |
2.17e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.61 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 37 EDLKTRLLEAENIIQDLRSERDalheSLVDKAGLNE---SVIIERSNKVSTQETRIYRR-------------DVTLLEDD 100
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERD----DLLAEAGLDDadaEAVEARREELEDRDEELRDRleecrvaaqahneEAESLRED 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 101 LKQKESQIRILQNRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELsaktheifsigEELKNKTMKLNE 180
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDL-----------GNAEDFLEELRE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 181 KNSQFQTKLAEISSENRNLERKVQKFREELI----------VKDQRSLEVHQDQEntqkvlKEVKQLSDRLDYLTPKRKD 250
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEALLEagkcpecgqpVEGSPHVETIEEDR------ERVEELEAELEDLEEEVEE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 251 VSRIKERDDFLQFSAKIIEetmsELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAmgDSEqatkylhAENMKLTR 330
Cdd:PRK02224 494 VEERLERAEDLVEAEDRIE----RLEERREDLEELIAERRETIEEKRERAEELRERAAEL--EAE-------AEEKREAA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 331 QKADIRCDllEARRNLKGFDEKREELeKQRDEALEDVRRITELKKNVEIELRSLKllaeEREEQIDELksrvagyEVLRR 410
Cdd:PRK02224 561 AEAEEEAE--EAREEVAELNSKLAEL-KERIESLERIRTLLAAIADAEDEIERLR----EKREALAEL-------NDERR 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 411 DHEAVKNE-LAKAEEKLNkmGAHLVMADKQSSHFKTLKETAEGSRRRAIEQCNEMVARIRGLEASLENQRKVEQELEMVk 489
Cdd:PRK02224 627 ERLAEKRErKRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREAL- 703
|
490 500
....*....|....*....|....*...
gi 17536671 490 AENVRQAKKIEFMKEEIQETHLDYREEL 517
Cdd:PRK02224 704 ENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
27-400 |
2.44e-12 |
|
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: 71.59 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 27 QVIDLNNESQEdLKTRLLEAENIIQDLRSERDALHESLVDKaglnESVIIERSNKVSTQEtriyrRDVTLLEDDLKQKES 106
Cdd:TIGR04523 350 ELTNSESENSE-KQRELEEKQNEIEKLKKENQSYKQEIKNL----ESQINDLESKIQNQE-----KLNQQKDEQIKKLQQ 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 107 QIRILQNRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIFSIGEELKNKTMKLNEKNSQfq 186
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE-- 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 187 tkLAEISSENRNLERKVQKFREElivkdQRSLEVHQDQENTQKVLKEvKQLSDrldyltpKRKDVSRIKERDDFLQFSAK 266
Cdd:TIGR04523 498 --LKKLNEEKKELEEKVKDLTKK-----ISSLKEKIEKLESEKKEKE-SKISD-------LEDELNKDDFELKKENLEKE 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 267 I--IEETMSELKLKNARLERELSEKEELVKVTKEELQELQKtvtqamgdsEQATKylhaenmkltrqkadircdllearr 344
Cdd:TIGR04523 563 IdeKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK---------EIEEK------------------------- 608
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 17536671 345 nlkgfDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKS 400
Cdd:TIGR04523 609 -----EKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
119-486 |
3.09e-12 |
|
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: 71.64 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 119 ETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDEL--SAKTHEIFSIGEELKnKTMKLNEKNSqFQTKLAEISSEN 196
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekAERYQALLKEKREYE-GYELLKEKEA-LERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 197 RNLERKVQKFREELivkDQRSLEVHQdqentqkVLKEVKQLSDRLDYLTPKRKdvSRIKERDDFLQFSAKIIEETMSELK 276
Cdd:TIGR02169 247 ASLEEELEKLTEEI---SELEKRLEE-------IEQLLEELNKKIKDLGEEEQ--LRVKEKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 277 LKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQAT---KYLHAENMKLTRQKADIRCDLLEARRNLKGFDEKR 353
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTeeyAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 354 EELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRVagyevlrrdhEAVKNELAKAEEKLNKMGAHL 433
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK----------EDKALEIKKQEWKLEQLAADL 464
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 17536671 434 VMADKQSSHFKTLKETAEGSRRRAIEQCNEMVARIRGLEASLENQRKVEQELE 486
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLK 517
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
34-377 |
6.41e-12 |
|
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: 70.48 E-value: 6.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 34 ESQEDLKTRLLEAENIIQDLRSERDALhESLVDKAglnesviiERSNKVSTQETRIYRRDVTLLEDDLKQKESQIRilqn 113
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRI-ENRLDEL--------SQELSDASRKIGEIEKEIEQLEQEEEKLKERLE---- 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 114 rclRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSA-KTHEIFSIGEELKNKTMKLNEKNSQFQTKLAEI 192
Cdd:TIGR02169 741 ---ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 193 SS-------ENRNLERKVQKFREELIVKDQRSLEVHQDQENTQKVLKE-----------VKQLSDRLDYLTPKRKDV--- 251
Cdd:TIGR02169 818 EQklnrltlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEleeeleeleaaLRDLESRLGDLKKERDELeaq 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 252 -SRIKERDDFLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEE------LQELQKTVtQAMgdsEQATKYLHAE 324
Cdd:TIGR02169 898 lRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAEL-QRV---EEEIRALEPV 973
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 17536671 325 NMKLTRQKAdircdllEARRNLKGFDEKREELEKQRDEALEDVRRITELKKNV 377
Cdd:TIGR02169 974 NMLAIQEYE-------EVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
251-608 |
7.28e-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: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 251 VSRIKERddflqfsakiIEETmsELKLKNAR--LERE---LSEKEElvkvtkeELQELQKtvtQAmgdsEQATKYLhaen 325
Cdd:COG1196 167 ISKYKER----------KEEA--ERKLEATEenLERLediLGELER-------QLEPLER---QA----EKAERYR---- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 326 mKLTRQKadircDLLEARRNLKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRVAGY 405
Cdd:COG1196 217 -ELKEEL-----KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 406 EVLRRDHEAVKNELAKAEEKLNKMGAHLVMADKQSSHFKTLKETAEGSRRRAIEQCNEMVARIRGLEASLENQRKVEQEL 485
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 486 EMVKAENVRQAKKIEFMKEEIQETHLDYREELSKLAKG-GGSHEADSQRDSELRSAKKTIQEVKADNKKLQQILEEVRQN 564
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAeEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 17536671 565 QSKVLEENVKLRKGMAEAIEKIEEFKRNWHSSREAGERLQLEAK 608
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
97-654 |
8.28e-12 |
|
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: 69.66 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 97 LEDDLKQKESQIRILQNRCLRLETEKQKMQDTISGYQED-------LKENEIRIENLNSRLHKLEDELSAKTHEIFSIGE 169
Cdd:TIGR04523 45 IKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQikdlndkLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 170 ELKNKTMKLNEKNSQFQTKLAEISSENRNLERKVQKFREelIVKDQRSLEVHQDQENTQKVLKEVKQLSDRLDYLTpKRK 249
Cdd:TIGR04523 125 ELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND--LKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK-LEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 250 DVSRIKERDDflqfSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLHAENMKLT 329
Cdd:TIGR04523 202 LLSNLKKKIQ----KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 330 RQKADIRcdllEARRNLKGFDEKREELEKQRDEALedvrrITELK---KNVEIELRSLKLLAEEREEQIDELKSRVAGYE 406
Cdd:TIGR04523 278 QNNKKIK----ELEKQLNQLKSEISDLNNQKEQDW-----NKELKselKNQEKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 407 V----LRRDHEAVKNELAKAEEKLNKMGAHLVMADKQSSHFKTLKETAEGSRRRAIEQCNEMVARIRGLEaslENQRKVE 482
Cdd:TIGR04523 349 KeltnSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ---QEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 483 QELEMVKAENVRQAKKIEFMKEEIQETHLDYRE----------ELSKLAKGGGSHEADS-QRDSELRSAKKTIQEVKADN 551
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNldntresletQLKVLSRSINKIKQNLeQKQKELKSKEKELKKLNEEK 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 552 KKLQQILEEVRQNQSKVLEENVKLRKGMAEAIEKIEEFKRNWHSSREAGERLQLEA---------KENEEKVLKVEEELQ 622
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKeideknkeiEELKQTQKSLKKKQE 585
|
570 580 590
....*....|....*....|....*....|..
gi 17536671 623 EKRLEVLEKEELVNYLQSQINTKQTKQPKLSR 654
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
235-542 |
1.32e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 235 KQLSDRLdyltpKRKDVSRIKERDDFLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDS 314
Cdd:COG1196 216 RELKEEL-----KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 315 EQATKYLHAENMKLTRQKADIRcdllEARRNLKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLkllAEEREEQ 394
Cdd:COG1196 291 YELLAELARLEQDIARLEERRR----ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA---EAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 395 IDELKsrvagyEVLRRDHEAVKNELAKAEEKLNKMGAHLVMADKQSShfktLKETAEGSRRRAIEQCNEMVARIRGLEAS 474
Cdd:COG1196 364 EEALL------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEE----LEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17536671 475 LENQRKVEQELEMVKAENVRQAKKIEFMKEEIQETHLDYREELSKLAKGGGSHEADSQRDSELRSAKK 542
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
29-632 |
2.32e-11 |
|
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: 68.56 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 29 IDLNNESQEDLKTRLLEAENIIQDLRSERDALHESLVDKAGLNESV---IIERSNKVSTQETRIYRRDVTLLE--DDLKQ 103
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLteeYAELKEELEDLRAELEEVDKEFAEtrDELKD 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 104 KESQIRILQNRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIfsigEELKNKTMKLNEKNS 183
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI----KKQEWKLEQLAADLS 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 184 QFQTKLAEISSENRNLERKVQKFREELIVKDQRSLEVHQDQEN---TQKVLKE--------VKQL--------------- 237
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGgraVEEVLKAsiqgvhgtVAQLgsvgeryataievaa 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 238 SDRLDY-------------------------------LTPKRKDVSRIKERD------DFLQFSAK-------IIEETMS 273
Cdd:TIGR02169 546 GNRLNNvvveddavakeaiellkrrkagratflplnkMRDERRDLSILSEDGvigfavDLVEFDPKyepafkyVFGDTLV 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 274 ELKLKNAR----------LERELSEK-----------EELVKVTKEELQELQKtvtqaMGDSEQAtkyLHAENMKLTRQK 332
Cdd:TIGR02169 626 VEDIEAARrlmgkyrmvtLEGELFEKsgamtggsrapRGGILFSRSEPAELQR-----LRERLEG---LKRELSSLQSEL 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 333 ADIRCDLLEARRNLKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRVAGYEVlrrdh 412
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE----- 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 413 eavknELAKAEEKLNKMGAHLVMadkqsSHFKTLKETAEGSRrraiEQCNEMVARIRGLEASLENQRKVEQELEMVKAEN 492
Cdd:TIGR02169 773 -----DLHKLEEALNDLEARLSH-----SRIPEIQAELSKLE----EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 493 VRQA------------------KKIEFMKEEIQETHL---DYREELSKLAKgggsheADSQRDSELRSAKKTIQEVKADN 551
Cdd:TIGR02169 839 QEQRidlkeqiksiekeienlnGKKEELEEELEELEAalrDLESRLGDLKK------ERDELEAQLRELERKIEELEAQI 912
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 552 KKLQQILEEVRQNQSKVLEENVKLRKGMAE---------AIEKIEEFKRNWHSSREAGERLQLEAKENEEKVLKVEEELQ 622
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELK 992
|
730
....*....|
gi 17536671 623 EKRlEVLEKE 632
Cdd:TIGR02169 993 EKR-AKLEEE 1001
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
232-689 |
3.13e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.14 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 232 KEVKQLSDRLDYLTPKRKDVSRIKERDDFLQFSAK---------------------IIEETMSELKLKNARLERELSEKE 290
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEEQREQARetrdeadevleeheerreeleTLEAEIEDLRETIAETEREREELA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 291 ELVKVTKEELQELQKTVTQAMGDSE---QATKYLHAENMKLTRQKADIRCDLLEAR-------RNLKGFDEKREELEKQR 360
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRvaaqahnEEAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 361 DEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRVAGYEVLRRD----HEAVKNELAKAEEKLNKMGAHLVMA 436
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNaedfLEELREERDELREREAELEATLRTA 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 437 DKQSSHFKTLKETA---------EGSRR-RAIEQCNEMVARIRGLEASLENQR-KVEQELEMVKaENVRQAKKIEFMKE- 504
Cdd:PRK02224 439 RERVEEAEALLEAGkcpecgqpvEGSPHvETIEEDRERVEELEAELEDLEEEVeEVEERLERAE-DLVEAEDRIERLEEr 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 505 --------EIQETHLDYREE-LSKLAKGGGSH--EADSQRD--SELRS-AKKTIQEVKADNKKLQQILEEVRQNQSkvLE 570
Cdd:PRK02224 518 redleeliAERRETIEEKRErAEELRERAAELeaEAEEKREaaAEAEEeAEEAREEVAELNSKLAELKERIESLER--IR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 571 ENVKLRKGMAEAIEKIEEfKRNWHSSREAGERLQLEAKenEEKVLKVEEELQEKRLEVL--EKEELVNYLQsqiNTKQTK 648
Cdd:PRK02224 596 TLLAAIADAEDEIERLRE-KREALAELNDERRERLAEK--RERKRELEAEFDEARIEEAreDKERAEEYLE---QVEEKL 669
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 17536671 649 QPKLSRRSTLMSTISEVDtstyvREVEEVRALEEQREELQA 689
Cdd:PRK02224 670 DELREERDDLQAEIGAVE-----NELEELEELRERREALEN 705
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
123-598 |
5.66e-11 |
|
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: 67.17 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 123 QKMQDTISGYQEDLKENEIRIENLnSRLHK--LEDE-LSAKTHEIFSigEELKNKTMKLNEKNSQFQTKLAEISSENRNL 199
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLESAELRL-SHLHFgyKSDEtLIASRQEERQ--ETSAELNQLLRTLDDQWKEKRDELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 200 ERKVQKFREELIVKDQRSL--------EVHQDQENTQKVLKEVKQLSDRLDYLTPKRKDVSRIKERddflqFSAKIIEET 271
Cdd:pfam12128 314 DAAVAKDRSELEALEDQHGafldadieTAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNR-----RRSKIKEQN 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 272 MSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGD-----SEQATKY-LHAENMKLTRQKADIRCDLLEARRN 345
Cdd:pfam12128 389 NRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAgklefNEEEYRLkSRLGELKLRLNQATATPELLLQLEN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 346 ----LKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELK---------------------- 399
Cdd:pfam12128 469 fderIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELElqlfpqagtllhflrkeapdwe 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 400 ---SRVAGYEVLRR----------------------------DH-------EAVKNELAKAEEKLN-----------KMG 430
Cdd:pfam12128 549 qsiGKVISPELLHRtdldpevwdgsvggelnlygvkldlkriDVpewaaseEELRERLDKAEEALQsarekqaaaeeQLV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 431 AHLVMADKQSSHFKTLKETAEGSRRRAIEQCNEMVARIRGLEASL-ENQRKVEQELEMVKAENVRQAKKIEFMKEEIQET 509
Cdd:pfam12128 629 QANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALaERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQ 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 510 HLDYREELSKLAKgggshEADSQRDSELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVL----EENVKLRKGMAEAIEK 585
Cdd:pfam12128 709 KREARTEKQAYWQ-----VVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdpDVIAKLKREIRTLERK 783
|
570
....*....|...
gi 17536671 586 IEEFKRNWHSSRE 598
Cdd:pfam12128 784 IERIAVRRQEVLR 796
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
85-446 |
2.90e-10 |
|
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: 65.09 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 85 QETRIYRRDVTLLEDDLKQKESQIRILQNRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEI 164
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 165 FSIGEELKNKTMKLNEknSQFQTKLAEISSenrnLERKVQKFREELIVKDQRSLEVHQDQENTQkvlKEVKQLSDRLDYL 244
Cdd:TIGR02169 775 HKLEEALNDLEARLSH--SRIPEIQAELSK----LEEEVSRIEARLREIEQKLNRLTLEKEYLE---KEIQELQEQRIDL 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 245 TPKRKDvsrikerddflqfsakiIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLhaE 324
Cdd:TIGR02169 846 KEQIKS-----------------IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI--E 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 325 NMKLTRQKADIRCDLLEARRNLKGFDEKREELEKQRD----EALEDVRRITELKKNVEIELRSLK---LLA-EEREEQID 396
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipEEELSLEDVQAELQRVEEEIRALEpvnMLAiQEYEEVLK 986
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 17536671 397 ELKSRVAGYEVLRRDHEAVKNELAKAEEKlnKMGAHLVMADKQSSHFKTL 446
Cdd:TIGR02169 987 RLDELKEKRAKLEEERKAILERIEEYEKK--KREVFMEAFEAINENFNEI 1034
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
11-610 |
3.38e-10 |
|
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: 64.74 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 11 SSKTPKSKSARYSSPYQVIDLNNESQ------EDLKtrlLEAENIIQDLRSERDALHESLVDKAGLNESVIIERSNKVS- 83
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNNIEkmilafEELR---VQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSl 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 84 ----TQETRIYRRDVTLLEDDLKQKESQIR---ILQNRCLRLETEKQkmqDTISGYQEDLKeneIRIENLNSRLHKLEDE 156
Cdd:pfam05483 245 lliqITEKENKMKDLTFLLEESRDKANQLEektKLQDENLKELIEKK---DHLTKELEDIK---MSLQRSMSTQKALEED 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 157 LSAKTHEIFSIGEELKNKTMKLNEKNSQFQTKLAEISSENRNLErkvqkfreELIVKDQRSLEVHQDQEN--TQKVLKEV 234
Cdd:pfam05483 319 LQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE--------ELLRTEQQRLEKNEDQLKiiTMELQKKS 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 235 KQLSDRLDYLTPKRKDVSRIKE---RDDFLQFSAKIIEETMSELKLKNARL-------ERELSEKEELVKVTKEELQELQ 304
Cdd:pfam05483 391 SELEEMTKFKNNKEVELEELKKilaEDEKLLDEKKQFEKIAEELKGKEQELifllqarEKEIHDLEIQLTAIKTSEEHYL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 305 KTVTQAMGDSEQA----------TKYLHAENMKLTRQKADIRCDLlearrnlKGFDEKREELEKQRDEALEDVRRITELK 374
Cdd:pfam05483 471 KEVEDLKTELEKEklknieltahCDKLLLENKELTQEASDMTLEL-------KKHQEDIINCKKQEERMLKQIENLEEKE 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 375 KNVEIELRSLKllaEEREEQIDELKSRVAGYEVLRRDHEAVKNELAKAEEKLNKMGAHL-VMADKQSSHFKTLKETAEGS 453
Cdd:pfam05483 544 MNLRDELESVR---EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLkKQIENKNKNIEELHQENKAL 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 454 RRRAI---EQCNEMVARIRGLEASLENQRKveqelemvKAENVRQAKKIEFMKEEIQETHLdyREELSKlAKGGGSHEAD 530
Cdd:pfam05483 621 KKKGSaenKQLNAYEIKVNKLELELASAKQ--------KFEEIIDNYQKEIEDKKISEEKL--LEEVEK-AKAIADEAVK 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 531 SQRDSELRSAKKTIQEVKADNKKLQQILEEVRQNQSKV-LEENVKLRKGMAEAIEKIE---------EFKRNWHSSREAG 600
Cdd:pfam05483 690 LQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELgLYKNKEQEQSSAKAALEIElsnikaellSLKKQLEIEKEEK 769
|
650
....*....|
gi 17536671 601 ERLQLEAKEN 610
Cdd:pfam05483 770 EKLKMEAKEN 779
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
274-704 |
3.71e-10 |
|
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: 64.38 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 274 ELKLKNAR--LERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLHAEnmkltrqkadircdlLEARRNLKGFDE 351
Cdd:pfam05557 22 ELEHKRARieLEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQ---------------AELNRLKKKYLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 352 KREELEKQRDEALEDVR--------RITELK---KNVEIELRSLKLLAEEREEQIDELKSRVAGYEVLRRDHEAVKNELA 420
Cdd:pfam05557 87 ALNKKLNEKESQLADARevisclknELSELRrqiQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 421 KAEEKLNKMGAHLVMADKQSSHFKTLKETAE--GSRRRAIEQCNEMVARIR--------------GLEASLENQRKVEQE 484
Cdd:pfam05557 167 EAEQRIKELEFEIQSQEQDSEIVKNSKSELAriPELEKELERLREHNKHLNenienklllkeeveDLKRKLEREEKYREE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 485 LEMVKAENVRQAKKIEFMKEEIQETHLDYR--EELSklakggGSHEADSQRDSELRSAKKTI-QEVKADNKKLQQILEEV 561
Cdd:pfam05557 247 AATLELEKEKLEQELQSWVKLAQDTGLNLRspEDLS------RRIEQLQQREIVLKEENSSLtSSARQLEKARRELEQEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 562 RQNQSKVLEENVKL--------------------RKGMAEAIEKIEEFKRNWHSSREAGERlqLEAKENEEKVLKVEEEL 621
Cdd:pfam05557 321 AQYLKKIEDLNKKLkrhkalvrrlqrrvllltkeRDGYRAILESYDKELTMSNYSPQLLER--IEEAEDMTQKMQAHNEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 622 QEKRLEVLEkEELVNYLQSQINTKQTKQPKLSRRSTLMSTISEVDTSTYVREVEEVRA----LEEQREELQAYLA--EKR 695
Cdd:pfam05557 399 MEAQLSVAE-EELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLELerqrLREQKNELEMELErrCLQ 477
|
....*....
gi 17536671 696 KMADLQKSR 704
Cdd:pfam05557 478 GDYDPKKTK 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-372 |
4.40e-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: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 33 NESQEDLKTRLLEAENIIQDLRSERDALHESLVDKAGLNESVIIERSNKVSTQETRIY-RRDVTLLEDDLKQKESQIRIL 111
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEElEAQIEQLKEELKALREALDEL 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 112 QNRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIFSIGEElknktmkLNEKNSQFQTKLAE 191
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL-------IEELESELEALLNE 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 192 ISSENRNLERkvQKFREELIVKDQRSLEvhqdqentqkvlKEVKQLSDRLDYLTPKRKDvsrikerddflqfsakiIEET 271
Cdd:TIGR02168 882 RASLEEALAL--LRSELEELSEELRELE------------SKRSELRRELEELREKLAQ-----------------LELR 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 272 MSELKLKNARLERELSEKEELvkvtkeELQELQKTVTQAMGDSEQATKYLHAENMKLTRQkADIRCDLLEARRNLKgfdE 351
Cdd:TIGR02168 931 LEGLEVRIDNLQERLSEEYSL------TLEEAEALENKIEDDEEEARRRLKRLENKIKEL-GPVNLAAIEEYEELK---E 1000
|
330 340
....*....|....*....|....
gi 17536671 352 KREELEKQRD---EALEDVRRITE 372
Cdd:TIGR02168 1001 RYDFLTAQKEdltEAKETLEEAIE 1024
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
249-704 |
6.30e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 249 KDVSRIKERDDFlQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTqamgdseqatkylhaENMKL 328
Cdd:PRK03918 149 KVVRQILGLDDY-ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLR---------------EINEI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 329 TRQKADIRCDLLEARRNLKGFDEKREELEKQRDEALE---DVRRITELKKNVEIELRSLKLLAEEREEQ---IDELKSRV 402
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKEEIEELEKELESlegSKRKLEEKIRELEERIEELKKEIEELEEKvkeLKELKEKA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 403 AGYEVLRRDHEA-------VKNELAKAEEKLNKMGAHLVMADKQSSHFKTLKETAEGSRRR--AIEQCNEMVARIRGLEA 473
Cdd:PRK03918 293 EEYIKLSEFYEEyldelreIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRleELEERHELYEEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 474 SLENQRKVEQELEMVKAEnvRQAKKIEFMKEEIQETHLDYREELSKLAKGGGSHEADSqrdSELRSAKKT---------- 543
Cdd:PRK03918 373 ELERLKKRLTGLTPEKLE--KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI---EELKKAKGKcpvcgrelte 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 544 ------IQEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAE-----AIEKIEEFKRNWHSSREAGERLQLEAKENEE 612
Cdd:PRK03918 448 ehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKELAEQLKELEEKLKKYNLEELEKKAEEY 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 613 KVLKVEEELQEKRLEVLEKE-----ELVNYLQSQINTKQTKQPKLSR-----RSTLMSTISEVDTStyVREVE------- 675
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKElekleELKKKLAELEKKLDELEEELAEllkelEELGFESVEELEER--LKELEpfyneyl 605
|
490 500 510
....*....|....*....|....*....|....*.
gi 17536671 676 -------EVRALEEQREELQAYLAEKRKMADLQKSR 704
Cdd:PRK03918 606 elkdaekELEREEKELKKLEEELDKAFEELAETEKR 641
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
346-705 |
1.01e-09 |
|
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: 63.16 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 346 LKGFDEKREELEKQRDEaLEDVR-RITELKKNVEIELRSLKLLAEERE--EQIDELKSR---------VAGYEVLRRDHE 413
Cdd:TIGR02169 162 IAGVAEFDRKKEKALEE-LEEVEeNIERLDLIIDEKRQQLERLRREREkaERYQALLKEkreyegyelLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 414 AVKNELAKAEEKLNKMGAHL-VMADKQSSHFKTLKETAEGSRRRAIEQCNEMVARIRGLEASLEN-QRKV-EQELEMVKA 490
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEIsELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASlERSIaEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 491 ENvrQAKKIEFMKEEIQETHLDYREELSKLAKgggsheadsqrdsELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVLE 570
Cdd:TIGR02169 321 EE--RLAKLEAEIDKLLAEIEELEREIEEERK-------------RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 571 ENVKLRKGMAEAIEKIEEFKRNWhssreagERLQLEAKENEEKVLKVEEELQEKRLEVLEKEELVNYLQSQINTKQTkqp 650
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKREL-------DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW--- 455
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 17536671 651 KLSRRSTLMSTISEvdtsTYVREVEEVRALEEQREELQAYLAEKRKMADLQKSRS 705
Cdd:TIGR02169 456 KLEQLAADLSKYEQ----ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
117-604 |
1.15e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 117 RLETEKQKMQDTISGYQ---EDLKEneiRIENLNSRLHKLEDELSAKTHEifsigeelknktmklneknsqfqTKLAEIS 193
Cdd:PRK02224 255 TLEAEIEDLRETIAETErerEELAE---EVRDLRERLEELEEERDDLLAE-----------------------AGLDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 194 SEnrnlerkvqkfreelIVKDQRSlEVHQDQENTQKVLKEVkqlsdrldyltpkRKDVSRIKERDDFLQFSAKIIEETMS 273
Cdd:PRK02224 309 AE---------------AVEARRE-ELEDRDEELRDRLEEC-------------RVAAQAHNEEAESLREDADDLEERAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 274 ELKLKNARLERELSEKEELVKVTKEELQELQK---TVTQAMGDSEQATKYLHAENMKLTRQKADIRCDLLEARRNLKGFD 350
Cdd:PRK02224 360 ELREEAAELESELEEAREAVEDRREEIEELEEeieELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 351 EKREElekqrDEALEDVRRITELKKNVEIELRSLKLlaEEREEQIDELKSRVagyEVLRRDHEAVKNELAKAEEklnkmg 430
Cdd:PRK02224 440 ERVEE-----AEALLEAGKCPECGQPVEGSPHVETI--EEDRERVEELEAEL---EDLEEEVEEVEERLERAED------ 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 431 ahLVMADKQSSHFKTLKETAEG--SRRRAI-----EQCNEMVARIRGLEASLENQRKVEQELEMVKAENVRQAKKIEFMK 503
Cdd:PRK02224 504 --LVEAEDRIERLEERREDLEEliAERRETieekrERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 504 EEIQEThldyREELSKLAKGGGSHEADSQRDSELRSAKKTIQEVKADNK-KLQQILEEVRQNQSKVLEENV-KLRKGMAE 581
Cdd:PRK02224 582 AELKER----IESLERIRTLLAAIADAEDEIERLREKREALAELNDERReRLAEKRERKRELEAEFDEARIeEAREDKER 657
|
490 500
....*....|....*....|...
gi 17536671 582 AIEKIEEFKRNWHSSREAGERLQ 604
Cdd:PRK02224 658 AEEYLEQVEEKLDELREERDDLQ 680
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
34-609 |
2.19e-09 |
|
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: 62.11 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 34 ESQEDLKTRLLEAENIIQDLRSERDALHESLVDKAglnesviiERSNKVSTQETRIYRRDvTLLEDDLKQKESQIRILQN 113
Cdd:pfam01576 19 ERQQKAESELKELEKKHQQLCEEKNALQEQLQAET--------ELCAEAEEMRARLAARK-QELEEILHELESRLEEEEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 114 RCLRLETEKQKMQDTISGYQEDLKENEIRIENLnsRLHKLEDELSAKTHEifsigeelkNKTMKLNEKNSQFQtklaeis 193
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKL--QLEKVTTEAKIKKLE---------EDILLLEDQNSKLS------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 194 SENRNLERKVQKFREELIVKDQRSLEVHQDQENTQKVLKEvkqLSDRLDYLTPKRKDVSRIKERddfLQFSAKIIEETMS 273
Cdd:pfam01576 152 KERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISD---LEERLKKEEKGRQELEKAKRK---LEGESTDLQEQIA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 274 ELKLKNARLERELSEKEelvkvtkEELQELQKTVTQAMGDSEQATKYLHaenmKLTRQKADIRCDlLEARRNLKGFDEKR 353
Cdd:pfam01576 226 ELQAQIAELRAQLAKKE-------EELQAALARLEEETAQKNNALKKIR----ELEAQISELQED-LESERAARNKAEKQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 354 -----EELEKQRDEaLEDVRRIT----ELKKNVEIELRSLKLLAEEreeqidELKSRVAGYEVLRRDHEAVKNELAKAEE 424
Cdd:pfam01576 294 rrdlgEELEALKTE-LEDTLDTTaaqqELRSKREQEVTELKKALEE------ETRSHEAQLQEMRQKHTQALEELTEQLE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 425 KLNKMGAHLVMAdKQS---------SHFKTL---KETAEGSRRRAIEQCNEMVARI----RGLEASLENQRKVEQELEMV 488
Cdd:pfam01576 367 QAKRNKANLEKA-KQAlesenaelqAELRTLqqaKQDSEHKRKKLEGQLQELQARLseseRQRAELAEKLSKLQSELESV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 489 KAE-NVRQAKKIEFMKEEIQ-ETHLDYREELskLAKGGGSHEADSQRDSELRSAKKTIQEVKADNKKLQQILEEVRQNQS 566
Cdd:pfam01576 446 SSLlNEAEGKNIKLSKDVSSlESQLQDTQEL--LQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQ 523
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 17536671 567 KVLEENVKLRKGMAEAIEKIEEFKRNWHSSREAgERLQLEAKE 609
Cdd:pfam01576 524 AQLSDMKKKLEEDAGTLEALEEGKKRLQRELEA-LTQQLEEKA 565
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
99-316 |
3.05e-09 |
|
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: 60.55 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 99 DDLKQKESQIRILQNRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSAktheifsIGEELKNKTMKL 178
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-------LEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 179 NEKNSQFQTKLAEISSENRNLERKVQKFREELIVKDQRSLEVHQDQENTQKVLKEVKQLSDRLdyltpkRKDVSRIKERD 258
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL------RADLAELAALR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17536671 259 DFLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQ 316
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
24-591 |
3.49e-09 |
|
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: 61.29 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 24 SPYQVIDLnnESQEDLKTRLLEAENIIQDLR---SERDALHESlvDKAGLNESVIierSNKVSTQETRIYRRDVTlledD 100
Cdd:pfam15921 63 SPRKIIAY--PGKEHIERVLEEYSHQVKDLQrrlNESNELHEK--QKFYLRQSVI---DLQTKLQEMQMERDAMA----D 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 101 LKQKESQIR-----ILQNRCLRLETEKQKMQDTisgyqedLKENEIRIENLNSRLHKLEDELsaktHEIFSIGEELKNKT 175
Cdd:pfam15921 132 IRRRESQSQedlrnQLQNTVHELEAAKCLKEDM-------LEDSNTQIEQLRKMMLSHEGVL----QEIRSILVDFEEAS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 176 -MKLNEKNS----QFQTKLAEISSENRNLERKVQKFREELI-VKDQrsLEVHQdQENTQKVLKEVKQLSDRLDYLTPKRK 249
Cdd:pfam15921 201 gKKIYEHDSmstmHFRSLGSAISKILRELDTEISYLKGRIFpVEDQ--LEALK-SESQNKIELLLQQHQDRIEQLISEHE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 250 -DVSRIKERDDFLQFSAKIIEETMsELKLKNARLERELSEKEelvkvtkeeLQELQKTVTQAMGDSEQATKYLHAENMKL 328
Cdd:pfam15921 278 vEITGLTEKASSARSQANSIQSQL-EIIQEQARNQNSMYMRQ---------LSDLESTVSQLRSELREAKRMYEDKIEEL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 329 TRQKADIRCDLLEARRNLKGFDEKREELEKQRDEALEDV-RRITELKKNVE-------------IELRSLKLLAEEREEQ 394
Cdd:pfam15921 348 EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLhKREKELSLEKEqnkrlwdrdtgnsITIDHLRRELDDRNME 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 395 IDEL-------KSRVAGYevLRRDHEAV--KNElakAEEKLNKMGAHL----VMADKQSSHFKTLKETAEGSRR------ 455
Cdd:pfam15921 428 VQRLeallkamKSECQGQ--MERQMAAIqgKNE---SLEKVSSLTAQLestkEMLRKVVEELTAKKMTLESSERtvsdlt 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 456 -------RAIEQCNEMVARIRG-----------LEASLENQRKVEQELEMVKAENVRQAKKIEFMKEEIQethlDYREEL 517
Cdd:pfam15921 503 aslqekeRAIEATNAEITKLRSrvdlklqelqhLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIE----NMTQLV 578
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17536671 518 SKLAKGGGSHEAD-SQRDSELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAEAIEKIEEFKR 591
Cdd:pfam15921 579 GQHGRTAGAMQVEkAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQ 653
|
|
| C1_MgcRacGAP |
cd20821 |
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ... |
739-795 |
4.48e-09 |
|
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and similar proteins; MgcRacGAP, also called Rac GTPase-activating protein 1 (RACGAP1) or protein CYK4, plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling; and ii) after phosphorylation by aurora B, MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain an N-terminal C1 domain, and a C-terminal RhoGAP domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410371 Cd Length: 55 Bit Score: 53.56 E-value: 4.48e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 17536671 739 IPHKWLEfrHYSVLSMKCSLCFVGITFFTKANKCSHCDVRVHASCAPRVNNTCGIPA 795
Cdd:cd20821 1 RPHRFVS--KTVIKPETCVVCGKRIKFGKKALKCKDCRVVCHPDCKDKLPLPCVPTS 55
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
222-426 |
9.16e-09 |
|
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: 59.01 E-value: 9.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 222 QDQENTQKVLKEVKQLSDRLDYLTPKRKDVSR-IKERDDFLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEEL 300
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKqLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 301 QELQKTV--TQAMGDSEQATKYLHAENMKLTRQKADIRCDLLEARRN-LKGFDEKREELEKQRDEALEDVRRITELKKNV 377
Cdd:COG4942 104 EELAELLraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17536671 378 EIELRSLKLLAEEREEQIDELKSRVAGYEV----LRRDHEAVKNELAKAEEKL 426
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAelaeLQQEAEELEALIARLEAEA 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
27-595 |
1.09e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 27 QVIDLNNESQEDLKTRLLEAENIIQDLRSERDALHESLVDKAGlnesviiersnkvstqetriyrRDVTLLEDDLKQKES 106
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG----------------------DRLEQLEREIERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 107 QIRILQNRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIFSigeelknktmKLNEKNSQFQ 186
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA----------ALRDLRRELR 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 187 TKLAEISS-ENR--NLERKVQKFRE-----------------ELI-VKDQ----------------RSLEVhqDQENTQK 229
Cdd:COG4913 423 ELEAEIASlERRksNIPARLLALRDalaealgldeaelpfvgELIeVRPEeerwrgaiervlggfaLTLLV--PPEHYAA 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 230 VLKEV--KQLSDRLDY--LTPKRKDVSRIKERDDFLqfSAKIieetmsELKLKNAR--LERELSEKEELVKV-TKEELQE 302
Cdd:COG4913 501 ALRWVnrLHLRGRLVYerVRTGLPDPERPRLDPDSL--AGKL------DFKPHPFRawLEAELGRRFDYVCVdSPEELRR 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 303 LQKTVTQA-MgdseqaTKylhaenMKLTRQKADIRCDLleARRNLKGFD--EKREELEKQRDEALEDVRRITElkknvei 379
Cdd:COG4913 573 HPRAITRAgQ------VK------GNGTRHEKDDRRRI--RSRYVLGFDnrAKLAALEAELAELEEELAEAEE------- 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 380 ELRSLKLLAEEREEQIDELkSRVAGYEVLRRDHEAVKNELAKAEEKLNKmgahlvmADKQSSHFKTLKEtaegsrrraie 459
Cdd:COG4913 632 RLEALEAELDALQERREAL-QRLAEYSWDEIDVASAEREIAELEAELER-------LDASSDDLAALEE----------- 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 460 qcnemvaRIRGLEASLEnqrKVEQELEMVKAENVRQAKKIEFMKEEIQEtHLDYREELSKLAKGGGSHEADSQRDSELRS 539
Cdd:COG4913 693 -------QLEELEAELE---ELEEELDELKGEIGRLEKELEQAEEELDE-LQDRLEAAEDLARLELRALLEERFAAALGD 761
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 17536671 540 AkktiqevkADNKKLQQILEEVRQNQSKVLEENVKLRKGMAeaiekieEFKRNWHS 595
Cdd:COG4913 762 A--------VERELRENLEERIDALRARLNRAEEELERAMR-------AFNREWPA 802
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
361-588 |
1.20e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 361 DEALEDVRRITELKKNVEIELRSLKLL------------AEEREEQIDELKSRVAGYEvLRRDHEAVKNELAKAEEKLNK 428
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLepirelaeryaaARERLAELEYLRAALRLWF-AQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 429 MGAHLVMADKQsshfktlKETAEGSRRRAIEQCNEM-VARIRGLEASLENQRKVEQELEMVKAENVRQAKKIEFMKEEIQ 507
Cdd:COG4913 307 LEAELERLEAR-------LDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 508 ETHLDYREELSKLAKGGGSHEADSQRdsELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAEAIEKIE 587
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEE--ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDE 457
|
.
gi 17536671 588 E 588
Cdd:COG4913 458 A 458
|
|
| C1 |
smart00109 |
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ... |
741-791 |
3.29e-08 |
|
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.
Pssm-ID: 197519 Cd Length: 50 Bit Score: 50.93 E-value: 3.29e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 17536671 741 HKWLEFRHYSvlSMKCSLCFVGITF-FTKANKCSHCDVRVHASCAPRVNNTC 791
Cdd:smart00109 1 HKHVFRTFTK--PTFCCVCRKSIWGsFKQGLRCSECKVKCHKKCADKVPKAC 50
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
85-708 |
3.98e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.13 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 85 QETRIYRRDVTLLEDDlKQKESQIRILQNRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSA---KT 161
Cdd:TIGR00606 200 QKVQEHQMELKYLKQY-KEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKAlksRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 162 HEIFSIGEELKNKTMK--------LNEKNSQFQTKLAEISSENRNLERKVQKFREELIVKDQRSLEVHQDQENTQKVLKE 233
Cdd:TIGR00606 279 KQMEKDNSELELKMEKvfqgtdeqLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 234 VKQLSDRLDYLTPKRKDVSRIkerdDFLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGD 313
Cdd:TIGR00606 359 HQEHIRARDSLIQSLATRLEL----DGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 314 SEQATKYLHAENMKLTRQKADIRCDLLEARRNLKGFD---EKREELEK-QRDEALEDVRRITELKKNVEIELRSLKLLAE 389
Cdd:TIGR00606 435 KKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDrilELDQELRKaERELSKAEKNSLTETLKKEVKSLQNEKADLD 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 390 EREEQIDELKSRVAGYEVLRRDHEAVKNELAKAEEKLNKMGA-HLVMADKQSSHFKTLKETAE--GSRRRAIEQCNEMVA 466
Cdd:TIGR00606 515 RKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSrHSDELTSLLGYFPNKKQLEDwlHSKSKEINQTRDRLA 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 467 RIRGLEASLE-NQRKVEQELEMVKAENVRQAKKI-EFMKEEIQETHLD-YREELSKlakgggsheadSQRDSELRSAKKT 543
Cdd:TIGR00606 595 KLNKELASLEqNKNHINNELESKEEQLSSYEDKLfDVCGSQDEESDLErLKEEIEK-----------SSKQRAMLAGATA 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 544 IQEvkadnkklQQILEEVRQNQS--KVLEENVKLRKGMAEAIEKIEEFKRNWHSSREAGERLqLEAKENEEKVLKVEEEL 621
Cdd:TIGR00606 664 VYS--------QFITQLTDENQSccPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESE-LKKKEKRRDEMLGLAPG 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 622 QEKRLEVLEKE--ELVNYLQSQINTKQTKQPKLSRRSTLMSTI-----SEVDTSTYVREVEEVRALEEQREELQAYLAEK 694
Cdd:TIGR00606 735 RQSIIDLKEKEipELRNKLQKVNRDIQRLKNDIEEQETLLGTImpeeeSAKVCLTDVTIMERFQMELKDVERKIAQQAAK 814
|
650
....*....|....
gi 17536671 695 RKMADLQKSRSTAN 708
Cdd:TIGR00606 815 LQGSDLDRTVQQVN 828
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
109-590 |
4.44e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 57.75 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 109 RILQNRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIFSI--GEELKNKTMKLNEKNSQFQ 186
Cdd:TIGR00606 573 KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgSQDEESDLERLKEEIEKSS 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 187 TKLAEISSENRNLErkvqKFREELIVKDQRSLEVHQDQENTQKVLKEVKQLSDRLDYLTPkrkdvSRIKERDDFLQFSAK 266
Cdd:TIGR00606 653 KQRAMLAGATAVYS----QFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAP-----DKLKSTESELKKKEK 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 267 IIEETMSELKLKNARLERELSEKEELvkvtKEELQELQKTVTQAMGDSEQATKYLHAENMKLTRQKadircDLLEARRNL 346
Cdd:TIGR00606 724 RRDEMLGLAPGRQSIIDLKEKEIPEL----RNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAK-----VCLTDVTIM 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 347 KGFDEKREELEKQRDEALEDVRRITELkknveielRSLKLLAEEREEQIDELKSRVAGYEVLRRDHEAVKNELAKAEEKL 426
Cdd:TIGR00606 795 ERFQMELKDVERKIAQQAAKLQGSDLD--------RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT 866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 427 NKMGAHLVMADKQSSHFKTLKETAEgSRRRAIEQCNEMVARIRG----LEASLENQRKVEQELEMVKAENVRQAK-KIEF 501
Cdd:TIGR00606 867 NELKSEKLQIGTNLQRRQQFEEQLV-ELSTEVQSLIREIKDAKEqdspLETFLEKDQQEKEELISSKETSNKKAQdKVND 945
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 502 MKEEIQETHLdYREELSKLAKgGGSHEADSQRDSELRSAKKTIQEVKADNKKLQQILEEVRQN------QSKVLEENVKL 575
Cdd:TIGR00606 946 IKEKVKNIHG-YMKDIENKIQ-DGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDidtqkiQERWLQDNLTL 1023
|
490
....*....|....*
gi 17536671 576 RKGMAEAIEKIEEFK 590
Cdd:TIGR00606 1024 RKRENELKEVEEELK 1038
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
29-398 |
4.71e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 29 IDLNNESQEDLKTRLLEAENIIQDLRSERDALHEslvdkaglnesviiersnkvstqetriyrrDVTLLEDDLKQKESQI 108
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREERDELRE------------------------------REAELEATLRTARERV 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 109 RilQNRCLRLE----TEKQKMQDtiSGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIFSIG---------EELKNKT 175
Cdd:PRK02224 443 E--EAEALLEAgkcpECGQPVEG--SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlveaedriERLEERR 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 176 MKLNEKNSQFQTKLAEISSENRNLERKVQKFREELIVKDQRSLEVHqdqENTQKVLKEVKQLSDRLDYLTPKRKDVSRIK 255
Cdd:PRK02224 519 EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAE---EEAEEAREEVAELNSKLAELKERIESLERIR 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 256 ERDDFLQFSAKIIEETMSELKLKNAR--LERE-LSEKEELVKVTKEELQElqKTVTQAMGDSEQATKYLHAENMKLTR-- 330
Cdd:PRK02224 596 TLLAAIADAEDEIERLREKREALAELndERRErLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDElr 673
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17536671 331 -QKADIRCDLLEARRNLKGFDEKREELE--KQRDEALEDVRRITELKKNVEIELRslkllAEEREEQIDEL 398
Cdd:PRK02224 674 eERDDLQAEIGAVENELEELEELRERREalENRVEALEALYDEAEELESMYGDLR-----AELRQRNVETL 739
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
85-599 |
4.98e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.60 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 85 QETRIYRRDVTLLEDDLKQKESQIRILQNRCLRLETEKQKMQDTISGYQEDLKE---NEIRIENLNSRLHKLEDELSA-- 159
Cdd:PRK01156 190 EKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNElssLEDMKNRYESEIKTAESDLSMel 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 160 -KTHEIFSIGEELKNKT-----MKLNEKNSQFQTKL-------------AEISSENRNLER--KVQKFREELIVKDQRS- 217
Cdd:PRK01156 270 eKNNYYKELEERHMKIIndpvyKNRNYINDYFKYKNdienkkqilsnidAEINKYHAIIKKlsVLQKDYNDYIKKKSRYd 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 218 ------LEVHQDQENTQKVLKEVKQLSDRLDYLTPKRKDVSRIKERDDFLQF-SAKIIEETMSELKLKNARLERELSEKE 290
Cdd:PRK01156 350 dlnnqiLELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEiDPDAIKKELNEINVKLQDISSKVSSLN 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 291 ELVKVTKEELQELQKTVTQAMGDS-----------EQATKYLHAENMKLTRQKADIRcdllEARRNLKGFDEKREELEKQ 359
Cdd:PRK01156 430 QRIRALRENLDELSRNMEMLNGQSvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIR----EIEIEVKDIDEKIVDLKKR 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 360 RDE-ALEDVRR-ITELKKnveieLRSLKLLAEEREEQIDELKSRVAGYEVLRRDHEAVKNEL--AKAEEKLNKMGahlVM 435
Cdd:PRK01156 506 KEYlESEEINKsINEYNK-----IESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDldSKRTSWLNALA---VI 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 436 ADKQSSHFKTLKETAEGSRRRAIEQCNEMVARIRGLEASLENQ-RKVEQELEMVKAE-NVRQAKKIefMKEEIQETHLDY 513
Cdd:PRK01156 578 SLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSiREIENEANNLNNKyNEIQENKI--LIEKLRGKIDNY 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 514 REELSKLAKGGGSHEADSQRDSE----LRSAKKTIQEVKADNKKLQQILEEVRQNQSKvLEENVKLRKGMAEAIEKIEEF 589
Cdd:PRK01156 656 KKQIAEIDSIIPDLKEITSRINDiednLKKSRKALDDAKANRARLESTIEILRTRINE-LSDRINDINETLESMKKIKKA 734
|
570
....*....|
gi 17536671 590 KRNWHSSREA 599
Cdd:PRK01156 735 IGDLKRLREA 744
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
350-705 |
1.58e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.13 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 350 DEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKsrvagyEVLRrdhEAVKNELAKAEEKLNKM 429
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELK------LKEQ---AKKALEYYQLKEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 430 GAHLVMADKQSSHFKTLKETaeGSRRRAIEQCNEMVARIRGLEASLENQRKVEQELEMvkaenvrqaKKIEFMKEEIQET 509
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLL--QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEE---------KEKKLQEEELKLL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 510 HLDYREELSKLAKGGGSHEADSQR----DSELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAEAIEK 585
Cdd:pfam02463 292 AKEEEELKSELLKLERRKVDDEEKlkesEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 586 ----IEEFKRNWHSSREAGERLQLEAKENEEKVLKVEEELQEKRLEVLEKEELVNYLQSQINTKQTKQPKLSRRSTLMST 661
Cdd:pfam02463 372 eeelLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE 451
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 17536671 662 ISEVDTST-----YVREVEEVRALEEQREELQAYLAEKRKMADLQKSRS 705
Cdd:pfam02463 452 ELEKQELKllkdeLELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQ 500
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
132-635 |
2.74e-07 |
|
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: 55.11 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 132 YQEDLKENEIRIENLNSRLH-KLEDELSAKTHEIFSIGEELKNKTMKLNEKNSQFQTKLAEISSENRNLERKVQKFREEL 210
Cdd:pfam05483 61 YQEGLKDSDFENSEGLSRLYsKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 211 ivkdQRSLEVHQDQENTQKVLKEVKQLSDRLDYLTpKRKDVSRIKERDDFLQFSAKIIEETMS--ELKLK--NARLEREL 286
Cdd:pfam05483 141 ----QENKDLIKENNATRHLCNLLKETCARSAEKT-KKYEYEREETRQVYMDLNNNIEKMILAfeELRVQaeNARLEMHF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 287 SEKEElvkvtKEELQELQKTVTQAMGDSEQATKYLHAENMKLTRQKADIRCDLLEAR--------------RNLKGFDEK 352
Cdd:pfam05483 216 KLKED-----HEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRdkanqleektklqdENLKELIEK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 353 REELEKQRDEALEDVRRITELKKNVE----IELRSLKLLAEEREEQIDELKSRVAGYEVLRRDHEAVKNELakaEEKLNK 428
Cdd:pfam05483 291 KDHLTKELEDIKMSLQRSMSTQKALEedlqIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSL---EELLRT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 429 MGAHLvmaDKQSSHFKTLkeTAEGSRRRAieQCNEMVARIRGLEASLENQRKVEQELEMVKAENvrqaKKIEFMKEEIQE 508
Cdd:pfam05483 368 EQQRL---EKNEDQLKII--TMELQKKSS--ELEEMTKFKNNKEVELEELKKILAEDEKLLDEK----KQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 509 THldyrEELSKL--AKGGGSHEADSQRDSELRSAKKTIQEVKA-----DNKKLQQIleEVRQNQSKVLEENVKLRKGMAE 581
Cdd:pfam05483 437 KE----QELIFLlqAREKEIHDLEIQLTAIKTSEEHYLKEVEDlktelEKEKLKNI--ELTAHCDKLLLENKELTQEASD 510
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 17536671 582 AIEKIEEFKRNWHSSREAGERLQLEAKENEEKVLKVEEELQEKRLEVLEKEELV 635
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEV 564
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
208-693 |
2.76e-07 |
|
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: 55.18 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 208 EELIVKDQRSLEVHQDQENTQKVLKEVK----QLSDRLDYLTPKrkdvsrikerddfLQFSAKII---EETMSELKLKNA 280
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEkkhqQLCEEKNALQEQ-------------LQAETELCaeaEEMRARLAARKQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 281 RLERELSEKEELVKVTKEELQELQ---KTVTQAMGDSEQATKYLHAENMKLTRQK--ADIRCDLLEARRNLkgFDEKREE 355
Cdd:pfam01576 72 ELEEILHELESRLEEEEERSQQLQnekKKMQQHIQDLEEQLDEEEAARQKLQLEKvtTEAKIKKLEEDILL--LEDQNSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 356 LEKQRdEALEDvrRITELKKNV---EIELRSLKLLAEEREEQIDELKSRVAGYEVLRRDHEAVKN----ELAKAEEKLNK 428
Cdd:pfam01576 150 LSKER-KLLEE--RISEFTSNLaeeEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRklegESTDLQEQIAE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 429 MGAHLVMADKQSSHFKTLKETAEGSRRRAIEQCNEMVARIRGLEASL-ENQRKVEQELEM-VKAENVRQ--AKKIEFMKE 504
Cdd:pfam01576 227 LQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQIsELQEDLESERAArNKAEKQRRdlGEELEALKT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 505 EIQEThldyreelskLAKGGGSHEADSQRDSELRSAKKTIQEvkaDNKKLQQILEEVRQNQSKVLEEnvklrkgMAEAIE 584
Cdd:pfam01576 307 ELEDT----------LDTTAAQQELRSKREQEVTELKKALEE---ETRSHEAQLQEMRQKHTQALEE-------LTEQLE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 585 KIEEFKRNWHSSREA--GERLQLEAKENEEKVLKVEEELQEKRLEVLEKEELVNYLQSQiNTKQTKQPKLSRRST----L 658
Cdd:pfam01576 367 QAKRNKANLEKAKQAleSENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESE-RQRAELAEKLSKLQSelesV 445
|
490 500 510
....*....|....*....|....*....|....*
gi 17536671 659 MSTISEVDTSTyVREVEEVRALEEQREELQAYLAE 693
Cdd:pfam01576 446 SSLLNEAEGKN-IKLSKDVSSLESQLQDTQELLQE 479
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
31-521 |
2.78e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 31 LNNESQEDLKTRLLEAENIIQDLRSERDALHESlvdKAGLNEsviIERSNKVSTQETRIYRRDVTLLEDDLKQKESQIRi 110
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEEL---EEELEE---LEAELEELREELEKLEKLLQLLPLYQELEALEAE- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 111 LQNRCLRLETEKQKMQdTISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIFsigEELKNKTMKLNEKNSQFQTKLA 190
Cdd:COG4717 141 LAELPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEEEL---QDLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 191 EISSENRNLERKVQKFREElivkdqrsLEVHQDQENTQKVLKEVKQLSDRLDYLTPKRKDVSRIKERDDFLQFSAKIIEE 270
Cdd:COG4717 217 EAQEELEELEEELEQLENE--------LEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 271 TMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSE-QATKYLHAENMKLTRQKADIRCDLLEARRNLKGF 349
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 350 DEKREELEKQRD-EALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRVAGYevlrrDHEAVKNELAKAEEKLnk 428
Cdd:COG4717 369 EQEIAALLAEAGvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL-----DEEELEEELEELEEEL-- 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 429 mgahlvmadkqsshfktlkETAEGSRRRAIEQCNEMVARIRGLEASLENQRKvEQELEMVKAENVRQAKKI-------EF 501
Cdd:COG4717 442 -------------------EELEEELEELREELAELEAELEQLEEDGELAEL-LQELEELKAELRELAEEWaalklalEL 501
|
490 500
....*....|....*....|
gi 17536671 502 MKEEIQETHLDYREELSKLA 521
Cdd:COG4717 502 LEEAREEYREERLPPVLERA 521
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
163-520 |
4.91e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 54.36 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 163 EIFSIGEELKNKTMKLNEK-NSQFQTklaeissENRNLERKVQkfreelIVKDQRSLEVHQDQENTQKVLKEvkqlsdrl 241
Cdd:pfam17380 241 ESFNLAEDVTTMTPEYTVRyNGQTMT-------ENEFLNQLLH------IVQHQKAVSERQQQEKFEKMEQE-------- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 242 dYLTPKRKDVSRIKERDDFLQFSAKIIEETMSELKLKNARLERELSEKE-ELVKVTKEELQ-ELQKTVTQAMgdSEQATK 319
Cdd:pfam17380 300 -RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERErELERIRQEERKrELERIRQEEI--AMEISR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 320 YLHAENMKLTRQKADIRC-DLLEARRNLKGFDEKREELEKQRDEALEDVRRITELKKNVEI---------ELRSLKLLAE 389
Cdd:pfam17380 377 MRELERLQMERQQKNERVrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVrrleeerarEMERVRLEEQ 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 390 EREEQIDELKSRVAGYEVLRRDHEAVKNELAKAEEKLNKMgahlvmadkqsshfktLKETAEGSRRRAIEQCNEMVARIR 469
Cdd:pfam17380 457 ERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI----------------LEKELEERKQAMIEEERKRKLLEK 520
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 17536671 470 GLEaslENQRKVEQELEMVKAENVRQAKKIEFMKEEIQETHLDYREELSKL 520
Cdd:pfam17380 521 EME---ERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRL 568
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
349-696 |
5.25e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 349 FDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAE------EREEQIDELKSRVAGYEVlrrdhEAVKNELAKA 422
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEkaerykELKAELRELELALLVLRL-----EELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 423 EEKLNKMgahlvmadkqsshfktlketaegsrrraIEQCNEMVARIRGLEASLEnqrkvEQELEMVKAENvrqakkiefM 502
Cdd:TIGR02168 245 QEELKEA----------------------------EEELEELTAELQELEEKLE-----ELRLEVSELEE---------E 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 503 KEEIQETHLDYREELSKLakgggsheadsqrDSELRSAKKTIQEVKADNKKLQQILEEVRQnQSKVLEENVKLRKgmaea 582
Cdd:TIGR02168 283 IEELQKELYALANEISRL-------------EQQKQILRERLANLERQLEELEAQLEELES-KLDELAEELAELE----- 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 583 iEKIEEFKRNWHSSREAGERLQLEAKENEEKVLKVEEELQEKRLEVLEKEELVNYLQSQIN--------TKQTKQPKLSR 654
Cdd:TIGR02168 344 -EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIErlearlerLEDRRERLQQE 422
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 17536671 655 RSTLMSTISEVDTSTYVREVEEVRA----LEEQREELQAYLAEKRK 696
Cdd:TIGR02168 423 IEELLKKLEEAELKELQAELEELEEeleeLQEELERLEEALEELRE 468
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
33-520 |
7.28e-07 |
|
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: 53.57 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 33 NESQEDLKTRLLEAENIIQDLRSERDALHESL------VDKAGLNESVIIERSNKVSTQETRI---YRRDVTLLEDDLKQ 103
Cdd:pfam05483 288 IEKKDHLTKELEDIKMSLQRSMSTQKALEEDLqiatktICQLTEEKEAQMEELNKAKAAHSFVvteFEATTCSLEELLRT 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 104 KESQIRILQNRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSAKThEIFSIGEELKNKTMKL----- 178
Cdd:pfam05483 368 EQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK-QFEKIAEELKGKEQELifllq 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 179 --NEKNSQFQTKLAEISSENRNLERKVQKFREELIVKDQRSLEVhqdQENTQKVLKEVKQL----SDRLDYLTPKRKDVS 252
Cdd:pfam05483 447 arEKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEL---TAHCDKLLLENKELtqeaSDMTLELKKHQEDII 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 253 RIKERDDFLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLHAENMKLTRQK 332
Cdd:pfam05483 524 NCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 333 ADIRCDLLEARRNLKGFDEKREELEKQRDealedvrrITELKKN-VEIELRSLKllaEEREEQIDELKSRVagyEVLRRD 411
Cdd:pfam05483 604 ENKNKNIEELHQENKALKKKGSAENKQLN--------AYEIKVNkLELELASAK---QKFEEIIDNYQKEI---EDKKIS 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 412 HEAVKNELAKAEEKLNKMGAHLVMADKQSSH----FKTLKETAEGSRRRAIEQCNEMVARIRGLEASLENQR-KVEQELE 486
Cdd:pfam05483 670 EEKLLEEVEKAKAIADEAVKLQKEIDKRCQHkiaeMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKaALEIELS 749
|
490 500 510
....*....|....*....|....*....|....
gi 17536671 487 MVKAENVRQAKKIEFMKEEIQETHLDYREELSKL 520
Cdd:pfam05483 750 NIKAELLSLKKQLEIEKEEKEKLKMEAKENTAIL 783
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
384-736 |
7.54e-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: 53.92 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 384 LKLLAEEREEQIDELksrvAGYEVLRRDHEAVKNELAKAEEKLNKMGAHLVMADKQSSHFKTLKETAE-----GSRRRAI 458
Cdd:TIGR02169 148 ISMSPVERRKIIDEI----AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryqalLKEKREY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 459 EQcNEMVARIRGLEASLENQRKVEQELEMVKAENVRQAKKIEFMKEEIQETHLDYREELSKLAKGggsheadsqrdsELR 538
Cdd:TIGR02169 224 EG-YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------------EQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 539 SAKKTIQEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAEAIEKIEEFKRNWHSSREAGERLQLEAKENEEKVLKVE 618
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 619 EELQEK-------RLEVLEKEELVNYLQSQINTKQTKQPKLSRRSTLMSTISEVDTSTYVREVEEVRALEEQREELQAYL 691
Cdd:TIGR02169 371 AELEEVdkefaetRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 17536671 692 AE-----KRKMADLQKSRSTANTTTLITSTTATEVSKSACELSYPPATMR 736
Cdd:TIGR02169 451 KKqewklEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| PH |
smart00233 |
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
813-915 |
1.21e-06 |
|
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.
Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 48.31 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 813 MNGWLRVyRDDLPESTWTSLWAMMDSNHVKFYRDAGADNLENPYFTIDLNKEQWILRTGQEvaipGDVMRNVLTIKLQTR 892
Cdd:smart00233 3 KEGWLYK-KSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKGSIDLSGCTVREAPDPD----SSKKPHCFEIKTSDR 77
|
90 100
....*....|....*....|....
gi 17536671 893 -SVHIVAPTPKSAERWAACLQNAQ 915
Cdd:smart00233 78 kTLLLQAESEEEREKWVEALRKAI 101
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
330-641 |
1.23e-06 |
|
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: 53.05 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 330 RQKADIRCDLLEARRNLKGFDEKREELEKQRDEALEDVRR--ITELKKNVEIELRSLKLLAEEREEQIDELKSRVAGYEV 407
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLkeKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 408 LRRDHEA-------VKNELAKAEEKLNKMGAHLVMADKQSSHFKTLKETAEGSRRRAIEQCNEMVARIRGLEASLENQRK 480
Cdd:pfam02463 256 SKQEIEKeeeklaqVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 481 VEQELEMVKAEnvrQAKKIEFMKEEIQETHLDYREELSKLAKGGGSHEADSQRDSELRSAKKTIQEVKADNKKLQQILEE 560
Cdd:pfam02463 336 EIEELEKELKE---LEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 561 VRQNQSKVLEENVKLRKGMAEAIEKIEEFKRNWHSSREAGERLQLEAKENEEKVLKVEEELQEKRLEVLEKEELVNYLQS 640
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
.
gi 17536671 641 Q 641
Cdd:pfam02463 493 Q 493
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
255-609 |
1.61e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.20 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 255 KERDDFLQ---FSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKY---LHAENMKL 328
Cdd:pfam07888 41 QERAELLQaqeAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASseeLSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 329 TRQKADIRCDLLEARRNLKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEqidELKSRVAGYEVL 408
Cdd:pfam07888 121 LAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE---ELRSLSKEFQEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 409 RRDHEAVKNELAKAEEKLNKMGAHLVMADKQSSHFKTLKETAEGSRRR--AIEQCnemVARIRGLEASLENQR-KVEQEL 485
Cdd:pfam07888 198 RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERlnASERK---VEGLGEELSSMAAQRdRTQAEL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 486 EMVKAENVRqakkiefMKEEIQETHLDYREELSKLAKgggsheadsQRDSELRSA---KKTIQEVKADNKKLQQILEEVR 562
Cdd:pfam07888 275 HQARLQAAQ-------LTLQLADASLALREGRARWAQ---------ERETLQQSAeadKDRIEKLSAELQRLEERLQEER 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 17536671 563 -QNQSKVLE---ENVKLRKGMAEAIEKIEEFKRNWHSSREAGERLQLEAKE 609
Cdd:pfam07888 339 mEREKLEVElgrEKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQE 389
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
102-407 |
1.85e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.43 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 102 KQKESQIRILQNRCLRLETEKQKM-----QDTISGYQEDLK-ENEIRIENLNSRLHKLEDElSAKTHEI---FSIGEELK 172
Cdd:pfam17380 303 QEKEEKAREVERRRKLEEAEKARQaemdrQAAIYAEQERMAmERERELERIRQEERKRELE-RIRQEEIameISRMRELE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 173 NKTMKLNEKNSQFQTKLaEISSENRNLERKVQKFREELIVKDQRsleVHQDQENTQKvlKEVKQLSDRldyltpKRKDVS 252
Cdd:pfam17380 382 RLQMERQQKNERVRQEL-EAARKVKILEEERQRKIQQQKVEMEQ---IRAEQEEARQ--REVRRLEEE------RAREME 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 253 RIKERDDFLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLHAENMKltRQK 332
Cdd:pfam17380 450 RVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE--RQK 527
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17536671 333 AdircdLLEARRNLKGFDEKREELEkqrdeaLEDVRRITELKKNVEIELRSLKLLAEERE--EQIDELKSRVAGYEV 407
Cdd:pfam17380 528 A-----IYEEERRREAEEERRKQQE------MEERRRIQEQMRKATEERSRLEAMEREREmmRQIVESEKARAEYEA 593
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
353-702 |
1.91e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 353 REELEKQRDEALedvrriTELKKNVEIELRSLKLLaeerEEQIDELKSRVAGYEVLRRDHEAVKNELAKAEEKLNKMGAH 432
Cdd:COG4717 48 LERLEKEADELF------KPQGRKPELNLKELKEL----EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 433 LVMADKQSSHFKTLKETAEGSRRRAIEQcnemvARIRGLEASLENQRKVEQELEMVKAENVRQAKKIEfmkEEIQETHLD 512
Cdd:COG4717 118 LEKLEKLLQLLPLYQELEALEAELAELP-----ERLEELEERLEELRELEEELEELEAELAELQEELE---ELLEQLSLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 513 YREELSKLAKgggSHEADSQRDSELRSAKKTIQEVKADNKklQQILEEVRQNQSKVLEENVKLRKGMAEAIEKIEEFKRN 592
Cdd:COG4717 190 TEEELQDLAE---ELEELQQRLAELEEELEEAQEELEELE--EELEQLENELEAAALEERLKEARLLLLIAAALLALLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 593 WHSSREAGERLQLEAKENEEKVLKVEEELQEKRLEVLEKEELVNYLQSQINTKQTKQPKLSRRSTLMSTISEVDTSTYVR 672
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350
....*....|....*....|....*....|
gi 17536671 673 EVEEVRALEEQREELQAYLAEKRKMADLQK 702
Cdd:COG4717 345 RIEELQELLREAEELEEELQLEELEQEIAA 374
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
343-708 |
2.09e-06 |
|
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: 52.28 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 343 RRNLKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRvagYEVLRRDHEAVKNELAKA 422
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD---YLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 423 EEKlnkmgahlvmaDKQSSHFKTLKETAEGSRRRAIEQCNEMVARIRGLEASLENQRKVEQELEMVKAENVRQAKKIEFM 502
Cdd:pfam02463 249 EQE-----------EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 503 KEEIQETHLDYREELSKLAKgggsheadSQRDSELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAEA 582
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEI--------EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 583 IEKIEEFKRNWHssrEAGERLQLEAKENEEKVLKVEEELQEKRLEVLEKEELVNYLQSQINTKQTKQPKLsrRSTLMSTI 662
Cdd:pfam02463 390 AKLKEEELELKS---EEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ--ELKLLKDE 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 17536671 663 SEVDTSTYVREVEEVRALEEQREELQAYLAEKRKMADLQKSRSTAN 708
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLK 510
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
264-484 |
2.42e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 264 SAKIIEETMSELKlknaRLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLHAENMKLTRQKADIRcdLLEAR 343
Cdd:COG4942 18 QADAAAEAEAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA--ELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 344 RnlkgfDEKREELEKQRDEALEDVRRITELKKNVEIEL--------------RSLKLLAEEREEQIDELKSRVAGYEVLR 409
Cdd:COG4942 92 I-----AELRAELEAQKEELAELLRALYRLGRQPPLALllspedfldavrrlQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17536671 410 RDHEAVKNELAKAEEKLNKmgAHLVMADKQSSHFKTLK--ETAEGSRRRAIEQCNEMVARIRGLEASLENQRKVEQE 484
Cdd:COG4942 167 AELEAERAELEALLAELEE--ERAALEALKAERQKLLArlEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
33-610 |
3.16e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.98 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 33 NESQEDLKTRLLEAENIIQDLRSERDAL--HESLVD--KAGLNESVII----ERSNKVSTQETRIYRRDVTLLEDDLKQK 104
Cdd:TIGR01612 754 NKILEDFKNKEKELSNKINDYAKEKDELnkYKSKISeiKNHYNDQINIdnikDEDAKQNYDKSKEYIKTISIKEDEIFKI 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 105 ESQIRILQ-------NRCLRLETE-KQKMQDTISGYQEDLK--ENEIRIENLNSRLHKLEDELSAKTHEIFSIGEELK-- 172
Cdd:TIGR01612 834 INEMKFMKddflnkvDKFINFENNcKEKIDSEHEQFAELTNkiKAEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQni 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 173 NKTMKLNEknsqfQTKLAEISSEN-RNLERKVQKFREEL-----IVKDQRSLE-VHQDQ-ENT--------QKVLKEVkQ 236
Cdd:TIGR01612 914 NTLKKVDE-----YIKICENTKESiEKFHNKQNILKEILnknidTIKESNLIEkSYKDKfDNTlidkinelDKAFKDA-S 987
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 237 LSDR-------LDYLTPKRKDVSRIKERDDFLQFSAKIIEETMSELKLKNA--------------------RLERELSEK 289
Cdd:TIGR01612 988 LNDYeaknnelIKYFNDLKANLGKNKENMLYHQFDEKEKATNDIEQKIEDAnknipnieiaihtsiyniidEIEKEIGKN 1067
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 290 EELvkVTKEELQELQKTVTQAMGDSEQATKY-----LHAENMKLTRQ----KADIRCDLLEARRNLKGFDEKRE------ 354
Cdd:TIGR01612 1068 IEL--LNKEILEEAEINITNFNEIKEKLKHYnfddfGKEENIKYADEinkiKDDIKNLDQKIDHHIKALEEIKKksenyi 1145
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 355 --------ELEKQRDEAL--EDVRRITELKKNVEIELRSLKLLAEEreeqIDELKSRVAGYEVLRRDHEAVKNELAKAEE 424
Cdd:TIGR01612 1146 deikaqinDLEDVADKAIsnDDPEEIEKKIENIVTKIDKKKNIYDE----IKKLLNEIAEIEKDKTSLEEVKGINLSYGK 1221
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 425 KLNKMGAHLVMADKQSShfktlkETAEGSRRRAIEQCNEMVARIRGLEASLENQRKVEQELEMVKAENVRQaKKIEFMKE 504
Cdd:TIGR01612 1222 NLGKLFLEKIDEEKKKS------EHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDD-KDHHIISK 1294
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 505 EIQETHLDYREELSKLAKgggsheaDSQRDSELRSAKKTIQ----EVKADNKKLQQILEEVrQNQSKVLEENvKLRKGMA 580
Cdd:TIGR01612 1295 KHDENISDIREKSLKIIE-------DFSEESDINDIKKELQknllDAQKHNSDINLYLNEI-ANIYNILKLN-KIKKIID 1365
|
650 660 670
....*....|....*....|....*....|...
gi 17536671 581 EAIE---KIEEFKRNWHSSREAGERLQLEAKEN 610
Cdd:TIGR01612 1366 EVKEytkEIEENNKNIKDELDKSEKLIKKIKDD 1398
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
193-425 |
4.45e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 193 SSENRNLERKVQKFREELivkDQRSLEVHQDQENTQKVLKEVKQLSDRLDYLTpkrkdvSRIKErddfLQFSAKIIEETM 272
Cdd:COG4942 19 ADAAAEAEAELEQLQQEI---AELEKELAALKKEEKALLKQLAALERRIAALA------RRIRA----LEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 273 SELKLKNARLERELSEKEELVKvtkEELQELQKTVTQA----------MGDSEQATKYLHAENMKLTRQKADIRCDLLEA 342
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELA---ELLRALYRLGRQPplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 343 RRNLKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRvagYEVLRRDHEAVKNELAKA 422
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE---AEELEALIARLEAEAAAA 239
|
...
gi 17536671 423 EEK 425
Cdd:COG4942 240 AER 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
99-598 |
4.89e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 99 DDLKQKESQIRILQNRCLRLEtEKQKMQDTISGYQEDLKENEIRIEnlnSRLHKLEDELSAKTHEIFSIGEELKNKTMKL 178
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAE-EAKKAEEAKKKAEEAKKADEAKKK---AEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 179 NEKNSQFQTKLAEISSENRNLERK-----VQKFREELIVKDQRSLEVHQDQENTQKVLKEVKQLSDRLDYLtpKRKDVSR 253
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAEEAkkadeAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL--RKAEEAK 1587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 254 IKERDDFLQFSAKIIEEtmSELKLKNARLERELSEKEELVKVTKEE---LQELQKTVTQAMGDSEQATKYLHAENMKLTR 330
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEE--KKMKAEEAKKAEEAKIKAEELKKAEEEkkkVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 331 QKADIRCDLLEARRNLKGFDEKREELEKQRDEAlEDVRRITELKKNVEIELRSLKLLAEEREEqidelksRVAGYEVLRR 410
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA-EEAKKAEELKKKEAEEKKKAEELKKAEEE-------NKIKAEEAKK 1737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 411 DHEAVK---NELAKAEEKLNKMGAHLVMADKQSSHFKTLKETA--EGSRRRAIEQCNEMVARIRGL--------EASLEN 477
Cdd:PTZ00121 1738 EAEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIKDIfdnfaniiEGGKEG 1817
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 478 QRKVEQELEMVKAENVRQAKKIEFMKEEIQETHLDYREELSKLAKGGGSHEADSQRDSELRSAKKTIQEVKaDNKKLQQI 557
Cdd:PTZ00121 1818 NLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEAD-EIEKIDKD 1896
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 17536671 558 LEEVRQNQSKVLEENVKLrkgMAEAIEKIEEFKRNWHSSRE 598
Cdd:PTZ00121 1897 DIEREIPNNNMAGKNNDI---IDDKLDKDEYIKRDAEETRE 1934
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
133-704 |
4.99e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 133 QEDLKENEIRIENLNSRLHKLEDELSAKTHEIFSIGEELKNKTMKLNEKNSQFQtKLAEISSENRNLERKVQKFREELIV 212
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN-ELSSLEDMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 213 KDQRSLEVHQDQENTQKVL--KEVKQLSDRLDYLTPKrKDVSRIKERDDFLQFSAKIIEETMSELklknARLERELSEKE 290
Cdd:PRK01156 268 ELEKNNYYKELEERHMKIIndPVYKNRNYINDYFKYK-NDIENKKQILSNIDAEINKYHAIIKKL----SVLQKDYNDYI 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 291 ELvKVTKEELQELQKTVTQAMGDSEQATKYLHAENMKLTRQKADIRCDLLEARRNLKGFDEKREELEKQRDEALEDVRRI 370
Cdd:PRK01156 343 KK-KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 371 TELKKNVEIELRSLKLLAEEREEQIDELKSRVA--------GYEVLRRDHEAVKNELAKAEEKLNKMGAHLVMADKQSSH 442
Cdd:PRK01156 422 SSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVD 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 443 FKTLKETAEGsrrraiEQCNEMVARIRGLEASLENQRKVEQELEMVKAENVrqakKIEFMKEEIQETHLDYREelsklAK 522
Cdd:PRK01156 502 LKKRKEYLES------EEINKSINEYNKIESARADLEDIKIKINELKDKHD----KYEEIKNRYKSLKLEDLD-----SK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 523 GGGSHEADSQRDS-ELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAEAIEKIEEFKRNWHSSREAGE 601
Cdd:PRK01156 567 RTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIE 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 602 RLQLEA---KENEEKVLKVEEELQEKRLEVLEKEELVNYLQSQIN-TKQTKQPKLSRRSTLMSTISEVDtstyvreveev 677
Cdd:PRK01156 647 KLRGKIdnyKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDdAKANRARLESTIEILRTRINELS----------- 715
|
570 580
....*....|....*....|....*..
gi 17536671 678 RALEEQREELQAYLAEKRKMADLQKSR 704
Cdd:PRK01156 716 DRINDINETLESMKKIKKAIGDLKRLR 742
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
118-402 |
5.35e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 118 LETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKL---EDELSAKTHeifsigeELKNKTMKLNEKNSQFQTKLAEISS 194
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELaekRDELNAQVK-------ELREEAQELREKRDELNEKVKELKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 195 ENRNLERKVQKFREELIVKDQRSLEVHQDQENTQKVLKEVKQLSDRLDyltpkRKDVSRIKERDDFLQFS--AKIIEETM 272
Cdd:COG1340 79 ERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQ-----TEVLSPEEEKELVEKIKelEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 273 SELKLKNarlerELSEKEELVKVTKEELQELQKTVTQAmgdSEQATKYLhaENMKLTRQKAD-IRCDLLEARRNLKGFDE 351
Cdd:COG1340 154 KALEKNE-----KLKELRAELKELRKEAEEIHKKIKEL---AEEAQELH--EEMIELYKEADeLRKEADELHKEIVEAQE 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 17536671 352 KREELEKQRDEALEDVRRITELKKNVEIELRSLKLlaEEREEQIDELKSRV 402
Cdd:COG1340 224 KADELHEEIIELQKELRELRKELKKLRKKQRALKR--EKEKEELEEKAEEI 272
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
126-363 |
7.26e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 7.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 126 QDTISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIFSIGEELKNKTMKLNEKNSQ---FQTKLAEISSENRNLERK 202
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQElaaLEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 203 VQKfREELIVKDQRSLEVHQDQENTQKVL--KEVKQLSDRLDYLtpkrKDVSRikerddFLQFSAKIIEETMSELKLKNA 280
Cdd:COG4942 99 LEA-QKEELAELLRALYRLGRQPPLALLLspEDFLDAVRRLQYL----KYLAP------ARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 281 RLERELSEKEELvkvtKEELQELQKTVTQAMGDSEQATKYLHAENMKLTRQKAdircDLLEARRNLKGFDEKREELEKQR 360
Cdd:COG4942 168 ELEAERAELEAL----LAELEEERAALEALKAERQKLLARLEKELAELAAELA----ELQQEAEELEALIARLEAEAAAA 239
|
...
gi 17536671 361 DEA 363
Cdd:COG4942 240 AER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
279-705 |
8.64e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 8.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 279 NARL--ERELSEKEELVKVTKEELQEL-QKTVTQAMGDSEQATKYLHAENMKLTRQKADIRCDLLEARRNLKGFDEKREE 355
Cdd:PRK02224 173 DARLgvERVLSDQRGSLDQLKAQIEEKeEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 356 LEkqrdEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRvagyevlrRDHEAVKNELAKAEeklnkmgahlvm 435
Cdd:PRK02224 253 LE----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE--------RDDLLAEAGLDDAD------------ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 436 ADKQSSHFKTLkETAEGSRRRAIEQCNemvARIRGLEASLENQRKVEQELEMVKAENVRQAKKIEFMKEEIQETHLDYRE 515
Cdd:PRK02224 309 AEAVEARREEL-EDRDEELRDRLEECR---VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRRE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 516 ELSKLakgggsheadsqrDSELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAEAIEKIEEfkrnwhs 595
Cdd:PRK02224 385 EIEEL-------------EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE------- 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 596 sreaGERLQLEAK------------------ENEEKVLKVEEELQEKRLEVLEKEELVNYLQSQINTKQTKQPKLSRRST 657
Cdd:PRK02224 445 ----AEALLEAGKcpecgqpvegsphvetieEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRED 520
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 17536671 658 LMSTISEVDTSTYVREvEEVRALEEQREELQAYLAEKRKMADLQKSRS 705
Cdd:PRK02224 521 LEELIAERRETIEEKR-ERAEELRERAAELEAEAEEKREAAAEAEEEA 567
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
72-216 |
1.20e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.47 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 72 ESVIIERSNKVSTQETRIYRRDVTLLEDDLKQKESQIRILQNRCLRLETEKQKMQDTIsgyqedlKENEIRIENLNSRLH 151
Cdd:COG2433 379 EEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAEL-------EEKDERIERLERELS 451
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17536671 152 KLEDELSAKTHEifsiGEELKnktmKLNEKNSQFQTKLAEISSENRNLERKVQKFReELIVKDQR 216
Cdd:COG2433 452 EARSEERREIRK----DREIS----RLDREIERLERELEEERERIEELKRKLERLK-ELWKLEHS 507
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
102-697 |
1.51e-05 |
|
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: 49.40 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 102 KQKESQIRILQNRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIFSIGEELKNKT-MKLN- 179
Cdd:pfam01576 408 KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETrQKLNl 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 180 ---------EKNSqFQTKLAEISSENRNLERKVQKFREELI----VKDQRSLEVHQDQENTQKVLKEVKQLSDRLDYLTP 246
Cdd:pfam01576 488 strlrqledERNS-LQEQLEEEEEAKRNVERQLSTLQAQLSdmkkKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAA 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 247 KRKDVSRIKER-----DDFL------------------QFSAKIIEETMSELKLKNAR--LERELSEKEELVKVTKEELQ 301
Cdd:pfam01576 567 AYDKLEKTKNRlqqelDDLLvdldhqrqlvsnlekkqkKFDQMLAEEKAISARYAEERdrAEAEAREKETRALSLARALE 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 302 ELQktvtQAMGDSEQATKYLHAENMKLTRQKADIRCDLLEARRNLKGFDEKREELEKQRDEaLEDVRRITE-LKKNVEIE 380
Cdd:pfam01576 647 EAL----EAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEE-LEDELQATEdAKLRLEVN 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 381 LRSLKLLAEE----REEQIDE----LKSRVAGYEVLRRDHEAVKNELAKAEEKL----NKMGAHLVMADKqsshfktlke 448
Cdd:pfam01576 722 MQALKAQFERdlqaRDEQGEEkrrqLVKQVRELEAELEDERKQRAQAVAAKKKLeldlKELEAQIDAANK---------- 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 449 taegSRRRAIEQCNEMVARIRGLEASLENQRKVEQELEMVKAENVRQAKKIEFMKEEIQETHldyreELSKLAKGGGSHE 528
Cdd:pfam01576 792 ----GREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDL-----AASERARRQAQQE 862
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 529 ADSQRDSELRSAKK---TIQEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAEAIEKIEE------FKRNWHSSREA 599
Cdd:pfam01576 863 RDELADEIASGASGksaLQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTElaaersTSQKSESARQQ 942
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 600 GERLQLEAKENEEKVLKVEEELQEKRLEVLEKEELVNYLQSQINTKQTKQP-KLSRRS--TLMSTISEVD-----TSTYV 671
Cdd:pfam01576 943 LERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAAnKLVRRTekKLKEVLLQVEderrhADQYK 1022
|
650 660 670
....*....|....*....|....*....|....
gi 17536671 672 REVEEV--------RALEEQREELQAYLAEKRKM 697
Cdd:pfam01576 1023 DQAEKGnsrmkqlkRQLEEAEEEASRANAARRKL 1056
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
86-703 |
1.60e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 86 ETRIYRRDVTLLEDDLKQKESQIRILQnrcLRLETEKQKMQDTISGYQEdlkeneiRIENLNSRLHKLEDELSA--KTHE 163
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLT---LRSQLLTLCTPCMPDTYHE-------RKQVLEKELKHLREALQQtqQSHA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 164 IFSIGEELKNKTMKLNEKNSQFQTKLAEISS-----ENRNLERKVQKFREELIVKDQRSLEVHQDQENTQKVLKEVK-QL 237
Cdd:TIGR00618 244 YLTQKREAQEEQLKKQQLLKQLRARIEELRAqeavlEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMrSR 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 238 SDRLDYLTPKRKDVSRIKERDDFLQ--FSAKI-IEETMSELKLKNARLERELSEKEELVKvtkeeLQELQKTVTQAMGDS 314
Cdd:TIGR00618 324 AKLLMKRAAHVKQQSSIEEQRRLLQtlHSQEIhIRDAHEVATSIREISCQQHTLTQHIHT-----LQQQKTTLTQKLQSL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 315 EQATKYLHAENMK---LTRQKADIRCDLLEARrnlkgfdeKREELEKQRDEALED-VRRITELKKNVEIELRSLKLLAEE 390
Cdd:TIGR00618 399 CKELDILQREQATidtRTSAFRDLQGQLAHAK--------KQQELQQRYAELCAAaITCTAQCEKLEKIHLQESAQSLKE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 391 REEQIDELKSRVAGYEVLRRDHEAVKNELAKAEEKLNKMGAHLVMAdkqsshfKTLKETAEGSRRRaieqcnemvarirg 470
Cdd:TIGR00618 471 REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPA-------RQDIDNPGPLTRR-------------- 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 471 LEASLENQRKVEQELEMVKAENVRQAKKIEFMKEEIQETHLD----------YREELSKLAKGGGSHEADSQRDSELRSA 540
Cdd:TIGR00618 530 MQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSfsiltqcdnrSKEDIPNLQNITVRLQDLTEKLSEAEDM 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 541 KKTIQEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAEAIEKI--EEFKRNWHSSREAGERLqLEAKENEekvlkvE 618
Cdd:TIGR00618 610 LACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqERVREHALSIRVLPKEL-LASRQLA------L 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 619 EELQEKRLEVLEKEELVNYLQSQINTKQTKQPKLSRRSTLMSTISEVDTSTYVREVEEVRALEEQREELQAYLAEKRKMA 698
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEA 762
|
....*
gi 17536671 699 DLQKS 703
Cdd:TIGR00618 763 HFNNN 767
|
|
| C1_ScPKC1-like_rpt2 |
cd20823 |
second protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ... |
737-796 |
1.73e-05 |
|
second protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae protein kinase C-like 1 (ScPKC1) and similar proteins; ScPKC1 is required for cell growth and for the G2 to M transition of the cell division cycle. It mediates a protein kinase cascade, activating BCK1 which itself activates MKK1/MKK2. The family also includes Schizosaccharomyces pombe PKC1 and PKC2, which are involved in the control of cell shape and act as targets of the inhibitor staurosporine. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410373 Cd Length: 59 Bit Score: 43.45 E-value: 1.73e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17536671 737 HDIPHKWLEFrhySVLSMK-CSLCFVGITFFTK-ANKCSHCDVRVHASCAPRVNNTCGIPAQ 796
Cdd:cd20823 1 HRIPHRFEPF---TNLGANwCCHCGQMLPLGRKqIRKCTECGKTAHAQCAHLVPNFCGLSME 59
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
331-571 |
1.80e-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: 48.61 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 331 QKADIRCDLLEARRNLKgfdEKREEL---EKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRVAgyeV 407
Cdd:COG4942 21 AAAEAEAELEQLQQEIA---ELEKELaalKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA---E 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 408 LRRDHEAVKNELAKAEEKLNKMGAH-----LVMADKQSSHFKTLK--ETAEGSRRRAIEQCNEMVARIRGLEASLENQRk 480
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQpplalLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAER- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 481 veQELEMVKAENVRQAKKIEFMKEEIQEThldyreeLSKLAKgggsheadsqrdsELRSAKKTIQEVKADNKKLQQILEE 560
Cdd:COG4942 174 --AELEALLAELEEERAALEALKAERQKL-------LARLEK-------------ELAELAAELAELQQEAEELEALIAR 231
|
250
....*....|.
gi 17536671 561 VRQNQSKVLEE 571
Cdd:COG4942 232 LEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
97-708 |
2.02e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 97 LEDDLKQKE--SQIRILQNRCLRLETEKQKMQDTISGYqeDLKENEIRIENLNSRLHKLEDELSaktheifsigeelknk 174
Cdd:COG4913 244 LEDAREQIEllEPIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELA---------------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 175 tmKLNEKNSQFQTKLAEISSENRNLERKVQKF---REELIVKDQRSLEVHQDQenTQKVLKEVKQLSDRLDYLTPKRKD- 250
Cdd:COG4913 306 --RLEAELERLEARLDALREELDELEAQIRGNggdRLEQLEREIERLERELEE--RERRRARLEALLAALGLPLPASAEe 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 251 ----VSRIKERDDFLQFSAKIIEETMSELKLKNARLERELSEKEElvkvtkeELQELQKTVTQAMGDSEQATKYLhAENM 326
Cdd:COG4913 382 faalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA-------EIASLERRKSNIPARLLALRDAL-AEAL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 327 KLTRQKADIRCDLLEARrnlKGFDEKREELEK----QR------DEALEDVRRITElKKNVEIELRSLKLLAEEREEQID 396
Cdd:COG4913 454 GLDEAELPFVGELIEVR---PEEERWRGAIERvlggFAltllvpPEHYAAALRWVN-RLHLRGRLVYERVRTGLPDPERP 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 397 ELKSRVAGYEVLRRDHEA---VKNELAKA--------EEKLnKMGAHLVMADKQSSHFKTL--KETAEGSRRR------A 457
Cdd:COG4913 530 RLDPDSLAGKLDFKPHPFrawLEAELGRRfdyvcvdsPEEL-RRHPRAITRAGQVKGNGTRheKDDRRRIRSRyvlgfdN 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 458 IEQCNEMVARIRGLEASLENQRKVEQELEMVKAENVRQAkkiefmkeEIQETHLDYREELSKLAkgggsheadsQRDSEL 537
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERR--------EALQRLAEYSWDEIDVA----------SAEREI 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 538 RSAKKTIQEVKADNKKLQQILEEVRQNQSKVLEenvkLRKGMAEAIEKIEEFKRNWHSSREAGERLQLEAKENEEKVLKV 617
Cdd:COG4913 671 AELEAELERLDASSDDLAALEEQLEELEAELEE----LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 618 EEELQEKRLEVLEKEELVNY----LQSQINTKQTKQPKLSRR-STLMSTISEV---DTSTYVREVEEVRALEEQREELQA 689
Cdd:COG4913 747 LRALLEERFAAALGDAVERElrenLEERIDALRARLNRAEEElERAMRAFNREwpaETADLDADLESLPEYLALLDRLEE 826
|
650 660
....*....|....*....|.
gi 17536671 690 Y-LAEKR-KMADLQKSRSTAN 708
Cdd:COG4913 827 DgLPEYEeRFKELLNENSIEF 847
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
9-428 |
2.97e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 9 PQSSKTPKSKSARYSSPYQVIDLNNESQEDLKTRLLEAENIIQDlrSERDALHESLVDKAGLNESVIIERSNkVSTQETR 88
Cdd:pfam02463 584 IPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEG--ILKDTELTKLKESAKAKESGLRKGVS-LEEGLAE 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 89 IYRRDVTLLEDDLKQKESQIRILQNRCLRLETEKQKMQDTISGYQEDLKENEIR-----IENLNSRLHKLEDELSAKTHE 163
Cdd:pfam02463 661 KSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKlkleaEELLADRVQEAQDKINEELKL 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 164 IFSIGEELKNKTMKLNEKNSQFQTKLAEISSENRNLERKVQKFREELIVKDQRSLEVHQDQENtQKVLKEVKQLSDRLDY 243
Cdd:pfam02463 741 LKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL-RALEEELKEEAELLEE 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 244 LTPKRKDVSRIKErddfLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLHA 323
Cdd:pfam02463 820 EQLLIEQEEKIKE----EELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKE 895
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 324 ENMKLTRQKADIRCDLLEARRNLKGFDEKREELEKQRDEALEdvRRITELKKNVEIELRSLKLLAEEREEQIDELKSRVA 403
Cdd:pfam02463 896 KEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEP--EELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG 973
|
410 420
....*....|....*....|....*
gi 17536671 404 GYEVLRRDHEAVKNELAKAEEKLNK 428
Cdd:pfam02463 974 KVNLMAIEEFEEKEERYNKDELEKE 998
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
255-641 |
3.06e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 255 KERDDFLQFSAKIIEETMSELKLKNARLeRELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLhaENMKLTRQKAD 334
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREEL--EKLEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 335 IRCDLLEARRNLKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSL-KLLAEEREEQIDELKSRVAGYEVLRRDHE 413
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 414 AVKNELAKAEEKLNKMGAHLVMADKQSSHFKTLKETAEGSRRRAIEQcneMVARIRGLEASLENQRK------------- 480
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA---ALLALLGLGGSLLSLILtiagvlflvlgll 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 481 --VEQELEMVKAENVRQAKKIEFMKEEIQETHLDYREELSKL-AKGGGSHEADSQRDSELRSAKKTIQEVKADNKKLQQI 557
Cdd:COG4717 287 alLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALgLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 558 LEEVRQNQ----------------SKVLEENVKLRKGMAEAIEKIEEFKRNWHSSREAGERLQLEAK--ENEEKVLKVEE 619
Cdd:COG4717 367 ELEQEIAAllaeagvedeeelraaLEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEEleELEEELEELEE 446
|
410 420
....*....|....*....|..
gi 17536671 620 ELQEKRLEVLEKEELVNYLQSQ 641
Cdd:COG4717 447 ELEELREELAELEAELEQLEED 468
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
97-242 |
4.20e-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: 46.46 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 97 LEDDLKQKESQIRILQNRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKL--EDELSAKTHEIfsigEELKNK 174
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEI----ESLKRR 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17536671 175 TMKLNEKNSQFQTKLAEISSENRNLERKVQKFREELI-VKDQRSLEVHQDQENTQKVLKEVKQLSDRLD 242
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEeKKAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
69-424 |
4.36e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 47.93 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 69 GLNESVIIERSNKVSTQETRIYRRDVTLLEDDLKQKESQIrilqnrclrLETEKQKMQDTISGYQEDLK--ENEIRIE-- 144
Cdd:PLN03229 406 GFQEGVPVDPERKVNMKKREAVKTPVRELEGEVEKLKEQI---------LKAKESSSKPSELALNEMIEklKKEIDLEyt 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 145 ------NLNSRLHKLEDELSAKTHEIFSIGEELKNKTMKLNEknsQFQTKLAEiSSENRNLERKVQKFRE-----ELIVK 213
Cdd:PLN03229 477 eaviamGLQERLENLREEFSKANSQDQLMHPVLMEKIEKLKD---EFNKRLSR-APNYLSLKYKLDMLNEfsrakALSEK 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 214 DQRSLEVHQDqentqkVLKEVKQLSDRLDyltpkrkdvsrIKERDDFLQfsAKIIEETMSelklKNARLERELseKEELV 293
Cdd:PLN03229 553 KSKAEKLKAE------INKKFKEVMDRPE-----------IKEKMEALK--AEVASSGAS----SGDELDDDL--KEKVE 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 294 KVTKEELQELQKtVTQAMGDSEQATKylhAENMKLTRQKADircdllearrnlKGFDEKREELEKQRDEALEDVRRITEL 373
Cdd:PLN03229 608 KMKKEIELELAG-VLKSMGLEVIGVT---KKNKDTAEQTPP------------PNLQEKIESLNEEINKKIERVIRSSDL 671
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17536671 374 KKNVEiELRS------------LKLLAEEREEQIDELKSRVAGYEVLRRDHEAVKNELAKAEE 424
Cdd:PLN03229 672 KSKIE-LLKLevakasktpdvtEKEKIEALEQQIKQKIAEALNSSELKEKFEELEAELAAARE 733
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
124-704 |
4.53e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 124 KMQDTISGYQEDLKE--NEI-RIENLNSRLHKLEDELSAKTHEIFSIG---EELKNKTMKLNEKNSQfqtkLAEISSENR 197
Cdd:PRK01156 139 EMDSLISGDPAQRKKilDEIlEINSLERNYDKLKDVIDMLRAEISNIDyleEKLKSSNLELENIKKQ----IADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 198 NLERKVQKFREELIVKDQrslevhqDQENTQKVLKEVKQLSDRldyltpKRKDVSRIKERDDFLQfsakIIEETMSELKL 277
Cdd:PRK01156 215 ITLKEIERLSIEYNNAMD-------DYNNLKSALNELSSLEDM------KNRYESEIKTAESDLS----MELEKNNYYKE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 278 KNARLERELSEKeelVKVTKEELQELQKTVTQAMGDSE-------QATKYlHAENMKLTRQKADiRCDLLEARRNLKGFD 350
Cdd:PRK01156 278 LEERHMKIINDP---VYKNRNYINDYFKYKNDIENKKQilsnidaEINKY-HAIIKKLSVLQKD-YNDYIKKKSRYDDLN 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 351 EKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQI-------DELKSRvagYEVLRRDHEAVKNELAKAE 423
Cdd:PRK01156 353 NQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILkiqeidpDAIKKE---LNEINVKLQDISSKVSSLN 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 424 EKLNKMGAHLV-------MADKQSSHFKTLKETAEGSRRRAIEQCNEMVARIRgleaslENQRKVEQELEMVKAENVRQA 496
Cdd:PRK01156 430 QRIRALRENLDelsrnmeMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLE------EKIREIEIEVKDIDEKIVDLK 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 497 KKIEFM-KEEIQETHLDYR----------EELSKLAKGGGSHEADSQRDSELRSAKKTIQEVKAD--NKKLQQI-LEEVR 562
Cdd:PRK01156 504 KRKEYLeSEEINKSINEYNkiesaradleDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTswLNALAVIsLIDIE 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 563 QNQSKVLEENVKLRkgmaEAIEKIEEFKRNWHSSREAGERLQLEAKENEEKVLKVEEELQEKRLEVLEKEELVNYLQSQI 642
Cdd:PRK01156 584 TNRSRSNEIKKQLN----DLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQI 659
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17536671 643 NTKQTKQPklsRRSTLMSTISEVDTstyvreveEVRALEEQREELQAYLAEKRKMADLQKSR 704
Cdd:PRK01156 660 AEIDSIIP---DLKEITSRINDIED--------NLKKSRKALDDAKANRARLESTIEILRTR 710
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
84-571 |
4.78e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.89 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 84 TQETRIYRRDVTLLEDDLKQKES---QIRILQNRCLRLETEKQKmqdtISGYQEDLKENEIRIENLNSRLHKLEDEL-SA 159
Cdd:pfam10174 184 TRRIAEAEMQLGHLEVLLDQKEKeniHLREELHRRNQLQPDPAK----TKALQTVIEMKDTKISSLERNIRDLEDEVqML 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 160 KTHEIFSI---GEELK--------NKTMK---------LNEKNSQ---FQTKLAEISSENRNLERKVQKFREELIVKDQR 216
Cdd:pfam10174 260 KTNGLLHTedrEEEIKqmevykshSKFMKnkidqlkqeLSKKESEllaLQTKLETLTNQNSDCKQHIEVLKESLTAKEQR 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 217 S--LEVHQD------QENTQKVLKEVKQLSDRLDyltPKRKDVSRIKERDDFLQfsakIIEETMSELKLKNARLERELSE 288
Cdd:pfam10174 340 AaiLQTEVDalrlrlEEKESFLNKKTKQLQDLTE---EKSTLAGEIRDLKDMLD----VKERKINVLQKKIENLQEQLRD 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 289 KEELVKVTKEELQELQK---TVTQAMGDSEQAtkylhaenmkltrqkadircdLLEARRNLKGFDEKREELEKQRDEALE 365
Cdd:pfam10174 413 KDKQLAGLKERVKSLQTdssNTDTALTTLEEA---------------------LSEKERIIERLKEQREREDRERLEELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 366 DVRRitELkKNVEIELRSLKLLAEEREEQIDELKSRVAGY--EVLRRDHEAVKNELA--KAEEKLNKMGAHLVMADKQSS 441
Cdd:pfam10174 472 SLKK--EN-KDLKEKVSALQPELTEKESSLIDLKEHASSLasSGLKKDSKLKSLEIAveQKKEECSKLENQLKKAHNAEE 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 442 HFKTLKETAEgsRRRAIEQ-----------CNEMVARIRGLEASLENQR----KVEQELEMVKAENVR-QAKKIEFMKEE 505
Cdd:pfam10174 549 AVRTNPEIND--RIRLLEQevarykeesgkAQAEVERLLGILREVENEKndkdKKIAELESLTLRQMKeQNKKVANIKHG 626
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17536671 506 IQETHLDYREELSKLAKGGGSHEADSQRD--SELRSA-KKTIQEVKADNKKL---QQILEE-------VRQNQSKVLEE 571
Cdd:pfam10174 627 QQEMKKKGAQLLEEARRREDNLADNSQQLqlEELMGAlEKTRQELDATKARLsstQQSLAEkdghltnLRAERRKQLEE 705
|
|
| C1_1 |
pfam00130 |
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ... |
741-792 |
4.84e-05 |
|
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.
Pssm-ID: 395079 Cd Length: 53 Bit Score: 42.04 E-value: 4.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 17536671 741 HKWLEFRHYSvlSMKCSLCfvGITFFTKAN---KCSHCDVRVHASCAPRVNNTCG 792
Cdd:pfam00130 1 HHFVHRNFKQ--PTFCDHC--GEFLWGLGKqglKCSWCKLNVHKRCHEKVPPECG 51
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
27-588 |
7.20e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.35 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 27 QVIDLNNESQEDLKTRlleAENIIQDLRSERDALhESLVDKAGLNESV--IIERSNKVSTQ---ETRIYRRDVTLLEDDL 101
Cdd:TIGR01612 1125 QKIDHHIKALEEIKKK---SENYIDEIKAQINDL-EDVADKAISNDDPeeIEKKIENIVTKidkKKNIYDEIKKLLNEIA 1200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 102 KQKESQIRILQNRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLeDELSAKTHEI---FSIGEELKNKTMKL 178
Cdd:TIGR01612 1201 EIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDL-DEIKEKSPEIeneMGIEMDIKAEMETF 1279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 179 NEKNSQFqtKLAEISSENRNleRKVQKFREE---LIVKDQRSLEVHQDQENTQKVLKEVKQLSDRLDYLTPKRKDVSRIK 255
Cdd:TIGR01612 1280 NISHDDD--KDHHIISKKHD--ENISDIREKslkIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNIL 1355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 256 ERDDFLQFSAKIIEETmSELKLKNARLERELSEKEELVKVTKEE--LQELQKTVTQAMGD----------SEQATKYLHA 323
Cdd:TIGR01612 1356 KLNKIKKIIDEVKEYT-KEIEENNKNIKDELDKSEKLIKKIKDDinLEECKSKIESTLDDkdidecikkiKELKNHILSE 1434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 324 ENMKLT--RQKADIRCDLLEARRNLKGFDEKREELEK-QRDEALEDVR-RITELKKNVEiELRSLKLLAEEREEQIDELK 399
Cdd:TIGR01612 1435 ESNIDTyfKNADENNENVLLLFKNIEMADNKSQHILKiKKDNATNDHDfNINELKEHID-KSKGCKDEADKNAKAIEKNK 1513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 400 SRVAGY-----EVLRRDHE-AVKNELAKAEEKLNKMGAHLVMADKQsshFKTLKETAEGS----RRRAIEQCNEMVARIR 469
Cdd:TIGR01612 1514 ELFEQYkkdvtELLNKYSAlAIKNKFAKTKKDSEIIIKEIKDAHKK---FILEAEKSEQKikeiKKEKFRIEDDAAKNDK 1590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 470 GLEASLENQRKVEQ-ELEMVKAENVRQA-----KKIEFMKEEIQETHLDYREelSKLAKGGGSHEADSQRDSELRSAKKT 543
Cdd:TIGR01612 1591 SNKAAIDIQLSLENfENKFLKISDIKKKindclKETESIEKKISSFSIDSQD--TELKENGDNLNSLQEFLESLKDQKKN 1668
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 17536671 544 IQEVKAD----NKKLQQILEEVRQNQSK----VLEENVKLRKGMAEAIEKIEE 588
Cdd:TIGR01612 1669 IEDKKKEldelDSEIEKIEIDVDQHKKNyeigIIEKIKEIAIANKEEIESIKE 1721
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
3-581 |
7.58e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 3 ESIYTTPQSSKTPKSKSARYSSPYQVIDLNNESQEDLKTRLLEAENIIQDLRSERDALHESLVDKAGLNESV-------- 74
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIhtlqqqkt 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 75 IIERSNKVSTQETRIYRRDV-TLLEDDLKQkesqiRILQNRCLRLETEkQKMQDTISGYQEDLKENEIRIENLNSR-LHK 152
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQaTIDTRTSAF-----RDLQGQLAHAKKQ-QELQQRYAELCAAAITCTAQCEKLEKIhLQE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 153 LEDELSAKTheifsigEELKNKTmKLNEKNSQFQTKLAEISSENRNLERKVQKFREELIVKDQRSLEVHQDQENTQKVLK 232
Cdd:TIGR00618 464 SAQSLKERE-------QQLQTKE-QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 233 EVKQLSDRLD----YLTPKRKDVSRIKE-----RDDFLQFSAKI------------IEETMSELKLKNARLERELSEKEE 291
Cdd:TIGR00618 536 TYAQLETSEEdvyhQLTSERKQRASLKEqmqeiQQSFSILTQCDnrskedipnlqnITVRLQDLTEKLSEAEDMLACEQH 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 292 LVKVTKE-ELQELQKTVTQAMGDSEQATKYLHAENMKLTRQKADIRCDLLEARRNLKGFDEKREELEKQRDEALEDVRRI 370
Cdd:TIGR00618 616 ALLRKLQpEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYW 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 371 TELKKNVEIELRSL--KLLAEEREEQIDELKSRVAGYEVLRRDhEAVKNELAKAEEKLNKMGAHLVMADKQsshfKTLKE 448
Cdd:TIGR00618 696 KEMLAQCQTLLRELetHIEEYDREFNEIENASSSLGSDLAARE-DALNQSLKELMHQARTVLKARTEAHFN----NNEEV 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 449 TAEGSRRRAIEQcnemvarirgLEASLENQRKVEQE----LEMVKAENVRQAKKIEFMKEEIQETHLDYREEL-SKLAKG 523
Cdd:TIGR00618 771 TAALQTGAELSH----------LAAEIQFFNRLREEdthlLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFlSRLEEK 840
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 17536671 524 GGSHEADSQRDSELRSAKKTIQEVKADNKKLQQILEEVR-QNQSKVLEENVKLRKGMAE 581
Cdd:TIGR00618 841 SATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNgINQIKIQFDGDALIKFLHE 899
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
244-458 |
8.79e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 244 LTPKRKDVSRIKERDDFLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLHA 323
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 324 ENMKLTR--------------QKADIRCDLLEARRN-LKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLA 388
Cdd:COG3883 98 SGGSVSYldvllgsesfsdflDRLSALSKIADADADlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 389 EEREEQIDELKSRVAGYEVLRRDHEAVKNELAKAEEKLNKMGAHLVMADKQSSHFKTLKETAEGSRRRAI 458
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
186-427 |
9.34e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 186 QTKLAEIS--SENRNL-ERKVQKFREELIvkdQRSLEVHQDQ-ENTQKVL-KEVKQLSDRLDYLtpkRKDVSRIKERDDF 260
Cdd:COG3206 134 GSNVIEISytSPDPELaAAVANALAEAYL---EQNLELRREEaRKALEFLeEQLPELRKELEEA---EAALEEFRQKNGL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 261 LQFS--AKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATkyLHAENMKLTRQKADIRCD 338
Cdd:COG3206 208 VDLSeeAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ--LRAQLAELEAELAELSAR 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 339 LLEARRNLKGFDEKREELEKQRDEALEDVRRitelkkNVEIELRSLKLLAEEREEQIDELKSRVAG-------YEVLRRD 411
Cdd:COG3206 286 YTPNHPDVIALRAQIAALRAQLQQEAQRILA------SLEAELEALQAREASLQAQLAQLEARLAElpeleaeLRRLERE 359
|
250
....*....|....*.
gi 17536671 412 HEAVKNELAKAEEKLN 427
Cdd:COG3206 360 VEVARELYESLLQRLE 375
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
351-605 |
9.76e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.82 E-value: 9.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 351 EKREELEKQRDEALEDvrrITELKKNVEielRSLKLLAEEREEQIDELksrvagyEVLRRDHEAVKNELAKAEEKLNKMG 430
Cdd:PLN02939 117 TNSKDGEQLSDFQLED---LVGMIQNAE---KNILLLNQARLQALEDL-------EKILTEKEALQGKINILEMRLSETD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 431 AHLVMADKQSSHFKTLKETAEGSRrraieqcNEMVARIrglEASLENQRKVEQELEMVKAENVRQAKKIEFMKEEIQETH 510
Cdd:PLN02939 184 ARIKLAAQEKIHVEILEEQLEKLR-------NELLIRG---ATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 511 lDYREELSKLAKGGGSHEA----------DSQRD-SELRSAKKTIQEVKADNkkLQQILEEVRQNQSK---VLEENVKLR 576
Cdd:PLN02939 254 -ETEERVFKLEKERSLLDAslreleskfiVAQEDvSKLSPLQYDCWWEKVEN--LQDLLDRATNQVEKaalVLDQNQDLR 330
|
250 260
....*....|....*....|....*....
gi 17536671 577 KgmaeAIEKIEEFKRNWHSSREAGERLQL 605
Cdd:PLN02939 331 D----KVDKLEASLKEANVSKFSSYKVEL 355
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
103-439 |
1.05e-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: 46.65 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 103 QKESQIRILQNRCLRLETEKQKMQD---TISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIFSI---GEELKNKT- 175
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESserTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLkneGDHLRNVQt 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 176 ------MKLNEKNSQFQTKLAEISS-----------------ENRNLERKVQKFREEL----IVKDQ-----RSLEVHQD 223
Cdd:pfam15921 549 ecealkLQMAEKDKVIEILRQQIENmtqlvgqhgrtagamqvEKAQLEKEINDRRLELqefkILKDKkdakiRELEARVS 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 224 QENTQKVlKEVKQLSDRLdyltpkrKDVSRIKERDDFLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQEL 303
Cdd:pfam15921 629 DLELEKV-KLVNAGSERL-------RAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 304 QKTVTQAMGDSEQATKYLHAENMKLTRQKADIRCDLLEARRNLKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRS 383
Cdd:pfam15921 701 LKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELST 780
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 17536671 384 lklLAEEREEQIDELksrvagyEVLRRDHEAVKNELAKAEEKLNKmgAHLVMADKQ 439
Cdd:pfam15921 781 ---VATEKNKMAGEL-------EVLRSQERRLKEKVANMEVALDK--ASLQFAECQ 824
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
53-305 |
1.06e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.46 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 53 LRSERDALHESLVDkagLNESVIIERSNKVSTQETRIYRRDVTLLE---DDLKQKESQIRILQNrcLRLETEKQKMQDTI 129
Cdd:PRK05771 14 LKSYKDEVLEALHE---LGVVHIEDLKEELSNERLRKLRSLLTKLSealDKLRSYLPKLNPLRE--EKKKVSVKSLEELI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 130 SGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIFSIgEELKNKTMKLNEKNSQ--FQTKLAEISSENRNLERKVQKFR 207
Cdd:PRK05771 89 KDVEEELEKIEKEIKELEEEISELENEIKELEQEIERL-EPWGNFDLDLSLLLGFkyVSVFVGTVPEDKLEELKLESDVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 208 EELIVKDQRSLE---VHQDQENTQKVLKEVKQLS-DRLDYLTPKRKD--VSRIKERddflqfsakiIEETMSELKLKNAR 281
Cdd:PRK05771 168 NVEYISTDKGYVyvvVVVLKELSDEVEEELKKLGfERLELEEEGTPSelIREIKEE----------LEEIEKERESLLEE 237
|
250 260
....*....|....*....|....*
gi 17536671 282 LERELSEKEELVKVTKEEL-QELQK 305
Cdd:PRK05771 238 LKELAKKYLEELLALYEYLeIELER 262
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
38-370 |
1.19e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 38 DLKTRLLEAENIIQDLRSERDALHESLVDKAGLNESVIIERSNKVSTQETRIYRrdvtlleddLKQKESQIRILQNRCLR 117
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEAR---------IRELEEDIKTLTQRVLE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 118 LETEKQKMQDTI--------------SGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIFSIGEELKNKTMKLNE--- 180
Cdd:pfam07888 148 RETELERMKERAkkagaqrkeeeaerKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTahr 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 181 KNSQFQTKLAEISSENRNL---ERKVQKFREELIV----KDQRSLEVHQdqentqkVLKEVKQLSDRLDYLTPK-RKDVS 252
Cdd:pfam07888 228 KEAENEALLEELRSLQERLnasERKVEGLGEELSSmaaqRDRTQAELHQ-------ARLQAAQLTLQLADASLAlREGRA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 253 R-IKERDDFLQfsakiieetmselklkNARLERELSEKeelvkvTKEELQELQKTVTQAMGDSEQATKYLHAENMKLTRQ 331
Cdd:pfam07888 301 RwAQERETLQQ----------------SAEADKDRIEK------LSAELQRLEERLQEERMEREKLEVELGREKDCNRVQ 358
|
330 340 350
....*....|....*....|....*....|....*....
gi 17536671 332 KADIRCDLLEARRNLKGFDEKREELEKQRDEALEDVRRI 370
Cdd:pfam07888 359 LSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQL 397
|
|
| C1 |
cd00029 |
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ... |
741-791 |
1.23e-04 |
|
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.
Pssm-ID: 410341 Cd Length: 50 Bit Score: 40.96 E-value: 1.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 17536671 741 HKWLEFRHYSvlSMKCSLCFVGITFFTKAN-KCSHCDVRVHASCAPRVNNTC 791
Cdd:cd00029 1 HRFVPTTFSS--PTFCDVCGKLIWGLFKQGlKCSDCGLVCHKKCLDKAPSPC 50
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
331-500 |
1.53e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 331 QKADIRCDLLEARRnlKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRVAgyEVL-R 409
Cdd:COG1579 13 QELDSELDRLEHRL--KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG--NVRnN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 410 RDHEAVKNELAKAEEKLNKmgahlvmADKQSSHFKTLKETAEGSRRRAIEQCNEMVARIRGLEASLENQR-KVEQELEMV 488
Cdd:COG1579 89 KEYEALQKEIESLKRRISD-------LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELaELEAELEEL 161
|
170
....*....|..
gi 17536671 489 KAENVRQAKKIE 500
Cdd:COG1579 162 EAEREELAAKIP 173
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
144-460 |
1.78e-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: 45.98 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 144 ENLNSRLHKLEDELSAKTHEIFSIGEELKNKTMKLnEKNSQFQTKLAEISSENRNLERKVQKFREELIVKDQRSLEVHQD 223
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGEL-EKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKD 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 224 QENTQ--KVLKEVKQLSDRLDYLTPKRKDVSRiKERDDFLQFSAKIIEETMSEL-KLKNARLERELSEKEELVKVTKE-- 298
Cdd:pfam12128 679 SANERlnSLEAQLKQLDKKHQAWLEEQKEQKR-EARTEKQAYWQVVEGALDAQLaLLKAAIAARRSGAKAELKALETWyk 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 299 ------------------ELQELQKTVTQAMGDSEQATKY-------LHAENMKLTRQKADIRCDLLEARRNLKGFDE-- 351
Cdd:pfam12128 758 rdlaslgvdpdviaklkrEIRTLERKIERIAVRRQEVLRYfdwyqetWLQRRPRLATQLSNIERAISELQQQLARLIAdt 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 352 --KREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEER--EEQIDELKSRVAGYEVLRRDHEAVKNELAKAEEKLN 427
Cdd:pfam12128 838 klRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDAnsEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFK 917
|
330 340 350
....*....|....*....|....*....|...
gi 17536671 428 KmgahlVMADKQSShfkTLKETAEGSRRRAIEQ 460
Cdd:pfam12128 918 N-----VIADHSGS---GLAETWESLREEDHYQ 942
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
342-572 |
2.41e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 342 ARRNLKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRVAgyevlrrdheAVKNELAK 421
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA----------EAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 422 AEEKLNKMGAHLVMADKQSSHFKTL---KETAE-----GSRRRAIEQCNEMVARIRGLEASLENQRKveqELEMVKAENV 493
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVLlgsESFSDfldrlSALSKIADADADLLEELKADKAELEAKKA---ELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 494 RQAKKIEFMKEEIQETHLDYREELSKLAKGGGSHEAD-SQRDSELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVLEEN 572
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQlAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
341-592 |
3.08e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.07 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 341 EARRNLKGFDEKREELEKQRDEALedvRRITELKKNVEiELRSLKLLAEErEEQIDELKSRVAGYEVLRRD----HEAVK 416
Cdd:COG0497 162 EAYRAWRALKKELEELRADEAERA---RELDLLRFQLE-ELEAAALQPGE-EEELEEERRRLSNAEKLREAlqeaLEALS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 417 NELAKAEEKLNKMGAHLvmaDKQSSHFKTLKETAEgSRRRAIEQCNEMVARIRGLEASLENQrkvEQELEMVKA--ENVR 494
Cdd:COG0497 237 GGEGGALDLLGQALRAL---ERLAEYDPSLAELAE-RLESALIELEEAASELRRYLDSLEFD---PERLEEVEErlALLR 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 495 QAKKiefmK-----EEIQETHLDYREELSKLakgggsheadSQRDSELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVL 569
Cdd:COG0497 310 RLAR----KygvtvEELLAYAEELRAELAEL----------ENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKL 375
|
250 260 270
....*....|....*....|....*....|.
gi 17536671 570 EENVK--LRK-GMAEA-----IEKIEEFKRN 592
Cdd:COG0497 376 EKAVTaeLADlGMPNArfeveVTPLEEPGPN 406
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
46-268 |
3.08e-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: 44.75 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 46 AENIIQDLRSERDALHESLVDKAGLNESviIERSNKVSTQETRIYRRDVTLLEDDLKQKESQIRILQNRCLRLETEKQKM 125
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAA--LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 126 QDTISGYQEDLKENEIRIENLNSR---------------------LHKLEDELSAKTHEIFSIGEELKNKTMKLNEKNSQ 184
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 185 FQTKLAEISSENRNLERKVQKfREELIVKDQRSLEvhQDQENTQKVLKEVKQLSDRLDYLTPKRKDVSRIKERDDFLQFS 264
Cdd:COG4942 176 LEALLAELEEERAALEALKAE-RQKLLARLEKELA--ELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
....
gi 17536671 265 AKII 268
Cdd:COG4942 253 GKLP 256
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
249-586 |
4.61e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.56 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 249 KDVSRIKERDDFLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLHAENMKL 328
Cdd:COG5185 154 GEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 329 TRQKADIRCDLLEARR----NLKGFDEKREELEKQR-DEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRVA 403
Cdd:COG5185 234 ALKGFQDPESELEDLAqtsdKLEKLVEQNTDLRLEKlGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATES 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 404 GYEVLRR-----DHEAVKNELAKAEEKL--NKMGAHLVMADKQSSHFKTLKETAEGSR-RRAIEQCNEMVARIRGLEASL 475
Cdd:COG5185 314 LEEQLAAaeaeqELEESKRETETGIQNLtaEIEQGQESLTENLEAIKEEIENIVGEVElSKSSEELDSFKDTIESTKESL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 476 ENQRKVEQELEMVKAENVRQAKKIEFMKEEIQETHLD----YREELSKLAKGGGSHEADSQRDSELRS-------AKKTI 544
Cdd:COG5185 394 DEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEqatsSNEEVSKLLNELISELNKVMREADEESqsrleeaYDEIN 473
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 17536671 545 QEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAEAIEKI 586
Cdd:COG5185 474 RSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGV 515
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
229-484 |
5.07e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 44.36 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 229 KVLKEVKQLSDRLDYLTPKRKDVSRiKERDDFLQFSAKIIEETMSELKLKNARLERELsekEELVKVTKEELQELQKtvt 308
Cdd:pfam09731 229 DNVEEKVEKAQSLAKLVDQYKELVA-SERIVFQQELVSIFPDIIPVLKEDNLLSNDDL---NSLIAHAHREIDQLSK--- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 309 qamgdseqatkylhaenmKLTRQKADIRCDLLEArrnlkgFDEKREELEKQRDE---ALEDVRRITELKKNVEIElRSLK 385
Cdd:pfam09731 302 ------------------KLAELKKREEKHIERA------LEKQKEELDKLAEElsaRLEEVRAADEAQLRLEFE-RERE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 386 LLAEEREEQIDElksrvagyeVLRRDHEAvknelakAEEKLNKMGAhLVMADKQSSHFKTLKETAEGSRRRAIEQCNEMV 465
Cdd:pfam09731 357 EIRESYEEKLRT---------ELERQAEA-------HEEHLKDVLV-EQEIELQREFLQDIKEKVEEERAGRLLKLNELL 419
|
250
....*....|....*....
gi 17536671 466 ARIRGLEASLENQRKVEQE 484
Cdd:pfam09731 420 ANLKGLEKATSSHSEVEDE 438
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
98-346 |
5.88e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 98 EDDLKQKESQIRILQNRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSAktheifsigeelknktmk 177
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE------------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 178 lneknsqfqtklaeissenrnLERKVQKFREELivKDQ-RSLEVHQDQENTQKVLKEVKQLSD---RLDYltpkrkdVSR 253
Cdd:COG3883 77 ---------------------AEAEIEERREEL--GERaRALYRSGGSVSYLDVLLGSESFSDfldRLSA-------LSK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 254 IKERDdflqfsAKIIEETMsELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLHAENMKLTRQKA 333
Cdd:COG3883 127 IADAD------ADLLEELK-ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
250
....*....|...
gi 17536671 334 DIRCDLLEARRNL 346
Cdd:COG3883 200 ELEAELAAAEAAA 212
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
468-704 |
9.20e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 468 IRGLEASLENQRKVEQELEMVKAENVRQAKKIEFMKEEIQETHLDYREELSKLAKgggSHEADSQRDSELRSAKKTIQEV 547
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEE---KYKELSASSEELSEEKDALLAQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 548 KADNK-KLQQILEEVRQNQSKVLEENVKLRKgMAEAIEKIEEFKRNWHSSREAgerLQLEAKENEEKVLKVEEELQEKRL 626
Cdd:pfam07888 124 RAAHEaRIRELEEDIKTLTQRVLERETELER-MKERAKKAGAQRKEEEAERKQ---LQAKLQQTEEELRSLSKEFQELRN 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17536671 627 EVLEKEELVNYLQSQINTKQTKQPKLSRRSTLMSTISEVDTSTYVREVEEVRALEEQREELQAYLAEK-RKMADLQKSR 704
Cdd:pfam07888 200 SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRdRTQAELHQAR 278
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
389-609 |
9.36e-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: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 389 EEREEQIDELKSRVAGyevLRRDHEAVKNELAKAEEKLNKMGahlvmadkqsshfKTLKETaEGSRRRAIEQCNEMVARI 468
Cdd:COG4942 30 EQLQQEIAELEKELAA---LKKEEKALLKQLAALERRIAALA-------------RRIRAL-EQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 469 RGLEASLENQRKVEQEL--------------EMVKAEN----VRQAKKIEFMKEEIQETHLDYREELSKLAkgggshead 530
Cdd:COG4942 93 AELRAELEAQKEELAELlralyrlgrqpplaLLLSPEDfldaVRRLQYLKYLAPARREQAEELRADLAELA--------- 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17536671 531 sQRDSELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVLEenvKLRKGMAEAIEKIEEFKRNWHSSREAGERLQLEAKE 609
Cdd:COG4942 164 -ALRAELEAERAELEALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
127-585 |
9.55e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.89 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 127 DTISGYQEDLKENEIRI-----ENLNSRLHKledELSAKTHEIFSIGEELKNKTMKLNEKNSQFQTKLAEISSENRNLER 201
Cdd:TIGR01612 510 DFMELYKPDEVPSKNIIgfdidQNIKAKLYK---EIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 202 KVQKFREELIVKDQRSLEvhqdqentqkvLKE-VKQLSDRLDYLTpKRKDVSRIKERDD-FLQFSAKIIEETMSE-LKLK 278
Cdd:TIGR01612 587 KYLEIDDEIIYINKLKLE-----------LKEkIKNISDKNEYIK-KAIDLKKIIENNNaYIDELAKISPYQVPEhLKNK 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 279 NARLErelSEKEELVKVTKEEL----QELQKTVTQAMGDSEQATKYLHAENMKLTRQKADIR-CDLLEARRNLKGFDEKR 353
Cdd:TIGR01612 655 DKIYS---TIKSELSKIYEDDIdalyNELSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQnMETATVELHLSNIENKK 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 354 EELEKQrdealedvrrITELKKNVEIEL-RSLKLLAEEREEQIDELKSRVagyevlrRDHEAVKNELAKAEEKLNKMGAH 432
Cdd:TIGR01612 732 NELLDI----------IVEIKKHIHGEInKDLNKILEDFKNKEKELSNKI-------NDYAKEKDELNKYKSKISEIKNH 794
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 433 LvmaDKQSShfktLKETAEGSRRRAIEQCNEMVARIRGLEaslENQRKVEQELEMVKAENVRQAKK-IEF---MKEEIQE 508
Cdd:TIGR01612 795 Y---NDQIN----IDNIKDEDAKQNYDKSKEYIKTISIKE---DEIFKIINEMKFMKDDFLNKVDKfINFennCKEKIDS 864
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17536671 509 THLDYREELSKLaKGGGSHEADSQRDSELRSAKKTIQEV-KADNKKLQQIleevrqNQSKVLEENVKLRKGMAEAIEK 585
Cdd:TIGR01612 865 EHEQFAELTNKI-KAEISDDKLNDYEKKFNDSKSLINEInKSIEEEYQNI------NTLKKVDEYIKICENTKESIEK 935
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
149-328 |
1.08e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 149 RLHKLEDELSAKTHEIFSIGEELKnktmKLNEKNSQFQTKLAEISSENRNLERKVQKFREELIVKDQRsLEVHQDQENTQ 228
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELA----ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-IKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 229 KVLKEVKQLSDRLDYLTpkrkdvSRIKERDDFLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVT 308
Cdd:COG1579 86 RNNKEYEALQKEIESLK------RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170 180
....*....|....*....|
gi 17536671 309 QAMGDSEQATKYLHAENMKL 328
Cdd:COG1579 160 ELEAEREELAAKIPPELLAL 179
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
34-429 |
1.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 34 ESQEDLKTRLLEAENIIQDLRSERDAL------HESLVDKAGLNESV--IIERSNKVSTQETRI--YRRDVTLLEDDLKQ 103
Cdd:COG4717 95 EELEELEEELEELEAELEELREELEKLekllqlLPLYQELEALEAELaeLPERLEELEERLEELreLEEELEELEAELAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 104 KESQIRILQNRCL--------RLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHE------------ 163
Cdd:COG4717 175 LQEELEELLEQLSlateeelqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllli 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 164 -------------------------------IFSIGEELKNKTMKLNEKNSQFQTKLAEISSENRNLERKVQKFREELIV 212
Cdd:COG4717 255 aaallallglggsllsliltiagvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 213 KDQRSLEVHQDQENTQKVLKEVKQLSDRLDYLtpkrkdvSRIKERDDFLQfSAKIIEETMSELKLKNARLERELsekeel 292
Cdd:COG4717 335 SPEELLELLDRIEELQELLREAEELEEELQLE-------ELEQEIAALLA-EAGVEDEEELRAALEQAEEYQEL------ 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 293 vkvtKEELQELQKTVTQAMGDSEQATKYLHAENMKLTRQKAdircdllearrnlkgfDEKREELEKQRDEALEDVRRITE 372
Cdd:COG4717 401 ----KEELEELEEQLEELLGELEELLEALDEEELEEELEEL----------------EEELEELEEELEELREELAELEA 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17536671 373 LKKNVEI--ELRSLKLLAEEREEQIDEL----KSRVAGYEVLRRDHEAVKNE-----LAKAEEKLNKM 429
Cdd:COG4717 461 ELEQLEEdgELAELLQELEELKAELRELaeewAALKLALELLEEAREEYREErlppvLERASEYFSRL 528
|
|
| C1_KSR |
cd20812 |
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ... |
739-792 |
1.20e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410362 Cd Length: 48 Bit Score: 38.07 E-value: 1.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 17536671 739 IPHKwleFRHYSVLSMKCSLCFVGItFFTKanKCSHCDVRVHASCAPRVNNTCG 792
Cdd:cd20812 1 IKHR---FSKKLFMRQTCDYCHKQM-FFGL--KCKDCKYKCHKKCAKKAPPSCG 48
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
152-373 |
1.29e-03 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 42.92 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 152 KLEDELSAKTHEIFSIGEELKNKTMKLNEKNSQFQTKLAEISSENrnlerkvQKFREELIVKDQRSLEVHQDQENTQKVL 231
Cdd:pfam09726 416 QTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAK-------QKDKQTVQQLEKRLKAEQEARASAEKQL 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 232 KEVKQlSDRLDYLTPKRKDVSRIKERDDflqfSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQK------ 305
Cdd:pfam09726 489 AEEKK-RKKEEEATAARAVALAAASRGE----CTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELRKykesek 563
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17536671 306 ------TVTQAMGDseqatKYLHAEN--MKLTRQKADIRCDLLEARRNLkgfdEKREELEKQRDEALEDVR-RITEL 373
Cdd:pfam09726 564 dtevlmSALSAMQD-----KNQHLENslSAETRIKLDLFSALGDAKRQL----EIAQGQIYQKDQEIKDLKqKIAEV 631
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
7-305 |
1.29e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.49 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 7 TTPQSSKTPKSKSARYSSPYQVIDLNNESQEDLKTRLLEAENIIQDLRSErdALHESLVDK-AGLNESVIIERSNKVSTQ 85
Cdd:pfam15905 48 STPATARKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQ--ALEEELEKVeAKLNAAVREKTSLSASVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 86 ETRIYRRDVTLLEDDLKQKESQI---RILQNRCLRLETEKQKMQDTisgyqedLKENEIRIENLNSRLHKLEDELSAKTH 162
Cdd:pfam15905 126 SLEKQLLELTRVNELLKAKFSEDgtqKKMSSLSMELMKLRNKLEAK-------MKEVMAKQEGMEGKLQVTQKNLEHSKG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 163 EIFSIGEELKNKTMKLNEKNSQFQTKLAEISsENRNLERKVQKFREELIVKDQRSLEVHQDQENTQKVLKEVKQLSDRLd 242
Cdd:pfam15905 199 KVAQLEEKLVSTEKEKIEEKSETEKLLEYIT-ELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQ- 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17536671 243 yltpkrkdvsrIKERDDFLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQK 305
Cdd:pfam15905 277 -----------IKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
94-394 |
1.30e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 94 VTLLEDDLKQKESQIRILQNRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIFSIGEELKn 173
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 174 ktmKLNEKNSQFQTKLAEISSENRNLERKVQKFREElivKDQRSLEVHQDQENTQKVLKEVKQLSDRLDYLTPKRKDVSR 253
Cdd:COG4372 105 ---SLQEEAEELQEELEELQKERQDLEQQRKQLEAQ---IAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 254 IKERDDFLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLHAENMKLTRQKA 333
Cdd:COG4372 179 AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILK 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17536671 334 DIRCDLLEARRNLKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQ 394
Cdd:COG4372 259 EIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLA 319
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
38-628 |
1.38e-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: 43.24 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 38 DLKTRLLEAENIIQDLRSERDALHESLVDkagLNESVIIERSNKVSTQETRIyrrdvtLLEDDLKQKESQIRILQNRCLR 117
Cdd:pfam01576 79 ELESRLEEEEERSQQLQNEKKKMQQHIQD---LEEQLDEEEAARQKLQLEKV------TTEAKIKKLEEDILLLEDQNSK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 118 LETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLE---DELSAKTHEIFSIGEELKNKTMKLNEKNSQFQTKLAEISS 194
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEamiSDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 195 ENRNLERKVQKFREELIVKDQRSLEVHQDQENTQKVLKEVK-QLSDRLDYLTPKRKDVSRI-KERDDFlqfsAKIIEETM 272
Cdd:pfam01576 230 QIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEaQISELQEDLESERAARNKAeKQRRDL----GEELEALK 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 273 SELK--LKNARLERELSEKEElvkvtkEELQELQKTVtqamgdsEQATKyLHAENMKLTRQK-----ADIRCDLLEARRN 345
Cdd:pfam01576 306 TELEdtLDTTAAQQELRSKRE------QEVTELKKAL-------EEETR-SHEAQLQEMRQKhtqalEELTEQLEQAKRN 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 346 LKGFDEKREELEKQRDEALEDVRRITELK-------KNVEIELRSLKLLAEEREEQIDELKSRVAGyevLRRDHEAVKNE 418
Cdd:pfam01576 372 KANLEKAKQALESENAELQAELRTLQQAKqdsehkrKKLEGQLQELQARLSESERQRAELAEKLSK---LQSELESVSSL 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 419 LAKAEEKLNKMGAHLVMADKQSSHFKTL--KET----AEGSRRRAIEqcNEMVARIRGLEASLENQRKVEQELEMVKAEN 492
Cdd:pfam01576 449 LNEAEGKNIKLSKDVSSLESQLQDTQELlqEETrqklNLSTRLRQLE--DERNSLQEQLEEEEEAKRNVERQLSTLQAQL 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 493 VRQAKKIEFMKEEIQETHLDYREELSKLAKGGGSHEADSQRDSELRSAKKTIQE------VKADN------------KKL 554
Cdd:pfam01576 527 SDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQelddllVDLDHqrqlvsnlekkqKKF 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 555 QQILEEVRQNQSKVLEEN--------------VKLRKGMAEAIEKIEEFKR---------------------NWHSSREA 599
Cdd:pfam01576 607 DQMLAEEKAISARYAEERdraeaeareketraLSLARALEEALEAKEELERtnkqlraemedlvsskddvgkNVHELERS 686
|
650 660 670
....*....|....*....|....*....|....
gi 17536671 600 GERLQLEAKENEEKVLKVEEELQEK-----RLEV 628
Cdd:pfam01576 687 KRALEQQVEEMKTQLEELEDELQATedaklRLEV 720
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
183-402 |
1.58e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 183 SQFQTKLAEISSENRNLERKVqkfreelivkdqRSLEVHQDQENtqKVLKEVKQLSDRLDylTPKRKDVSRIKERDdflQ 262
Cdd:PRK04863 445 EEFQAKEQEATEELLSLEQKL------------SVAQAAHSQFE--QAYQLVRKIAGEVS--RSEAWDVARELLRR---L 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 263 FSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAmGDSEQATKYLHAENMKLTRQKADIRCDLLEA 342
Cdd:PRK04863 506 REQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE-DELEQLQEELEARLESLSESVSEARERRMAL 584
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17536671 343 RRNLKGFDEKREELEKQR-----------------DEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRV 402
Cdd:PRK04863 585 RQQLEQLQARIQRLAARApawlaaqdalarlreqsGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEI 661
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
341-486 |
1.92e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 341 EARRNLKGFDEKREE----LEKQRDEALEDVRRITELKKNVEIELRSLKLLAEEREEQIDELKSRVagyevlrrdHEAVK 416
Cdd:PRK00409 506 EAKKLIGEDKEKLNEliasLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---------EKEAQ 576
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 417 NELAKAEEKLNKMGAHLVMADKQSSHFKTLKETAEgsRRRAIEQCNEMvarirgLEASLENQRKVEQELE 486
Cdd:PRK00409 577 QAIKEAKKEADEIIKELRQLQKGGYASVKAHELIE--ARKRLNKANEK------KEKKKKKQKEKQEELK 638
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
33-366 |
2.46e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 33 NESQEDLKTRLLEAENIIQDLRSERDALHESLVDKAGLNESViiersnKVSTQETRIYRRDVTLLEDDLKQKESQIRILQ 112
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL------QAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 113 NRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKLEDELSAKTHEIFSIGEELKNKTMKLNEKNSQFQTKLAEI 192
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 193 SSENRNLERKVQKFREELIVKDQRSLEVHQDQENTQKVLKEVKQLSDRldyltpKRKDVSRIKERDDFLQFSAKIIEETM 272
Cdd:COG4372 202 LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE------ELLEEVILKEIEELELAILVEKDTEE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 273 SELKLKNARLERELSEKEELVKVTKEELQELQKTVTQAMGDSEQATKYLHAENMKLTRQKADIRCDLLEARRNLKGFDEK 352
Cdd:COG4372 276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDV 355
|
330
....*....|....
gi 17536671 353 REELEKQRDEALED 366
Cdd:COG4372 356 LELLSKGAEAGVAD 369
|
|
| PH |
pfam00169 |
PH domain; PH stands for pleckstrin homology. |
813-914 |
2.87e-03 |
|
PH domain; PH stands for pleckstrin homology.
Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 38.70 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 813 MNGWLRVYRDDLPeSTWTSLWAMMDSNHVKFYRDAGADNLENPYFTIDLNKEQWILRTGQEVAIPGDVMRNVLTIKLQTR 892
Cdd:pfam00169 3 KEGWLLKKGGGKK-KSWKKRYFVLFDGSLLYYKDDKSGKSKEPKGSISLSGCEVVEVVASDSPKRKFCFELRTGERTGKR 81
|
90 100
....*....|....*....|..
gi 17536671 893 SVHIVAPTPKSAERWAACLQNA 914
Cdd:pfam00169 82 TYLLQAESEEERKDWIKAIQSA 103
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
152-439 |
2.90e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 152 KLEDELSAKTHEIFSIGEELKNKTMKLNEKNSQFQTKLAEISSENRNLERKVQKFREELIVKDQRSLEVHQDQENTQKVL 231
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 232 KEV-KQLSDRLDYLTPKRKDVSRIKERDDFLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTVTQA 310
Cdd:COG4372 83 EELnEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 311 MGDSEQATKYLHAENMKLTRQKADIRCDLLEARRNLKGFDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLAEE 390
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17536671 391 REEQIDELKSRVAGYEVLRRDHEAVKNELAKAEEKLNKMGAHLVMADKQ 439
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEA 291
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
82-393 |
2.96e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 82 VSTQETRIYRRDVTLLEDDLKQKESQIRILQNRCLRLET-EKQKMQDTISGYQEDLkenEIRIENLNSRLH--------- 151
Cdd:COG3206 61 VEPQSSDVLLSGLSSLSASDSPLETQIEILKSRPVLERVvDKLNLDEDPLGEEASR---EAAIERLRKNLTvepvkgsnv 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 152 ---KLED---ELSAKT----HEIFsIGEELKNKTMKLNEKNSQFQTKLAEISSENRNLERKVQKFREE---LIVKDQRSL 218
Cdd:COG3206 138 ieiSYTSpdpELAAAVanalAEAY-LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglVDLSEEAKL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 219 EVHQDQENTQKVLK---EVKQLSDRLDYLtpkRKDVSRIKERDDFLQFSAKI--IEETMSELKLKNARLERELSEKEELV 293
Cdd:COG3206 217 LLQQLSELESQLAEaraELAEAEARLAAL---RAQLGSGPDALPELLQSPVIqqLRAQLAELEAELAELSARYTPNHPDV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 294 KVTKEELQELQKTVTQAMGdseqatkylhaenmkltRQKADIRCDLLEARRNLKGFDEKREELEKQRDEALEDVRRITEL 373
Cdd:COG3206 294 IALRAQIAALRAQLQQEAQ-----------------RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRL 356
|
330 340
....*....|....*....|
gi 17536671 374 KKNVEIELRSLKLLAEEREE 393
Cdd:COG3206 357 EREVEVARELYESLLQRLEE 376
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
76-304 |
3.53e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 76 IERSNKVSTQETRIYRRDVTLLEDDLKQKESQIRIL--QNRCLRLETEKQKMQDTISGYQEDLKENEIRIENLNSRLHKL 153
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 154 EDELSAKTHEIFSIGEElkNKTMKLNEKNSQFQTKLAEISSENRNLERKVQKFREELivKDQRSLEVHQDQENTQKVLKE 233
Cdd:COG3206 246 RAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI--AALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17536671 234 VKQLSDRLDYLtpkRKDVSRIKERddflqfsAKIIEETMSELklknARLERELSEKEELVKVTKEELQELQ 304
Cdd:COG3206 322 LEALQAREASL---QAQLAQLEAR-------LAELPELEAEL----RRLEREVEVARELYESLLQRLEEAR 378
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
228-401 |
3.60e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 228 QKVLKEVKQLSDRLDYLtpkRKDVSRIKERDDFLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKEELQELQKTv 307
Cdd:COG1579 13 QELDSELDRLEHRLKEL---PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 308 tqamgdseqatKYLHAenmkLTRQKADIRCDLLEARRNLKGFDEKREELEKQRDEALEdvrRITELKKNVEIELRSLKLL 387
Cdd:COG1579 89 -----------KEYEA----LQKEIESLKRRISDLEDEILELMERIEELEEELAELEA---ELAELEAELEEKKAELDEE 150
|
170
....*....|....
gi 17536671 388 AEEREEQIDELKSR 401
Cdd:COG1579 151 LAELEAELEELEAE 164
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
281-605 |
3.77e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 281 RLERELSEKEELVKVTKEELQEL-------QKTVTQAMGDSEQATKYLHAENMKLTRQKADIRCDLLEARRNLKGFD--- 350
Cdd:PRK04778 109 EIESLLDLIEEDIEQILEELQELleseeknREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQFVelt 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 351 ------EKREELEKQRDE--ALE-DVRRITELKKNVEIELRslkllaeereEQIDELKsrvAGYEVLRR-----DHEAVK 416
Cdd:PRK04778 189 esgdyvEAREILDQLEEElaALEqIMEEIPELLKELQTELP----------DQLQELK---AGYRELVEegyhlDHLDIE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 417 NELAKAEEKLNKMGAHLVMADkqsshfktLKETAEgsrrrAIEQCNEmvaRIRGLEASLE-----------NQRKVEQEL 485
Cdd:PRK04778 256 KEIQDLKEQIDENLALLEELD--------LDEAEE-----KNEEIQE---RIDQLYDILErevkarkyvekNSDTLPDFL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 486 EMVKAENVRQAKKIEFMKE--EIQETHLDYREELSK-LAKGGGSHEADSQRdseLRSAKKTIQEVKADNKKLQQILEEVR 562
Cdd:PRK04778 320 EHAKEQNKELKEEIDRVKQsyTLNESELESVRQLEKqLESLEKQYDEITER---IAEQEIAYSELQEELEEILKQLEEIE 396
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 17536671 563 QNQSKVLEENVKLRKGMAEAIEKIEEFKRNWHSSREAGERLQL 605
Cdd:PRK04778 397 KEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSNL 439
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
535-707 |
3.91e-03 |
|
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: 41.29 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 535 SELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAEAIEKIEEFKRNWHSSREAGERLQLEAKENEEKV 614
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 615 LKVEEELQEkRLEVLEKEELVNYLQSQINTKQTKQpkLSRRSTLMSTISEVD---TSTYVREVEEVRA----LEEQREEL 687
Cdd:COG4942 100 EAQKEELAE-LLRALYRLGRQPPLALLLSPEDFLD--AVRRLQYLKYLAPARreqAEELRADLAELAAlraeLEAERAEL 176
|
170 180
....*....|....*....|....
gi 17536671 688 QAYLAE----KRKMADLQKSRSTA 707
Cdd:COG4942 177 EALLAEleeeRAALEALKAERQKL 200
|
|
| C1_DGK_rpt2 |
cd20805 |
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase ... |
741-791 |
4.14e-03 |
|
second protein kinase C conserved region 1 (C1 domain) found in the diacylglycerol kinase family; The diacylglycerol kinase (DGK, EC 2.7.1.107) family of enzymes plays critical roles in lipid signaling pathways by converting diacylglycerol to phosphatidic acid, thereby downregulating signaling by the former and upregulating signaling by the latter second messenger. Ten DGK family isozymes have been identified to date, which possess different interaction motifs imparting distinct temporal and spatial control of DGK activity to each isozyme. They have been classified into five types (I-V), according to domain architecture and some common features. All DGK isozymes, except for DGKtheta, contain two copies of the C1 domain. This model corresponds to the second one. DGKtheta harbors three C1 domains. Its third C1 domain is included here. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410355 Cd Length: 55 Bit Score: 36.66 E-value: 4.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 17536671 741 HKWLEfRHYSVlSMKCSLC--FVGITFFTKANKCSHCDVRVHASCAPRV-NNTC 791
Cdd:cd20805 1 HHWVE-GNLPS-GAKCSVCgkKCGSSFGLAGYRCSWCKRTVHSECIDKLgPEEC 52
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
270-606 |
5.25e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 270 ETMSELKLKNARLERELSEKEELVKVTKEELQELQktvtqamgdsEQATKYlhaenmkltRQKADircdllEARRNLKGF 349
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELN----------EELKEL---------AEKRD------ELNAQVKEL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 350 DEKREELEKQRDEALEDVRRITELKKNVEIELRSLKllaeereEQIDELKSRVAGYEVLRRDHEAVKNELAKAEEKLnkm 429
Cdd:COG1340 56 REEAQELREKRDELNEKVKELKEERDELNEKLNELR-------EELDELRKELAELNKAGGSIDKLRKEIERLEWRQ--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 430 gahlvmadkQSSHFKTLKEtaegsrRRAIEQCNEMVARIRGLEASLENQRKV---EQELEMVKAENVRQAKKIEFMKEEI 506
Cdd:COG1340 126 ---------QTEVLSPEEE------KELVEKIKELEKELEKAKKALEKNEKLkelRAELKELRKEAEEIHKKIKELAEEA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 507 QETHldyrEELSKLAKgggshEADSQRDsELRSAKKTIQE----VKADNKKLQQILEEVRQNQSKV-----LEENVKLRK 577
Cdd:COG1340 191 QELH----EEMIELYK-----EADELRK-EADELHKEIVEaqekADELHEEIIELQKELRELRKELkklrkKQRALKREK 260
|
330 340
....*....|....*....|....*....
gi 17536671 578 GMAEAIEKIEEFKrnwhSSREAGERLQLE 606
Cdd:COG1340 261 EKEELEEKAEEIF----EKLKKGEKLTTE 285
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
139-470 |
6.23e-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: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 139 NEIRIENLNSRLHKLEDELSAktheifsigeelknktmklneknsqfqtkLAEISSENRNLERKVQKFREELivkdQRSL 218
Cdd:COG4913 608 NRAKLAALEAELAELEEELAE-----------------------------AEERLEALEAELDALQERREAL----QRLA 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 219 EVHQDQENTQKVLKEVKQLSDRLDYLTPKRKDVSRIKERDDFLQFSAKIIEETMSELKLKNARLERELSEKEELVKVTKE 298
Cdd:COG4913 655 EYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 299 ELQELQKTVTQAmgDSEQATKYLHAENMKLTRQkadircdllEARRNLkgfDEKREELEKQRDEALEDVRRI-------- 370
Cdd:COG4913 735 RLEAAEDLARLE--LRALLEERFAAALGDAVER---------ELRENL---EERIDALRARLNRAEEELERAmrafnrew 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 371 TELKKNVEIELRS----LKLLAE-------EREEQIDELKSRVAGYEV------LRRDHEAVKNELakaeEKLNKMGAH- 432
Cdd:COG4913 801 PAETADLDADLESlpeyLALLDRleedglpEYEERFKELLNENSIEFVadllskLRRAIREIKERI----DPLNDSLKRi 876
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 17536671 433 ---------LVMADKQSSHFKT----LKETAEGS-------RRRAIEQCNEMVARIRG 470
Cdd:COG4913 877 pfgpgrylrLEARPRPDPEVREfrqeLRAVTSGAslfdeelSEARFAALKRLIERLRS 934
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
370-691 |
6.27e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 370 ITELKKNVEIELRSLKLLAEEREEQIDELKSRVAGYEVLRRDHEAVKNELAKAEEKLNKMGAHLVMADKQSSHFKTLKET 449
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 450 AEGSRRRAIEQCNEMVARIRGLEASLENQRKVEQELEMVKAENVRQAKKIEFMKEEIQETHLDYREELSKLAKgggsHEA 529
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE----AEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 530 DSQRDSELRSAKKTIQEVKADNKKLQQILEEVRQNQSKVLEENVKLRKGMAEAIEKIEEFKRNWHSSREAGERLQLEAKE 609
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 610 NEEKVLKVEEELQEKRLEVLEKEELVNYLQSQINTKQTKQPKLSRRSTLMSTISEVDTSTYVREVEEVRALEEQREELQA 689
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
..
gi 17536671 690 YL 691
Cdd:COG4372 342 LL 343
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
264-434 |
6.38e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 264 SAKIIE-ETMSELKLKNARLERELSEKEELVKVtKEELQELQktvtqamgdsEQATKYLHAENMKLTRQKadirCDLLEA 342
Cdd:PRK12704 30 EAKIKEaEEEAKRILEEAKKEAEAIKKEALLEA-KEEIHKLR----------NEFEKELRERRNELQKLE----KRLLQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 343 RRNLkgfDEKREELEKQRDEALEDVRRITELKKNVEIELRSLKLLaeeREEQIDELkSRVAGYEVlrrdHEAVKNELAKA 422
Cdd:PRK12704 95 EENL---DRKLELLEKREEELEKKEKELEQKQQELEKKEEELEEL---IEEQLQEL-ERISGLTA----EEAKEILLEKV 163
|
170
....*....|..
gi 17536671 423 EEKLNKMGAHLV 434
Cdd:PRK12704 164 EEEARHEAAVLI 175
|
|
| PRK04184 |
PRK04184 |
DNA topoisomerase VI subunit B; Validated |
335-432 |
6.39e-03 |
|
DNA topoisomerase VI subunit B; Validated
Pssm-ID: 235246 [Multi-domain] Cd Length: 535 Bit Score: 40.65 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536671 335 IRCDLLEARRNLKGFDEKREELEKQRdealedvRRITELKKNVEIELRSLKLLAEEREEQIDELKSRVAGYEVLRRDHEA 414
Cdd:PRK04184 444 IRLALQEVARKLKKYLSRKRKEEEAK-------KKAKTFEKYIPEIARKLAEILEKEEPDIEEVLAKLIGKKLEEEEVEE 516
|
90
....*....|....*...
gi 17536671 415 VKNELAKAEEKLNKMGAH 432
Cdd:PRK04184 517 EEEEEAVVVESAKNYTEK 534
|
|
| |
