|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
12-488 |
9.98e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 88.58 E-value: 9.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 12 QLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLE--KELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAA 89
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 90 LSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNS------GIMDEVDELRKRVldmegKDEELIKMEEQCRDLNKRL 163
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHElyeeakAKKEELERLKKRL-----TGLTPEKLEKELEELEKAK 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 164 EKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNL--EKEKMTTKQLSEELESLNARIKELEAIESRLEK 241
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELteEHRKELLEEYTAELKRIEKELKEIEEKERKLRK 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 242 TEITLKDDLTKLKTLTVMlvderKTMSEKLKQTEDKLQS-TTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMySV 320
Cdd:PRK03918 481 ELRELEKVLKKESELIKL-----KELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE-EL 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 321 TKERDDLRNKLKAEEEKGHDLLSK--------VTILKNRLQSLEAIEKDFVKNKlnqdsskstAALHQENNKIKELSQEV 392
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKEleelgfesVEELEERLKELEPFYNEYLELK---------DAEKELEREEKELKKLE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 393 ENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAqfLSQELEHAKMELAKyKLAEKTEssheqwLFRRLQEEEAKS 472
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAG-LRAELEE------LEKRREEIKKTL 696
|
490
....*....|....*.
gi 295424124 473 GHLSREVDALKEKIHE 488
Cdd:PRK03918 697 EKLKEELEEREKAKKE 712
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-527 |
2.35e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 7 QRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQK 86
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 87 LAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGKDEELIKMEEQCRDLNKRLEKE 166
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 167 TVQSKDFKLEV--------DKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESR 238
Cdd:COG1196 395 AAELAAQLEELeeaeeallERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 239 LEKTEITLKDDLTKLKTLTVMLVDERKTMSE--------KLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSK 310
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGflegvkaaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 311 TDAEEKMY-SVTKERDDLR------NKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQENN 383
Cdd:COG1196 555 DDEVAAAAiEYLKAAKAGRatflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 384 KIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKLAEKTESSHEQWLFR 463
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295424124 464 RLQEEEAKSGHLSREVDALKEKIHEYMATEDLICHLQGDHSLLQK-KLNQQENRNRDLGREIENL 527
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPpDLEELERELERLEREIEAL 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
92-436 |
2.97e-15 |
|
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: 80.50 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 92 RQIDELEETNRSLRKAEEELQDIKDKINKgeygnsgIMDEVDELRKRVLDMEGKDEELIKMEEQcrdLNKRLEKETVQSK 171
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRR-------IENRLDELSQELSDASRKIGEIEKEIEQ---LEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 172 DFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKE--KMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDD 249
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 250 LTKLKTLTVMLVDERKTMSEKLKQTEDKLQSttsqLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRN 329
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKS----IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 330 KLKAEEEKGHDLLSKVTILKNRLQSLEAieKDFVKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDL 409
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKA--KLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVN 974
|
330 340
....*....|....*....|....*..
gi 295424124 410 MKTEDEYETLERRYANERDKAQFLSQE 436
Cdd:TIGR02169 975 MLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
18-532 |
4.79e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.72 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 18 QKIQALTTSAKETQGKLALAEARAQEEEQKATRLEkELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALS---RQI 94
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvKEL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 95 DELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGKDEELikmeeqcRDLNKR---LEKETVQSK 171
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-------EELKKKlkeLEKRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 172 DFKLEVDKLSVRITALEKLEDAL-DKSKQECYSLKCNLEKEKmttKQLSEELESLNARIKELEAIESRLEKTEITLKDDL 250
Cdd:PRK03918 359 ERHELYEEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAK---EEIEEEISKITARIGELKKEIKELKKAIEELKKAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 251 TKLKTLTVMLVDERK-----TMSEKLKQTEDKLQSTTSQLQAEQNKVTTVtEKLIEETKRALKSKT------DAEEKMYS 319
Cdd:PRK03918 436 GKCPVCGRELTEEHRkelleEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKElaeqlkELEEKLKK 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 320 VTKErddlrnKLKAEEEKGHDLLSKVTILKNRLQSLeaiEKDFvkNKLNQDSSKSTAAlhqeNNKIKELSQEVENLKLKL 399
Cdd:PRK03918 515 YNLE------ELEKKAEEYEKLKEKLIKLKGEIKSL---KKEL--EKLEELKKKLAEL----EKKLDELEEELAELLKEL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 400 KDMK-AIEDDLMKTEDEYETLERRYANERDKAQFLSQELEhaKMELAKYKLAEKtessheqwlFRRLQEEEAKSGHLSRE 478
Cdd:PRK03918 580 EELGfESVEELEERLKELEPFYNEYLELKDAEKELEREEK--ELKKLEEELDKA---------FEELAETEKRLEELRKE 648
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 295424124 479 VDALKEKI--HEYMATEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTKELE 532
Cdd:PRK03918 649 LEELEKKYseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5-535 |
2.78e-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: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 5 EQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEK---ELQTQTTEFHQNQDKIMAKLTNEDSQNR 81
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEkleELKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 82 QLRQKLAALSRQIDELEETNRSLRK----AEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDM--EGKDEELIKMEEQ 155
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNeierLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAelEELEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 156 CRDLNKRLEKETVQSK-------DFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEEL------ 222
Cdd:TIGR02168 456 LERLEEALEELREELEeaeqaldAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdegy 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 223 -----------------ESLNARIKELEA---------------------IESRLEKTEITLKDDLTKLKTLTVMLVDER 264
Cdd:TIGR02168 536 eaaieaalggrlqavvvENLNAAKKAIAFlkqnelgrvtflpldsikgteIQGNDREILKNIEGFLGVAKDLVKFDPKLR 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 265 KTMSEKLKQTE--DKLQSTTSQLQAEQNKVTTVTE--KLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHD 340
Cdd:TIGR02168 616 KALSYLLGGVLvvDDLDNALELAKKLRPGYRIVTLdgDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAE 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 341 LLSKVTILKNRLQSLEAIEKDfvknkLNQDSSKSTAALHQENNKIKELSQEVENLklkLKDMKAIEDDLMKTEDEYETLE 420
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQ-----LRKELEELSRQISALRKDLARLEAEVEQL---EERIAQLSKELTELEAEIEELE 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 421 RRYANERDKAQFLSQELEHAKMELAKYKlaektessheqwlfRRLQEEEAKSGHLSREVDALKEKIHEYMATEDlicHLQ 500
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLK--------------EELKALREALDELRAELTLLNEEAANLRERLE---SLE 830
|
570 580 590
....*....|....*....|....*....|....*
gi 295424124 501 GDHSLLQKKLNQQENRNRDLGREIENLTKELERYR 535
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
66-532 |
6.44e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.26 E-value: 6.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 66 QDKIMAKLTNEDSQNRQLRQKLaalsrQIDELEetnrslrKAEEELQDIKDKINKgeygnsgimdEVDELRKRVLDMEGK 145
Cdd:PRK03918 134 QGEIDAILESDESREKVVRQIL-----GLDDYE-------NAYKNLGEVIKEIKR----------RIERLEKFIKRTENI 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 146 DEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESL 225
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 226 NARIKELEAIESRLEKTEitlkddltklktltvMLVDERKTMSEKLKQTEDKLQsttsqlqaEQNKVTTVTEKLIEETKR 305
Cdd:PRK03918 272 KKEIEELEEKVKELKELK---------------EKAEEYIKLSEFYEEYLDELR--------EIEKRLSRLEEEINGIEE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 306 ALKSKTDAEEKMYSVTKERDDLRNKLkAEEEKGHDLLSKVTILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQENNKI 385
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEI 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 386 KELSQEVENLKLKLKDMKAIEDDLMK------------TEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKLAEKT 453
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 454 ESSHEQWLFRRL----QEEEAKSGHLSREVDALKEKIHEYMATEDLICHLQGDHSLLQ---KKLNQQENRNRDLGREIEN 526
Cdd:PRK03918 488 VLKKESELIKLKelaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKkelEKLEELKKKLAELEKKLDE 567
|
....*.
gi 295424124 527 LTKELE 532
Cdd:PRK03918 568 LEEELA 573
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
64-547 |
1.08e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.49 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 64 QNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKgeygnsgIMDEVDELRKRVLDME 143
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-------LKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 144 GKDEELikmEEQCRDLNKRLEKETVQSKDFK---LEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKekmttkqLSE 220
Cdd:PRK03918 252 GSKRKL---EEKIRELEERIEELKKEIEELEekvKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR-------LEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 221 ELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLtvmlvDERKTMSEKLKQTEDKLQSTTSQLQAEQnkvttvTEKLI 300
Cdd:PRK03918 322 EINGIEERIKELEEKEERLEELKKKLKELEKRLEEL-----EERHELYEEAKAKKEELERLKKRLTGLT------PEKLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 301 EETKRALKSKTDAEEKMYSVTKERDDLRNKLKA----------------------EEEKGHDLLSKVTI----LKNRLQS 354
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKElkkaieelkkakgkcpvcgrelTEEHRKELLEEYTAelkrIEKELKE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 355 LEAIEKDFVKNKLNQDsskSTAALHQENNKIKELSQEVENLKLKLKDMKAieDDLMKTEDEYETLERRYANERDKAQFLS 434
Cdd:PRK03918 471 IEEKERKLRKELRELE---KVLKKESELIKLKELAEQLKELEEKLKKYNL--EELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 435 QELEHA-----KMELAKYKLAEKTESSHEqwLFRRLQEEEAKS-GHLSREVDALKEKIHEYMATEDlichlqgdhslLQK 508
Cdd:PRK03918 546 KELEKLeelkkKLAELEKKLDELEEELAE--LLKELEELGFESvEELEERLKELEPFYNEYLELKD-----------AEK 612
|
490 500 510
....*....|....*....|....*....|....*....
gi 295424124 509 KLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSLNE 547
Cdd:PRK03918 613 ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-340 |
1.59e-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: 75.10 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 4 DEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKltnedsqnrql 83
Cdd:TIGR02169 688 RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV----------- 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 84 RQKLAALSRQIDELEETnrsLRKAEEELQDIKDKINKGEYGNsgIMDEVDELRKRVLDMEGKDEElIKMEEQCRDLNKRL 163
Cdd:TIGR02169 757 KSELKELEARIEELEED---LHKLEEALNDLEARLSHSRIPE--IQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 164 EKETVQSKdfKLEVDKLSVRITALEKLEDALDKSKQEcysLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTE 243
Cdd:TIGR02169 831 LEKEIQEL--QEQRIDLKEQIKSIEKEIENLNGKKEE---LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 244 ITLKDDLTKLKTLTVMLVDERKTMSEKLKQTED----------------KLQSTTSQLQAEQNKVTTVTEKLIEETKRAL 307
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkgedeeipeeelsleDVQAELQRVEEEIRALEPVNMLAIQEYEEVL 985
|
330 340 350
....*....|....*....|....*....|...
gi 295424124 308 KSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHD 340
Cdd:TIGR02169 986 KRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-566 |
3.04e-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: 73.94 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 3 VDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQ-NQDKIMAKltnedSQNR 81
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRlEQQKQILR-----ERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 82 QLRQKLAALSRQIDELEetnRSLRKAEEELQDIKDKINkgeygnsGIMDEVDELRKRVLDMEGKDEElikMEEQCRDLNK 161
Cdd:TIGR02168 313 NLERQLEELEAQLEELE---SKLDELAEELAELEEKLE-------ELKEELESLEAELEELEAELEE---LESRLEELEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 162 RLEKETVQSKDFKLEVDKLSVRITALEK----LEDALDKSKQECYSLKCNLEKEKMttKQLSEELESLNARIKELEAIES 237
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEIERLEArlerLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 238 RLEKTEITLKDDLTKLKTLTVMLVDE------RKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIE------ETKR 305
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERElaqlqaRLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSElisvdeGYEA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 306 AL-------------KSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDFVK-------- 364
Cdd:TIGR02168 538 AIeaalggrlqavvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKfdpklrka 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 365 ---------------------NKLNQDSSKSTAALH-------------QENNKIKELSQEVENLKLKLKDMKAIEDDLM 410
Cdd:TIGR02168 618 lsyllggvlvvddldnalelaKKLRPGYRIVTLDGDlvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 411 KTEDEYETLERRYANERDKAQFLSQELEHAKMELakYKLAEKTESSHEQWLfRRLQEEEAKSGHLSREVDALKEKIHEym 490
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISAL--RKDLARLEAEVEQLE-ERIAQLSKELTELEAEIEELEERLEE-- 772
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295424124 491 aTEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTKEL--ERYRHFSKSLRPSLNERRISDPQVFSKEVQTEAAD 566
Cdd:TIGR02168 773 -AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtlLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
16-358 |
7.35e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 72.77 E-value: 7.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 16 QRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMA-----------------KLTNEDS 78
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEleeeieelrerfgdapvDLGNAED 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 79 QNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYG----NSGIMDEVDELRKRVLDMEgkdEELIKMEE 154
Cdd:PRK02224 413 FLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGqpveGSPHVETIEEDRERVEELE---AELEDLEE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 155 QCRDLNKRLE--KETVQSKDfklEVDKLSVRITALEKL----EDALDKSKQECYSLK---------------------CN 207
Cdd:PRK02224 490 EVEEVEERLEraEDLVEAED---RIERLEERREDLEELiaerRETIEEKRERAEELReraaeleaeaeekreaaaeaeEE 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 208 LEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEiTLKDDLTKLKtltvmlvDERKTMSEKLKQTEDKLQST---TSQ 284
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERIESLERIRTLLAAIA-DAEDEIERLR-------EKREALAELNDERRERLAEKrerKRE 638
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295424124 285 LQAEQNKvtTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNK---LKAEEEKGHDLLSKVTILKNRLQSLEAI 358
Cdd:PRK02224 639 LEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELRERREALENRVEALEAL 713
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-488 |
9.99e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.48 E-value: 9.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 14 ALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMA--KLTNEDSQNRQLRQKLAALS 91
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaeKKKEEAKKKADAAKKKAEEK 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 92 RQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMD--EVDELRKRVLDMEGKDEELIKMEEqcrdlnKRLEKETVQ 169
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEkkKADEAKKKAEEAKKADEAKKKAEE------AKKAEEAKK 1464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 170 SKDFKLEVDKLSVRITALEKLEDAldKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDD 249
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEA--KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 250 LTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTtvteKLIEETKRALKSKTDAEEKMYSVTKERDDLRN 329
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA----KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 330 KLKAEEekghdlLSKVTILKNRLQSLEAIEKDFVKN--KLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIED 407
Cdd:PTZ00121 1619 KIKAEE------LKKAEEEKKKVEQLKKKEAEEKKKaeELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 408 DLMKTEDE---YETLERRYANERDKAQFLSQELE--HAKMELAKYKLAEKTESSHEqwlFRRLQEEEAKSGHLSREVDAL 482
Cdd:PTZ00121 1693 ALKKEAEEakkAEELKKKEAEEKKKAEELKKAEEenKIKAEEAKKEAEEDKKKAEE---AKKDEEEKKKIAHLKKEEEKK 1769
|
....*.
gi 295424124 483 KEKIHE 488
Cdd:PTZ00121 1770 AEEIRK 1775
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
4-531 |
1.66e-12 |
|
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: 71.69 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 4 DEQQRLTAQLALQRQKIQALTTsakETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQL 83
Cdd:pfam15921 253 ESQNKIELLLQQHQDRIEQLIS---EHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 84 RQKLAALSRQI-DELEETNRSLRKAEEELQDIKDKINKGEYgNSGIMDevDELRKRVLDMEGKDEELIKMEEQCRDLNKR 162
Cdd:pfam15921 330 RSELREAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQ-ESGNLD--DQLQKLLADLHKREKELSLEKEQNKRLWDR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 163 LEKETVQSKDFKLEVDKLSVRITALEKLEDALdksKQECYSL-----------KCNLEKEKMTTKQLSEELESLNARIKE 231
Cdd:pfam15921 407 DTGNSITIDHLRRELDDRNMEVQRLEALLKAM---KSECQGQmerqmaaiqgkNESLEKVSSLTAQLESTKEMLRKVVEE 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 232 LEAIESRLEKTEITLKD-----------------DLTKLKTltvmLVDERKTMSEKLKQTEDKLQSTTSQLQA------E 288
Cdd:pfam15921 484 LTAKKMTLESSERTVSDltaslqekeraieatnaEITKLRS----RVDLKLQELQHLKNEGDHLRNVQTECEAlklqmaE 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 289 QNKVTTVTEKLIEETKRALKSKTDAEEKMY----SVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEaiekdFVK 364
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGQHGRTAGAMQvekaQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE-----LEK 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 365 NKLNQDSSKSTAAlhqennkIKELSQEVENLklkLKDMKAIEDDLMKTEDEYETLERRYANErdkaqflSQELEhakMEL 444
Cdd:pfam15921 635 VKLVNAGSERLRA-------VKDIKQERDQL---LNEVKTSRNELNSLSEDYEVLKRNFRNK-------SEEME---TTT 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 445 AKYKLAEKTESSHEQWLFRRLQEEEAKSGHLSREVDALKEKIheyMATEDLICHLQGDHSLLQKKLNQQENRNRDLGREI 524
Cdd:pfam15921 695 NKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQI---TAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEK 771
|
....*..
gi 295424124 525 ENLTKEL 531
Cdd:pfam15921 772 NKLSQEL 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
81-448 |
2.10e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 81 RQLRQKLAALSRQIDELEETNRSLRKAE------EELQDIKDKINKGEYGNSGimDEVDELRKRvldMEGKDEELIKMEE 154
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLErqaekaERYKELKAELRELELALLV--LRLEELREE---LEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 155 QCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALdkskqecYSLKCNLEKEKMttkQLSEELESLNARIKELEA 234
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL-------ANEISRLEQQKQ---ILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 235 IESRLEKTEITLKDDLTKLktltvmlvderktmseklkqtEDKLQSTTSQLQAEQNKVTTVTEKLIEetkralksktdAE 314
Cdd:TIGR02168 324 QLEELESKLDELAEELAEL---------------------EEKLEELKEELESLEAELEELEAELEE-----------LE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 315 EKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEaiekdfvKNKLNQDSSKSTAALHQENNKIKELSQEVEN 394
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE-------DRRERLQQEIEELLKKLEEAELKELQAELEE 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 295424124 395 LKLKLKDmkaieddlmkTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYK 448
Cdd:TIGR02168 445 LEEELEE----------LQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
94-468 |
2.29e-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: 71.25 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 94 IDEL---EETNRSLRKAEEELQDIKDKINKGEygnsgIMdeVDELRKRVLDMEGKDEELIKMEEQcrdlnkRLEKETVQS 170
Cdd:TIGR02169 159 IDEIagvAEFDRKKEKALEELEEVEENIERLD-----LI--IDEKRQQLERLRREREKAERYQAL------LKEKREYEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 171 KDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEkmtTKQLSEELESLNARIKELEAIESRLEKTEI-TLKDD 249
Cdd:TIGR02169 226 YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR---LEEIEQLLEELNKKIKDLGEEEQLRVKEKIgELEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 250 LTKLKTLTVMLVDERKTMSEKLKQTE---DKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDD 326
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEaeiDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 327 LRNKLKAEEEKGHDLLSKVTILKNRLQSLEAiekdfVKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLkdmKAIE 406
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELDRLQE-----ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI---KKQE 454
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295424124 407 DDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKyKLAEKTESSHEQWLFRRLQEE 468
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE-AEAQARASEERVRGGRAVEEV 515
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
38-559 |
2.41e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.33 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 38 EARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKlaalsRQIDELEETnRSLRKAEEELQDIKDK 117
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK-----KKADEAKKA-EEKKKADEAKKKAEEA 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 118 INKGEygnsgIMDEVDELRKRVLDMEGKDEELIKMEEQCRDLNKRLEKETVQSKDfKLEVDKLsvRITALEKLEDALDKS 197
Cdd:PTZ00121 1315 KKADE-----AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAEK--KKEEAKKKADAAKKK 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 198 KQECYSLKcNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEitlKDDLTKLKTltvmlvDERKTMSEKLKQTEDK 277
Cdd:PTZ00121 1387 AEEKKKAD-EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK---KADEAKKKA------EEAKKADEAKKKAEEA 1456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 278 LQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEA 357
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 358 IEKDFVKNKLNQDSSKSTAALH--QENNKIKELSQEVENLKLKLK---DMKAIE----DDLMKTEDEYETLE----RRYA 424
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKkaEEKKKAEEAKKAEEDKNMALRkaeEAKKAEeariEEVMKLYEEEKKMKaeeaKKAE 1616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 425 NERDKAQFLSQElEHAKMELAKYKLAEKTESSHEQWLFRRLQEEEAKSGHLSREVDALKEKIHEYMATEDlichlqgdhs 504
Cdd:PTZ00121 1617 EAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE---------- 1685
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 295424124 505 lLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSLNERRISDPQVFSKE 559
Cdd:PTZ00121 1686 -DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA 1739
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
17-563 |
3.94e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.56 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 17 RQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEfhqnqdkIMAKLTNEDSQNRQLRQKLAALSRQIDE 96
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD-------EAKKKAEEAKKADEAKKKAEEAKKKADA 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 97 LEETNRSLRKAEE----ELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGKDEELIKMEEqcrdLNKRLEKEtvqskd 172
Cdd:PTZ00121 1334 AKKKAEEAKKAAEaakaEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE----AKKKAEED------ 1403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 173 fKLEVDKLSVRITALEKLEDALDKSKQEcysLKCNLEKEKMTTKQLSEELESlnaRIKELEAIESRLEKTEITLKDDLTK 252
Cdd:PTZ00121 1404 -KKKADELKKAAAAKKKADEAKKKAEEK---KKADEAKKKAEEAKKADEAKK---KAEEAKKAEEAKKKAEEAKKADEAK 1476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 253 LKTLTVMLVDERKTMSEKLKQTEDKLQsttsqlQAEQNKVTTVTEKLIEETKRALKSKTdAEEKmysvtKERDDLRnklK 332
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAK------KAAEAKKKADEAKKAEEAKKADEAKK-AEEA-----KKADEAK---K 1541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 333 AEEEKGHDLLSKVTILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQENNKIKELSQEV-ENLKLKLKDMKAIEDDLMK 411
Cdd:PTZ00121 1542 AEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYeEEKKMKAEEAKKAEEAKIK 1621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 412 TED---------EYETLERRYANERDKAQFLSQELEHAKMELAKYKLAEKTESSHEQWLFRRLQEEEAKSGHLSRE---- 478
Cdd:PTZ00121 1622 AEElkkaeeekkKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeea 1701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 479 --VDALKEKIHEYMATEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSLNERRISDPQVF 556
Cdd:PTZ00121 1702 kkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
....*..
gi 295424124 557 SKEVQTE 563
Cdd:PTZ00121 1782 EEELDEE 1788
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
14-337 |
5.77e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 14 ALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTnedsQNRQLRQKLAALSRQ 93
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR----QISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 94 IDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVldmegkDEELIKMEEQCRDLNKRLEKETVQSKDF 173
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL------EAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 174 KLEVDKLSVRITALEKLEDALDKSKQEcyslkcnLEKEKmttKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKL 253
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLED-------LEEQI---EELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 254 KTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKL------IEETKRALKSK-----TDAEEKMYSVTK 322
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLeglevrIDNLQERLSEEysltlEEAEALENKIED 965
|
330
....*....|....*
gi 295424124 323 ERDDLRNKLKAEEEK 337
Cdd:TIGR02168 966 DEEEARRRLKRLENK 980
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
9-547 |
6.88e-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: 69.71 E-value: 6.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 9 LTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQ-------TTEFHQNQDKIM---AKLTNEDS 78
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEErkrrdklTEEYAELKEELEdlrAELEEVDK 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 79 QNRQLRQKLAALSRQID----ELEETNRS-------LRKAEEELQDIKDKInkgeygnSGIMDEVDELRKRVLDmegKDE 147
Cdd:TIGR02169 379 EFAETRDELKDYREKLEklkrEINELKREldrlqeeLQRLSEELADLNAAI-------AGIEAKINELEEEKED---KAL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 148 ELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQecySLKCNLEKEKMTTKQLSEELESLNA 227
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR---ASEERVRGGRAVEEVLKASIQGVHG 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 228 RIKEL--------EAIES----RLEKteITLKDDLT-----------KLKTLTVMLVDERKTMSEKLK------------ 272
Cdd:TIGR02169 526 TVAQLgsvgeryaTAIEVaagnRLNN--VVVEDDAVakeaiellkrrKAGRATFLPLNKMRDERRDLSilsedgvigfav 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 273 ---QTEDKLQS----------------TTSQLQAEQNKVT---------------TVTEKLIEETKRALKSKT-DAEEKM 317
Cdd:TIGR02169 604 dlvEFDPKYEPafkyvfgdtlvvedieAARRLMGKYRMVTlegelfeksgamtggSRAPRGGILFSRSEPAELqRLRERL 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 318 YSVTKERDDLRNKLKAEEEKGHDLLSKVTILKnrlQSLEAIEKDfvKNKLNQDSSKSTAALHQENNKIKELSQEVENLKL 397
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDAS---RKIGEIEKE--IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 398 KLKDMKA----IEDDLMKTEDEYETLERRYANERDK---AQFLSQELEHAKMELAKYKLAEKTESSHEqwlfrRLQEEEA 470
Cdd:TIGR02169 759 ELKELEArieeLEEDLHKLEEALNDLEARLSHSRIPeiqAELSKLEEEVSRIEARLREIEQKLNRLTL-----EKEYLEK 833
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295424124 471 KSGHLSREVDALKEKIHEYMATEDLichLQGDHSLLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSLNE 547
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIEN---LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-535 |
7.14e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 7.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 2 VVDEQQRLTAQLALQRQKIQALTTSAKETqgKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNR 81
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEIERLEAR--LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 82 QLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGKDE---ELIKMEEQCR- 157
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlsELISVDEGYEa 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 158 ----DLNKRLEKETVQSKD-FKLEVDKL--------------SVRITALEKLEDALDKSKQECYSLKCNLEKekmTTKQL 218
Cdd:TIGR02168 538 aieaALGGRLQAVVVENLNaAKKAIAFLkqnelgrvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVK---FDPKL 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 219 SEELESLNARIKELEAIESRLEK--------TEITLKDDL-------TKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTS 283
Cdd:TIGR02168 615 RKALSYLLGGVLVVDDLDNALELakklrpgyRIVTLDGDLvrpggviTGGSAKTNSSILERRREIEELEEKIEELEEKIA 694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 284 QLQAEQNKVTTVTEKLIEETKRALKSKTDAEekmysvtKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEkdfv 363
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELS-------RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI---- 763
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 364 kNKLNQDSSKSTAALHQENNKIKELSQEVENLKlklKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKME 443
Cdd:TIGR02168 764 -EELEERLEEAEEELAEAEAEIEELEAQIEQLK---EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 444 LAKYKLAEKTESSHEQWLFRRLQEEEAKSGHLSREVDALKEkihEYMATEDLICHLQGDHSLLQKKLNQQENRNRDLGRE 523
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN---ERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
570
....*....|..
gi 295424124 524 IENLTKELERYR 535
Cdd:TIGR02168 917 LEELREKLAQLE 928
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
5-448 |
1.21e-11 |
|
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: 68.51 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 5 EQQRLTAQLALQRQKIQALTTSAKETQGKLalaearaQEEEQKATRLEKELQTQTTEFHQNQDKImaklTNEDSQNRQLR 84
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEISNTQTQL-------NQLKDEQNKIKKQLSEKQKELEQNNKKI----KELEKQLNQLK 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 85 QKLAALSRQIDE--LEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEG----KDEELIKMEEQCRD 158
Cdd:TIGR04523 295 SEISDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESenseKQRELEEKQNEIEK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 159 LNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEkmtTKQLSEELESLNARIKELEAIESR 238
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE---IERLKETIIKNNSEIKDLTNQDSV 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 239 LEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLqaeqNKVTTVTEKLIEETKRALKSKTDAEEKMY 318
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL----KKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 319 SVTKERDDLRNKLKAEEEKghdLLSKVTILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQENNKIKELSQEVENL--K 396
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDE---LNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLikE 604
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 295424124 397 LKLKDMKA--IEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYK 448
Cdd:TIGR04523 605 IEEKEKKIssLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
19-324 |
1.48e-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: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 19 KIQALTTSAKETQGKLALAEARAQEEEQKAtrLEKELQTQTTEFHQNQDKImakltnedsqnRQLRQKLAALSRQIDELE 98
Cdd:TIGR02169 212 RYQALLKEKREYEGYELLKEKEALERQKEA--IERQLASLEEELEKLTEEI-----------SELEKRLEEIEQLLEELN 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 99 EtnRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGK----DEELIKMEEQCRDLNKRLEKEtvqskdfK 174
Cdd:TIGR02169 279 K--KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERlaklEAEIDKLLAEIEELEREIEEE-------R 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 175 LEVDKLsvrITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRL--EKTEIT-----LK 247
Cdd:TIGR02169 350 KRRDKL---TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeELQRLSeeladLN 426
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295424124 248 DDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKL--IEETKRALKSKTDAEEKMYSVTKER 324
Cdd:TIGR02169 427 AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYdrVEKELSKLQRELAEAEAQARASEER 505
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3-461 |
7.44e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.94 E-value: 7.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 3 VDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQttEFHQNQDKIMAKLTNEDSQNRQ 82
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL--PLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 83 LRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGN-SGIMDEVDELRKRVLDMEgkdEELIKMEEQCRDLNK 161
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELE---EELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 162 RLEKETVQSKDFKLE--VDKLSV------RITALEKLEDALDKSKQEC-----------YSLKCNLEKEKMTTKQLSEEL 222
Cdd:COG4717 228 ELEQLENELEAAALEerLKEARLllliaaALLALLGLGGSLLSLILTIagvlflvlgllALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 223 ESLNARikeleaieSRLEKTEIT-LKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQnkvttvteklIE 301
Cdd:COG4717 308 QALPAL--------EELEEEELEeLLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE----------LE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 302 ETKRALKSKTDAEekmysvtkERDDLRNKLKAEEEKgHDLLSKVTILKNRLQSL----EAIEKDFVKNKLNQDSSKSTAA 377
Cdd:COG4717 370 QEIAALLAEAGVE--------DEEELRAALEQAEEY-QELKEELEELEEQLEELlgelEELLEALDEEELEEELEELEEE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 378 LHQENNKIKELSQEVENLKLKLKDMKAiEDDLMKTEDEYETLerryanerdKAQFLSQELEHAKMELAKYKLAEKTESSH 457
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEE-DGELAELLQELEEL---------KAELRELAEEWAALKLALELLEEAREEYR 510
|
....
gi 295424124 458 EQWL 461
Cdd:COG4717 511 EERL 514
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
35-535 |
9.54e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 9.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 35 ALAEARAQEEEQKatrlEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDI 114
Cdd:PRK02224 188 SLDQLKAQIEEKE----EKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 115 KDKINKGEYGNSGIMDEVDELRKRVLDMEGKD---------------------EELIKMEEQCRDlnkRLEKETVQSKDF 173
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERddllaeaglddadaeavearrEELEDRDEELRD---RLEECRVAAQAH 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 174 KLEVDKLSVRITALE----KLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIK----ELEAIESRLEKTEIT 245
Cdd:PRK02224 341 NEEAESLREDADDLEeraeELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvDLGNAEDFLEELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 246 LKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKL------------IEETKRALKSKTDA 313
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRerveeleaeledLEEEVEEVEERLER 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 314 EEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSL---------EAIEKDFVKNKLNQDSSKSTAALHQENNK 384
Cdd:PRK02224 501 AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELreraaeleaEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 385 IKELSQEVENLklklkdmKAIEDDLMKTEDEYETLERRyaNERDKAQflsQELEHAKMElakyKLAEKTEssheqwlfRR 464
Cdd:PRK02224 581 LAELKERIESL-------ERIRTLLAAIADAEDEIERL--REKREAL---AELNDERRE----RLAEKRE--------RK 636
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 295424124 465 LQEEEAKSGHLSREVDALKEKIHEYMATEDlichlqgdhsllqKKLNQQENRNRDLGREI---ENLTKELERYR 535
Cdd:PRK02224 637 RELEAEFDEARIEEAREDKERAEEYLEQVE-------------EKLDELREERDDLQAEIgavENELEELEELR 697
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
36-537 |
1.26e-10 |
|
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: 65.63 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 36 LAEARAQEEEQKAT-RLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAE-EELQD 113
Cdd:pfam12128 272 TLIASRQEERQETSaELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADqEQLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 114 IKDKINKGEygnsgimDEVDELRKRVLDMEGKDEELI-KMEEQCRDLNKRLEKETVQSKDFKleVDKLSVRITALEKLED 192
Cdd:pfam12128 352 WQSELENLE-------ERLKALTGKHQDVTAKYNRRRsKIKEQNNRDIAGIKDKLAKIREAR--DRQLAVAEDDLQALES 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 193 ALDKS--------KQECYSLKCNLEKEKMTTKQL---SEELESLNARIKELEAIESRLE---KTEITLKDDLTKLKTLtv 258
Cdd:pfam12128 423 ELREQleagklefNEEEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERAREEQEaanAEVERLQSELRQARKR-- 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 259 mlvdeRKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTK-ERDDLRNKLKAEEEK 337
Cdd:pfam12128 501 -----RDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELlHRTDLDPEVWDGSVG 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 338 GHDLLSKVTIlknRLQSLEAIEKDFVKNKLNQDSSKSTAALHQENNKIKELSQ-------EVENLKLKLKDMKAI----E 406
Cdd:pfam12128 576 GELNLYGVKL---DLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEqlvqangELEKASREETFARTAlknaR 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 407 DDLMKTEDEYETLERR----YANERDKAQFLSQELEHAKMELA---KYKLAEKTESSHE---QWLFRRLQEEEAKSGHLS 476
Cdd:pfam12128 653 LDLRRLFDEKQSEKDKknkaLAERKDSANERLNSLEAQLKQLDkkhQAWLEEQKEQKREartEKQAYWQVVEGALDAQLA 732
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295424124 477 ReVDALKEKIHEYMATEDLICHLQGDHSLlqKKLNQQENRNRDLGREIENLTKELERYRHF 537
Cdd:pfam12128 733 L-LKAAIAARRSGAKAELKALETWYKRDL--ASLGVDPDVIAKLKREIRTLERKIERIAVR 790
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
19-545 |
1.36e-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: 65.47 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 19 KIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEdsqNRQLRQKLAALSRQI---- 94
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE---QLRVKEKIGELEAEIasle 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 95 DELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEgkdEELIKMEEQCRDLNKRLEKEtvqSKDFK 174
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT---EEYAELKEELEDLRAELEEV---DKEFA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 175 LEVDKLSVRITALEKLedaldksKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEA----IESRLEKTEITLKDDL 250
Cdd:TIGR02169 382 ETRDELKDYREKLEKL-------KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAkineLEEEKEDKALEIKKQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 251 TKLKTLTVMLVDERKTMsEKLKQTEDKLQSTTSQLQAEQNKVTTvTEKLIEETKRALKSKTD------------------ 312
Cdd:TIGR02169 455 WKLEQLAADLSKYEQEL-YDLKEEYDRVEKELSKLQRELAEAEA-QARASEERVRGGRAVEEvlkasiqgvhgtvaqlgs 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 313 ------------AEEKMYSVTKERDDLR--------------------NKLKAEE------------------------- 335
Cdd:TIGR02169 533 vgeryataievaAGNRLNNVVVEDDAVAkeaiellkrrkagratflplNKMRDERrdlsilsedgvigfavdlvefdpky 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 336 -----------------EKGHDLLSK---VTILKNRLQSLEAIEKDFVKNKLNQDSSKS-TAALHQENNKIKELSQEVEN 394
Cdd:TIGR02169 613 epafkyvfgdtlvvediEAARRLMGKyrmVTLEGELFEKSGAMTGGSRAPRGGILFSRSePAELQRLRERLEGLKRELSS 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 395 LKLKLKDMK------------------AIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKY--KLAEKTE 454
Cdd:TIGR02169 693 LQSELRRIEnrldelsqelsdasrkigEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELeaRIEELEE 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 455 SSHEqwlfrrLQEEEAK-----SGHLSREVDALKEKIHEYMA--------TEDLICHLQGDHSLLQKKLNQQENRNRDL- 520
Cdd:TIGR02169 773 DLHK------LEEALNDlearlSHSRIPEIQAELSKLEEEVSriearlreIEQKLNRLTLEKEYLEKEIQELQEQRIDLk 846
|
650 660 670
....*....|....*....|....*....|....*...
gi 295424124 521 ------GREIENLTK-------ELERYRHFSKSLRPSL 545
Cdd:TIGR02169 847 eqiksiEKEIENLNGkkeeleeELEELEAALRDLESRL 884
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-445 |
2.27e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 98 EETNRSLRKAEEELQDIKDkinkgeygnsgIMDEV----DELRK--------RVLDMEgkdEELIKMEEQCRDLNKRLEK 165
Cdd:COG1196 175 EEAERKLEATEENLERLED-----------ILGELerqlEPLERqaekaeryRELKEE---LKELEAELLLLKLRELEAE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 166 ETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQEcyslkcnLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEIT 245
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLE-------LEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 246 LKDDLTKLKtltvmlvDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERD 325
Cdd:COG1196 314 LEERLEELE-------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 326 DLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDfvKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAI 405
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEE--LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 295424124 406 EDDLMKTEDEYETL--ERRYANERDKAQFLSQELEHAKMELA 445
Cdd:COG1196 465 LAELLEEAALLEAAlaELLEELAEAAARLLLLLEAEADYEGF 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5-328 |
2.37e-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: 64.69 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 5 EQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEfhqnQDKIMAKLTNEDSQNRQLR 84
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 85 QKLAALSRQIDELEETnrsLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEG----KDEELIKMEEQCRDLN 160
Cdd:TIGR02168 761 AEIEELEERLEEAEEE---LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaanLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 161 KRLEKETVQSKDFKLEVDKLSVRI----TALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELE--- 233
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIeeleELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRrel 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 234 --------AIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKR 305
Cdd:TIGR02168 918 eelreklaQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEE 997
|
330 340
....*....|....*....|...
gi 295424124 306 ALKSKTDAEEKMYSVTKERDDLR 328
Cdd:TIGR02168 998 LKERYDFLTAQKEDLTEAKETLE 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
9-362 |
2.81e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 9 LTAQLA-LQRQKIQALTtsaketqgklaLAEARAQEEEQKATRLEKELqtqttefhqnqDKIMAKLTNEDSQNRQLRQKL 87
Cdd:COG1196 198 LERQLEpLERQAEKAER-----------YRELKEELKELEAELLLLKL-----------RELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 88 AALSRQIDELEETNRSLRKAEEELQdikdkinkgeygnsgimDEVDELRKRVLDMEgkdEELIKMEEQCRDLNKRLEKET 167
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELE-----------------LELEEAQAEEYELL---AELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 168 VQSKDFKLEVDKLSVRITALEKLEDALDKSKQEcysLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLK 247
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEE---AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 248 DDLTKLKTltvmLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDL 327
Cdd:COG1196 393 RAAAELAA----QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
330 340 350
....*....|....*....|....*....|....*
gi 295424124 328 RNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDF 362
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
37-396 |
5.13e-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: 63.55 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 37 AEARAQEEEQKATRLEKELQtqttEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDEL----EETNRSLRKAEEELQ 112
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIekeiEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 113 DIKDKINKGEYGNSGIMDEVDELRKRVLDMEgkdEELIKMEEQCRDLNKRLEKETVQSKDFKL-----EVDKLSVRITAL 187
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELE---EDLHKLEEALNDLEARLSHSRIPEIQAELskleeEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 188 EKLEDALDKSKQECYSLKCNLE--------KEKMTTKQLSE---ELESLNARIKELEAIESRLEKTEITLKddltklktl 256
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQeqridlkeQIKSIEKEIENlngKKEELEEELEELEAALRDLESRLGDLK--------- 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 257 tvmlvDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLiEETKRALKSKTDAEEKMYSVTKERDDLRnKLKAEEE 336
Cdd:TIGR02169 889 -----KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL-EALEEELSEIEDPKGEDEEIPEEELSLE-DVQAELQ 961
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295424124 337 KghdllskvtiLKNRLQSLEAI------EKDFVKNKLNQDSSKStAALHQENNKIKELSQEVENLK 396
Cdd:TIGR02169 962 R----------VEEEIRALEPVnmlaiqEYEEVLKRLDELKEKR-AKLEEERKAILERIEEYEKKK 1016
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
46-412 |
7.49e-10 |
|
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: 62.73 E-value: 7.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 46 QKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRkaeEELQDIKDKINKGEYGN 125
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQ---RELEEKQNEIEKLKKEN 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 126 SGIMDEVDELRKRVLDMEGK-----------DEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDAL 194
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKiqnqeklnqqkDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 195 DKS----KQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEK 270
Cdd:TIGR04523 460 DNTreslETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 271 LKQTEDKLQS-----TTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKV 345
Cdd:TIGR04523 540 ISDLEDELNKddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL 619
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295424124 346 TILKNRLQSLEAIEK--DFVKNKLNQDsskstaaLHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKT 412
Cdd:TIGR04523 620 EKAKKENEKLSSIIKniKSKKNKLKQE-------VKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIEL 681
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
29-369 |
1.82e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 29 ETQGKLA--LAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRK 106
Cdd:TIGR02168 206 ERQAEKAerYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 107 AEEELQDIKDKINKGeygnsgimdevdELRKRVLdmegkDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITA 186
Cdd:TIGR02168 286 LQKELYALANEISRL------------EQQKQIL-----RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 187 LEKLEDALDKSKQECYSLKCNLEKEKmttKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTklktltvMLVDERKT 266
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRL---EELEEQLETLRSKVAQLELQIASLNNEIERLEARLE-------RLEDRRER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 267 MSEKLKQTEDKLQSttsqlqAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVT 346
Cdd:TIGR02168 419 LQQEIEELLKKLEE------AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
330 340
....*....|....*....|...
gi 295424124 347 ILKNRLQSLEAIEKDFVKNKLNQ 369
Cdd:TIGR02168 493 SLERLQENLEGFSEGVKALLKNQ 515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-279 |
6.53e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 6.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 4 DEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQL 83
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 84 RQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGKDEELikmEEQCRDLNKRL 163
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL---RRELEELREKL 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 164 EKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMttKQLSEELESLN----ARIKELEAIESRL 239
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL--KRLENKIKELGpvnlAAIEEYEELKERY 1002
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 295424124 240 EKTEiTLKDDLTK-LKTLTVMLVDERKTMSEKLKQTEDKLQ 279
Cdd:TIGR02168 1003 DFLT-AQKEDLTEaKETLEEAIEEIDREARERFKDTFDQVN 1042
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
125-438 |
1.13e-08 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 58.79 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 125 NSGIMdEVDELRKrvldmEGKDEELIKMEEQCRDLNKRLEK-ETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQEcys 203
Cdd:PRK05771 27 ELGVV-HIEDLKE-----ELSNERLRKLRSLLTKLSEALDKlRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEK--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 204 lkcnLEKEkmtTKQLSEELESLNARIKELEAIESRLEKteitlkddltkLKTLTVMLVDERKtmseklkqtedklqstts 283
Cdd:PRK05771 98 ----IEKE---IKELEEEISELENEIKELEQEIERLEP-----------WGNFDLDLSLLLG------------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 284 qlqaeqNKVTTVTEKLIEETKralksktdaeekmYSVTKERDDLRNKLKAEEEKGHDLLSkVTILKNRLQSLEAI--EKD 361
Cdd:PRK05771 142 ------FKYVSVFVGTVPEDK-------------LEELKLESDVENVEYISTDKGYVYVV-VVVLKELSDEVEEElkKLG 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295424124 362 FVKNKLNqDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYetlerrYANERDKAQFLSQELE 438
Cdd:PRK05771 202 FERLELE-EEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY------LEIELERAEALSKFLK 271
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1-454 |
1.18e-08 |
|
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: 59.03 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 1 MVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTtEFHQNQDKIMAKLTNEDSQn 80
Cdd:pfam01576 142 LLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEE-KGRQELEKAKRKLEGESTD- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 81 rqLRQKLAALSRQIDELEEtnrSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVL----DMEGKDEELIKMEEQC 156
Cdd:pfam01576 220 --LQEQIAELQAQIAELRA---QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISelqeDLESERAARNKAEKQR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 157 RDLNKRLEketvqskdfklevdklsvritALE-KLEDALD----------KSKQECYSLKCNLEKE-KMTTKQLSE---- 220
Cdd:pfam01576 295 RDLGEELE---------------------ALKtELEDTLDttaaqqelrsKREQEVTELKKALEEEtRSHEAQLQEmrqk 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 221 ---ELESLNARIKELEAIESRLEKTEITLKDDLTKLKTltvmlvdERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTtvte 297
Cdd:pfam01576 354 htqALEELTEQLEQAKRNKANLEKAKQALESENAELQA-------ELRTLQQAKQDSEHKRKKLEGQLQELQARLS---- 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 298 klieETKRAlksKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDFVKNKLN--------- 368
Cdd:pfam01576 423 ----ESERQ---RAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNlstrlrqle 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 369 QDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKA--QFLSQELEHAKMELAK 446
Cdd:pfam01576 496 DERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALtqQLEEKAAAYDKLEKTK 575
|
....*...
gi 295424124 447 YKLAEKTE 454
Cdd:pfam01576 576 NRLQQELD 583
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
6-531 |
3.44e-08 |
|
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: 57.42 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 6 QQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKiMAKLTNEDSQNRQLRQ 85
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEK-KDHLTKELEDIKMSLQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 86 KLAALSRQIDE-LEETNRSLRKAEEELQDIKDKINKGEYGNSGImdeVDELRKRVLDMEgkdeELIKMEEQcrdlnkRLE 164
Cdd:pfam05483 307 RSMSTQKALEEdLQIATKTICQLTEEKEAQMEELNKAKAAHSFV---VTEFEATTCSLE----ELLRTEQQ------RLE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 165 KETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEI 244
Cdd:pfam05483 374 KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIH 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 245 TLKDDLTKLKTLT---VMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETK--------------RAL 307
Cdd:pfam05483 454 DLEIQLTAIKTSEehyLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKkhqediinckkqeeRML 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 308 KSKTDAEEK-------MYSVTKE----RDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDFVKNKLNQdsSKSTA 376
Cdd:pfam05483 534 KQIENLEEKemnlrdeLESVREEfiqkGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENK--NKNIE 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 377 ALHQENNKIKELSQeVENLKLKLKDMKA--IEDDLMKTEDEYETLERRYANERDKAQfLSQELEHAKMELAKYKLAEKTe 454
Cdd:pfam05483 612 ELHQENKALKKKGS-AENKQLNAYEIKVnkLELELASAKQKFEEIIDNYQKEIEDKK-ISEEKLLEEVEKAKAIADEAV- 688
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295424124 455 ssheqwlfrRLQEE-EAKSGHLSREVDALKEK-IHEYmatEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTKEL 531
Cdd:pfam05483 689 ---------KLQKEiDKRCQHKIAEMVALMEKhKHQY---DKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAEL 755
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
45-452 |
4.06e-08 |
|
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: 56.95 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 45 EQKATRLEKELQTQTTEFHQNQDKI----------MAKLTNEDSQNRQLRQKLAALSRQI----DELEETNRSLRKAEEE 110
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELknldknlnkdEEKINNSNNKIKILEQQIKDLNDKLkknkDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 111 LQDIKDKINKGEygnsgimDEVDELRKrvldmegkdeELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKL 190
Cdd:TIGR04523 112 IKNDKEQKNKLE-------VELNKLEK----------QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 191 EDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEK 270
Cdd:TIGR04523 175 LNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 271 LKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAE---------------EKMYSVTKERDDLRNKLKAEE 335
Cdd:TIGR04523 255 LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnqkeqdwnkelkSELKNQEKKLEEIQNQISQNN 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 336 EKGHDLLSKVTILKNRLQSLEAiekdfVKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDM-----------KA 404
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSES-----ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLeskiqnqeklnQQ 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 295424124 405 IEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKLAEK 452
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
85-548 |
6.05e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 85 QKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEygnsgimDEVDELRKRVLDMEgKDEELIKMEEQCRDLNKRLE 164
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELE-------AELEELREELEKLE-KLLQLLPLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 165 KETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNL-EKEKMTTKQLSEELESLNARIKELEAIESRLEKTE 243
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 244 ITLKDDLTKLKTLTvmlvdERKTMSEKLKQTEDKLQSTTSQL------QAEQNKVTTVTEKLIEETKRALKSKTDAEEKM 317
Cdd:COG4717 223 EELEEELEQLENEL-----EAAALEERLKEARLLLLIAAALLallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 318 YSVTKERDDLRNKLKAEEEKGHDLLSkvtiLKNRLQSLEAIEKDFVKNKLNQdssksTAALHQENNKIKELSQEVENLKL 397
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEE----LLAALGLPPDLSPEELLELLDR-----IEELQELLREAEELEEELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 398 KLKDMKAIEDDLMKTEDEYE---TLERRYANERDKAQFLSQELEHAKMELAKYKLAEKTESSHEQW--LFRRLQEEEAKS 472
Cdd:COG4717 369 EQEIAALLAEAGVEDEEELRaalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELeeLEEELEELEEEL 448
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295424124 473 GHLSREVDALKEKIHEyMATEDLICHLQGDHSLLQKKLNQQENRNR--DLGREIenLTKELERYRhfsKSLRPSLNER 548
Cdd:COG4717 449 EELREELAELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWAalKLALEL--LEEAREEYR---EERLPPVLER 520
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
34-306 |
1.03e-07 |
|
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: 55.16 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 34 LALAEARAQEEEQKAtrLEKELQtqttEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEetnRSLRKAEEELQD 113
Cdd:COG4942 10 LLALAAAAQADAAAE--AEAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---RRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 114 IKDKINKGEygnsgimDEVDELRKRvldmegkdeelikMEEQCRDLNKRLEKETVQSKDFKLEVdklsvritaLEKLEDA 193
Cdd:COG4942 81 LEAELAELE-------KEIAELRAE-------------LEAQKEELAELLRALYRLGRQPPLAL---------LLSPEDF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 194 LDKSKqecyslkcNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVML---VDERKTMSEK 270
Cdd:COG4942 132 LDAVR--------RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALealKAERQKLLAR 203
|
250 260 270
....*....|....*....|....*....|....*.
gi 295424124 271 LKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRA 306
Cdd:COG4942 204 LEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
207-445 |
1.54e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 207 NLEKEKMTTKQLSEELEslnariKELEAIESRLEKTEITLKDdlTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQ 286
Cdd:COG3206 165 NLELRREEARKALEFLE------EQLPELRKELEEAEAALEE--FRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 287 AEQNKVTTVTEKLieETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAiekdfvknK 366
Cdd:COG3206 237 EAEARLAALRAQL--GSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA--------Q 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295424124 367 LNQDSSKSTAALHQEnnkIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELA 445
Cdd:COG3206 307 LQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
209-549 |
1.65e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 209 EKEKMTTKQL---SEELESLNARIKELEA----IESRLEKTE--ITLKDDLTKL-KTLTVMLVDERKtmsEKLKQTEDKL 278
Cdd:TIGR02168 172 ERRKETERKLertRENLDRLEDILNELERqlksLERQAEKAEryKELKAELRELeLALLVLRLEELR---EELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 279 QSTTSQLQAEQNKVTTVTEKLieETKRALKSKtdAEEKMYSVTKERDDLRNKLkaeeekgHDLLSKVTILKNRLQSLEai 358
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKL--EELRLEVSE--LEEEIEELQKELYALANEI-------SRLEQQKQILRERLANLE-- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 359 ekdfvknklnQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLmktEDEYETLERRYANERDKAQFLSQELE 438
Cdd:TIGR02168 316 ----------RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL---EAELEELEAELEELESRLEELEEQLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 439 HAKMELAKYKLAEKTESSHEQWLFRRLQEEEAKSGHLSREVDALKEKIHEYMATEdlichLQGDHSLLQKKLNQQENRNR 518
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE-----LQAELEELEEELEELQEELE 457
|
330 340 350
....*....|....*....|....*....|.
gi 295424124 519 DLGREIENLTKELERYRHFSKSLRPSLNERR 549
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
108-533 |
2.04e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 108 EEELQDIKDKINKGEYGNSGI-MDEVDELRKRVLDMEGKDEELIKMEEQCRDLNKRLEketvqskDFKLEVDKLSVRITA 186
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELnLKELKELEEELKEAEEKEEEYAELQEELEELEEELE-------ELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 187 LEKLEDALDKSKQecyslkcnLEKEKMTTKQLSEELESLNARIKELEAIESRLEKteitLKDDLTKLKTltvmlvDERKT 266
Cdd:COG4717 121 LEKLLQLLPLYQE--------LEALEAELAELPERLEELEERLEELRELEEELEE----LEAELAELQE------ELEEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 267 MSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLieETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEE---------- 336
Cdd:COG4717 183 LEQLSLATEEELQDLAEELEELQQRLAELEEEL--EEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaalla 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 337 ---KGHDLLSKVTILKNRLQSLEAI------EKDFVKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIED 407
Cdd:COG4717 261 llgLGGSLLSLILTIAGVLFLVLGLlallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 408 DLMKTEDEYETLERRYANERDKAQFlsQELEHAKMELAKYKLAEkTESSHEQWL--FRRLQEEEAKSGHLSREVDALKEK 485
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQL--EELEQEIAALLAEAGVE-DEEELRAALeqAEEYQELKEELEELEEQLEELLGE 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 295424124 486 IHEYMATEDLichlqgdhSLLQKKLNQQENRNRDLGREIENLTKELER 533
Cdd:COG4717 418 LEELLEALDE--------EELEEELEELEEELEELEEELEELREELAE 457
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
4-243 |
2.29e-07 |
|
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: 54.00 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 4 DEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQL 83
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 84 RQKLAALSRQIDELEETNRS-----LRKAEEELQDIKDKINKGEYgnsgimdeVDELRKRVLDMEGKDEELikmeeqcRD 158
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQpplalLLSPEDFLDAVRRLQYLKYL--------APARREQAEELRADLAEL-------AA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 159 LNKRLEKETvqskdfklevDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKmttKQLSEELESLNARIKELEAIESR 238
Cdd:COG4942 165 LRAELEAER----------AELEALLAELEEERAALEALKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIAR 231
|
....*
gi 295424124 239 LEKTE 243
Cdd:COG4942 232 LEAEA 236
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
176-488 |
2.60e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 176 EVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEkmtTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKT 255
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEE---LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 256 LTVMLVDERKTMSEKLKQTEDKLQsttsQLQAEQNKVTTVTEKLIEETKrALKSKTDAEEKMYSVTKER-DDLRNKLKAE 334
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELA----EAEAEIEELEAQIEQLKEELK-ALREALDELRAELTLLNEEaANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 335 EEKGHDllsKVTILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQEnnKIKELSQEVENLKLKLKDMKAIEDDLMKTED 414
Cdd:TIGR02168 830 ERRIAA---TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES--ELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 415 EYET----LERRYANERDKAQFLSQELEHAKMELA--KYKLAEKTESSHEQwLFRRLQEEEAKSGHLSREVDALKEKIHE 488
Cdd:TIGR02168 905 ELESkrseLRRELEELREKLAQLELRLEGLEVRIDnlQERLSEEYSLTLEE-AEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
4-327 |
2.72e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.59 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 4 DEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQL 83
Cdd:pfam02463 680 ELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKK 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 84 RQKLA----ALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGKDEELIKMEEQCRDL 159
Cdd:pfam02463 760 EEKEEekseLSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELA 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 160 NKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRL 239
Cdd:pfam02463 840 LELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEI 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 240 EKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYS 319
Cdd:pfam02463 920 EERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999
|
....*...
gi 295424124 320 VTKERDDL 327
Cdd:pfam02463 1000 LEEEKKKL 1007
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
175-575 |
2.73e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.52 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 175 LEVDKLSvriTALEKLEDALDKSKQECYSLkcNLEKEKMTTKQLseELESLNARIKELEAIESRLEKTEITLKDDLTKLK 254
Cdd:PRK01156 159 LEINSLE---RNYDKLKDVIDMLRAEISNI--DYLEEKLKSSNL--ELENIKKQIADDEKSHSITLKEIERLSIEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 255 TLTVMLVDERKTMS---EKLKQTEDKLQSTTSQLQAEQNKVTTVTEkLIEETKRALKSKtdaeekmysVTKERDDLRNKL 331
Cdd:PRK01156 232 DDYNNLKSALNELSsleDMKNRYESEIKTAESDLSMELEKNNYYKE-LEERHMKIINDP---------VYKNRNYINDYF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 332 KAEEekghDLLSKVTILKNRLQSLEAIEkdfvknklnqDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMK 411
Cdd:PRK01156 302 KYKN----DIENKKQILSNIDAEINKYH----------AIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNS 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 412 TEDEYETLERRYANERDKAQFLSQELEHAkmeLAKYKLAEKTESSHEQWLFRRLQEEEAKSGHLSREVDALKEK---IHE 488
Cdd:PRK01156 368 YLKSIESLKKKIEEYSKNIERMSAFISEI---LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENldeLSR 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 489 YMA-------------------TEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTKELER-----------YRHFS 538
Cdd:PRK01156 445 NMEmlngqsvcpvcgttlgeekSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYleseeinksinEYNKI 524
|
410 420 430
....*....|....*....|....*....|....*..
gi 295424124 539 KSLRPSLNERRISDPQVFSKEVQTEAADSEppdYKSL 575
Cdd:PRK01156 525 ESARADLEDIKIKINELKDKHDKYEEIKNR---YKSL 558
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2-469 |
3.03e-07 |
|
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: 54.67 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 2 VVDEQQRLTAQLALQRQKIQALTTSAKEtqgkLALAEARAQEEEQKATrlEKELQTQTTEFhqnqdkimakltneDSQNR 81
Cdd:TIGR00606 459 VIKELQQLEGSSDRILELDQELRKAERE----LSKAEKNSLTETLKKE--VKSLQNEKADL--------------DRKLR 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 82 QLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGKDEELIKMEEQCRDLNK 161
Cdd:TIGR00606 519 KLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNK 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 162 RLEKETVQSKDFKLEVDKLSVRITALE-KLEDALDKSKQECY--SLKCNLEKEKMTTKQLSEELESLNARIKELEAIES- 237
Cdd:TIGR00606 599 ELASLEQNKNHINNELESKEEQLSSYEdKLFDVCGSQDEESDleRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQs 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 238 ------RLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVtEKLIEETKRALKSKT 311
Cdd:TIGR00606 679 ccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLK-EKEIPELRNKLQKVN 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 312 DAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQENNKIKE---- 387
Cdd:TIGR00606 758 RDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEkqhe 837
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 388 ---LSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAK----YKLAEKTESSHEQW 460
Cdd:TIGR00606 838 ldtVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSlireIKDAKEQDSPLETF 917
|
....*....
gi 295424124 461 LFRRLQEEE 469
Cdd:TIGR00606 918 LEKDQQEKE 926
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
33-242 |
5.61e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 33 KLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMA-----KLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKA 107
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaEYSWDEIDVASAEREIAELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 108 EEELQDIKDKINKGEygnsgimDEVDELRKRvldMEGKDEELIKMEEQCRDLNKRLEKETvqskdfklEVDKLSVRITAL 187
Cdd:COG4913 691 EEQLEELEAELEELE-------EELDELKGE---IGRLEKELEQAEEELDELQDRLEAAE--------DLARLELRALLE 752
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 295424124 188 EKLEDALDKskqecyslkcnlEKEKMTTKQLSEELESLNARIKELeaiESRLEKT 242
Cdd:COG4913 753 ERFAAALGD------------AVERELRENLEERIDALRARLNRA---EEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
216-432 |
6.16e-07 |
|
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: 52.46 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 216 KQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTV 295
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 296 TEKLIEETKRALK--------------SKTDAEEKMY---SVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAi 358
Cdd:COG4942 103 KEELAELLRALYRlgrqpplalllspeDFLDAVRRLQylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLA- 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 295424124 359 EKDFVKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQF 432
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
16-331 |
1.66e-06 |
|
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: 52.10 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 16 QRQKIQALTtSAKETQGKLALAEAR---AQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSR 92
Cdd:pfam01576 762 RKQRAQAVA-AKKKLELDLKELEAQidaANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEA 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 93 QIDELEE----TNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEgkdEELIKMEEQCRDLNKRLEKETV 168
Cdd:pfam01576 841 ELLQLQEdlaaSERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLE---EELEEEQSNTELLNDRLRKSTL 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 169 QSKDFKLEvdkLSVRITALEKLEDALDKSKQECYSLKCNLE--------KEKMTTKQLSEEL----ESLNARIKELEAIE 236
Cdd:pfam01576 918 QVEQLTTE---LAAERSTSQKSESARQQLERQNKELKAKLQemegtvksKFKSSIAALEAKIaqleEQLEQESRERQAAN 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 237 SRLEKTEITLKDdltklktlTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEK 316
Cdd:pfam01576 995 KLVRRTEKKLKE--------VLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATES 1066
|
330
....*....|....*
gi 295424124 317 MYSVTKERDDLRNKL 331
Cdd:pfam01576 1067 NESMNREVSTLKSKL 1081
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
39-545 |
2.48e-06 |
|
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: 51.28 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 39 ARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKI 118
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELEL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 119 NKGEYGNSGIMDEVDELRKRVLDMEGKDEELIKMEEQCRDLNKR---LEKETVQSKDFKLEVDKLSVRITALEKLEDALD 195
Cdd:pfam05557 128 QSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRikeLEFEIQSQEQDSEIVKNSKSELARIPELEKELE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 196 KSKQECYSLKCNLEKEKMttkqLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMseklkQTE 275
Cdd:pfam05557 208 RLREHNKHLNENIENKLL----LKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNL-----RSP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 276 DKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSL 355
Cdd:pfam05557 279 EDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGY 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 356 EAIEKDFVKNKLNQDSSKstaalhQENNKIKELSQEVENLKLKLKDMKAieddlmktedEYETLERRYANERDKAQFLSQ 435
Cdd:pfam05557 359 RAILESYDKELTMSNYSP------QLLERIEEAEDMTQKMQAHNEEMEA----------QLSVAEEELGGYKQQAQTLER 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 436 ELEhakmelakyklaektessheqwlFRRLQEEEAKSGHLSREVDALKEKIHEYMAT-----------EDLICH--LQGD 502
Cdd:pfam05557 423 ELQ-----------------------ALRQQESLADPSYSKEEVDSLRRKLETLELErqrlreqknelEMELERrcLQGD 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 295424124 503 HSL-----LQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSL 545
Cdd:pfam05557 480 YDPkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDL 527
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
231-527 |
4.32e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 231 ELEAIESRLEKTEITLKDDLTKLKTLTvmlvDERKTmSEKLKQTEDKLQSTTSQLQAEQnkvttvTEKLIEETKRALKSK 310
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLR----REREK-AERYQALLKEKREYEGYELLKE------KEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 311 TDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVtilkNRLQSLEAIEkdfVKNKLnqdsSKSTAALHQENNKIKELSQ 390
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI----KDLGEEEQLR---VKEKI----GELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 391 EVENLKLKLKDmkaIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKyklaektessheqwLFRRLQEEEA 470
Cdd:TIGR02169 316 ELEDAEERLAK---LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED--------------LRAELEEVDK 378
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 295424124 471 KSGHLSREVDALKEKIHEYmatEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENL 527
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKL---KREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
12-483 |
5.11e-06 |
|
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: 50.43 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 12 QLALQRQKIQALTTSA--KETQGKLALAEARAQEEEQKATRLEKELQTQTTefhqnqdkimaKLTNEDSQNRQLRQKLAA 89
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQlcADLQSKERLKQEQADEIRDEKKGLGRTIELKKE-----------ILEKKQEELKFVIKELQQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 90 LSRQIDELEETNRSLRKAEEEL------QDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGKDEE---LIKME------- 153
Cdd:TIGR00606 466 LEGSSDRILELDQELRKAERELskaeknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHtttRTQMEmltkdkm 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 154 ---EQCRDLNKRLEKE-TVQSKDF---KLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLN 226
Cdd:TIGR00606 546 dkdEQIRKIKSRHSDElTSLLGYFpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYE 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 227 ARIKEL---EAIESRLEKteitLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNkvttvTEKLIEET 303
Cdd:TIGR00606 626 DKLFDVcgsQDEESDLER----LKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQ-----TEAELQEF 696
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 304 KRALKSKTdaeekmYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDFVK--NKLNQDSSKSTAALHQE 381
Cdd:TIGR00606 697 ISDLQSKL------RLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNklQKVNRDIQRLKNDIEEQ 770
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 382 NNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDeyetLERRYANERDKAQFLSQELEHAKMELAKYKLAEK--TESSHEQ 459
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKD----VERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHEldTVVSKIE 846
|
490 500
....*....|....*....|....
gi 295424124 460 WLFRRLQEEEAKSGHLSREVDALK 483
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELK 870
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
4-527 |
6.16e-06 |
|
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: 50.35 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 4 DEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKaTRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQL 83
Cdd:TIGR00618 362 EVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDIL-QREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYA 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 84 RQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGKDEELikmEEQCRDLNKRL 163
Cdd:TIGR00618 441 ELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL---CGSCIHPNPAR 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 164 eketVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTE 243
Cdd:TIGR00618 518 ----QDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 244 ITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQN---KVTTVTEKLI-----EETKRALKSKTDAEE 315
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQElalKLTALHALQLtltqeRVREHALSIRVLPKE 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 316 KMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDFvkNKLNQDSSKSTAALHQENNKIKELSQEVENL 395
Cdd:TIGR00618 674 LLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREF--NEIENASSSLGSDLAAREDALNQSLKELMHQ 751
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 396 K------LKLKDMKAIEDDLM--KTEDEYETLERRYANERDKAQFLSQELehakmelakyklaEKTESSHEQWLFRRLQE 467
Cdd:TIGR00618 752 ArtvlkaRTEAHFNNNEEVTAalQTGAELSHLAAEIQFFNRLREEDTHLL-------------KTLEAEIGQEIPSDEDI 818
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 468 EEAKSGHLSREVDALKEKIHEYMATEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENL 527
Cdd:TIGR00618 819 LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
42-547 |
7.17e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 49.47 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 42 QEEEQKATRLEKELQTQTT--EFHQNQDKIMAKltnedsqnrqlrqKLAALSRQIDELEETNRSLR--KAEEELQDIKDK 117
Cdd:pfam06160 28 QEELSKVKKLNLTGETQEKfeEWRKKWDDIVTK-------------SLPDIEELLFEAEELNDKYRfkKAKKALDEIEEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 118 INKGEygnsgimDEVDELRKRVLDMEGKDEELIKMEEQCRDLNKRLeKETVQSKDFKLEvdklsvriTALEKLEDALDK- 196
Cdd:pfam06160 95 LDDIE-------EDIKQILEELDELLESEEKNREEVEELKDKYREL-RKTLLANRFSYG--------PAIDELEKQLAEi 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 197 ----SKQECYSLKCNLEKEKMTTKQLSEELESLNARIkelEAIESRLEKTEITLKDDLTKLK-TLTVMLVD----ERKTM 267
Cdd:pfam06160 159 eeefSQFEELTESGDYLEAREVLEKLEEETDALEELM---EDIPPLYEELKTELPDQLEELKeGYREMEEEgyalEHLNV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 268 SEKLKQTEDKLQSTTSQLqaEQNKVTTVtEKLIEETKRALKSKTDAEEKMY----SVTKERDDLRNKLKAEEEKGHDLLS 343
Cdd:pfam06160 236 DKEIQQLEEQLEENLALL--ENLELDEA-EEALEEIEERIDQLYDLLEKEVdakkYVEKNLPEIEDYLEHAEEQNKELKE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 344 KVTILK-------NRLQSLEAIEKDFvkNKLNQDSSKSTAALHqenNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEY 416
Cdd:pfam06160 313 ELERVQqsytlneNELERVRGLEKQL--EELEKRYDEIVERLE---EKEVAYSELQEELEEILEQLEEIEEEQEEFKESL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 417 ETLERRYANERDKAQFLSQELEHAKMELAKYKL--------AEKTESSHE-QWLFRRLQEEEAKSGHLSREVDALKEKIH 487
Cdd:pfam06160 388 QSLRKDELEAREKLDEFKLELREIKRLVEKSNLpglpesylDYFFDVSDEiEDLADELNEVPLNMDEVNRLLDEAQDDVD 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295424124 488 E-YMATEDLIchlqgDHSLLQKKLNQQENRnrdlgreienltkelerYRHFSKSLRPSLNE 547
Cdd:pfam06160 468 TlYEKTEELI-----DNATLAEQLIQYANR-----------------YRSSNPEVAEALTE 506
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-413 |
9.22e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 5 EQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEK-------ELQTQTTEFHQNQDKIMAKLTNED 77
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeekkkaDELKKAEELKKAEEKKKAEEAKKA 1572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 78 SQNRQLRQKLAALSRQIDElEETNRSLRKAEEELQDIKDKINKGEYGNSGI--MDEVDELRKRVLDMEGKDEELIKMEEQ 155
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEE-ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeeLKKAEEEKKKVEQLKKKEAEEKKKAEE 1651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 156 CR-----------DLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQecysLKCNLEKEKMTTKQLSEELES 224
Cdd:PTZ00121 1652 LKkaeeenkikaaEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE----LKKKEAEEKKKAEELKKAEEE 1727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 225 LNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQsttSQLQAEQNKVTTVTEKLIEETK 304
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE---EELDEEDEKRRMEVDKKIKDIF 1804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 305 ralksktDAEEKMYSVTKERDDLRNKLKAEEEKGhdlLSKVTILKN--RLQSLEAIEKDFVKNKLNQDSSKSTAALHQEN 382
Cdd:PTZ00121 1805 -------DNFANIIEGGKEGNLVINDSKEMEDSA---IKEVADSKNmqLEEADAFEKHKFNKNNENGEDGNKEADFNKEK 1874
|
410 420 430
....*....|....*....|....*....|.
gi 295424124 383 NKIKELSQEVEnlklKLKDMKAIEDDLMKTE 413
Cdd:PTZ00121 1875 DLKEDDEEEIE----EADEIEKIDKDDIERE 1901
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
84-337 |
1.04e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 84 RQKLAALSRQIDELEETnrsLRKAEEELQDIKDkinkgeygnsgIMDEVDELRKRVLDMEGKDEELIKMEEQCRdlnkrl 163
Cdd:COG4913 609 RAKLAALEAELAELEEE---LAEAEERLEALEA-----------ELDALQERREALQRLAEYSWDEIDVASAER------ 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 164 eketvqskdfklevdklsvRITALEKLEDALDKSkqecyslkcnlekekmttkqlSEELESLNARIKELEAIESRLEKTE 243
Cdd:COG4913 669 -------------------EIAELEAELERLDAS---------------------SDDLAALEEQLEELEAELEELEEEL 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 244 ITLKDDLTKLKtltvmlvderktmsEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKE 323
Cdd:COG4913 709 DELKGEIGRLE--------------KELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEER 774
|
250
....*....|....
gi 295424124 324 RDDLRNKLKAEEEK 337
Cdd:COG4913 775 IDALRARLNRAEEE 788
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
186-542 |
1.18e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.20 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 186 ALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKEleaiesRLEKTEITLKDDLTKLKtltvmlvDERK 265
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL------ELEEEYLLYLDYLKLNE-------ERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 266 TMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETkralKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKV 345
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEE----KEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 346 TILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQENNKIKE---------LSQEVENLKLKLKDMKAIEDDLMKTEDEY 416
Cdd:pfam02463 317 KESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEeeleklqekLEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 417 ETLERRYANERDKAQFLSQELEHAKMELAKYKLAEKTESSHEQWLFRR--------LQEEEAKSGHLSREVDALKEKIHE 488
Cdd:pfam02463 397 LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGklteekeeLEKQELKLLKDELELKKSEDLLKE 476
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 295424124 489 YMATEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLR 542
Cdd:pfam02463 477 TQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGR 530
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
51-272 |
1.31e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.86 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 51 LEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQD-IKDKINKGEYGNSGIM 129
Cdd:PHA02562 179 LNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDeLLNLVMDIEDPSAALN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 130 DEVDELRKRVLDMEGKDEElIKMEE----------QCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQ 199
Cdd:PHA02562 259 KLNTAAAKIKSKIEQFQKV-IKMYEkggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSK 337
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295424124 200 ECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAiESRLEKTEI-TLKDDLTKL---KTLTVMLVDERKTMSEKLK 272
Cdd:PHA02562 338 KLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA-EFVDNAEELaKLQDELDKIvktKSELVKEKYHRGIVTDLLK 413
|
|
| DUF4407 |
pfam14362 |
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ... |
52-193 |
2.10e-05 |
|
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 597 amino acids in length. There is a single completely conserved residue R that may be functionally important.
Pssm-ID: 464151 [Multi-domain] Cd Length: 295 Bit Score: 47.25 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 52 EKELQTQTTEFHQN-QDKIMAKLTNE-DSQNRQLRQKLAALSRQIDELE-ETNRSLRKAEEEL-QDIKDKINKGEYGNSG 127
Cdd:pfam14362 105 EKEIDRELLEIQQEeADAAKAQLAAAyRARLAELEAQIAALDAEIDAAEaRLDALQAEARCELdGTPGTGTGVPGDGPVA 184
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295424124 128 --IMDEVDELRKRVLDMEGK-DEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDA 193
Cdd:pfam14362 185 ktKQAQLDAAQAELAALQAQnDARLAALRAELARLTAERAAARARSQAAIDGDDGLLARLEALNRLTTE 253
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
192-527 |
2.43e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 192 DALDKSKQecyslkcNLEKEKMTTKQLSEELESLNAR---IKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMS 268
Cdd:PRK11281 46 DALNKQKL-------LEAEDKLVQQDLEQTLALLDKIdrqKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 269 EK--LKQTEDKLQSTTSQLQAEQNKVTTVTEKLIeetkrALKSKTD-AEEKMYSVTKERDDLRNKLKAEEEKGHDLL-SK 344
Cdd:PRK11281 119 STlsLRQLESRLAQTLDQLQNAQNDLAEYNSQLV-----SLQTQPErAQAALYANSQRLQQIRNLLKGGKVGGKALRpSQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 345 VTILKNRLQSLEAiekdfvKNKLNQDSSKSTAALhQE---------NNKIKELSQEVENLKLKLKDMKAIEDDlmKTEDE 415
Cdd:PRK11281 194 RVLLQAEQALLNA------QNDLQRKSLEGNTQL-QDllqkqrdylTARIQRLEHQLQLLQEAINSKRLTLSE--KTVQE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 416 YETLERryANERDKAQFLSQELEHAKmELAKYkLAEKTESSHE---------QWLFRRLQEEEaksghlsrevdALKEKI 486
Cdd:PRK11281 265 AQSQDE--AARIQANPLVAQELEINL-QLSQR-LLKATEKLNTltqqnlrvkNWLDRLTQSER-----------NIKEQI 329
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 295424124 487 HEymatedlichLQGdhSL-LQKKLNQQENR------NRDLGREIENL 527
Cdd:PRK11281 330 SV----------LKG--SLlLSRILYQQQQAlpsadlIEGLADRIADL 365
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
159-411 |
2.91e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 159 LNKRLEKE-TVQSKDFKLEVDKLSVRITALEKLEDALDK-SKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEaie 236
Cdd:PHA02562 171 LNKDKIRElNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKkNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLV--- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 237 srleKTEITLKDDLTKLKTLTVMLVDERKTMS--EKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRaLKSKTDAE 314
Cdd:PHA02562 248 ----MDIEDPSAALNKLNTAAAKIKSKIEQFQkvIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHS-LEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 315 EKMYSVTKERDDLRNKLkaeeekgHDLLSKVTILKNRLQSLEAIEKDFVK--NKLNQDSSKSTAALHQENNKIKELSQEV 392
Cdd:PHA02562 323 DELEEIMDEFNEQSKKL-------LELKNKISTNKQSLITLVDKAKKVKAaiEELQAEFVDNAEELAKLQDELDKIVKTK 395
|
250
....*....|....*....
gi 295424124 393 ENLKLKlKDMKAIEDDLMK 411
Cdd:PHA02562 396 SELVKE-KYHRGIVTDLLK 413
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
352-556 |
3.08e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 352 LQSLEAIEKDFVKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQ 431
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 432 FLSQELEHAKMELAKYKLAEKTESSHEQWlfRRLQEEEAKSGHLSREVDALKEKIHEY------------MATEDLICHL 499
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERL--EELEERLEELRELEEELEELEAELAELqeeleelleqlsLATEEELQDL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 295424124 500 QGDHSLLQKKLNQQENRNRDLGREIENLTKELERYrhfSKSLRPSLNERRISDPQVF 556
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQL---ENELEAAALEERLKEARLL 251
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
10-608 |
3.71e-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: 47.66 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 10 TAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQnqdKIMAKLTNEDSQNRQLRQKLAA 89
Cdd:pfam02463 178 LIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL---KLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 90 LSRQIDELEET--NRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGKDEELIKMEEQcrdlNKRLEKET 167
Cdd:pfam02463 255 SSKQEIEKEEEklAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE----KKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 168 VQSKDFKLEvdklsvritaLEKLEDALDKSKQECYSLKCNLEKEKmttkqlseelesLNARIKELEAIESRLEKTEITLK 247
Cdd:pfam02463 331 KKEKEEIEE----------LEKELKELEIKREAEEEEEEELEKLQ------------EKLEQLEEELLAKKKLESERLSS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 248 DDLTKLKTLTVMLVDERKtmSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAE--------EKMYS 319
Cdd:pfam02463 389 AAKLKEEELELKSEEEKE--AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELekqelkllKDELE 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 320 VTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQENNKIKelsQEVENLKLKL 399
Cdd:pfam02463 467 LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD---LGVAVENYKV 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 400 KDMKAIEDDLMKTEDEYETLERRYANERDKAQF---LSQELEHAKMELAKYKLAEKTESSHEQWLFRRLQE--EEAKSGH 474
Cdd:pfam02463 544 AISTAVIVEVSATADEVEERQKLVRALTELPLGarkLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEadEDDKRAK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 475 LSREVDALKEKIHEYMATEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSLNERRISDPQ 554
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 295424124 555 VFSKEVQTEAADSEPPDYKSLIPLERAVINGQFYEENEDQDDDPNEEESVLSFR 608
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL 757
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
291-533 |
3.96e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 291 KVTTVTEKLIEETKRALKSKTDAEEkmysvtkeRDDLRNKLkaEEEKGHDLLSKVTILknrLQSLEAIEKDFvkNKLNQD 370
Cdd:TIGR02169 188 RLDLIIDEKRQQLERLRREREKAER--------YQALLKEK--REYEGYELLKEKEAL---ERQKEAIERQL--ASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 371 SSKSTAALHQENNKIKELSQEVENLKLKLKDMKaiEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKLA 450
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLG--EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 451 -EKTESSHEQwLFRRLQEEEAKSGHLSREVDALKEkihEYMATEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTK 529
Cdd:TIGR02169 331 iDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKE---ELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
....
gi 295424124 530 ELER 533
Cdd:TIGR02169 407 ELDR 410
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
90-547 |
4.18e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 90 LSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGKDEELIKMEEQCRDLNKRLEKETVQ 169
Cdd:PRK01156 192 LKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEK 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 170 SKDFKlEVDKLSVRITaleklEDALDKSKQEC---YSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITL 246
Cdd:PRK01156 272 NNYYK-ELEERHMKII-----NDPVYKNRNYIndyFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 247 KDdltklktltvmlVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDD 326
Cdd:PRK01156 346 SR------------YDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 327 LRNKLKAEEEKGHDLLSKVTILKNRLQSLE-------------AIEKDFVKNKLNQDSSKSTAALHQENNKIKELSQEVE 393
Cdd:PRK01156 414 INVKLQDISSKVSSLNQRIRALRENLDELSrnmemlngqsvcpVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVK 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 394 NLKLKLKDMKAIEDDLMKTEdeyetlERRYANERDKAQFLSQELEHAKMELAKYKLAEktessheqwlfrrLQEEEAKSG 473
Cdd:PRK01156 494 DIDEKIVDLKKRKEYLESEE------INKSINEYNKIESARADLEDIKIKINELKDKH-------------DKYEEIKNR 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 474 HLSREVDALKEKIHEY---MATEDLIC--HLQGDHSLLQKKLNQQENRNRDLGREIENLT----KELERYRHFSKSLRPS 544
Cdd:PRK01156 555 YKSLKLEDLDSKRTSWlnaLAVISLIDieTNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsyidKSIREIENEANNLNNK 634
|
...
gi 295424124 545 LNE 547
Cdd:PRK01156 635 YNE 637
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2-552 |
6.23e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 2 VVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFhQNQDKIMAKLTNEDSQNR 81
Cdd:PRK01156 174 VIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDY-NNLKSALNELSSLEDMKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 82 QLRQKLAALSRQIDELEETNRSLRKAEEELQDIkdkINKGEYGNSGIMDEVDELRKRVLD----MEGKDEELIKMEEQCR 157
Cdd:PRK01156 253 RYESEIKTAESDLSMELEKNNYYKELEERHMKI---INDPVYKNRNYINDYFKYKNDIENkkqiLSNIDAEINKYHAIIK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 158 DLNKrLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEEL-ESLNARIKELEAIE 236
Cdd:PRK01156 330 KLSV-LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFIsEILKIQEIDPDAIK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 237 SRLEKTEITLKDDLTKLKTLTVMLvderktmsEKLKQTEDKLQSTTSQLQAeQNKVTTVTEKLIEETKRALKSktDAEEK 316
Cdd:PRK01156 409 KELNEINVKLQDISSKVSSLNQRI--------RALRENLDELSRNMEMLNG-QSVCPVCGTTLGEEKSNHIIN--HYNEK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 317 MYSVTKERDDLRNKLKAEEEKGHDLLSkvtiLKNRLQSlEAIEKDFVKNKLNQDSSKSTAALHQENNKIKELSQEVENLK 396
Cdd:PRK01156 478 KSRLEEKIREIEIEVKDIDEKIVDLKK----RKEYLES-EEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIK 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 397 LKLKDMKaIEDDLMKTEDEYETLERRYA----NERDKAQFLSQELEHAKMELAKYKLAEKTESSHEQWLFRRLQEE---- 468
Cdd:PRK01156 553 NRYKSLK-LEDLDSKRTSWLNALAVISLidieTNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEannl 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 469 ---EAKSGHLSREVDALKEKIHEYMATEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSL 545
Cdd:PRK01156 632 nnkYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRI 711
|
....*....
gi 295424124 546 NE--RRISD 552
Cdd:PRK01156 712 NElsDRIND 720
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
330-535 |
6.51e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 330 KLKAEEEKgHDLLSKVTILKNRLQSLEAIEKDfvKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAiedDL 409
Cdd:COG1196 217 ELKEELKE-LEAELLLLKLRELEAELEELEAE--LEELEAELEELEAELAELEAELEELRLELEELELELEEAQA---EE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 410 MKTEDEYETLERRYANERDKAQFLSQELEHAKMELA----KYKLAEKTESSHEQWLFRRLQEEEAKSGHLSREVDALKEK 485
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAeleeELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 295424124 486 IHEYMATEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTKELERYR 535
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
7-163 |
7.07e-05 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 46.77 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 7 QRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMA---KLTNEDSQNRQL 83
Cdd:COG5283 10 KPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQagiDTRQLSAAQRRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 84 RQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINK-GEYGNSGI-------------MDEVDELR--KRVLDMEGKDE 147
Cdd:COG5283 90 RSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQRlAGAGAAAAaigaalaasvkpaIDFEDAMAdvAATVDLDKSSE 169
|
170
....*....|....*.
gi 295424124 148 ELIKMEEQCRDLNKRL 163
Cdd:COG5283 170 QFKALGKQARELSAQT 185
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
77-291 |
7.43e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 77 DSQNRQLRQKLAALSRQIDELEETnrsLRKAEEELQDIKDKINKGEygnsgimDEVDELRKRvldMEGKDEELIKMEEQC 156
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAE---LDALQAELEELNEEYNELQ-------AELEALQAE---IDKLQAEIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 157 RDLNKRLEKETVQSKDFKLEVDKLSV------------RITALEKLEDALDKSKQECYSLKCNLEKEKmttKQLSEELES 224
Cdd:COG3883 82 EERREELGERARALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKK---AELEAKLAE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295424124 225 LNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNK 291
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1-464 |
7.57e-05 |
|
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: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 1 MVVDEQQRLTAQLALQRQKIQALTTSAK-ETQGKLALAEARAQ---EEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNE 76
Cdd:pfam15921 412 ITIDHLRRELDDRNMEVQRLEALLKAMKsECQGQMERQMAAIQgknESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 77 DSQNRQLRQKLAALSRQIDELEETNRSLRK----AEEELQDIKDKINKGEYGNSgIMDEVDELRkrvLDMEGKDEELIKM 152
Cdd:pfam15921 492 ESSERTVSDLTASLQEKERAIEATNAEITKlrsrVDLKLQELQHLKNEGDHLRN-VQTECEALK---LQMAEKDKVIEIL 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 153 EEQCRDLNK-----------------RLEKET----VQSKDFKLEVDKLSVRITALE----------------------- 188
Cdd:pfam15921 568 RQQIENMTQlvgqhgrtagamqvekaQLEKEIndrrLELQEFKILKDKKDAKIRELEarvsdlelekvklvnagserlra 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 189 ---------KLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIK-ELEAIESRLEKTEITLKD---------- 248
Cdd:pfam15921 648 vkdikqerdQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKmQLKSAQSELEQTRNTLKSmegsdghamk 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 249 -DLTKLKTLT------------VMLVDERKTMSEK----LKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKT 311
Cdd:pfam15921 728 vAMGMQKQITakrgqidalqskIQFLEEAMTNANKekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVA 807
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 312 DAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDFVKNKL-----------NQDSSKSTAA-LH 379
Cdd:pfam15921 808 NMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQGPGYTSNSSMKPRLlqpasftrthsNVPSSQSTASfLS 887
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 380 QENNKIKELSQE-VENLKLKLKDMKAI-----EDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKLaeKT 453
Cdd:pfam15921 888 HHSRKTNALKEDpTRDLKQLLQELRSVineepTVQLSKAEDKGRAPSLGALDDRVRDCIIESSLRSDICHSSSNSL--QT 965
|
570
....*....|.
gi 295424124 454 ESSHEQWLFRR 464
Cdd:pfam15921 966 EGSKSSETCSR 976
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
4-309 |
9.79e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.48 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 4 DEQQRLTAQ--LALQ-RQKIQALttsaKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKimakLTNEDSQN 80
Cdd:COG3096 400 DYQQALDVQqtRAIQyQQAVQAL----EKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQK----LSVADAAR 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 81 RQLRQKLAALSRQIDELEeTNRSLRKAEEELQDIKDKINkgeygnsgIMDEVDELRKRVLDMEGKDEELIKMEEQCRDLN 160
Cdd:COG3096 472 RQFEKAYELVCKIAGEVE-RSQAWQTARELLRRYRSQQA--------LAQRLQQLRAQLAELEQRLRQQQNAERLLEEFC 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 161 KRLEKEtVQSKDfklevdklsvritALEKLEDALDKSKQECYSLKCNLEKEKMTTKQlseELESLNARIKELEAIESRLe 240
Cdd:COG3096 543 QRIGQQ-LDAAE-------------ELEELLAELEAQLEELEEQAAEAVEQRSELRQ---QLEQLRARIKELAARAPAW- 604
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295424124 241 kteITLKDDLTKLktltvmlvderktmSEKLKQTEDKLQSTTSQLQ--AEQNKVTTVTEKLIEETKRALKS 309
Cdd:COG3096 605 ---LAAQDALERL--------------REQSGEALADSQEVTAAMQqlLEREREATVERDELAARKQALES 658
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
4-189 |
1.03e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 4 DEQQRLTAQLALQRQKIQALTTSAKETqgKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKImakltneDSQNRQL 83
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEARLDALREEL-------DELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 84 RQ----KLAALSRQIDELEETnrsLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVldmegkDEELIKMEEQCRDL 159
Cdd:COG4913 333 RGnggdRLEQLEREIERLERE---LEERERRRARLEALLAALGLPLPASAEEFAALRAEA------AALLEALEEELEAL 403
|
170 180 190
....*....|....*....|....*....|
gi 295424124 160 NKRLEKETVQSKDFKLEVDKLSVRITALEK 189
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-233 |
1.04e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 3 VDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQD-------KIMAKLTN 75
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnlngkkeELEEELEE 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 76 EDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQdikdkinkgeygnsgimDEVDELRKRVLDMEGKDEELIKMEEQ 155
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELE-----------------AQIEKKRKRLSELKAKLEALEEELSE 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 156 CRDLNKRLE---KETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTtkqLSEELESLNARIKEL 232
Cdd:TIGR02169 936 IEDPKGEDEeipEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAK---LEEERKAILERIEEY 1012
|
.
gi 295424124 233 E 233
Cdd:TIGR02169 1013 E 1013
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
54-406 |
1.26e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 54 ELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNR----SLRKAEEELQDIKDkinkgEYGN--SG 127
Cdd:PRK01156 406 AIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcGTTLGEEKSNHIIN-----HYNEkkSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 128 IMDEVDELRKRVLDMEGKDEELIKMEEQCRDLN-KRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKC 206
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEiNKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKL 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 207 NLEKEKMTtkqlseELESLNARIK--ELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQ 284
Cdd:PRK01156 561 EDLDSKRT------SWLNALAVISliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNK 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 285 LqaeqnkvttvteKLIEETKRA---LKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVtilknrlqsleaiEKD 361
Cdd:PRK01156 635 Y------------NEIQENKILiekLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKS-------------RKA 689
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 295424124 362 FVKNKLNQDSSKSTAALHQENNKikELSQEVENLKLKLKDMKAIE 406
Cdd:PRK01156 690 LDDAKANRARLESTIEILRTRIN--ELSDRINDINETLESMKKIK 732
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
21-471 |
1.48e-04 |
|
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: 45.81 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 21 QALTTSAKETQGKLALAEaRAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKL----AALSRQIDE 96
Cdd:TIGR00606 667 QFITQLTDENQSCCPVCQ-RVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLApgrqSIIDLKEKE 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 97 LEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEvDELRKRVLDMEGKDEELikmEEQCRDLNKRLEKETVQSKDFKLE 176
Cdd:TIGR00606 746 IPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE-EESAKVCLTDVTIMERF---QMELKDVERKIAQQAAKLQGSDLD 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 177 VDKLSVRITALEKLEDaLDKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTL 256
Cdd:TIGR00606 822 RTVQQVNQEKQEKQHE-LDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSL 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 257 TVMLVDERKTMSeKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKlkaeeE 336
Cdd:TIGR00606 901 IREIKDAKEQDS-PLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLK-----Q 974
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 337 KGHDLLSKVTILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQEN-------NKIKELSQEVENLKLKLKDMKAIE--D 407
Cdd:TIGR00606 975 KETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNltlrkreNELKEVEEELKQHLKEMGQMQVLQmkQ 1054
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 295424124 408 DLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKLAEKTESSHEQWLFRRLQEEEAK 471
Cdd:TIGR00606 1055 EHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNK 1118
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
77-242 |
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: 44.15 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 77 DSQNRQLRQKLAALSRQIDELEET----NRSLRKAEEELQDIKDKINKGEygnsgimDEVDELRKRVLDMEGKDEELIKM 152
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDElaalEARLEAAKTELEDLEKEIKRLE-------LEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 153 EEQcRDLNKRLEKEtvqskdfKLEVDKLSVRI----TALEKLEDALDKSKQECYSLKCNLEKEKmttKQLSEELESLNAR 228
Cdd:COG1579 89 KEY-EALQKEIESL-------KRRISDLEDEIlelmERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAE 157
|
170
....*....|....
gi 295424124 229 IKELEAIESRLEKT 242
Cdd:COG1579 158 LEELEAEREELAAK 171
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
68-460 |
1.55e-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: 45.81 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 68 KIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEE-LQDIKDKINKGEY-----GNSGIMDEVDELRKRVLD 141
Cdd:TIGR01612 483 KDIDENSKQDNTVKLILMRMKDFKDIIDFMELYKPDEVPSKNIiGFDIDQNIKAKLYkeieaGLKESYELAKNWKKLIHE 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 142 ----MEGKDEELIKMEEQCRDL-NKRLE--KETVQSKDFKLEVDklsvritalEKLEDALDKSK--QECYSLKCNLEKE- 211
Cdd:TIGR01612 563 ikkeLEEENEDSIHLEKEIKDLfDKYLEidDEIIYINKLKLELK---------EKIKNISDKNEyiKKAIDLKKIIENNn 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 212 -------KMTTKQLSEELESLNariKELEAIESRLEKTeitLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQ 284
Cdd:TIGR01612 634 ayidelaKISPYQVPEHLKNKD---KIYSTIKSELSKI---YEDDIDALYNELSSIVKENAIDNTEDKAKLDDLKSKIDK 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 285 LQAEQNKVTTVTEKL----IEETKRALkSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNrlqslEAIEK 360
Cdd:TIGR01612 708 EYDKIQNMETATVELhlsnIENKKNEL-LDIIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAK-----EKDEL 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 361 DFVKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKaqFLSQELEHa 440
Cdd:TIGR01612 782 NKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDK--FINFENNC- 858
|
410 420
....*....|....*....|
gi 295424124 441 kmelakyklAEKTESSHEQW 460
Cdd:TIGR01612 859 ---------KEKIDSEHEQF 869
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
40-459 |
1.97e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 45.00 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 40 RAQEEEQK-ATRLEKELQTQTTEFHQNQDKimakltNEDSQNRQLRQKLAALSRQIdeLEETNRSLRKAEEEL-QDIKDK 117
Cdd:NF033838 51 SGNESQKEhAKEVESHLEKILSEIQKSLDK------RKHTQNVALNKKLSDIKTEY--LYELNVLKEKSEAELtSKTKKE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 118 INKGeygNSGIMDEVDELRKRVLDMEGKDEELIKMEEQCRDLNKRlEKETVQSKDFKLEVDKLSVRITalekledaldKS 197
Cdd:NF033838 123 LDAA---FEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRR-NYPTNTYKTLELEIAESDVEVK----------KA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 198 KQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDL-TKLKTLTVMLVD--ERKTMSEKLKQ- 273
Cdd:NF033838 189 ELELVKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRAdAKLKEAVEKNVAtsEQDKPKRRAKRg 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 274 ------TEDKlqsttSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKerddlrnklKAEEEKGHDLLSKVTI 347
Cdd:NF033838 269 vlgepaTPDK-----KENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKK---------KAKDQKEEDRRNYPTN 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 348 LKNRLQsLEAIEKDFVKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEyetlERRYANER 427
Cdd:NF033838 335 TYKTLE-LEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEE----AKRKAAEE 409
|
410 420 430
....*....|....*....|....*....|..
gi 295424124 428 DKAQFLSQELEHAKMELAKYKLAEKTESSHEQ 459
Cdd:NF033838 410 DKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQ 441
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
4-299 |
2.05e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 45.28 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 4 DEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQ- 82
Cdd:pfam15964 325 EAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGAt 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 83 ---LRQKLAALSRQIDELEETNRSLRKAEEELQ---------------DIKDKINKGEYGNSGIMDEVDELRKRVL-DME 143
Cdd:pfam15964 405 mlaLSQNVAQLEAQVEKVTREKNSLVSQLEEAQkqlasqemdvtkvcgEMRYQLNQTKMKKDEAEKEHREYRTKTGrQLE 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 144 GKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSvriTALEKLEDALDKSKQECYSLKCNLEKE-KMTTKQLSEEL 222
Cdd:pfam15964 485 IKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLT---ELLGESEHQLHLTRLEKESIQQSFSNEaKAQALQAQQRE 561
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295424124 223 ESLNARIKELEAiesRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKL 299
Cdd:pfam15964 562 QELTQKMQQMEA---QHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQKSRSEVEQLSQEKEYLQDRLEKL 635
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
29-187 |
2.14e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 29 ETQGKLALAEARaQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAE 108
Cdd:PRK12704 52 EAIKKEALLEAK-EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 109 EELQDIKDKINKGEYGNSGImdEVDELRKRVLDmegkdeeliKMEEQCRD----LNKRLEKETvqskdfKLEVDKLSVRI 184
Cdd:PRK12704 131 EELEELIEEQLQELERISGL--TAEEAKEILLE---------KVEEEARHeaavLIKEIEEEA------KEEADKKAKEI 193
|
...
gi 295424124 185 TAL 187
Cdd:PRK12704 194 LAQ 196
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
35-254 |
2.99e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 35 ALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKltneDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDI 114
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEEL----NEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 115 KDKINKGEYGNSGIMDEVDELrkrvldMEGKDEElikmeeqcrDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDAL 194
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVL------LGSESFS---------DFLDRLSALSKIADADADLLEELKADKAELEAKKAEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 195 DKSKQECYSLKcnlekekmttKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLK 254
Cdd:COG3883 153 EAKLAELEALK----------AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
5-115 |
3.14e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 5 EQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLtneDSQNRQLR 84
Cdd:COG3206 250 GSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASL---EAELEALQ 326
|
90 100 110
....*....|....*....|....*....|.
gi 295424124 85 QKLAALSRQIDELEETNRSLRKAEEELQDIK 115
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAELRRLE 357
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2-103 |
3.30e-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: 43.98 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 2 VVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNR 81
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
90 100
....*....|....*....|..
gi 295424124 82 QLRQKLAALSRQIDELEETNRS 103
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPA 245
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
4-250 |
3.42e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 4 DEQQRLTAQ--LALQ-RQKIQALTtSAKETQGKLAL---------AEARAQEEEQKATRLEKELQTQTTEFHQNQ----- 66
Cdd:PRK04863 401 DYQQALDVQqtRAIQyQQAVQALE-RAKQLCGLPDLtadnaedwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQfeqay 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 67 ---DKIMAKLTNEDSQN------------RQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNsgimDE 131
Cdd:PRK04863 480 qlvRKIAGEVSRSEAWDvarellrrlreqRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE----DE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 132 VDELRkrvldmEGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRIT-------ALEKLED---ALDKSKQEC 201
Cdd:PRK04863 556 LEQLQ------EELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPawlaaqdALARLREqsgEEFEDSQDV 629
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 295424124 202 YSLKCN-LEKEKMTTK---QLSEELESLNARIKELEAIESRLEKTEITLKDDL 250
Cdd:PRK04863 630 TEYMQQlLERERELTVerdELAARKQALDEEIERLSQPGGSEDPRLNALAERF 682
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
4-535 |
3.63e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 4 DEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEE--------EQKATRLEKELQTQTTEFHQNQDKI-MAKLT 74
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLaALGLP 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 75 NEDS------QNRQLRQKLAALSRQIDELE----ETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEG 144
Cdd:COG4913 375 LPASaeefaaLRAEAAALLEALEEELEALEealaEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALG 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 145 KDE-------ELIKMEEQCRDLNKRLEK--------------------ETVQSKDFKLEVDKLSVRITALEKLEDALDKS 197
Cdd:COG4913 455 LDEaelpfvgELIEVRPEEERWRGAIERvlggfaltllvppehyaaalRWVNRLHLRGRLVYERVRTGLPDPERPRLDPD 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 198 kqecyslkcnlekekmttkQLSEELEslnarIKELEA---IESRLEKTeitlkddltklktLTVMLVDErktmSEKLKQT 274
Cdd:COG4913 535 -------------------SLAGKLD-----FKPHPFrawLEAELGRR-------------FDYVCVDS----PEELRRH 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 275 EdklQSTTSQLQAEQNKvtTVTEKlieETKRALKSK----TDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKN 350
Cdd:COG4913 574 P---RAITRAGQVKGNG--TRHEK---DDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQE 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 351 RLQSLEAIEKDfvknklnQDSSKSTAALHQEnnkIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKA 430
Cdd:COG4913 646 RREALQRLAEY-------SWDEIDVASAERE---IAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEI 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 431 QFLSQELEHAKMELAKYK-LAEKTESSHEQWLFRRLQE----------EEAKSGHLSREVDALKEKIHEymATEDLIchl 499
Cdd:COG4913 716 GRLEKELEQAEEELDELQdRLEAAEDLARLELRALLEErfaaalgdavERELRENLEERIDALRARLNR--AEEELE--- 790
|
570 580 590
....*....|....*....|....*....|....*.
gi 295424124 500 qgdhSLLQKKLNQQENRNRDLGREIENLTKELERYR 535
Cdd:COG4913 791 ----RAMRAFNREWPAETADLDADLESLPEYLALLD 822
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
76-312 |
3.76e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 76 EDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKinKGEYGNSGIMDEVDELRKRVLDMEGKDEELIKMEEQ 155
Cdd:PRK05771 41 SNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVK--SLEELIKDVEEELEKIEKEIKELEEEISELENEIKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 156 CRDLNKRLEKetvqSKDFKLEVDKL-----------SVRITALEKLEDALDKSKQECYS--------------------- 203
Cdd:PRK05771 119 LEQEIERLEP----WGNFDLDLSLLlgfkyvsvfvgTVPEDKLEELKLESDVENVEYIStdkgyvyvvvvvlkelsdeve 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 204 ---LKCNLEKEKM-TTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVD---ERKTMSEKLKQTEd 276
Cdd:PRK05771 195 eelKKLGFERLELeEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEielERAEALSKFLKTD- 273
|
250 260 270
....*....|....*....|....*....|....*.
gi 295424124 277 klqsTTSQLQAeqnkvtTVTEKLIEETKRALKSKTD 312
Cdd:PRK05771 274 ----KTFAIEG------WVPEDRVKKLKELIDKATG 299
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
104-253 |
3.85e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 104 LRKAEEELQDIKDKINKgeygnsgimdEVDELRKRVLdMEGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVR 183
Cdd:PRK12704 33 IKEAEEEAKRILEEAKK----------EAEAIKKEAL-LEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295424124 184 ITALEKLEDALDKSKQECYSLKCNLEK-----EKMTTKQLsEELESLNARIKElEAIESRLEKTEITLKDDLTKL 253
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKkeeelEELIEEQL-QELERISGLTAE-EAKEILLEKVEEEARHEAAVL 174
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
33-446 |
4.11e-04 |
|
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: 44.04 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 33 KLALAEARAQEEEQKATRLEKELQTQTTEFHQNQdkimaKLTNEDSQNRQLRQKLAALSRQIDELEetnRSLRKAEEELQ 112
Cdd:pfam10174 186 RIAEAEMQLGHLEVLLDQKEKENIHLREELHRRN-----QLQPDPAKTKALQTVIEMKDTKISSLE---RNIRDLEDEVQ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 113 DIKDKINKGEYGNSGIMDEVDELRKRVLDMEGK----DEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALE 188
Cdd:pfam10174 258 MLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKidqlKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 189 KLEDALdksKQECYSLKCNL-EKEKM---TTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDER 264
Cdd:pfam10174 338 QRAAIL---QTEVDALRLRLeEKESFlnkKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKD 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 265 KTMSEkLKQTEDKLQSTTSQlqaEQNKVTTVTEKLIEETK--RALKSKTDAEEKMYsvTKERDDLRNKLKaeeekghDLL 342
Cdd:pfam10174 415 KQLAG-LKERVKSLQTDSSN---TDTALTTLEEALSEKERiiERLKEQREREDRER--LEELESLKKENK-------DLK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 343 SKVTILKNRLQSLEAIEKDFVKNKLNQDSSKStaalhQENNKIKELSQEVENlklKLKDMKAIEDDLMKTEdEYETLERR 422
Cdd:pfam10174 482 EKVSALQPELTEKESSLIDLKEHASSLASSGL-----KKDSKLKSLEIAVEQ---KKEECSKLENQLKKAH-NAEEAVRT 552
|
410 420
....*....|....*....|....
gi 295424124 423 YANERDKAQFLSQELEHAKMELAK 446
Cdd:pfam10174 553 NPEINDRIRLLEQEVARYKEESGK 576
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-169 |
4.18e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 1 MVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQtqtTEFHQNQDKIMAKLTNEDSQN 80
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERL---EEELEEEALEEQLEAEREELL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 81 RQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGKDEELIKMEEQCRDLN 160
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAI 818
|
....*....
gi 295424124 161 KRLEKETVQ 169
Cdd:COG1196 819 EEIDRETRE 827
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
90-247 |
4.95e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 90 LSRQIDELEETNR---SLRKAEEELQDIKDKINKGEygnsgimDEVDELRKRVLDMEGKDEELikmEEQCRDLNKRLEKE 166
Cdd:PRK03918 590 LEERLKELEPFYNeylELKDAEKELEREEKELKKLE-------EELDKAFEELAETEKRLEEL---RKELEELEKKYSEE 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 167 TVQSKDFKLEvdKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITL 246
Cdd:PRK03918 660 EYEELREEYL--ELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALL 737
|
.
gi 295424124 247 K 247
Cdd:PRK03918 738 K 738
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
131-317 |
5.51e-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: 42.60 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 131 EVDELRKRVLDMEgkdEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSvriTALEKLEDALDKSKqecyslkcnlek 210
Cdd:COG1579 18 ELDRLEHRLKELP---AELAELEDELAALEARLEAAKTELEDLEKEIKRLE---LEIEEVEARIKKYE------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 211 EKMTTKQLSEELESLNariKELEAIESRLEKTEITLKDdltklktltvmLVDERKTMSEKLKQTEDKLQSTTSQLQAEQN 290
Cdd:COG1579 80 EQLGNVRNNKEYEALQ---KEIESLKRRISDLEDEILE-----------LMERIEELEEELAELEAELAELEAELEEKKA 145
|
170 180
....*....|....*....|....*..
gi 295424124 291 KVTTVTEKLIEETKRALKSKTDAEEKM 317
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAKI 172
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
4-155 |
5.51e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 4 DEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLE-----KELQTQTTEFHQNQDKIMAKLTNEDS 78
Cdd:COG3206 212 EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLqspviQQLRAQLAELEAELAELSARYTPNHP 291
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295424124 79 QNRQLRQKLAALSRQIDelEETNRSLRKAEEELQDIKDKINKgeygnsgIMDEVDELRKRVLDMEGKDEELIKMEEQ 155
Cdd:COG3206 292 DVIALRAQIAALRAQLQ--QEAQRILASLEAELEALQAREAS-------LQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
55-564 |
5.81e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 55 LQTQTTEFHQNQD-KIMAKLTNEDSQNRQLRQklaalsRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNsgimDEVD 133
Cdd:PTZ00121 1013 LTANTIDFNQNFNiEKIEELTEYGNNDDVLKE------KDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKD----FDFD 1082
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 134 ELRKRVLDmEGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDklSVRITALEKLEDAldkskqecyslkcnlekekm 213
Cdd:PTZ00121 1083 AKEDNRAD-EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAED--ARKAEEARKAEDA-------------------- 1139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 214 ttKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKtmSEKLKQTEDKLQSTTSQLQAEQNKVT 293
Cdd:PTZ00121 1140 --RKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRK--AEELRKAEDARKAEAARKAEEERKAE 1215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 294 TV----TEKLIEETKRALKSKTDAEEKMySVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDFVKNKLNQ 369
Cdd:PTZ00121 1216 EArkaeDAKKAEAVKKAEEAKKDAEEAK-KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADE 1294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 370 ----------DSSKSTAalhQENNKIKELSQEVENLKLKLKDMK------AIEDDLMKTEDEYETLERRYANERDKAQFL 433
Cdd:PTZ00121 1295 akkaeekkkaDEAKKKA---EEAKKADEAKKKAEEAKKKADAAKkkaeeaKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 434 SQELEHAKMELAKYKLAEKT---ESSHEQWLFRRLQEEEAKSGHLSREVDALKEKIHEYMATEDLichlqgDHSLLQKKL 510
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKkadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA------KKKAEEAKK 1445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 295424124 511 NQQENRNRDLGREIENLTKELERYRHFSKSLRPSLNERRISDPQVFSKEVQTEA 564
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
5-165 |
6.31e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.12 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 5 EQQRLTAQLALQRQKIQALTTSAKE--TQGKLALAEArAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLtnedsqnRQ 82
Cdd:COG1842 52 NQKRLERQLEELEAEAEKWEEKARLalEKGREDLARE-ALERKAELEAQAEALEAQLAQLEEQVEKLKEAL-------RQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 83 LRQKLAALSRQIDELeetnrslrKAEEELQDIKDKINK--GEYGNSGIMDEVDELRKRVLDMEGKDEELIKMEEQcRDLN 160
Cdd:COG1842 124 LESKLEELKAKKDTL--------KARAKAAKAQEKVNEalSGIDSDDATSALERMEEKIEEMEARAEAAAELAAG-DSLD 194
|
....*
gi 295424124 161 KRLEK 165
Cdd:COG1842 195 DELAE 199
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
6-292 |
7.13e-04 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 43.61 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 6 QQRLTAQ-LALQRQK--IQALTTSAKETQGKL-----ALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNED 77
Cdd:pfam18971 562 ENKLTAKgLSLQEANklIKDFLSSNKELAGKAlnfnkAVAEAKSTGNYDEVKKAQKDLEKSLRKREHLEKEVEKKLESKS 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 78 SQNRQLRQKLAALSrQIDEL-----EETNR---------SLRKAEEELQDIKDKINKGEYGNSGIMDEVDelrkrvldmE 143
Cdd:pfam18971 642 GNKNKMEAKAQANS-QKDEIfalinKEANRdaraiaytqNLKGIKRELSDKLEKISKDLKDFSKSFDEFK---------N 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 144 GKDEELIKMEEQCRDLNKRLeKETVQSKDFKLEVDKLSvriTALEKLEDALDKSKQECYSLKCNLE---KEKMTTKQLSE 220
Cdd:pfam18971 712 GKNKDFSKAEETLKALKGSV-KDLGINPEWISKVENLN---AALNEFKNGKNKDFSKVTQAKSDLEnsvKDVIINQKVTD 787
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295424124 221 ELESLNARIKELEAIE--SRLEKTeitlkddLTKLKTLTvmlvdeRKTMSEKLKQTEDKLQSTTSQL-QAEQNKV 292
Cdd:pfam18971 788 KVDNLNQAVSVAKAMGdfSRVEQV-------LADLKNFS------KEQLAQQAQKNEDFNTGKNSELyQSVKNSV 849
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
81-422 |
7.25e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 81 RQLRQKLAALSRQIDELEETNRSLRkaeEELQDIK--DKINKGEYGnsGIMDEVDELRKRVLD--------MEGKDEELI 150
Cdd:PRK04778 101 RKAKHEINEIESLLDLIEEDIEQIL---EELQELLesEEKNREEVE--QLKDLYRELRKSLLAnrfsfgpaLDELEKQLE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 151 KMEEQ---------------CRDLNKRLEKETVQSKDFKLEVDKLSVRITA-----LEKLEDALDKSKQECYSLK-CNLE 209
Cdd:PRK04778 176 NLEEEfsqfveltesgdyveAREILDQLEEELAALEQIMEEIPELLKELQTelpdqLQELKAGYRELVEEGYHLDhLDIE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 210 KEkmtTKQLSEELESLNARIKELE---------AIESRL-----------------EKTEITLKDDLTKLKTLTVMLVDE 263
Cdd:PRK04778 256 KE---IQDLKEQIDENLALLEELDldeaeekneEIQERIdqlydilerevkarkyvEKNSDTLPDFLEHAKEQNKELKEE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 264 RKTMSEKLKQTEDKLQsTTSQLQAEQNKVTTVTEKLIEEtkralkskTDAEEKMYSVTKER-DDLRNKLKAEEEKGHDll 342
Cdd:PRK04778 333 IDRVKQSYTLNESELE-SVRQLEKQLESLEKQYDEITER--------IAEQEIAYSELQEElEEILKQLEEIEKEQEK-- 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 343 skvtiLKNRLQSLEAIEKDfVKNKLNQ-DSSKSTAALHQEN------------------NKIKELSQEVENLKLklkDMK 403
Cdd:PRK04778 402 -----LSEMLQGLRKDELE-AREKLERyRNKLHEIKRYLEKsnlpglpedylemffevsDEIEALAEELEEKPI---NME 472
|
410
....*....|....*....
gi 295424124 404 AIEDDLMKTEDEYETLERR 422
Cdd:PRK04778 473 AVNRLLEEATEDVETLEEE 491
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
28-579 |
8.20e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 28 KETQGKLALAEARAQEEEQkatrLEKELQTQTTEFHQNQDKIMAKLTNEdsqNRQLRQKLAALSRQIDELEETNRSLRKA 107
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTL----CTPCMPDTYHERKQVLEKELKHLREA---LQQTQQSHAYLTQKREAQEEQLKKQQLL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 108 EEELQDIKDKINkgEYGNSGIMDEVDELRKRVLDMEGKDEELIKMEEQCRDLNKRL-EKETVQSKDFKLEVDKLSVRiTA 186
Cdd:TIGR00618 263 KQLRARIEELRA--QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELqSKMRSRAKLLMKRAAHVKQQ-SS 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 187 LEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELEsLNARIKELEAIESRLEKTEITLKDDLTKLKTLtVMLVDERKT 266
Cdd:TIGR00618 340 IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT-LTQHIHTLQQQKTTLTQKLQSLCKELDILQRE-QATIDTRTS 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 267 MSEKLKQtedKLQSTTSQLQAEQnKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERD----DLRNKLKAEEEKGhdll 342
Cdd:TIGR00618 418 AFRDLQG---QLAHAKKQQELQQ-RYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREqqlqTKEQIHLQETRKK---- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 343 skvTILKNRLQSLEAIEKDFvknklnqdsSKSTAALHQEnnkikelSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERR 422
Cdd:TIGR00618 490 ---AVVLARLLELQEEPCPL---------CGSCIHPNPA-------RQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQ 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 423 YANERDKAQFLSQELEHAKMELAkyKLAEKTESSHE-------------QWLFRRLQEEEAKSGHLSREVDALKEKIHEY 489
Cdd:TIGR00618 551 LTSERKQRASLKEQMQEIQQSFS--ILTQCDNRSKEdipnlqnitvrlqDLTEKLSEAEDMLACEQHALLRKLQPEQDLQ 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 490 mateDLICHLQGDHSLLQKKLNQqenrnrdLGREIENLTKELERYRHF-SKSLRPSLNERRISDPQVFSKEVQTEAADSE 568
Cdd:TIGR00618 629 ----DVRLHLQQCSQELALKLTA-------LHALQLTLTQERVREHALsIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697
|
570
....*....|.
gi 295424124 569 PPDYKSLIPLE 579
Cdd:TIGR00618 698 MLAQCQTLLRE 708
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
42-370 |
9.30e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 42.75 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 42 QEEEQKATRLEKELQT---QTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEEL---QDIK 115
Cdd:pfam05622 172 EEELKKANALRGQLETykrQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRETNEELrcaQLQQ 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 116 DKINKGEYGNSGIMDEVDELRKRVLDMEGKdEELIKMEEQcrdlNKRL-EKETVQSKDfklevdklsvRITALEKLedal 194
Cdd:pfam05622 252 AELSQADALLSPSSDPGDNLAAEIMPAEIR-EKLIRLQHE----NKMLrLGQEGSYRE----------RLTELQQL---- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 195 dkskqecyslkcnLEKEKMTTKQLSEELESLNARIKELEAiesRLEKTEITLKDDLTKLKTlTVMLVDERKTMSEKLKQT 274
Cdd:pfam05622 313 -------------LEDANRRKNELETQNRLANQRILELQQ---QVEELQKALQEQGSKAED-SSLLKQKLEEHLEKLHEA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 275 EDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTD----AEE--KMY-----SVTKERDDLRNKLKAEEekghdlls 343
Cdd:pfam05622 376 QSELQKKKEQIEELEPKQDSNLAQKIDELQEALRKKDEdmkaMEEryKKYvekakSVIKTLDPKQNPASPPE-------- 447
|
330 340 350
....*....|....*....|....*....|.
gi 295424124 344 kVTILKNRLQ----SLEAIEKDFVKNKLNQD 370
Cdd:pfam05622 448 -IQALKNQLLekdkKIEHLERDFEKSKLQRE 477
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7-533 |
9.46e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 7 QRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQK 86
Cdd:COG4913 341 EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 87 LAALSRQIDELEETNRSLrkaEEELQDIKDKINKgeygNSGImDEVD-----ELrkrvLDMEGKDEE------------- 148
Cdd:COG4913 421 LRELEAEIASLERRKSNI---PARLLALRDALAE----ALGL-DEAElpfvgEL----IEVRPEEERwrgaiervlggfa 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 149 --LIKMEEQCRDLNKRLEketvqSKDFKLEVDKLSVRITALEKLEDALDKSkqecySLkcnleKEKMTTKQ--LSEELES 224
Cdd:COG4913 489 ltLLVPPEHYAAALRWVN-----RLHLRGRLVYERVRTGLPDPERPRLDPD-----SL-----AGKLDFKPhpFRAWLEA 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 225 LNARIKELEAIES----RLEKTEITL------------KDDLTKLKTLTVMLVDER---KTMSEKLKQTEDKLQSTTSQL 285
Cdd:COG4913 554 ELGRRFDYVCVDSpeelRRHPRAITRagqvkgngtrheKDDRRRIRSRYVLGFDNRaklAALEAELAELEEELAEAEERL 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 286 QAEQNKVTTVTEKLieETKRALKSKTDAEEKMYSVTKERDDLRNKLkAEEEKGHDLLSKvtiLKNRLQSLEAIEKDFVKn 365
Cdd:COG4913 634 EALEAELDALQERR--EALQRLAEYSWDEIDVASAEREIAELEAEL-ERLDASSDDLAA---LEEQLEELEAELEELEE- 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 366 klnqdsskstaALHQENNKIKELSQEVENLKLKLKDMKAIEDDL--MKTEDEYETLERRYAN------ERDKAQFLSQEL 437
Cdd:COG4913 707 -----------ELDELKGEIGRLEKELEQAEEELDELQDRLEAAedLARLELRALLEERFAAalgdavERELRENLEERI 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 438 EHAKMELAkyKLAEKTESSHEQwlFRRLQEEEAksGHLSREVDALKE--KIHEYMATEDLICHlqgdhsllQKKLNQQEN 515
Cdd:COG4913 776 DALRARLN--RAEEELERAMRA--FNREWPAET--ADLDADLESLPEylALLDRLEEDGLPEY--------EERFKELLN 841
|
570
....*....|....*...
gi 295424124 516 RNrdLGREIENLTKELER 533
Cdd:COG4913 842 EN--SIEFVADLLSKLRR 857
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
16-541 |
1.04e-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: 42.85 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 16 QRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKE-------LQTQTTEFHQNQD-----------------KIMA 71
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEknalqeqLQAETELCAEAEEmrarlaarkqeleeilhELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 72 KLTNEDSQNRQL-------RQKLAALSRQIDELEETNRSLR----KAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVL 140
Cdd:pfam01576 83 RLEEEEERSQQLqnekkkmQQHIQDLEEQLDEEEAARQKLQlekvTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 141 DME---GKDEELIKM--------EEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITAL-----------EKLEDALDKSK 198
Cdd:pfam01576 163 EFTsnlAEEEEKAKSlsklknkhEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLqeqiaelqaqiAELRAQLAKKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 199 QECYSLKCNLEKEKMTTKQLSEELESLNARIKELE-------AIESRLEKTEITLKDDLTKLKTLTVMLVD--------- 262
Cdd:pfam01576 243 EELQAALARLEEETAQKNNALKKIRELEAQISELQedleserAARNKAEKQRRDLGEELEALKTELEDTLDttaaqqelr 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 263 -ERKTMSEKLKQT-EDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHD 340
Cdd:pfam01576 323 sKREQEVTELKKAlEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 341 LLSKVTILKNRLQSLEA--IEKDFVKNKLNQDSSKS-------TAALHQENNKIKELSQEVENLKLKLKDMK-------- 403
Cdd:pfam01576 403 SEHKRKKLEGQLQELQArlSESERQRAELAEKLSKLqselesvSSLLNEAEGKNIKLSKDVSSLESQLQDTQellqeetr 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 404 ---AIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKLAEKTESSHEQWLfrrlqeEEAKSgHLSREVD 480
Cdd:pfam01576 483 qklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEAL------EEGKK-RLQRELE 555
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295424124 481 ALKEKIHEYMATEDlichlqgdhsllqkKLNQQENRnrdLGREIENLTKELERYRHFSKSL 541
Cdd:pfam01576 556 ALTQQLEEKAAAYD--------------KLEKTKNR---LQQELDDLLVDLDHQRQLVSNL 599
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
160-500 |
1.21e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 160 NKRLEKETVQSKDFKLEVDKLSVRITA-LEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESL-------NARIKE 231
Cdd:pfam07888 54 NRQREKEKERYKRDREQWERQRRELESrVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALlaqraahEARIRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 232 LEAIESRLEKTEITLKDDLTKLKTLTVMLV-------DERKTMSEKLKQTEDKLQSTTSQLQ------AEQNKVTTVTEK 298
Cdd:pfam07888 134 LEEDIKTLTQRVLERETELERMKERAKKAGaqrkeeeAERKQLQAKLQQTEEELRSLSKEFQelrnslAQRDTQVLQLQD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 299 LIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEkghdllsKVTILKNRLQSLEAIEkdfvknklnqdsSKSTAAL 378
Cdd:pfam07888 214 TITTLTQKLTTAHRKEAENEALLEELRSLQERLNASER-------KVEGLGEELSSMAAQR------------DRTQAEL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 379 HQENNKIKELSQEVENLKLKLKDMKAieddlmKTEDEYETLERRYANERDKAQFLSQEL---------EHAKMELAKYKL 449
Cdd:pfam07888 275 HQARLQAAQLTLQLADASLALREGRA------RWAQERETLQQSAEADKDRIEKLSAELqrleerlqeERMEREKLEVEL 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 295424124 450 AEKTESSHEQW--LFRRLQEEEAKSGHLSREVDALKEKIHEYMateDLICHLQ 500
Cdd:pfam07888 349 GREKDCNRVQLseSRRELQELKASLRVAQKEKEQLQAEKQELL---EYIRQLE 398
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
44-180 |
1.22e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 44 EEQKATRLEKELQTQTTEFHQNQdkimAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQdikdkinkgey 123
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEE----RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLE----------- 447
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 295424124 124 gnsgimDEVDELRKRVLDMEGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKL 180
Cdd:COG2433 448 ------RELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
21-420 |
1.30e-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: 42.47 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 21 QALTTSAKETQGKLALAEARAQEEEQKATRLEKELQtqttefhqnqdKIMAKLTNEDSQNRQLRQKLAALSrqiDELEET 100
Cdd:pfam01576 380 QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQ-----------ELQARLSESERQRAELAEKLSKLQ---SELESV 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 101 NRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGKdeeLIKMEEQCRDLNKRLEKETVQSKDFKLEVDKL 180
Cdd:pfam01576 446 SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTR---LRQLEDERNSLQEQLEEEEEAKRNVERQLSTL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 181 SVRITALEKledaldksKQECYSLkcNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDltkLKTLTVML 260
Cdd:pfam01576 523 QAQLSDMKK--------KLEEDAG--TLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQE---LDDLLVDL 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 261 VDERKTMSeklkqTEDKLQSTTSQLQAEQNkvtTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEkghd 340
Cdd:pfam01576 590 DHQRQLVS-----NLEKKQKKFDQMLAEEK---AISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELER---- 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 341 llskvtilKNRLQSLEAieKDFVKNKlnQDSSKStaaLHQENNKIKELSQEVENLKLKLKDMkaiEDDLMKTEDEYETLE 420
Cdd:pfam01576 658 --------TNKQLRAEM--EDLVSSK--DDVGKN---VHELERSKRALEQQVEEMKTQLEEL---EDELQATEDAKLRLE 719
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
67-336 |
1.34e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 42.35 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 67 DKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELqdikdkinkgeygnSGIMDEVDELRKRVLDMEGKD 146
Cdd:pfam05911 562 SKEALDDQDTSSDSSELSEVLQQFSATCNDVLSGKADLEDFVLEL--------------SHILDWISNHCFSLLDVSSME 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 147 EELIKMEeqCRDLNKRLEKETVQSKDFKLEVDKLS--VRITALEKLEDALDKSKQ-ECYSLKCNLEKEKMTTKQLSEELE 223
Cdd:pfam05911 628 DEIKKHD--CIDKVTLSENKVAQVDNGCSEIDNLSsdPEIPSDGPLVSGSNDLKTeENKRLKEEFEQLKSEKENLEVELA 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 224 SLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEET 303
Cdd:pfam05911 706 SCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEAELNELRQKFEALEVELEEEK 785
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 295424124 304 K---RALKSKTDAEEKMYSVTKER------DDLRNKLKAEEE 336
Cdd:pfam05911 786 NcheELEAKCLELQEQLERNEKKEssncdaDQEDKKLQQEKE 827
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
81-330 |
1.87e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 81 RQLRQKLAALSRQIDELEETNRSLRKAEEE---LQDIKDKINKGEyGNSGIMDEVDELRKRvLDMEGKDEELIKMEEQCR 157
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQielLEPIRELAERYA-AARERLAELEYLRAA-LRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 158 DLNKRLEKETVQSKDFKLEVDKLSVRitaLEKLEDALDKSKQEcyslkcNLEkekmttkQLSEELESLNARIKELEAIES 237
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREE---LDELEAQIRGNGGD------RLE-------QLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 238 RLEKTeitlkddltkLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTtvteklieetkRALKSKTDAEEKM 317
Cdd:COG4913 363 RLEAL----------LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA-----------EAEAALRDLRREL 421
|
250
....*....|...
gi 295424124 318 YSVTKERDDLRNK 330
Cdd:COG4913 422 RELEAEIASLERR 434
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
4-369 |
1.89e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 4 DEQQRLTAQLALQRQKIQALTTSAKETQGK-LALAEARAQEEEQKATRleKELQTQTTEfhqnqdkimakLTNEDSQNRQ 82
Cdd:PRK04863 796 EELAERYATLSFDVQKLQRLHQAFSRFIGShLAVAFEADPEAELRQLN--RRRVELERA-----------LADHESQEQQ 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 83 LRQKLAALSRQIDELEETNRSLRKAEEElqdikdkinkgeygnsGIMDEVDELRkrvldmegkdEELIKMEEQCRDLNK- 161
Cdd:PRK04863 863 QRSQLEQAKEGLSALNRLLPRLNLLADE----------------TLADRVEEIR----------EQLDEAEEAKRFVQQh 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 162 -----RLEKE--TVQSKDFKLEVDKLSVritalEKLEDALDKSKQECYSLKCNLEK---------EKMTTKQlSEELESL 225
Cdd:PRK04863 917 gnalaQLEPIvsVLQSDPEQFEQLKQDY-----QQAQQTQRDAKQQAFALTEVVQRrahfsyedaAEMLAKN-SDLNEKL 990
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 226 NARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKR 305
Cdd:PRK04863 991 RQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARRDELHARLS 1070
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295424124 306 ALKSKTDAEEKMYSVTK-ERDDLRNKLKAEEEKGHDLLSKVTILKNRLQS-LEAIEKDFVKNKLNQ 369
Cdd:PRK04863 1071 ANRSRRNQLEKQLTFCEaEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAvLRLVKDNGVERRLHR 1136
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
75-297 |
1.98e-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: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 75 NEDSQNRQLRQKLAALSRQIDELEEtnrSLRKAEEELQDIKDK---INKGEYGNSgIMDEVDELRKRVLDMEgkdEELIK 151
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRK---ELEEAEAALEEFRQKnglVDLSEEAKL-LLQQLSELESQLAEAR---AELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 152 MEEQCRDLNKRLEKETVQSKDFK--LEVDKLSVRITALEKLEDALDKS-----------KQECYSLKCNLEKE-KMTTKQ 217
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLqsPVIQQLRAQLAELEAELAELSARytpnhpdvialRAQIAALRAQLQQEaQRILAS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 218 LSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTvmlvDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTE 297
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLE----REVEVARELYESLLQRLEEARLAEALTVGNVRVIDP 393
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
88-252 |
2.01e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 88 AALSRQI-----DELEETNRSLRKAEEELQDIKDKINKGEygnsgimDEVDELRKRVLDMEG----KDEELIKMEEQCRD 158
Cdd:COG2433 380 EALEELIekelpEEEPEAEREKEHEERELTEEEEEIRRLE-------EQVERLEAEVEELEAeleeKDERIERLERELSE 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 159 LNKRLEKETVQSKdfklEVDKLSVRITALEKLedaldkskqecyslkcnLEKEKMTtkqlSEELESLNARIKELEAIESR 238
Cdd:COG2433 453 ARSEERREIRKDR----EISRLDREIERLERE-----------------LEEERER----IEELKRKLERLKELWKLEHS 507
|
170
....*....|....
gi 295424124 239 LEKTEITLKDDLTK 252
Cdd:COG2433 508 GELVPVKVVEKFTK 521
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
7-137 |
2.18e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 7 QRLTAQLALQRQKIQALTTSAKETQGKLALAEA--------------RAQEEEQKATRLEKELQTQTTEFHQNQDKImaK 72
Cdd:PRK09039 63 AELADLLSLERQGNQDLQDSVANLRASLSAAEAersrlqallaelagAGAAAEGRAGELAQELDSEKQVSARALAQV--E 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295424124 73 LTNEdsQNRQLRQKLAALSRQIDELEETNRSlrkAEEELQDIkdkinkGEYGNSGIMDEVDELRK 137
Cdd:PRK09039 141 LLNQ--QIAALRRQLAALEAALDASEKRDRE---SQAKIADL------GRRLNVALAQRVQELNR 194
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
153-545 |
2.19e-03 |
|
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: 41.96 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 153 EEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEEleslnarikEL 232
Cdd:TIGR00606 233 LESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDE---------QL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 233 EAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKlkQTEDKLQSTTSQLQAEQNKVTTVTEKLiEETKRALKSKTD 312
Cdd:TIGR00606 304 NDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQE--KTELLVEQGRLQLQADRHQEHIRARDS-LIQSLATRLELD 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 313 AEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVT---ILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQENNKIKELS 389
Cdd:TIGR00606 381 GFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCadlQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVI 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 390 QEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKLAEKTESSHEQWLFRRLQEEE 469
Cdd:TIGR00606 461 KELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEML 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 470 AKS---------GHLSREVDALKEKIHEYMATEDLICHLQGdhslLQKKLNQQENRNRDLGREIENLTKELERYRHFSKS 540
Cdd:TIGR00606 541 TKDkmdkdeqirKIKSRHSDELTSLLGYFPNKKQLEDWLHS----KSKEINQTRDRLAKLNKELASLEQNKNHINNELES 616
|
....*
gi 295424124 541 LRPSL 545
Cdd:TIGR00606 617 KEEQL 621
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
6-149 |
2.43e-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: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 6 QQRL-TAQLALQ--RQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQ 82
Cdd:COG3206 188 RKELeEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ 267
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295424124 83 LRQKLAALSRQIDELE----ETNRSLRKAEEELQDIKDKINK-GEYGNSGIMDEVDELRKRVLDMEGKDEEL 149
Cdd:COG3206 268 LRAQLAELEAELAELSarytPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQL 339
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
42-406 |
2.50e-03 |
|
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: 41.96 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 42 QEEEQKATRLEKELQTQTTEFHQNQD--KIMAKLTNEDSQNRQLRQKLaalsRQIDELEETNRSLR-KAEEELQDIKDKI 118
Cdd:TIGR01612 1946 EKEPEIYTKIRDSYDTLLDIFKKSQDlhKKEQDTLNIIFENQQLYEKI----QASNELKDTLSDLKyKKEKILNDVKLLL 2021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 119 NKgeygnsgimdeVDELRKRVLDMEGKDEEL-IKMEEQCRDLNKRLEKET---VQSKDFKLEVDKLSVRITALEKLEDAL 194
Cdd:TIGR01612 2022 HK-----------FDELNKLSCDSQNYDTILeLSKQDKIKEKIDNYEKEKekfGIDFDVKAMEEKFDNDIKDIEKFENNY 2090
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 195 DKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEaiESRLEKTEitLKDDLTKLKTLTVMLvdERKTMSEKLKQT 274
Cdd:TIGR01612 2091 KHSEKDNHDFSEEKDNIIQSKKKLKELTEAFNTEIKIIE--DKIIEKND--LIDKLIEMRKECLLF--SYATLVETLKSK 2164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 275 edklQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVtilKNRLQS 354
Cdd:TIGR01612 2165 ----VINHSEFITSAAKFSKDFFEFIEDISDSLNDDIDALQIKYNLNQTKKHMISILADATKDHNNLIEKE---KEATKI 2237
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 295424124 355 LEAIEKDFVKNKLNQDSSkstaALHQENNKI----KELSQEVENLKLKLKDMKAIE 406
Cdd:TIGR01612 2238 INNLTELFTIDFNNADAD----ILHNNKIQIiyfnSELHKSIESIKKLYKKINAFK 2289
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
82-561 |
2.63e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.21 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 82 QLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVldmEGKDEELIKMeEQCRDlnk 161
Cdd:pfam05622 11 ELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQL---EQLQEENFRL-ETARD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 162 rleketvqskDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLekekmttkqlsEELESLNARIKELEA-IESRLE 240
Cdd:pfam05622 84 ----------DYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEM-----------DILRESSDKVKKLEAtVETYKK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 241 KTEitlkdDLTKLKTlTVMLVDERKTMSEKLK-QTEDKLQSTT---SQLQAEQNKVTTVTEKLIEETKRALKSKTD---A 313
Cdd:pfam05622 143 KLE-----DLGDLRR-QVKLLEERNAEYMQRTlQLEEELKKANalrGQLETYKRQVQELHGKLSEESKKADKLEFEykkL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 314 EEKMYSVTKERDDLRNK----------LKAEEEKGHDLLSKVTILKNRLQSLEAIEKDFVKNKLnqdssKSTAALHQENN 383
Cdd:pfam05622 217 EEKLEALQKEKERLIIErdtlretneeLRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEI-----REKLIRLQHEN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 384 KIKELSQEvENLKLKLKDMKAIEDDLMKTEDEYETlERRYANERDKaqflsqELEHAKMELAKYKLAEKTESSHEQWLFR 463
Cdd:pfam05622 292 KMLRLGQE-GSYRERLTELQQLLEDANRRKNELET-QNRLANQRIL------ELQQQVEELQKALQEQGSKAEDSSLLKQ 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 464 RLQEEEAKSGHLSREVDALKEKIHEYMATEDLICHLQGDHslLQKKLNQQENRNRDLGreiENLTKELERYRHFSKSLRP 543
Cdd:pfam05622 364 KLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDE--LQEALRKKDEDMKAME---ERYKKYVEKAKSVIKTLDP 438
|
490
....*....|....*...
gi 295424124 544 SLNERRISDPQVFSKEVQ 561
Cdd:pfam05622 439 KQNPASPPEIQALKNQLL 456
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
152-415 |
2.90e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 152 MEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQEcyslkcnlEKEKMttKQLSEELESLNARIKE 231
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE--------LREEA--QELREKRDELNEKVKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 232 LEaiESRLEKTEI--TLKDDLTKLKTLTVMLVDER---KTMSEKLKQTEDKLQSTTSQLQAEQnkvttvteKLIEETKRa 306
Cdd:COG1340 76 LK--EERDELNEKlnELREELDELRKELAELNKAGgsiDKLRKEIERLEWRQQTEVLSPEEEK--------ELVEKIKE- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 307 LKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAI------EKDFVK---NKLNQDSSKSTAA 377
Cdd:COG1340 145 LEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEmielykEADELRkeaDELHKEIVEAQEK 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 295424124 378 LHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDE 415
Cdd:COG1340 225 ADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
52-279 |
3.35e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 52 EKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNrsLRKAEEE-----------LQDIKDKINK 120
Cdd:COG0497 153 LEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAA--LQPGEEEeleeerrrlsnAEKLREALQE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 121 G----EYGNSGIMDEVDELRKRVLDMEGKDEELikmeeqcRDLNKRLEKETVQSKDFKLEVDKLSVRITA----LEKLED 192
Cdd:COG0497 231 AlealSGGEGGALDLLGQALRALERLAEYDPSL-------AELAERLESALIELEEAASELRRYLDSLEFdperLEEVEE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 193 ALDkskqECYSLKcnlEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKL- 271
Cdd:COG0497 304 RLA----LLRRLA---RKYGVTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLe 376
|
....*...
gi 295424124 272 KQTEDKLQ 279
Cdd:COG0497 377 KAVTAELA 384
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
51-411 |
3.82e-03 |
|
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: 41.19 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 51 LEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQ-----LRQKLAALSRQ--IDELEETNRslrkaeeeLQDIKDKINKgEY 123
Cdd:TIGR01612 639 LAKISPYQVPEHLKNKDKIYSTIKSELSKIYEddidaLYNELSSIVKEnaIDNTEDKAK--------LDDLKSKIDK-EY 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 124 GNSGIMdEVDELRKRVLDMEGKDEELIKM---------EEQCRDLNKRLEketvqskDFKLEVDKLSVRITALEKLEDAL 194
Cdd:TIGR01612 710 DKIQNM-ETATVELHLSNIENKKNELLDIiveikkhihGEINKDLNKILE-------DFKNKEKELSNKINDYAKEKDEL 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 195 DKSKQECYSLKC------------------NLEKEKMTTKQLSEELESLNARIKELEaiesrlekteiTLKDDLTKLKTL 256
Cdd:TIGR01612 782 NKYKSKISEIKNhyndqinidnikdedakqNYDKSKEYIKTISIKEDEIFKIINEMK-----------FMKDDFLNKVDK 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 257 TVMLVDERKtmsEKLKQTEDKLQSTTSQLQAE-QNKVTTVTEKLIEETKRALKSKTDAEEKMY---SVTKERDDLRNKLK 332
Cdd:TIGR01612 851 FINFENNCK---EKIDSEHEQFAELTNKIKAEiSDDKLNDYEKKFNDSKSLINEINKSIEEEYqniNTLKKVDEYIKICE 927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 333 AEEEKGHDLLSKVTILKNRL-QSLEAIEKDFVKNKLNQDSSKSTAAlhqenNKIKELSQEVENlkLKLKDMKAIEDDLMK 411
Cdd:TIGR01612 928 NTKESIEKFHNKQNILKEILnKNIDTIKESNLIEKSYKDKFDNTLI-----DKINELDKAFKD--ASLNDYEAKNNELIK 1000
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
59-234 |
3.85e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 40.81 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 59 TTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINkgeygnsGIMDEVDELRK- 137
Cdd:pfam13166 278 DDEFTEFQNRLQKLIEKVESAISSLLAQLPAVSDLASLLSAFELDVEDIESEAEVLNSQLD-------GLRRALEAKRKd 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 138 --RVLDMEGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKL--SVRITALEKLEDALDKSKQECYSLKCNLEKEKM 213
Cdd:pfam13166 351 pfKSIELDSVDAKIESINDLVASINELIAKHNEITDNFEEEKNKAkkKLRLHLVEEFKSEIDEYKDKYAGLEKAINSLEK 430
|
170 180
....*....|....*....|.
gi 295424124 214 TTKQLSEELESLNARIKELEA 234
Cdd:pfam13166 431 EIKNLEAEIKKLREEIKELEA 451
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
40-120 |
5.14e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 40 RAQEE-EQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDEL-EETNRSLRKAEEEL-QDIKD 116
Cdd:pfam03938 19 AAQAQlEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLqQKAQQELQKKQQELlQPIQD 98
|
....
gi 295424124 117 KINK 120
Cdd:pfam03938 99 KINK 102
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
301-383 |
5.17e-03 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 40.58 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 301 EETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKghDLLSKVTILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQ 380
Cdd:PTZ00400 561 EKKKELVDAKNEAETLIYSVEKQLSDLKDKISDADKD--ELKQKITKLRSTLSSEDVDSIKDKTKQLQEASWKISQQAYK 638
|
...
gi 295424124 381 ENN 383
Cdd:PTZ00400 639 QGN 641
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
4-333 |
5.27e-03 |
|
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: 40.59 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 4 DEQQRLTAQLALQRQKIQALttSAKETQGKLALAEARaqEEEQKATRLEKELQTQTTE-FHQNQDKIMAKLTNEDSQNRQ 82
Cdd:pfam12128 618 EKQAAAEEQLVQANGELEKA--SREETFARTALKNAR--LDLRRLFDEKQSEKDKKNKaLAERKDSANERLNSLEAQLKQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 83 LRQKLAALSRQIDELEETNRSLRKA-----EEELQD----IKDKINKGEYGNSGIMDEVDELRKRVLDMEGKDEE-LIKM 152
Cdd:pfam12128 694 LDKKHQAWLEEQKEQKREARTEKQAywqvvEGALDAqlalLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDvIAKL 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 153 EEQCRDLNKRLEKetvqskdfkLEVDKLSVRitalekledALDKSKQECYSLkcnlEKEKMTTkqlseeleslnarikEL 232
Cdd:pfam12128 774 KREIRTLERKIER---------IAVRRQEVL---------RYFDWYQETWLQ----RRPRLAT---------------QL 816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 233 EAIESRLEKteitLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTE--------KLIEETK 304
Cdd:pfam12128 817 SNIERAISE----LQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEdanseqaqGSIGERL 892
|
330 340 350
....*....|....*....|....*....|..
gi 295424124 305 RA---LKSKTDAEekMYSVTKERDDLRNKLKA 333
Cdd:pfam12128 893 AQledLKLKRDYL--SESVKKYVEHFKNVIAD 922
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
82-458 |
5.54e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.80 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 82 QLRQKLAALSRQI--------DELEETNRSLRKAEEELQDIK----DKINKGEYGNSGIMDEVDELRKRVLDMEGKDEE- 148
Cdd:PTZ00108 1003 KLERELARLSNKVrfikhvinGELVITNAKKKDLVKELKKLGyvrfKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEEl 1082
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 149 --------LIKM------EEQCRDLNKRLEkETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQEcyslkcnLEKEKMT 214
Cdd:PTZ00108 1083 gaavsydyLLSMpiwsltKEKVEKLNAELE-KKEKELEKLKNTTPKDMWLEDLDKFEEALEEQEEV-------EEKEIAK 1154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 215 TKQLS--EELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKV 292
Cdd:PTZ00108 1155 EQRLKskTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTK 1234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 293 ttvtEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHdlLSKVTILKNRLQSLEAIEKDFvknklnqdSS 372
Cdd:PTZ00108 1235 ----PKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKR--VSAVQYSPPPPSKRPDGESNG--------GS 1300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 373 KSTAALHQENNKIKELSQEVENLKLKLKDmKAIEDDLMKTEDEYETLERRYANERDKAQFLSQELEhakmELAKYKLAEK 452
Cdd:PTZ00108 1301 KPSSPTKKKVKKRLEGSLAALKKKKKSEK-KTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSS----EDDDDSEVDD 1375
|
....*.
gi 295424124 453 TESSHE 458
Cdd:PTZ00108 1376 SEDEDD 1381
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
3-182 |
6.22e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 3 VDEQQRLTAQLALQRQKIQALTTSAKETQ---GKLALAEARAQEEEQKATRLEKELQ------TQTTEFHQNQDKImAKL 73
Cdd:PHA02562 226 VEEAKTIKAEIEELTDELLNLVMDIEDPSaalNKLNTAAAKIKSKIEQFQKVIKMYEkggvcpTCTQQISEGPDRI-TKI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 74 TNedsQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKrvlDMEGKDEELIKME 153
Cdd:PHA02562 305 KD---KLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKA---AIEELQAEFVDNA 378
|
170 180
....*....|....*....|....*....
gi 295424124 154 EQCRDLNKRLEKETVQSKDFKLEVDKLSV 182
Cdd:PHA02562 379 EELAKLQDELDKIVKTKSELVKEKYHRGI 407
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
9-225 |
6.46e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 9 LTAQLALQrQKIQALTTSAKETQGKLALA---EARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQ 85
Cdd:PLN02939 162 LTEKEALQ-GKINILEMRLSETDARIKLAaqeKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 86 KLAALSRQIDELEETNRSLRKAEEE-------LQDIKDKINKGEYGNSGI--------MDEVDELRKRVLDMEGKDEELI 150
Cdd:PLN02939 241 DIQFLKAELIEVAETEERVFKLEKErslldasLRELESKFIVAQEDVSKLsplqydcwWEKVENLQDLLDRATNQVEKAA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 151 KMEEQCRDLNKRLEK------ETVQSKDFKLEVDKLSVRITAlekLEDALDKSKQECYSlkcNLEKEKMTTKQLSEELES 224
Cdd:PLN02939 321 LVLDQNQDLRDKVDKleaslkEANVSKFSSYKVELLQQKLKL---LEERLQASDHEIHS---YIQLYQESIKEFQDTLSK 394
|
.
gi 295424124 225 L 225
Cdd:PLN02939 395 L 395
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
368-487 |
9.36e-03 |
|
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.
Pssm-ID: 407228 [Multi-domain] Cd Length: 340 Bit Score: 39.19 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295424124 368 NQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMkaiEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKME-LAK 446
Cdd:pfam17060 132 NLKPQESPETPRRINRKYKSLELRVESMKDELEFK---DETIMEKDRELTELTSTISKLKDKYDFLSREFEFYKQHhEHG 208
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 295424124 447 YKLAEKTESSHE---QWLFRRLQEEEAKSGHLSREVDALKEKIH 487
Cdd:pfam17060 209 GNNSIKTATKHEfiiSELKRKLQEQNRLIRILQEQIQFDPGALH 252
|
|
|