|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-581 |
3.21e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.91 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 40 KTLKEELTKLKSFALmvVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQN 119
Cdd:COG1196 216 RELKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 120 QDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGK 199
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 200 DEELIKMEEQCRDLNKRLEKETVQSKDFKLEV--------DKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQ 271
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELeeaeeallERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 272 LSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSE--------KLKQTEDKLQSTTSQLQAEQ 343
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflegvkaaLLLAGLRGLAGAVAVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 344 NKVTTVTEKLIEETKRALKSKTDAEEKMY-SVTKERDDLR------NKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDF 416
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEDDEVAAAAiEYLKAAKAGRatflplDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 417 VKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKM 496
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 497 ELAKYKLAEKTESSHEQWLFRRLQEEEAKSGHLSREVDALKEKIHEYMATEDLICHLQGDHSLLQK-KLNQQENRNRDLG 575
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPpDLEELERELERLE 773
|
....*.
gi 1720388026 576 REIENL 581
Cdd:COG1196 774 REIEAL 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
104-601 |
5.32e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.27 E-value: 5.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 104 RLEKELQTQTTEFHQNQDKIMAKLtnedsqnRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIM 183
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSEL-------PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 184 DEVDELRKRVLDMEGKDEELIKME---EQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLK- 259
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKk 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 260 --CNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEI-TLKDDLTKLKTLTVMLVDERKTMSEK---LKQTEDKLQ 333
Cdd:PRK03918 346 klKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPeKLEKELEELEKAKEEIEEEISKITARigeLKKEIKELK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 334 STTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAE-EKMYSVTKERDDLRNKLKAEEEKGHDLL---SKVTILKNRLQSL 409
Cdd:PRK03918 426 KAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAElKRIEKELKEIEEKERKLRKELRELEKVLkkeSELIKLKELAEQL 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 410 EAIEKDFVKNKLnQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAqflsQ 489
Cdd:PRK03918 506 KELEEKLKKYNL-EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL----E 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 490 ELEHAKMELAKYKLAEkTESSHEQWL-----FRRLQEEEAKSGHLSREVDALKEKIHEymaTEDLICHLQGDHSLLQKKL 564
Cdd:PRK03918 581 ELGFESVEELEERLKE-LEPFYNEYLelkdaEKELEREEKELKKLEEELDKAFEELAE---TEKRLEELRKELEELEKKY 656
|
490 500 510
....*....|....*....|....*....|....*..
gi 1720388026 565 NQQENRNrdLGREIENLTKELERYRHFSKSLRPSLNE 601
Cdd:PRK03918 657 SEEEYEE--LREEYLELSRELAGLRAELEELEKRREE 691
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
38-545 |
5.74e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.27 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 38 RIKTLKEELTKLKSfalmVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLE----------- 106
Cdd:PRK03918 194 LIKEKEKELEEVLR----EINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEekireleerie 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 107 ------KELQTQTTEFHQNQ-------------DKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQD 167
Cdd:PRK03918 270 elkkeiEELEEKVKELKELKekaeeyiklsefyEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 168 IKDKINKGEYGNS------GIMDEVDELRKRVldmegKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITAL 241
Cdd:PRK03918 350 LEKRLEELEERHElyeeakAKKEELERLKKRL-----TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 242 EKLEDALDKSKQECYSLKCNL--EKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMlvderK 319
Cdd:PRK03918 425 KKAIEELKKAKGKCPVCGRELteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL-----K 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 320 TMSEKLKQTEDKLQS-TTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMySVTKERDDLRNKLKAEEEKGHDLLSK 398
Cdd:PRK03918 500 ELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAELEKKLDELEEELAELLKE 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 399 --------VTILKNRLQSLEAIEKDFVK---------------NKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKd 455
Cdd:PRK03918 579 leelgfesVEELEERLKELEPFYNEYLElkdaekelereekelKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS- 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 456 mkaiEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKlAEKTEssheqwlFRRLQEEEAKSGHLSREVDA 535
Cdd:PRK03918 658 ----EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK-EELEE-------REKAKKELEKLEKALERVEE 725
|
570
....*....|
gi 1720388026 536 LKEKIHEYMA 545
Cdd:PRK03918 726 LREKVKKYKA 735
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
22-589 |
1.20e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 82.03 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 22 DQETASQEKKEQEKEKRIKTLKEELTKLKSFA--------------LMVVDEQQRLTAQLALQRQKIQALTTSAKETQGK 87
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVseleeeieelqkelYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 88 LALAEARAQEEEQKATRLEK---ELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRK---- 160
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEkleELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeier 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 161 AEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDM--EGKDEELIKMEEQCRDLNKRLEKETVQSK-------DFKLEV 231
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAelEELEEELEELQEELERLEEALEELREELEeaeqaldAAEREL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 232 DKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEEL-----------------------ESLNARIKELEA 288
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdegyeaaieaalggrlqavvvENLNAAKKAIAF 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 289 IE--------------------------------------SRLEKTEITLKDDLTKLKTlTVMLVDERKTMSEKLKQTED 330
Cdd:TIGR02168 565 LKqnelgrvtflpldsikgteiqgndreilkniegflgvaKDLVKFDPKLRKALSYLLG-GVLVVDDLDNALELAKKLRP 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 331 KLQ--------------------STTSQLQAEQNKVTTVTEKL------IEETKRALKsktDAEEKMYSVTKERDDLRNK 384
Cdd:TIGR02168 644 GYRivtldgdlvrpggvitggsaKTNSSILERRREIEELEEKIeeleekIAELEKALA---ELRKELEELEEELEQLRKE 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 385 LKAEEEKGHDLLSKVTILKNRLQSLEA---------IEKDFVKNKLNQDSSKSTAALHQENNKIKELSQEVENLKlklKD 455
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEEriaqlskelTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK---EE 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 456 MKAIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKLAEKTESSHEQWLFRRLQEEEAKSGHLSREVDA 535
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1720388026 536 LKEkihEYMATEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTKELERYR 589
Cdd:TIGR02168 878 LLN---ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
146-490 |
2.34e-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: 80.88 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 146 RQIDELEETNRSLRKAEEELQDIKDKINKgeygnsgIMDEVDELRKRVLDMEGKDEELIKMEEQcrdLNKRLEKETVQSK 225
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRR-------IENRLDELSQELSDASRKIGEIEKEIEQ---LEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 226 DFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKE--KMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDD 303
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 304 LTKLKTLTVMLVDERKTMSEKLKQTEDKLQSttsqLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRN 383
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKS----IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 384 KLKAEEEKGHDLLSKVTILKNRLQSLEAieKDFVKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDL 463
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKA--KLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVN 974
|
330 340
....*....|....*....|....*..
gi 1720388026 464 MKTEDEYETLERRYANERDKAQFLSQE 490
Cdd:TIGR02169 975 MLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-587 |
1.78e-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: 78.17 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 38 RIKTLKEELTKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFH 117
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 118 Q---NQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKgeyGNSGIMDEVDELRKRVL 194
Cdd:TIGR02168 313 NlerQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES---RLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 195 DMEGK----DEELIKMEEQCRDLNKRLEK-----ETVQSKDFKLEVDKLSVRI----TALEKLEDALDKSKQECYSLKCN 261
Cdd:TIGR02168 390 QLELQiaslNNEIERLEARLERLEDRRERlqqeiEELLKKLEEAELKELQAELeeleEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 262 LEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTvmlvDERKTMSEKLKQTEDKLQSTTSQLQA 341
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS----GILGVLSELISVDEGYEAAIEAALGG 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 342 EQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDllSKVTILKNRLQSLEAIEKDF----- 416
Cdd:TIGR02168 546 RLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIE--GFLGVAKDLVKFDPKLRKALsyllg 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 417 -------VKNKLNQ---------------------------DSSKSTAALHQENN-------------KIKELSQEVENL 449
Cdd:TIGR02168 624 gvlvvddLDNALELakklrpgyrivtldgdlvrpggvitggSAKTNSSILERRREieeleekieeleeKIAELEKALAEL 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 450 KLKLKDMKAIEDDLMKTEDEYET----LERRYANERDKAQFLSQELEHAKMELAKYKLAEKTESSHEQWLFRRLQEEEAK 525
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRqisaLRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720388026 526 SGHLSREVDALKEkihEYMATEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTKELER 587
Cdd:TIGR02168 784 IEELEAQIEQLKE---ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
120-586 |
3.97e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.03 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 120 QDKIMAKLTNEDSQNRQLRQKLaalsrQIDELEetnrslrKAEEELQDIKDKINKgeygnsgimdEVDELRKRVLDMEGK 199
Cdd:PRK03918 134 QGEIDAILESDESREKVVRQIL-----GLDDYE-------NAYKNLGEVIKEIKR----------RIERLEKFIKRTENI 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 200 DEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESL 279
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 280 NARIKELEAIESRLEKTEitlkddltklktltvMLVDERKTMSEKLKQTEDKLQsttsqlqaEQNKVTTVTEKLIEETKR 359
Cdd:PRK03918 272 KKEIEELEEKVKELKELK---------------EKAEEYIKLSEFYEEYLDELR--------EIEKRLSRLEEEINGIEE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 360 ALKSKTDAEEKMYSVTKERDDLRNKLkAEEEKGHDLLSKVTILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQENNKI 439
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEI 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 440 KELSQEVENLKLKLKDMKAIEDDLMK------------TEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKLAEKT 507
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 508 ESSHEQWLFRRL----QEEEAKSGHLSREVDALKEKIHEYMATEDLICHLQGDHSLLQ---KKLNQQENRNRDLGREIEN 580
Cdd:PRK03918 488 VLKKESELIKLKelaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKkelEKLEELKKKLAELEKKLDE 567
|
....*.
gi 1720388026 581 LTKELE 586
Cdd:PRK03918 568 LEEELA 573
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
38-585 |
4.54e-14 |
|
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: 76.70 E-value: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 38 RIKTLKEELTKLKSfalmvvDEQQRLTAQLALQRQKIQALTTsakETQGKLALAEARAQEEEQKATRLEKELQTQTTEFH 117
Cdd:pfam15921 239 RIFPVEDQLEALKS------ESQNKIELLLQQHQDRIEQLIS---EHEVEITGLTEKASSARSQANSIQSQLEIIQEQAR 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 118 QNQDKIMAKLTNEDSQNRQLRQKLAALSRQI-DELEETNRSLRKAEEELQDIKDKINKGEYgNSGIMDevDELRKRVLDM 196
Cdd:pfam15921 310 NQNSMYMRQLSDLESTVSQLRSELREAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQ-ESGNLD--DQLQKLLADL 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 197 EGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALdksKQECYSL-----------KCNLEKE 265
Cdd:pfam15921 387 HKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAM---KSECQGQmerqmaaiqgkNESLEKV 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 266 KMTTKQLSEELESLNARIKELEAIESRLEKTEITLKD-----------------DLTKLKTltvmLVDERKTMSEKLKQT 328
Cdd:pfam15921 464 SSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDltaslqekeraieatnaEITKLRS----RVDLKLQELQHLKNE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 329 EDKLQSTTSQLQA------EQNKVTTVTEKLIEETKRALKSKTDAEEKMY----SVTKERDDLRNKLKAEEEKGHDLLSK 398
Cdd:pfam15921 540 GDHLRNVQTECEAlklqmaEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvekaQLEKEINDRRLELQEFKILKDKKDAK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 399 VTILKNRLQSLEaiekdFVKNKLNQDSSKSTAAlhqennkIKELSQEVENLklkLKDMKAIEDDLMKTEDEYETLERRYA 478
Cdd:pfam15921 620 IRELEARVSDLE-----LEKVKLVNAGSERLRA-------VKDIKQERDQL---LNEVKTSRNELNSLSEDYEVLKRNFR 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 479 NErdkaqflSQELEhakMELAKYKLAEKTESSHEQWLFRRLQEEEAKSGHLSREVDALKEKIheyMATEDLICHLQGDHS 558
Cdd:pfam15921 685 NK-------SEEME---TTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQI---TAKRGQIDALQSKIQ 751
|
570 580
....*....|....*....|....*..
gi 1720388026 559 LLQKKLNQQENRNRDLGREIENLTKEL 585
Cdd:pfam15921 752 FLEEAMTNANKEKHFLKEEKNKLSQEL 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
47-394 |
5.54e-14 |
|
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: 76.65 E-value: 5.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 47 TKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMA- 125
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSl 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 126 --KLTNEdsqnrqlRQKLAALSRQIDELEETnrsLRKAEEELQDIKDKINKGEYGNsgIMDEVDELRKRVLDMEGKDEEl 203
Cdd:TIGR02169 750 eqEIENV-------KSELKELEARIEELEED---LHKLEEALNDLEARLSHSRIPE--IQAELSKLEEEVSRIEARLRE- 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 204 IKMEEQCRDLNKRLEKETVQSKdfKLEVDKLSVRITALEKLEDALDKSKQEcysLKCNLEKEKMTTKQLSEELESLNARI 283
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQEL--QEQRIDLKEQIKSIEKEIENLNGKKEE---LEEELEELEAALRDLESRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 284 KELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTED----------------KLQSTTSQLQAEQNKVT 347
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkgedeeipeeelsleDVQAELQRVEEEIRALE 971
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1720388026 348 TVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHD 394
Cdd:TIGR02169 972 PVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-620 |
7.00e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.25 E-value: 7.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 38 RIKTLKEELTKLKSFALMV-----VDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQ 112
Cdd:TIGR02168 214 RYKELKAELRELELALLVLrleelREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 113 TTEFHQ-NQDKIMAKltnedSQNRQLRQKLAALSRQIDELEetnRSLRKAEEELQDIKDKINkgeygnsGIMDEVDELRK 191
Cdd:TIGR02168 294 ANEISRlEQQKQILR-----ERLANLERQLEELEAQLEELE---SKLDELAEELAELEEKLE-------ELKEELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 192 RVLDMEGKDEElikMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEK----LEDALDKSKQECYSLKCNLEKEKM 267
Cdd:TIGR02168 359 ELEELEAELEE---LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEArlerLEDRRERLQQEIEELLKKLEEAEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 268 ttKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDE------RKTMSEKLKQTEDKLQSTTSQLQA 341
Cdd:TIGR02168 436 --KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERElaqlqaRLDSLERLQENLEGFSEGVKALLK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 342 EQNKVTTVTEKLIE------ETKRAL-------------KSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTIL 402
Cdd:TIGR02168 514 NQSGLSGILGVLSElisvdeGYEAAIeaalggrlqavvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 403 KNRLQSLEAIEKDFVK-----------------------------NKLNQDSSKSTAALH-------------QENNKIK 440
Cdd:TIGR02168 594 LKNIEGFLGVAKDLVKfdpklrkalsyllggvlvvddldnalelaKKLRPGYRIVTLDGDlvrpggvitggsaKTNSSIL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 441 ELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELakYKLAEKTESSHEQWLfRRLQ 520
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL--RKDLARLEAEVEQLE-ERIA 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 521 EEEAKSGHLSREVDALKEKIHEymaTEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTKEL--ERYRHFSKSLRPS 598
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEE---AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtlLNEEAANLRERLE 827
|
650 660
....*....|....*....|..
gi 1720388026 599 LNERRISDPQVFSKEVQTEAAD 620
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEE 849
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
70-412 |
3.98e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.54 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 70 QRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMA-----------------KLTNEDS 132
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEleeeieelrerfgdapvDLGNAED 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 133 QNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYG----NSGIMDEVDELRKRVLDMEgkdEELIKMEE 208
Cdd:PRK02224 413 FLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGqpveGSPHVETIEEDRERVEELE---AELEDLEE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 209 QCRDLNKRLE--KETVQSKDfklEVDKLSVRITALEKL----EDALDKSKQECYSLK---------------------CN 261
Cdd:PRK02224 490 EVEEVEERLEraEDLVEAED---RIERLEERREDLEELiaerRETIEEKRERAEELReraaeleaeaeekreaaaeaeEE 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 262 LEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEiTLKDDLTKLKtltvmlvDERKTMSEKLKQTEDKLQST---TSQ 338
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERIESLERIRTLLAAIA-DAEDEIERLR-------EKREALAELNDERRERLAEKrerKRE 638
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720388026 339 LQAEQNKvtTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNK---LKAEEEKGHDLLSKVTILKNRLQSLEAI 412
Cdd:PRK02224 639 LEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELRERREALENRVEALEAL 713
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
135-502 |
1.29e-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: 72.01 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 135 RQLRQKLAALSRQIDELEETNRSLRKAE------EELQDIKDKINKGEYGNSGimDEVDELRKRvldMEGKDEELIKMEE 208
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLErqaekaERYKELKAELRELELALLV--LRLEELREE---LEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 209 QCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALdkskqecYSLKCNLEKEKMttkQLSEELESLNARIKELEA 288
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL-------ANEISRLEQQKQ---ILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 289 IESRLEKTEITLKDDLTKLktltvmlvderktmseklkqtEDKLQSTTSQLQAEQNKVTTVTEKLIEetkralksktdAE 368
Cdd:TIGR02168 324 QLEELESKLDELAEELAEL---------------------EEKLEELKEELESLEAELEELEAELEE-----------LE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 369 EKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEaiekdfvKNKLNQDSSKSTAALHQENNKIKELSQEVEN 448
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE-------DRRERLQQEIEELLKKLEEAELKELQAELEE 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1720388026 449 LKLKLKDmkaieddlmkTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYK 502
Cdd:TIGR02168 445 LEEELEE----------LQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
71-617 |
2.55e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.33 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 71 RQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEfhqnqdkIMAKLTNEDSQNRQLRQKLAALSRQIDE 150
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD-------EAKKKAEEAKKADEAKKKAEEAKKKADA 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 151 LEETNRSLRKAEE----ELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGKDEELIKMEEqcrdLNKRLEKEtvqskd 226
Cdd:PTZ00121 1334 AKKKAEEAKKAAEaakaEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE----AKKKAEED------ 1403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 227 fKLEVDKLSVRITALEKLEDALDKSKQEcysLKCNLEKEKMTTKQLSEELESlnaRIKELEAIESRLEKTEITLKDDLTK 306
Cdd:PTZ00121 1404 -KKKADELKKAAAAKKKADEAKKKAEEK---KKADEAKKKAEEAKKADEAKK---KAEEAKKAEEAKKKAEEAKKADEAK 1476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 307 LKTLTVMLVDERKTMSEKLKQTEDKLQsttsqlQAEQNKVTTVTEKLIEETKRALKSKTdAEEKmysvtKERDDLRnklK 386
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAK------KAAEAKKKADEAKKAEEAKKADEAKK-AEEA-----KKADEAK---K 1541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 387 AEEEKGHDLLSKVTILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQENNKIKELSQEV-ENLKLKLKDMKAIEDDLMK 465
Cdd:PTZ00121 1542 AEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYeEEKKMKAEEAKKAEEAKIK 1621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 466 TED---------EYETLERRYANERDKAQFLSQELEHAKMELAKYKLAEKTESSHEQWLFRRLQEEEAKSGHLSRE---- 532
Cdd:PTZ00121 1622 AEElkkaeeekkKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeea 1701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 533 --VDALKEKIHEYMATEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSLNERRISDPQVF 610
Cdd:PTZ00121 1702 kkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
....*..
gi 1720388026 611 SKEVQTE 617
Cdd:PTZ00121 1782 EEELDEE 1788
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
16-601 |
2.59e-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: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 16 RLKKLIDQETASQEKKEQEKEKRIKTLKEELTKLKSF----ALMVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALA 91
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 92 EARAQEEEQKATRLEKELQTQ-------TTEFHQNQDKIM---AKLTNEDSQNRQLRQKLAALSRQID----ELEETNRS 157
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIEEErkrrdklTEEYAELKEELEdlrAELEEVDKEFAETRDELKDYREKLEklkrEINELKRE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 158 -------LRKAEEELQDIKDKInkgeygnSGIMDEVDELRKRvldMEGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLE 230
Cdd:TIGR02169 408 ldrlqeeLQRLSEELADLNAAI-------AGIEAKINELEEE---KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 231 VDKLSVRITALEKLEDALDKSKQecySLKCNLEKEKMTTKQLSEELESLNARIKEL--------EAIES----RLEKteI 298
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQAR---ASEERVRGGRAVEEVLKASIQGVHGTVAQLgsvgeryaTAIEVaagnRLNN--V 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 299 TLKDDLT-----------KLKTLTVMLVDERKTMSEKLK---------------QTEDKLQS----------------TT 336
Cdd:TIGR02169 553 VVEDDAVakeaiellkrrKAGRATFLPLNKMRDERRDLSilsedgvigfavdlvEFDPKYEPafkyvfgdtlvvedieAA 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 337 SQLQAEQNKVT---------------TVTEKLIEETKRALKSKT-DAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVT 400
Cdd:TIGR02169 633 RRLMGKYRMVTlegelfeksgamtggSRAPRGGILFSRSEPAELqRLRERLEGLKRELSSLQSELRRIENRLDELSQELS 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 401 ILKnrlQSLEAIEKDfvKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKA----IEDDLMKTEDEYETLERR 476
Cdd:TIGR02169 713 DAS---RKIGEIEKE--IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEArieeLEEDLHKLEEALNDLEAR 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 477 YANERDK---AQFLSQELEHAKMELAKYKLAEKTESSHEqwlfrRLQEEEAKSGHLSREVDALKEKIHEYMATEDLichL 553
Cdd:TIGR02169 788 LSHSRIPeiqAELSKLEEEVSRIEARLREIEQKLNRLTL-----EKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN---L 859
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1720388026 554 QGDHSLLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSLNE 601
Cdd:TIGR02169 860 NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
68-391 |
4.04e-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: 70.47 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 68 ALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTnedsQNRQLRQKLAALSRQ 147
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR----QISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 148 IDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVldmegkDEELIKMEEQCRDLNKRLEKETVQSKDF 227
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL------EAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 228 KLEVDKLSVRITALEKLEDALDKSKQEcyslkcnLEKEKmttKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKL 307
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLED-------LEEQI---EELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 308 KTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKL------IEETKRALKSK-----TDAEEKMYSVTK 376
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLeglevrIDNLQERLSEEysltlEEAEALENKIED 965
|
330
....*....|....*
gi 1720388026 377 ERDDLRNKLKAEEEK 391
Cdd:TIGR02168 966 DEEEARRRLKRLENK 980
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
73-378 |
1.15e-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: 68.94 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 73 KIQALTTSAKETQGKLALAEARAQEEEQKATrlEKELQTQTTEFHQNQDKImakltnedsqnRQLRQKLAALSRQIDELE 152
Cdd:TIGR02169 212 RYQALLKEKREYEGYELLKEKEALERQKEAI--ERQLASLEEELEKLTEEI-----------SELEKRLEEIEQLLEELN 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 153 EtnRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGK----DEELIKMEEQCRDLNKRLEKEtvqskdfK 228
Cdd:TIGR02169 279 K--KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERlaklEAEIDKLLAEIEELEREIEEE-------R 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 229 LEVDKLsvrITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRL--EKTEIT-----LK 301
Cdd:TIGR02169 350 KRRDKL---TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeELQRLSeeladLN 426
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720388026 302 DDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKL--IEETKRALKSKTDAEEKMYSVTKER 378
Cdd:TIGR02169 427 AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYdrVEKELSKLQRELAEAEAQARASEER 505
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
59-542 |
3.60e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.47 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 59 EQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEfhqnqdkIMAKLTNEDSQNRQLR 138
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD-------AAKKKAEEKKKADEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 139 QKLAALSRQIDELEETNRSLRKAEEELQDIKDKinkgeygnsgimDEVDELRKRVLDMEGKDEELIKMEEqcrdlnKRLE 218
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEK------------KKADEAKKKAEEAKKADEAKKKAEE------AKKA 1459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 219 KETVQSKDFKLEVDKLSVRITALEKLEDAldKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEI 298
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADEA--KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD 1537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 299 TLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTtvteKLIEETKRALKSKTDAEEKMYSVTKER 378
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA----KKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 379 DDLRNKLKAEEekghdlLSKVTILKNRLQSLEAIEKDFVKN--KLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDM 456
Cdd:PTZ00121 1614 KAEEAKIKAEE------LKKAEEEKKKVEQLKKKEAEEKKKaeELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 457 KAIEDDLMKTEDE---YETLERRYANERDKAQFLSQELE--HAKMELAKYKLAEKTESSHEqwlFRRLQEEEAKSGHLSR 531
Cdd:PTZ00121 1688 KKAAEALKKEAEEakkAEELKKKEAEEKKKAEELKKAEEenKIKAEEAKKEAEEDKKKAEE---AKKDEEEKKKIAHLKK 1764
|
490
....*....|.
gi 1720388026 532 EVDALKEKIHE 542
Cdd:PTZ00121 1765 EEEKKAEEIRK 1775
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
57-515 |
4.35e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 57 VDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQttEFHQNQDKIMAKLTNEDSQNRQ 136
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL--PLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 137 LRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGN-SGIMDEVDELRKRVLDMEgkdEELIKMEEQCRDLNK 215
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELE---EELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 216 RLEKETVQSKDFKLE--VDKLSV------RITALEKLEDALDKSKQEC-----------YSLKCNLEKEKMTTKQLSEEL 276
Cdd:COG4717 228 ELEQLENELEAAALEerLKEARLllliaaALLALLGLGGSLLSLILTIagvlflvlgllALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 277 ESLNARikeleaieSRLEKTEIT-LKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQnkvttvteklIE 355
Cdd:COG4717 308 QALPAL--------EELEEEELEeLLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE----------LE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 356 ETKRALKSKTDAEekmysvtkERDDLRNKLKAEEEKgHDLLSKVTILKNRLQSL----EAIEKDFVKNKLNQDSSKSTAA 431
Cdd:COG4717 370 QEIAALLAEAGVE--------DEEELRAALEQAEEY-QELKEELEELEEQLEELlgelEELLEALDEEELEEELEELEEE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 432 LHQENNKIKELSQEVENLKLKLKDMKAiEDDLMKTEDEYETLerryanerdKAQFLSQELEHAKMELAKYKLAEKTESSH 511
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEE-DGELAELLQELEEL---------KAELRELAEEWAALKLALELLEEAREEYR 510
|
....
gi 1720388026 512 EQWL 515
Cdd:COG4717 511 EERL 514
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
89-589 |
5.20e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.60 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 89 ALAEARAQEEEQKatrlEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDI 168
Cdd:PRK02224 188 SLDQLKAQIEEKE----EKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 169 KDKINKGEYGNSGIMDEVDELRKRVLDMEGKD---------------------EELIKMEEQCRDlnkRLEKETVQSKDF 227
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERddllaeaglddadaeavearrEELEDRDEELRD---RLEECRVAAQAH 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 228 KLEVDKLSVRITALE----KLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIK----ELEAIESRLEKTEIT 299
Cdd:PRK02224 341 NEEAESLREDADDLEeraeELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvDLGNAEDFLEELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 300 LKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKL------------IEETKRALKSKTDA 367
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRerveeleaeledLEEEVEEVEERLER 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 368 EEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSL---------EAIEKDFVKNKLNQDSSKSTAALHQENNK 438
Cdd:PRK02224 501 AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELreraaeleaEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 439 IKELSQEVENLklklkdmKAIEDDLMKTEDEYETLERRyaNERDKAQflsQELEHAKMElakyKLAEKTEssheqwlfRR 518
Cdd:PRK02224 581 LAELKERIESL-------ERIRTLLAAIADAEDEIERL--REKREAL---AELNDERRE----RLAEKRE--------RK 636
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720388026 519 LQEEEAKSGHLSREVDALKEKIHEYMATEDlichlqgdhsllqKKLNQQENRNRDLGREI---ENLTKELERYR 589
Cdd:PRK02224 637 RELEAEFDEARIEEAREDKERAEEYLEQVE-------------EKLDELREERDDLQAEIgavENELEELEELR 697
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
43-599 |
5.43e-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: 67.02 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 43 KEELTKLKSFALMVVDEQQRLTAQLAlqrqKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDK 122
Cdd:TIGR02169 205 REREKAERYQALLKEKREYEGYELLK----EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 123 IMAKLTNEdsqNRQLRQKLAALSRQI----DELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEg 198
Cdd:TIGR02169 281 IKDLGEEE---QLRVKEKIGELEAEIasleRSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 199 kdEELIKMEEQCRDLNKRLEKEtvqSKDFKLEVDKLSVRITALEKLedaldksKQECYSLKCNLEKEKMTTKQLSEELES 278
Cdd:TIGR02169 357 --EEYAELKEELEDLRAELEEV---DKEFAETRDELKDYREKLEKL-------KREINELKRELDRLQEELQRLSEELAD 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 279 LNARIKELEA----IESRLEKTEITLKDDLTKLKTLTVMLVDERKTMsEKLKQTEDKLQSTTSQLQAEQNKVTTvTEKLI 354
Cdd:TIGR02169 425 LNAAIAGIEAkineLEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL-YDLKEEYDRVEKELSKLQRELAEAEA-QARAS 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 355 EETKRALKSKTD------------------------------AEEKMYSVTKERDDLR--------------------NK 384
Cdd:TIGR02169 503 EERVRGGRAVEEvlkasiqgvhgtvaqlgsvgeryataievaAGNRLNNVVVEDDAVAkeaiellkrrkagratflplNK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 385 LKAEE------------------------------------------EKGHDLLSK---VTILKNRLQSLEAIEKDFVKN 419
Cdd:TIGR02169 583 MRDERrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvvediEAARRLMGKyrmVTLEGELFEKSGAMTGGSRAP 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 420 KLNQDSSKS-TAALHQENNKIKELSQEVENLKLKLKDMK------------------AIEDDLMKTEDEYETLERRYANE 480
Cdd:TIGR02169 663 RGGILFSRSePAELQRLRERLEGLKRELSSLQSELRRIEnrldelsqelsdasrkigEIEKEIEQLEQEEEKLKERLEEL 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 481 RDKAQFLSQELEHAKMELAKY--KLAEKTESSHEqwlfrrLQEEEAK-----SGHLSREVDALKEKIHEYMA-------- 545
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELeaRIEELEEDLHK------LEEALNDlearlSHSRIPEIQAELSKLEEEVSriearlre 816
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720388026 546 TEDLICHLQGDHSLLQKKLNQQENRNRDL-------GREIENLTK-------ELERYRHFSKSLRPSL 599
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqiksiEKEIENLNGkkeeleeELEELEAALRDLESRL 884
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
52-591 |
7.19e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 66.40 E-value: 7.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 52 FALMVVDEQQRLTAQLALQrqkiqALTTSAKETQgklaLAEARAQEEEQKAT-RLEKELQTQTTEFHQNQDKIMAKLTNE 130
Cdd:pfam12128 243 FTKLQQEFNTLESAELRLS-----HLHFGYKSDE----TLIASRQEERQETSaELNQLLRTLDDQWKEKRDELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 131 DSQNRQLRQKLAALSRQIDELEETNRSLRKAE-EELQDIKDKINKGEygnsgimDEVDELRKRVLDMEGKDEELI-KMEE 208
Cdd:pfam12128 314 DAAVAKDRSELEALEDQHGAFLDADIETAAADqEQLPSWQSELENLE-------ERLKALTGKHQDVTAKYNRRRsKIKE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 209 QCRDLNKRLEKETVQSKDFKleVDKLSVRITALEKLEDALDKS--------KQECYSLKCNLEKEKMTTKQL---SEELE 277
Cdd:pfam12128 387 QNNRDIAGIKDKLAKIREAR--DRQLAVAEDDLQALESELREQleagklefNEEEYRLKSRLGELKLRLNQAtatPELLL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 278 SLNARIKELEAIESRLE---KTEITLKDDLTKLKTLtvmlvdeRKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLI 354
Cdd:pfam12128 465 QLENFDERIERAREEQEaanAEVERLQSELRQARKR-------RDQASEALRQASRRLEERQSALDELELQLFPQAGTLL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 355 EETKRALKSKTDAEEKMYSVTK-ERDDLRNKLKAEEEKGHDLLSKVTIlknRLQSLEAIEKDFVKNKLNQDSSKSTAALH 433
Cdd:pfam12128 538 HFLRKEAPDWEQSIGKVISPELlHRTDLDPEVWDGSVGGELNLYGVKL---DLKRIDVPEWAASEEELRERLDKAEEALQ 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 434 QENNKIKELSQ-------EVENLKLKLKDMKAI----EDDLMKTEDEYETLERR----YANERDKAQFLSQELEHAKMEL 498
Cdd:pfam12128 615 SAREKQAAAEEqlvqangELEKASREETFARTAlknaRLDLRRLFDEKQSEKDKknkaLAERKDSANERLNSLEAQLKQL 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 499 A---KYKLAEKTESSHE---QWLFRRLQEEEAKSGHLSReVDALKEKIHEYMATEDLICHLQGDHSLlqKKLNQQENRNR 572
Cdd:pfam12128 695 DkkhQAWLEEQKEQKREartEKQAYWQVVEGALDAQLAL-LKAAIAARRSGAKAELKALETWYKRDL--ASLGVDPDVIA 771
|
570
....*....|....*....
gi 1720388026 573 DLGREIENLTKELERYRHF 591
Cdd:pfam12128 772 KLKREIRTLERKIERIAVR 790
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
38-466 |
1.29e-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: 65.43 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 38 RIKTLKEELTKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQE-EEQKATRLEKELQTQTTEF 116
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlNNQKEQDWNKELKSELKNQ 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 117 HQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRkaeEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDM 196
Cdd:TIGR04523 320 EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQ---RELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 197 EGK-----------DEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKS----KQECYSLKCN 261
Cdd:TIGR04523 397 ESKiqnqeklnqqkDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTreslETQLKVLSRS 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 262 LEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQS-----TT 336
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKddfelKK 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 337 SQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEK-- 414
Cdd:TIGR04523 557 ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKni 636
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1720388026 415 DFVKNKLNQDsskstaaLHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKT 466
Cdd:TIGR04523 637 KSKKNKLKQE-------VKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIEL 681
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
20-498 |
1.75e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 20 LIDQETASQEKKEQEKEKRIKTLKEELTKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEE 99
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 100 QKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGN 179
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 180 SGIMDEVDELRKRVLDMEGKDEELIKMEEQCRDLNKRLE--------------------KETVQSKDFKLEVDKLSVRIT 239
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAarllllleaeadyegflegvKAALLLAGLRGLAGAVAVLIG 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 240 ALEKLEDAL---------------DKSKQEC--YSLKCNLEK------EKMTTKQLSEELESLNARIKELEAIESRLEKT 296
Cdd:COG1196 532 VEAAYEAALeaalaaalqnivvedDEVAAAAieYLKAAKAGRatflplDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 297 EITLKD--DLTKLKTLTVMLVDERKTMSEKLKQTEDKL----------QSTTSQLQAEQNKVTTVTEKLIEETKRALKSK 364
Cdd:COG1196 612 DARYYVlgDTLLGRTLVAARLEAALRRAVTLAGRLREVtlegeggsagGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 365 TDAEEKmysVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDFvKNKLNQDSSKSTAALHQENNKIKELSQ 444
Cdd:COG1196 692 ELELEE---ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE-LLEEEELLEEEALEELPEPPDLEELER 767
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720388026 445 EVENLKLKLKDMKAIEddlMKTEDEYETLERRYanerdkaQFLSQE---LEHAKMEL 498
Cdd:COG1196 768 ELERLEREIEALGPVN---LLAIEEYEELEERY-------DFLSEQredLEEARETL 814
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
59-382 |
1.95e-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: 65.08 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 59 EQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEfhqnQDKIMAKLTNEDSQNRQLR 138
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 139 QKLAALSRQIDELEETnrsLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEG----KDEELIKMEEQCRDLN 214
Cdd:TIGR02168 761 AEIEELEERLEEAEEE---LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaanLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 215 KRLEKETVQSKDFKLEVDKLSVRI----TALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELE--- 287
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIeeleELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRrel 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 288 --------AIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKR 359
Cdd:TIGR02168 918 eelreklaQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEE 997
|
330 340
....*....|....*....|...
gi 1720388026 360 ALKSKTDAEEKMYSVTKERDDLR 382
Cdd:TIGR02168 998 LKERYDFLTAQKEDLTEAKETLE 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
152-524 |
2.38e-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: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 152 EETNRSLRKAEEELQDIKDKInkgeygnsgimdevDELRKRVldmegkdEELikmEEQCRDLNKRLE-KETVQSKDFKLE 230
Cdd:COG1196 175 EEAERKLEATEENLERLEDIL--------------GELERQL-------EPL---ERQAEKAERYRElKEELKELEAELL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 231 VDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKtl 310
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE-- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 311 tvmlvDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKR---ALKSKTDAEEKMYSVTKERDDLRNKLKA 387
Cdd:COG1196 309 -----ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEleeAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 388 EEEKGHDLLSKVTILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTE 467
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720388026 468 DEYETLERRYANERDKAQFLSQELEHAKMELAKYKLAEKTESSHEQWLFRRLQEEEA 524
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
41-508 |
3.82e-10 |
|
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: 64.04 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 41 TLKEELTKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTtEFHQNQ 120
Cdd:pfam01576 128 TTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEE-KGRQEL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 121 DKIMAKLTNEDSQnrqLRQKLAALSRQIDELEEtnrSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVL----DM 196
Cdd:pfam01576 207 EKAKRKLEGESTD---LQEQIAELQAQIAELRA---QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISelqeDL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 197 EGKDEELIKMEEQCRDLNKRLEketvqskdfklevdklsvritALE-KLEDALD----------KSKQECYSLKCNLEKE 265
Cdd:pfam01576 281 ESERAARNKAEKQRRDLGEELE---------------------ALKtELEDTLDttaaqqelrsKREQEVTELKKALEEE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 266 -KMTTKQLSE-------ELESLNARIKELEAIESRLEKTEITLKDDLTKLKTltvmlvdERKTMSEKLKQTEDKLQSTTS 337
Cdd:pfam01576 340 tRSHEAQLQEmrqkhtqALEELTEQLEQAKRNKANLEKAKQALESENAELQA-------ELRTLQQAKQDSEHKRKKLEG 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 338 QLQAEQNKVTtvteklieETKRAlksKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDFV 417
Cdd:pfam01576 413 QLQELQARLS--------ESERQ---RAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEET 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 418 KNKLN---------QDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKA--QF 486
Cdd:pfam01576 482 RQKLNlstrlrqleDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALtqQL 561
|
490 500
....*....|....*....|..
gi 1720388026 487 LSQELEHAKMELAKYKLAEKTE 508
Cdd:pfam01576 562 EEKAAAYDKLEKTKNRLQQELD 583
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-333 |
6.23e-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: 63.54 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 38 RIKTLKEELTKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFH 117
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 118 QNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDME 197
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 198 GKDEELikmEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQecyslkcnlEKEKMTTKQLSEELE 277
Cdd:TIGR02168 908 SKRSEL---RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE---------NKIEDDEEEARRRLK 975
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720388026 278 SLNARIKE-----LEAIE--SRLEKTEITL---KDDLTK-LKTLTVMLVDERKTMSEKLKQTEDKLQ 333
Cdd:TIGR02168 976 RLENKIKElgpvnLAAIEeyEELKERYDFLtaqKEDLTEaKETLEEAIEEIDREARERFKDTFDQVN 1042
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
131-490 |
7.06e-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: 63.16 E-value: 7.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 131 DSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKinKGEYgnsgimdevDELRKRVLDMEGKD--EELIKMEE 208
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREK--AERY---------QALLKEKREYEGYEllKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 209 QCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKS------------KQECYSLKCNLEKEKMTTKQLSEEL 276
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikdlgeeeqlrvKEKIGELEAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 277 ESLNARIKELEAIESRLEKTEITLKDDLTKLKTltvmlvdERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTvtekLIEE 356
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERK-------RRDKLTEEYAELKEELEDLRAELEEVDKEFAE----TRDE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 357 TKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDFVKnklnqdsskstaalhqen 436
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL------------------ 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720388026 437 nKIKELSQEVENLKLKLKDMK----AIEDDLMKTEDEYETLERRYANERDKAQFLSQE 490
Cdd:TIGR02169 449 -EIKKQEWKLEQLAADLSKYEqelyDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
73-502 |
8.13e-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: 8.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 73 KIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQN----------QDKIMAKLTNEDSQNRQLRQKLA 142
Cdd:TIGR04523 205 NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTqtqlnqlkdeQNKIKKQLSEKQKELEQNNKKIK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 143 ALSRQIDELE----------------ETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEG----KDEE 202
Cdd:TIGR04523 285 ELEKQLNQLKseisdlnnqkeqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESenseKQRE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 203 LIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEkmtTKQLSEELESLNAR 282
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE---IERLKETIIKNNSE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 283 IKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLqaeqNKVTTVTEKLIEETKRALK 362
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL----KKLNEEKKELEEKVKDLTK 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 363 SKTDAEEKMYSVTKERDDLRNKLKAEEEKghdLLSKVTILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQENNKIKEL 442
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDE---LNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK 594
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720388026 443 SQEVENL--KLKLKDMKA--IEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYK 502
Cdd:TIGR04523 595 EKEKKDLikEIEEKEKKIssLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
63-416 |
3.39e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 63 LTAQLA-LQRQKIQA-----LTTSAKETQGKLALAEARAQEEEQKatRLEKELQTQTTEfhqnQDKIMAKLTNEDSQNRQ 136
Cdd:COG1196 198 LERQLEpLERQAEKAeryreLKEELKELEAELLLLKLRELEAELE--ELEAELEELEAE----LEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 137 LRQKLAALSRQIDELEETNRSLRKAEEELQdikdkinkgeygnsgimdevdelrkrvldmegkdEELIKMEEQCRDLNKR 216
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLE----------------------------------QDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 217 LEKETVQskdfklevdklsvritaLEKLEDALDKSKQEcyslkcnlekekmtTKQLSEELESLNARIKELEA----IESR 292
Cdd:COG1196 318 LEELEEE-----------------LAELEEELEELEEE--------------LEELEEELEEAEEELEEAEAelaeAEEA 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 293 LEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTE-------------DKLQSTTSQLQAEQNKVTTVTEKLIEETKR 359
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEeleeaeeallerlERLEEELEELEEALAELEEEEEEEEEALEE 446
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720388026 360 ALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDF 416
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
38-220 |
3.71e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 38 RIKTLKEELTKLKSfalmvvdEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEF- 116
Cdd:COG4942 35 EIAELEKELAALKK-------EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELa 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 117 --------HQNQDKIMAKLTNEDSQ------------NRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGE 176
Cdd:COG4942 108 ellralyrLGRQPPLALLLSPEDFLdavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720388026 177 YGNSGIMDE----VDELRKRVLDMEGKDEELIKMEEQCRDLNKRLEKE 220
Cdd:COG4942 188 AALEALKAErqklLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
60-585 |
7.73e-09 |
|
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: 59.74 E-value: 7.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 60 QQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKiMAKLTNEDSQNRQLRQ 139
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEK-KDHLTKELEDIKMSLQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 140 KLAALSRQIDE-LEETNRSLRKAEEELQDIKDKINKGEYGNSGImdeVDELRKRVLDMEgkdeELIKMEEQcrdlnkRLE 218
Cdd:pfam05483 307 RSMSTQKALEEdLQIATKTICQLTEEKEAQMEELNKAKAAHSFV---VTEFEATTCSLE----ELLRTEQQ------RLE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 219 KETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEI 298
Cdd:pfam05483 374 KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIH 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 299 TLKDDLTKLKTLTVMLVDERKTM-----SEKLKQTEdkLQSTTSQLQAEQNKVTTVTEKLIEETK--------------R 359
Cdd:pfam05483 454 DLEIQLTAIKTSEEHYLKEVEDLkteleKEKLKNIE--LTAHCDKLLLENKELTQEASDMTLELKkhqediinckkqeeR 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 360 ALKSKTDAEEK-------MYSVTKE----RDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDFVKNKLNQdsSKS 428
Cdd:pfam05483 532 MLKQIENLEEKemnlrdeLESVREEfiqkGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENK--NKN 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 429 TAALHQENNKIKELSQeVENLKLKLKDMKA--IEDDLMKTEDEYETLERRYANERDKAQfLSQELEHAKMELAKYKLAEK 506
Cdd:pfam05483 610 IEELHQENKALKKKGS-AENKQLNAYEIKVnkLELELASAKQKFEEIIDNYQKEIEDKK-ISEEKLLEEVEKAKAIADEA 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 507 TessheqwlfrRLQEE-EAKSGHLSREVDALKEK-IHEYmatEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTKE 584
Cdd:pfam05483 688 V----------KLQKEiDKRCQHKIAEMVALMEKhKHQY---DKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAE 754
|
.
gi 1720388026 585 L 585
Cdd:pfam05483 755 L 755
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
179-492 |
1.22e-08 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 58.79 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 179 NSGIMdEVDELRKrvldmEGKDEELIKMEEQCRDLNKRLEK-ETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQEcys 257
Cdd:PRK05771 27 ELGVV-HIEDLKE-----ELSNERLRKLRSLLTKLSEALDKlRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEK--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 258 lkcnLEKEkmtTKQLSEELESLNARIKELEAIESRLEKteitlkddltkLKTLTVMLVDERKtmseklkqtedklqstts 337
Cdd:PRK05771 98 ----IEKE---IKELEEEISELENEIKELEQEIERLEP-----------WGNFDLDLSLLLG------------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 338 qlqaeqNKVTTVTEKLIEETKralksktdaeekmYSVTKERDDLRNKLKAEEEKGHDLLSkVTILKNRLQSLEAI--EKD 415
Cdd:PRK05771 142 ------FKYVSVFVGTVPEDK-------------LEELKLESDVENVEYISTDKGYVYVV-VVVLKELSDEVEEElkKLG 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720388026 416 FVKNKLNqDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYetlerrYANERDKAQFLSQELE 492
Cdd:PRK05771 202 FERLELE-EEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY------LEIELERAEALSKFLK 271
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
99-506 |
1.67e-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: 58.49 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 99 EQKATRLEKELQTQTTEFHQNQDKI----------MAKLTNEDSQNRQLRQKLAALSRQI----DELEETNRSLRKAEEE 164
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELknldknlnkdEEKINNSNNKIKILEQQIKDLNDKLkknkDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 165 LQDIKDKINKGEygnsgimDEVDELRKrvldmegkdeELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKL 244
Cdd:TIGR04523 112 IKNDKEQKNKLE-------VELNKLEK----------QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 245 EDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEK 324
Cdd:TIGR04523 175 LNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 325 LKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAE---------------EKMYSVTKERDDLRNKLKAEE 389
Cdd:TIGR04523 255 LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnqkeqdwnkelkSELKNQEKKLEEIQNQISQNN 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 390 EKGHDLLSKVTILKNRLQSLEAiekdfVKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDM-----------KA 458
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSES-----ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLeskiqnqeklnQQ 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1720388026 459 IEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKLAEK 506
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
200-575 |
1.69e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 200 DEELIKMEEQCRDLNKRLEKETVQS------KDFKLEVDKLSVRITALEKLEdaldkskqecysLKCNLEKEKMTTKQLS 273
Cdd:TIGR02168 185 RENLDRLEDILNELERQLKSLERQAekaeryKELKAELRELELALLVLRLEE------------LREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 274 EELESLNARIKELEA--IESRLEKTEitLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQsttsQLQAEQNKVTTVTE 351
Cdd:TIGR02168 253 EELEELTAELQELEEklEELRLEVSE--LEEEIEELQKELYALANEISRLEQQKQILRERLA----NLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 352 KLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEaiekdfvknklnqdsskstAA 431
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR-------------------SK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 432 LHQENNKIKELSQEVENLKLKLKDmkaIEDDLMKTEDEYETLERRYanERDKAQFLSQELEHAKMELAKyklAEKTESSH 511
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLER---LEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELEE---LQEELERL 459
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720388026 512 EQWLfRRLQEEEAKsghLSREVDALKEKIHEYMATEDLICHLQGDHSLLQKKLNQQENRNRDLG 575
Cdd:TIGR02168 460 EEAL-EELREELEE---AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
39-523 |
2.34e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.13 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 39 IKTLKEELTKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSAKEtqgkLALAEARAQEEEQKATrlEKELQTQTTEFhq 118
Cdd:TIGR00606 442 IELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERE----LSKAEKNSLTETLKKE--VKSLQNEKADL-- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 119 nqdkimakltneDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEG 198
Cdd:TIGR00606 514 ------------DRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHS 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 199 KDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALE-KLEDALDKSKQECY--SLKCNLEKEKMTTKQLSEE 275
Cdd:TIGR00606 582 KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEdKLFDVCGSQDEESDleRLKEEIEKSSKQRAMLAGA 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 276 LESLNARIKELEAIES-------RLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTT 348
Cdd:TIGR00606 662 TAVYSQFITQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 349 VtEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDFVKNKLNQDSSKS 428
Cdd:TIGR00606 742 K-EKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDL 820
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 429 TAALHQENNKIKE-------LSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAK- 500
Cdd:TIGR00606 821 DRTVQQVNQEKQEkqheldtVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSl 900
|
490 500
....*....|....*....|....*.
gi 1720388026 501 ---YKLAEKTESSHEQWLFRRLQEEE 523
Cdd:TIGR00606 901 ireIKDAKEQDSPLETFLEKDQQEKE 926
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
40-381 |
4.00e-08 |
|
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: 57.67 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 40 KTLKEELTKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQN 119
Cdd:pfam02463 662 SEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLL 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 120 QDKIMAKLTNEDSQNRQLRQKLA----ALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLD 195
Cdd:pfam02463 742 KQKIDEEEEEEEKSRLKKEEKEEekseLSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQ 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 196 MEGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEE 275
Cdd:pfam02463 822 LLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 276 LESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIE 355
Cdd:pfam02463 902 LEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE 981
|
330 340
....*....|....*....|....*.
gi 1720388026 356 ETKRALKSKTDAEEKMYSVTKERDDL 381
Cdd:pfam02463 982 EFEEKEERYNKDELEKERLEEEKKKL 1007
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
139-550 |
4.26e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 139 QKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEygnsgimDEVDELRKRVLDMEgKDEELIKMEEQCRDLNKRLE 218
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELE-------AELEELREELEKLE-KLLQLLPLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 219 KETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNL-EKEKMTTKQLSEELESLNARIKELEAIESRLEKTE 297
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 298 ITLKDDLTKLKTLTVMLVDERKTMSEK-----------LKQTEDKLQSTTSQLQA--------------EQNKVTTVTEK 352
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGvlflvlgllallflLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 353 LIEETkRALKSKTDAEEKMYSVTKERDDLRNKLKAEE--------EKGHDLLSKVTILKNRLQsLEAIEKDFVK--NKLN 422
Cdd:COG4717 303 EAEEL-QALPALEELEEEELEELLAALGLPPDLSPEEllelldriEELQELLREAEELEEELQ-LEELEQEIAAllAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 423 QDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEyETLERRYANERDKAQFLSQELEHAKMELAKYK 502
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-EELEEELEELEEELEELEEELEELREELAELE 459
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1720388026 503 LA-EKTESSHEqwLFRRLQEEEaksgHLSREVDALKEKIHEYMATEDLI 550
Cdd:COG4717 460 AElEQLEEDGE--LAELLQELE----ELKAELRELAEEWAALKLALELL 502
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
37-603 |
8.36e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.52 E-value: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 37 KRIKTLKEELTKLKSFAL---MVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQT 113
Cdd:pfam02463 205 QAKKALEYYQLKEKLELEeeyLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQ 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 114 TEfhqNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKD---KINKGEYGNSGIM-DEVDEL 189
Cdd:pfam02463 285 EE---ELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEeleKELKELEIKREAEeEEEEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 190 RKRVLDMEGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTT 269
Cdd:pfam02463 362 EKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 270 KQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMS-EKLKQTEDKLQSTTSQLQAEQNKVTT 348
Cdd:pfam02463 442 KQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKlEERSQKESKARSGLKVLLALIKDGVG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 349 VTEKLIEETKRALKSKTDAEEKMYSVTkeRDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEaIEKDFVKNKLNQDSSKS 428
Cdd:pfam02463 522 GRIISAHGRLGDLGVAVENYKVAISTA--VIVEVSATADEVEERQKLVRALTELPLGARKLR-LLIPKLKLPLKSIAVLE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 429 TAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTedeyeTLERRYANERDKAQFLSQELEHAKMELAKYKLAEKTE 508
Cdd:pfam02463 599 IDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTK-----LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTK 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 509 SSHE-QWLFRRLQEEEAKSGHLSREVDALKEKIHEymATEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTKELER 587
Cdd:pfam02463 674 ELLEiQELQEKAESELAKEEILRRQLEIKKKEQRE--KEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEE 751
|
570
....*....|....*.
gi 1720388026 588 YRHFSKSLRPSLNERR 603
Cdd:pfam02463 752 EEKSRLKKEEKEEEKS 767
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
88-360 |
9.06e-08 |
|
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: 55.54 E-value: 9.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 88 LALAEARAQEEEQKAtrLEKELQtqttEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEetnRSLRKAEEELQD 167
Cdd:COG4942 10 LLALAAAAQADAAAE--AEAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---RRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 168 IKDKINKGEygnsgimDEVDELRKRvldmegkdeelikMEEQCRDLNKRLEKETVQSKDFKLEVdklsvritaLEKLEDA 247
Cdd:COG4942 81 LEAELAELE-------KEIAELRAE-------------LEAQKEELAELLRALYRLGRQPPLAL---------LLSPEDF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 248 LDKSKqecyslkcNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVML---VDERKTMSEK 324
Cdd:COG4942 132 LDAVR--------RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALealKAERQKLLAR 203
|
250 260 270
....*....|....*....|....*....|....*.
gi 1720388026 325 LKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRA 360
Cdd:COG4942 204 LEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
98-542 |
9.99e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 9.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 98 EEQKATRLEKELQTQTTEFHQNQDKIMAKLTN---EDSQNRQLRQKLAALSRQIDELEETnRSLRKAEEELQDIKDKink 174
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETgkaEEARKAEEAKKKAEDARKAEEARKA-EDARKAEEARKAEDAK--- 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 175 geygNSGIMDEVDELRKrvLDMEGKDEELIKMEEQCRDLNKRLEKETVQSKDF-KLEVDKLSVRITALEKLEDALDKSKQ 253
Cdd:PTZ00121 1153 ----RVEIARKAEDARK--AEEARKAEDAKKAEAARKAEEVRKAEELRKAEDArKAEAARKAEEERKAEEARKAEDAKKA 1226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 254 ECYSlKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDdltklktltvmlvdERKTMSEKLKQTEDKLQ 333
Cdd:PTZ00121 1227 EAVK-KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA--------------EEARKADELKKAEEKKK 1291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 334 STTSQLQAEQNKVTTVTEKlIEETKRALKSKTDAEEkmysVTKERDDLrnKLKAEEEKGHDLLSKVTiLKNRLQSLEAIE 413
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKK-AEEAKKADEAKKKAEE----AKKKADAA--KKKAEEAKKAAEAAKAE-AEAAADEAEAAE 1363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 414 KDFVKNKLNQDSSKSTAalhQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLE--RRYANERDKAQFLSQEL 491
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKA---DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADeaKKKAEEKKKADEAKKKA 1440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1720388026 492 EHA-KMELAKYKLAE--KTESSHEQWLFRRLQEEEAKSGHLSREVDALKEKIHE 542
Cdd:PTZ00121 1441 EEAkKADEAKKKAEEakKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE 1494
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
261-499 |
1.36e-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: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 261 NLEKEKMTTKQLSEELEslnariKELEAIESRLEKTEITLKDdlTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQ 340
Cdd:COG3206 165 NLELRREEARKALEFLE------EQLPELRKELEEAEAALEE--FRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 341 AEQNKVTTVTEKLieETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAiekdfvknK 420
Cdd:COG3206 237 EAEARLAALRAQL--GSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA--------Q 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720388026 421 LNQDSSKSTAALHQEnnkIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELA 499
Cdd:COG3206 307 LQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
162-587 |
1.47e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 162 EEELQDIKDKINKGEYGNSGI-MDEVDELRKRVLDMEGKDEELIKMEEQCRDLNKRLEketvqskDFKLEVDKLSVRITA 240
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELnLKELKELEEELKEAEEKEEEYAELQEELEELEEELE-------ELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 241 LEKLEDALDKSKQecyslkcnLEKEKMTTKQLSEELESLNARIKELEAIESRLEKteitLKDDLTKLKTltvmlvDERKT 320
Cdd:COG4717 121 LEKLLQLLPLYQE--------LEALEAELAELPERLEELEERLEELRELEEELEE----LEAELAELQE------ELEEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 321 MSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLieETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEE---------- 390
Cdd:COG4717 183 LEQLSLATEEELQDLAEELEELQQRLAELEEEL--EEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaalla 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 391 ---KGHDLLSKVTILKNRLQSLEAI------EKDFVKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIED 461
Cdd:COG4717 261 llgLGGSLLSLILTIAGVLFLVLGLlallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 462 DLMKTEDEYETLERRYANERDKAQFlsQELEHAKMELAKYKLAEkTESSHEQWL--FRRLQEEEAKSGHLSREVDALKEK 539
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQL--EELEQEIAALLAEAGVE-DEEELRAALeqAEEYQELKEELEELEEQLEELLGE 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1720388026 540 IHEYMATEDLichlqgdhSLLQKKLNQQENRNRDLGREIENLTKELER 587
Cdd:COG4717 418 LEELLEALDE--------EELEEELEELEEELEELEEELEELREELAE 457
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
230-542 |
1.90e-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: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 230 EVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEkmtTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKT 309
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEE---LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 310 LTVMLVDERKTMSEKLKQTEDKLQsttsQLQAEQNKVTTVTEKLIEETKrALKSKTDAEEKMYSVTKER-DDLRNKLKAE 388
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELA----EAEAEIEELEAQIEQLKEELK-ALREALDELRAELTLLNEEaANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 389 EEKGHDllsKVTILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQEnnKIKELSQEVENLKLKLKDMKAIEDDLMKTED 468
Cdd:TIGR02168 830 ERRIAA---TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES--ELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 469 EYET----LERRYANERDKAQFLSQELEHAKMELA--KYKLAEKTESSHEQwLFRRLQEEEAKSGHLSREVDALKEKIHE 542
Cdd:TIGR02168 905 ELESkrseLRRELEELREKLAQLELRLEGLEVRIDnlQERLSEEYSLTLEE-AEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
38-612 |
3.35e-07 |
|
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: 54.26 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 38 RIKTLKEELTKLKSfalmvvdEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQtqttEFH 117
Cdd:TIGR04523 69 KINNSNNKIKILEQ-------QIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKK----ENK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 118 QNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELE----ETNRSLRKAEEELQDIKDKINKGEYGNSGI---MDEVDELR 190
Cdd:TIGR04523 138 KNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELEnelnLLEKEKLNIQKNIDKIKNKLLKLELLLSNLkkkIQKNKSLE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 191 KRVLDME------------------GKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLedaLDKSK 252
Cdd:TIGR04523 218 SQISELKkqnnqlkdniekkqqeinEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ---LNQLK 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 253 QECYSLkcNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKL 332
Cdd:TIGR04523 295 SEISDL--NNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 333 Q-----------------STTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDL 395
Cdd:TIGR04523 373 EklkkenqsykqeiknleSQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 396 LSKVTILKNRLQSLEAIEKDFVK--NKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYET- 472
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRsiNKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESe 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 473 ---LERRYANERDKAQFLSQELEHAKMELAKYKLAEKTESSHEQW--LFRRLQEEEAKSGHLSREVDALKEKIHEYMATE 547
Cdd:TIGR04523 533 kkeKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQksLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI 612
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720388026 548 dlichlqgdhSLLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSLNERRISDPQVFSK 612
Cdd:TIGR04523 613 ----------SSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKK 667
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
58-622 |
4.23e-07 |
|
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: 54.20 E-value: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 58 DEQQRLTAQLALQRQKIQALTTsaketQGKLALAEARAQEEEQKATRLEKELQTQ------------------------- 112
Cdd:TIGR00618 226 KELKHLREALQQTQQSHAYLTQ-----KREAQEEQLKKQQLLKQLRARIEELRAQeavleetqerinrarkaaplaahik 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 113 -TTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKgEYGNSGIMDEVDELRK 191
Cdd:TIGR00618 301 aVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEV-ATSIREISCQQHTLTQ 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 192 RVLDMEGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQEC-YSLKCNLEKEKMTTK 270
Cdd:TIGR00618 380 HIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCaAAITCTAQCEKLEKI 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 271 QLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVM--LVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVT- 347
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAq 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 348 ------TVTEKLIEETKRALKSKTDAEEKMYSVTKeRDDLRNKLKAEEEKGH---DLLSKVTILKNRLQSLEAIEKDFVK 418
Cdd:TIGR00618 540 letseeDVYHQLTSERKQRASLKEQMQEIQQSFSI-LTQCDNRSKEDIPNLQnitVRLQDLTEKLSEAEDMLACEQHALL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 419 NKLNQDSSKSTAALHQEnNKIKELSQE---VENLKLKLKDMKAIEDDLMKTEDEYETLERRyANERDKAQFLSQELEHAK 495
Cdd:TIGR00618 619 RKLQPEQDLQDVRLHLQ-QCSQELALKltaLHALQLTLTQERVREHALSIRVLPKELLASR-QLALQKMQSEKEQLTYWK 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 496 MELAKYKLAEKTESSHEQWLFRRLQEEEAKSG----HLSREVDALKEKIHEYMATED-LICHLQGDHSLLQKKLNQQENR 570
Cdd:TIGR00618 697 EMLAQCQTLLRELETHIEEYDREFNEIENASSslgsDLAAREDALNQSLKELMHQARtVLKARTEAHFNNNEEVTAALQT 776
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1720388026 571 N---RDLGREIENLTKELERYRHFSKSLRPSLNERRISDPQVFSKEVQTEAADSE 622
Cdd:TIGR00618 777 GaelSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEE 831
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
87-296 |
5.15e-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: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 87 KLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMA-----KLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKA 161
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaEYSWDEIDVASAEREIAELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 162 EEELQDIKDKINKGEygnsgimDEVDELRKRvldMEGKDEELIKMEEQCRDLNKRLEKETvqskdfklEVDKLSVRITAL 241
Cdd:COG4913 691 EEQLEELEAELEELE-------EELDELKGE---IGRLEKELEQAEEELDELQDRLEAAE--------DLARLELRALLE 752
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720388026 242 EKLEDALDKskqecyslkcnlEKEKMTTKQLSEELESLNARIKELeaiESRLEKT 296
Cdd:COG4913 753 ERFAAALGD------------AVERELRENLEERIDALRARLNRA---EEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
270-486 |
6.03e-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: 52.84 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 270 KQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTV 349
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 350 TEKLIEETKRALK--------------SKTDAEEKMY---SVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAi 412
Cdd:COG4942 103 KEELAELLRALYRlgrqpplalllspeDFLDAVRRLQylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLA- 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720388026 413 EKDFVKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQF 486
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
38-391 |
6.21e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 6.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 38 RIKTLKEELTKLKSF--ALMVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTE 115
Cdd:COG4717 110 ELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 116 FHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEEtNRSLRKAEEELQDIKDKINKGEY---------GNSGIMDEV 186
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLllliaaallALLGLGGSL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 187 DELRKRVLDM------------EGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQE 254
Cdd:COG4717 269 LSLILTIAGVlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 255 CYSLKCNLEK--EKMTTKQLSEELESL--NARIKELEAIESRLEKTEiTLKDDLTKLKTLTVMLVDERKTMSEKLKQT-- 328
Cdd:COG4717 349 LQELLREAEEleEELQLEELEQEIAALlaEAGVEDEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALde 427
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720388026 329 ---EDKLQSTTSQLQAEQNKVTTVTEKL--IEETKRALKSKTDAEEKMYsvtkERDDLRNKLKAEEEK 391
Cdd:COG4717 428 eelEEELEELEEELEELEEELEELREELaeLEAELEQLEEDGELAELLQ----ELEELKAELRELAEE 491
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
70-385 |
9.22e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.87 E-value: 9.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 70 QRQKIQALTtSAKETQGKLALAEAR---AQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSR 146
Cdd:pfam01576 762 RKQRAQAVA-AKKKLELDLKELEAQidaANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEA 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 147 QIDELEE----TNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEgkdEELIKMEEQCRDLNKRLEKETV 222
Cdd:pfam01576 841 ELLQLQEdlaaSERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLE---EELEEEQSNTELLNDRLRKSTL 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 223 QSKDFKLEvdkLSVRITALEKLEDALDKSKQECYSLKCNLE--------KEKMTTKQLSEEL----ESLNARIKELEAIE 290
Cdd:pfam01576 918 QVEQLTTE---LAAERSTSQKSESARQQLERQNKELKAKLQemegtvksKFKSSIAALEAKIaqleEQLEQESRERQAAN 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 291 SRLEKTEITLKDdltklktlTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEK 370
Cdd:pfam01576 995 KLVRRTEKKLKE--------VLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATES 1066
|
330
....*....|....*
gi 1720388026 371 MYSVTKERDDLRNKL 385
Cdd:pfam01576 1067 NESMNREVSTLKSKL 1081
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
93-599 |
1.16e-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: 52.44 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 93 ARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKI 172
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELEL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 173 NKGEYGNSGIMDEVDELRKRVLDMEGKDEELIKMEEQCRDLNKR---LEKETVQSKDFKLEVDKLSVRITALEKLEDALD 249
Cdd:pfam05557 128 QSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRikeLEFEIQSQEQDSEIVKNSKSELARIPELEKELE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 250 KSKQECYSLKCNLEKEKMttkqLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMseklkQTE 329
Cdd:pfam05557 208 RLREHNKHLNENIENKLL----LKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNL-----RSP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 330 DKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSL 409
Cdd:pfam05557 279 EDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGY 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 410 EAIEKDFVKNKLNQDSSKstaalhQENNKIKELSQEVENLKLKLKDMKAieddlmktedEYETLERRYANERDKAQFLSQ 489
Cdd:pfam05557 359 RAILESYDKELTMSNYSP------QLLERIEEAEDMTQKMQAHNEEMEA----------QLSVAEEELGGYKQQAQTLER 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 490 ELEhakmelakyklaektessheqwlFRRLQEEEAKSGHLSREVDALKEKIHEYMAT-----------EDLICH--LQGD 556
Cdd:pfam05557 423 ELQ-----------------------ALRQQESLADPSYSKEEVDSLRRKLETLELErqrlreqknelEMELERrcLQGD 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1720388026 557 HSL-----LQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSL 599
Cdd:pfam05557 480 YDPkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDL 527
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
38-581 |
1.16e-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: 52.66 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 38 RIKTLKEELTKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSAKET-QGKLALAEARAQEEEQKATRLEKELQTQTTEF 116
Cdd:TIGR00618 315 ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHeVATSIREISCQQHTLTQHIHTLQQQKTTLTQK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 117 HQNQDKIMAKLTNE-------DSQNRQLRQKLAALSRQIDELEETNRSLRKA-EEELQDIKDKI---NKGEYGnsgiMDE 185
Cdd:TIGR00618 395 LQSLCKELDILQREqatidtrTSAFRDLQGQLAHAKKQQELQQRYAELCAAAiTCTAQCEKLEKihlQESAQS----LKE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 186 VDELRKRVLDMEGKDEELIKMEEQCRDLNKRLEKETVQS-------KDFKLEVDKLSVRITALE----KLEDALDKSKQE 254
Cdd:TIGR00618 471 REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGScihpnpaRQDIDNPGPLTRRMQRGEqtyaQLETSEEDVYHQ 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 255 CYSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQS 334
Cdd:TIGR00618 551 LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDV 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 335 TTSQLQAEQN---KVTTVTEKLI-----EETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRL 406
Cdd:TIGR00618 631 RLHLQQCSQElalKLTALHALQLtltqeRVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELE 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 407 QSLEAIEKDFvkNKLNQDSSKSTAALHQENNKIKELSQEVENLK------LKLKDMKAIEDDLM--KTEDEYETLERRYA 478
Cdd:TIGR00618 711 THIEEYDREF--NEIENASSSLGSDLAAREDALNQSLKELMHQArtvlkaRTEAHFNNNEEVTAalQTGAELSHLAAEIQ 788
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 479 NERDKAQFLSQELehakmelakyklaEKTESSHEQWLFRRLQEEEAKSGHLSREVDALKEKIHEYMATEDLICHLQGDHS 558
Cdd:TIGR00618 789 FFNRLREEDTHLL-------------KTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYE 855
|
570 580
....*....|....*....|...
gi 1720388026 559 LLQKKLNQQENRNRDLGREIENL 581
Cdd:TIGR00618 856 ECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
38-587 |
2.09e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 38 RIKTLKEELTKLKSFALMVVDEQQRLtaQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKAT-------------- 103
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEARLDALREELDeleaqirgnggdrl 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 104 --------RLEKELQTQTTEFHQNQDKI-MAKLTNEDS------QNRQLRQKLAALSRQIDELE----ETNRSLRKAEEE 164
Cdd:COG4913 341 eqlereieRLERELEERERRRARLEALLaALGLPLPASaeefaaLRAEAAALLEALEEELEALEealaEAEAALRDLRRE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 165 LQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGKDE-------ELIKMEEQCRDLNKRLEK------------------ 219
Cdd:COG4913 421 LRELEAEIASLERRKSNIPARLLALRDALAEALGLDEaelpfvgELIEVRPEEERWRGAIERvlggfaltllvppehyaa 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 220 --ETVQSKDFKLEVDKLSVRITALEKLEDALDKSkqecySLkcnleKEKMTTKQ--LSEELESLNARIKELEAIES---- 291
Cdd:COG4913 501 alRWVNRLHLRGRLVYERVRTGLPDPERPRLDPD-----SL-----AGKLDFKPhpFRAWLEAELGRRFDYVCVDSpeel 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 292 RLEKTEITL------------KDDLTKLKTLTVMLVDER---KTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLieE 356
Cdd:COG4913 571 RRHPRAITRagqvkgngtrheKDDRRRIRSRYVLGFDNRaklAALEAELAELEEELAEAEERLEALEAELDALQERR--E 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 357 TKRALKSKTDAEEKMYSVTKERDDLRNKLkAEEEKGHDLLSKvtiLKNRLQSLEAIEKDFVKnklnqdsskstaALHQEN 436
Cdd:COG4913 649 ALQRLAEYSWDEIDVASAEREIAELEAEL-ERLDASSDDLAA---LEEQLEELEAELEELEE------------ELDELK 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 437 NKIKELSQEVENLKLKLKDMKAIEDDL--MKTEDEYETLERRYAN------ERDKAQFLSQELEHAKMELAkyKLAEKTE 508
Cdd:COG4913 713 GEIGRLEKELEQAEEELDELQDRLEAAedLARLELRALLEERFAAalgdavERELRENLEERIDALRARLN--RAEEELE 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 509 SSHEQwlFRRLQEEEAksGHLSREVDALKE--KIHEYMATEDLICHlqgdhsllQKKLNQQENRNrdLGREIENLTKELE 586
Cdd:COG4913 791 RAMRA--FNREWPAET--ADLDADLESLPEylALLDRLEEDGLPEY--------EERFKELLNEN--SIEFVADLLSKLR 856
|
.
gi 1720388026 587 R 587
Cdd:COG4913 857 R 857
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
285-581 |
3.02e-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: 51.22 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 285 ELEAIESRLEKTEITLKDDLTKLKTLTvmlvDERKTmSEKLKQTEDKLQSTTSQLQAEQnkvttvTEKLIEETKRALKSK 364
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLR----REREK-AERYQALLKEKREYEGYELLKE------KEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 365 TDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVtilkNRLQSLEAIEkdfVKNKLnqdsSKSTAALHQENNKIKELSQ 444
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI----KDLGEEEQLR---VKEKI----GELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 445 EVENLKLKLKDmkaIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKyklaektessheqwLFRRLQEEEA 524
Cdd:TIGR02169 316 ELEDAEERLAK---LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED--------------LRAELEEVDK 378
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720388026 525 KSGHLSREVDALKEKIHEYmatEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENL 581
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKL---KREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
96-601 |
3.44e-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: 50.62 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 96 QEEEQKATRLEKELQTQTT--EFHQNQDKIMAKltnedsqnrqlrqKLAALSRQIDELEETNRSLR--KAEEELQDIKDK 171
Cdd:pfam06160 28 QEELSKVKKLNLTGETQEKfeEWRKKWDDIVTK-------------SLPDIEELLFEAEELNDKYRfkKAKKALDEIEEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 172 INKGEygnsgimDEVDELRKRVLDMEGKDEELIKMEEQCRDLNKRLeKETVQSKDFKLEvdklsvriTALEKLEDALDK- 250
Cdd:pfam06160 95 LDDIE-------EDIKQILEELDELLESEEKNREEVEELKDKYREL-RKTLLANRFSYG--------PAIDELEKQLAEi 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 251 ----SKQECYSLKCNLEKEKMTTKQLSEELESLNARIkelEAIESRLEKTEITLKDDLTKLK-TLTVMLVD----ERKTM 321
Cdd:pfam06160 159 eeefSQFEELTESGDYLEAREVLEKLEEETDALEELM---EDIPPLYEELKTELPDQLEELKeGYREMEEEgyalEHLNV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 322 SEKLKQTEDKLQSTTSQLqaEQNKVTTVtEKLIEETKRALKSKTDAEEKMY----SVTKERDDLRNKLKAEEEKGHDLLS 397
Cdd:pfam06160 236 DKEIQQLEEQLEENLALL--ENLELDEA-EEALEEIEERIDQLYDLLEKEVdakkYVEKNLPEIEDYLEHAEEQNKELKE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 398 KVTILK-------NRLQSLEAIEKDFvkNKLNQDSSKSTAALHqenNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEY 470
Cdd:pfam06160 313 ELERVQqsytlneNELERVRGLEKQL--EELEKRYDEIVERLE---EKEVAYSELQEELEEILEQLEEIEEEQEEFKESL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 471 ETLERRYANERDKAQFLSQELEHAKMELAKYKL--------AEKTESSHE-QWLFRRLQEEEAKSGHLSREVDALKEKIH 541
Cdd:pfam06160 388 QSLRKDELEAREKLDEFKLELREIKRLVEKSNLpglpesylDYFFDVSDEiEDLADELNEVPLNMDEVNRLLDEAQDDVD 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720388026 542 E-YMATEDLIchlqgDHSLLQKKLNQQENRnrdlgreienltkelerYRHFSKSLRPSLNE 601
Cdd:pfam06160 468 TlYEKTEELI-----DNATLAEQLIQYANR-----------------YRSSNPEVAEALTE 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
377-587 |
6.83e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 377 ERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAiEKDFVKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDM 456
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEA-ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 457 KAIEDDLMKTEDEYETLERRYANerdkaqfLSQELEHAKMELAKYKLAEKTESSHEQWLFRRLQEEEAKSGHLSREVDAL 536
Cdd:COG1196 312 RELEERLEELEEELAELEEELEE-------LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720388026 537 KEKIHEymatedlichLQGDHSLLQKKLNQQENRNRDLGREIENLTKELER 587
Cdd:COG1196 385 AEELLE----------ALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
105-326 |
1.28e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.86 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 105 LEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQD-IKDKINKGEYGNSGIM 183
Cdd:PHA02562 179 LNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDeLLNLVMDIEDPSAALN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 184 DEVDELRKRVLDMEGKDEElIKMEE----------QCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQ 253
Cdd:PHA02562 259 KLNTAAAKIKSKIEQFQKV-IKMYEkggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSK 337
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720388026 254 ECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAiESRLEKTEI-TLKDDLTKL---KTLTVMLVDERKTMSEKLK 326
Cdd:PHA02562 338 KLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA-EFVDNAEELaKLQDELDKIvktKSELVKEKYHRGIVTDLLK 413
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
39-606 |
1.59e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 39 IKTLKEELTKLKSfalmVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFhQ 118
Cdd:PRK01156 161 INSLERNYDKLKD----VIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDY-N 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 119 NQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIkdkINKGEYGNSGIMDEVDELRKRVLD--- 195
Cdd:PRK01156 236 NLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKI---INDPVYKNRNYINDYFKYKNDIENkkq 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 196 -MEGKDEELIKMEEQCRDLNKrLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSE 274
Cdd:PRK01156 313 iLSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 275 EL-ESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLvderktmsEKLKQTEDKLQSTTSQLQAeQNKVTTVTEKL 353
Cdd:PRK01156 392 FIsEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRI--------RALRENLDELSRNMEMLNG-QSVCPVCGTTL 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 354 IEETKRALKSktDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSkvtiLKNRLQSlEAIEKDFVKNKLNQDSSKSTAALH 433
Cdd:PRK01156 463 GEEKSNHIIN--HYNEKKSRLEEKIREIEIEVKDIDEKIVDLKK----RKEYLES-EEINKSINEYNKIESARADLEDIK 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 434 QENNKIKELSQEVENLKLKLKDMKaIEDDLMKTEDEYETLERRYA----NERDKAQFLSQELEHAKMELAKYKLAEKTES 509
Cdd:PRK01156 536 IKINELKDKHDKYEEIKNRYKSLK-LEDLDSKRTSWLNALAVISLidieTNRSRSNEIKKQLNDLESRLQEIEIGFPDDK 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 510 SHEQWLFRRLQEE-------EAKSGHLSREVDALKEKIHEYMATEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLT 582
Cdd:PRK01156 615 SYIDKSIREIENEannlnnkYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAK 694
|
570 580
....*....|....*....|....*.
gi 1720388026 583 KELERYRHFSKSLRPSLNE--RRISD 606
Cdd:PRK01156 695 ANRARLESTIEILRTRINElsDRIND 720
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
21-287 |
1.78e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 21 IDQETASQEKKEQEKEKRIKTLKEELTKLK--------SFALMVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAE 92
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEealndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 93 ARAQEEEQKATRLEKELQTQTTEFHQNQD-------KIMAKLTNEDSQNRQLRQKLAALSRQIDELEEtnrSLRKAEEEL 165
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIEnlngkkeELEEELEELEAALRDLESRLGDLKKERDELEA---QLRELERKI 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 166 QDIKdkinkgeygnsgimDEVDELRKRVLDMEGKDEELIKMEEQCRDLNKRLE---KETVQSKDFKLEVDKLSVRITALE 242
Cdd:TIGR02169 906 EELE--------------AQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipEEELSLEDVQAELQRVEEEIRALE 971
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1720388026 243 KLEDALDKSKQECYSLKCNLEKEKMTtkqLSEELESLNARIKELE 287
Cdd:TIGR02169 972 PVNMLAIQEYEEVLKRLDELKEKRAK---LEEERKAILERIEEYE 1013
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
39-595 |
1.94e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 39 IKTLKEELTKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQ 118
Cdd:pfam01576 14 LQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 119 NQdkimakltnedSQNRQLRQKLAALSRQIDELEETNRSLR----KAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVL 194
Cdd:pfam01576 94 LQ-----------NEKKKMQQHIQDLEEQLDEEEAARQKLQlekvTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 195 DME---GKDEELIKM--------EEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITAL-----------EKLEDALDKSK 252
Cdd:pfam01576 163 EFTsnlAEEEEKAKSlsklknkhEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLqeqiaelqaqiAELRAQLAKKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 253 QECYSLKCNLEKEKMTTKQLSEELESLNARIKELE-------AIESRLEKTEITLKDDLTKLKTLTVMLVD--------- 316
Cdd:pfam01576 243 EELQAALARLEEETAQKNNALKKIRELEAQISELQedleserAARNKAEKQRRDLGEELEALKTELEDTLDttaaqqelr 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 317 -ERKTMSEKLKQT-EDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHD 394
Cdd:pfam01576 323 sKREQEVTELKKAlEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 395 LLSKVTILKNRLQSLEA--IEKDFVKNKLNQDSSKS-------TAALHQENNKIKELSQEVENLKLKLKDMK-------- 457
Cdd:pfam01576 403 SEHKRKKLEGQLQELQArlSESERQRAELAEKLSKLqselesvSSLLNEAEGKNIKLSKDVSSLESQLQDTQellqeetr 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 458 ---AIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELA--KYKLAEKTESSHeqwlfrrlQEEEAKSgHLSRE 532
Cdd:pfam01576 483 qklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSdmKKKLEEDAGTLE--------ALEEGKK-RLQRE 553
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720388026 533 VDALKEKIHEYMATEDlichlqgdhsllqkKLNQQENRnrdLGREIENLTKELERYRHFSKSL 595
Cdd:pfam01576 554 LEALTQQLEEKAAAYD--------------KLEKTKNR---LQQELDDLLVDLDHQRQLVSNL 599
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
246-581 |
2.14e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 246 DALDKSKQecyslkcNLEKEKMTTKQLSEELESLNAR---IKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMS 322
Cdd:PRK11281 46 DALNKQKL-------LEAEDKLVQQDLEQTLALLDKIdrqKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 323 EK--LKQTEDKLQSTTSQLQAEQNKVTTVTEKLIeetkrALKSKTD-AEEKMYSVTKERDDLRNKLKAEEEKGHDLL-SK 398
Cdd:PRK11281 119 STlsLRQLESRLAQTLDQLQNAQNDLAEYNSQLV-----SLQTQPErAQAALYANSQRLQQIRNLLKGGKVGGKALRpSQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 399 VTILKNRLQSLEAiekdfvKNKLNQDSSKSTAALhQE---------NNKIKELSQEVENLKLKLKDMKAIEDDlmKTEDE 469
Cdd:PRK11281 194 RVLLQAEQALLNA------QNDLQRKSLEGNTQL-QDllqkqrdylTARIQRLEHQLQLLQEAINSKRLTLSE--KTVQE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 470 YETLERryANERDKAQFLSQELEHAKmELAKYkLAEKTESSHE---------QWLFRRLQEEEaksghlsrevdALKEKI 540
Cdd:PRK11281 265 AQSQDE--AARIQANPLVAQELEINL-QLSQR-LLKATEKLNTltqqnlrvkNWLDRLTQSER-----------NIKEQI 329
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1720388026 541 HEymatedlichLQGdhSL-LQKKLNQQENR------NRDLGREIENL 581
Cdd:PRK11281 330 SV----------LKG--SLlLSRILYQQQQAlpsadlIEGLADRIADL 365
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
18-525 |
2.23e-05 |
|
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: 48.50 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 18 KKLIDQETASQEKKEQEKEKRIKTLKEELTKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQE 97
Cdd:TIGR00606 572 KKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKS 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 98 EEQKA-----TRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQI-DELEETNRSLRKAEEELQDIKDK 171
Cdd:TIGR00606 652 SKQRAmlagaTAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLApDKLKSTESELKKKEKRRDEMLGL 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 172 INKGEYGNSGIMDEVDELRKRV----LDMEGKDEELIKMEEQCRDLNKRLEKETVQSKD------FKLEVDKLSVRITAL 241
Cdd:TIGR00606 732 APGRQSIIDLKEKEIPELRNKLqkvnRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDvtimerFQMELKDVERKIAQQ 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 242 EKLEDA--LDKSKQECYSLKCNLEKEKMTTKQLSEELESL----NARIKELEAIESRLEKTEITLKDDLTKLKTL---TV 312
Cdd:TIGR00606 812 AAKLQGsdLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLiqdqQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFeeqLV 891
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 313 MLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEE-- 390
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDdy 971
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 391 ---KGHDLLSKVTILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQEN-------NKIKELSQEVENLKLKLKDMKAIE 460
Cdd:TIGR00606 972 lkqKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNltlrkreNELKEVEEELKQHLKEMGQMQVLQ 1051
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720388026 461 --DDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKLAEKTESSHEQWLFRRLQEEEAK 525
Cdd:TIGR00606 1052 mkQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNK 1118
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
64-662 |
2.50e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 64 TAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQnqdKIMAKLTNEDSQNRQLRQKLAA 143
Cdd:pfam02463 178 LIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL---KLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 144 LSRQIDELEET--NRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDMEGKDEELIKMEEQcrdlNKRLEKET 221
Cdd:pfam02463 255 SSKQEIEKEEEklAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE----KKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 222 VQSKDFKLEvdklsvritaLEKLEDALDKSKQECYSLKCNLEKEKmttkqlseelesLNARIKELEAIESRLEKTEITLK 301
Cdd:pfam02463 331 KKEKEEIEE----------LEKELKELEIKREAEEEEEEELEKLQ------------EKLEQLEEELLAKKKLESERLSS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 302 DDLTKLKTLTVMLVDERKtmSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAE--------EKMYS 373
Cdd:pfam02463 389 AAKLKEEELELKSEEEKE--AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELekqelkllKDELE 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 374 VTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQENNKIKelsQEVENLKLKL 453
Cdd:pfam02463 467 LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD---LGVAVENYKV 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 454 KDMKAIEDDLMKTEDEYETLERRYANERDKAQF---LSQELEHAKMELAKYKLAEKTESSHEQWLFRRLQE--EEAKSGH 528
Cdd:pfam02463 544 AISTAVIVEVSATADEVEERQKLVRALTELPLGarkLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEadEDDKRAK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 529 LSREVDALKEKIHEYMATEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSLNERRISDPQ 608
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1720388026 609 VFSKEVQTEAADSEPPDYKSLIPLERAVINGQFYEENEDQDDDPNEEESVLSFR 662
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL 757
|
|
| DUF4407 |
pfam14362 |
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ... |
106-247 |
2.52e-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: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 106 EKELQTQTTEFHQN-QDKIMAKLTNE-DSQNRQLRQKLAALSRQIDELE-ETNRSLRKAEEEL-QDIKDKINKGEYGNSG 181
Cdd:pfam14362 105 EKEIDRELLEIQQEeADAAKAQLAAAyRARLAELEAQIAALDAEIDAAEaRLDALQAEARCELdGTPGTGTGVPGDGPVA 184
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720388026 182 --IMDEVDELRKRVLDMEGK-DEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDA 247
Cdd:pfam14362 185 ktKQAQLDAAQAELAALQAQnDARLAALRAELARLTAERAAARARSQAAIDGDDGLLARLEALNRLTTE 253
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
213-465 |
2.62e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 213 LNKRLEKE-TVQSKDFKLEVDKLSVRITALEKLEDALDK-SKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEaie 290
Cdd:PHA02562 171 LNKDKIRElNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKkNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLV--- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 291 srleKTEITLKDDLTKLKTLTVMLVDERKTMS--EKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRaLKSKTDAE 368
Cdd:PHA02562 248 ----MDIEDPSAALNKLNTAAAKIKSKIEQFQkvIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHS-LEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 369 EKMYSVTKERDDLRNKLkaeeekgHDLLSKVTILKNRLQSLEAIEKDFVK--NKLNQDSSKSTAALHQENNKIKELSQEV 446
Cdd:PHA02562 323 DELEEIMDEFNEQSKKL-------LELKNKISTNKQSLITLVDKAKKVKAaiEELQAEFVDNAEELAKLQDELDKIVKTK 395
|
250
....*....|....*....
gi 1720388026 447 ENLKLKlKDMKAIEDDLMK 465
Cdd:PHA02562 396 SELVKE-KYHRGIVTDLLK 413
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
406-610 |
2.79e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 406 LQSLEAIEKDFVKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQ 485
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 486 FLSQELEHAKMELAKYKLAEKTESSHEQWlfRRLQEEEAKSGHLSREVDALKEKIHEY------------MATEDLICHL 553
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERL--EELEERLEELRELEEELEELEAELAELqeeleelleqlsLATEEELQDL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720388026 554 QGDHSLLQKKLNQQENRNRDLGREIENLTKELERYrhfSKSLRPSLNERRISDPQVF 610
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQL---ENELEAAALEERLKEARLL 251
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
345-587 |
3.14e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 345 KVTTVTEKLIEETKRALKSKTDAEEkmysvtkeRDDLRNKLkaEEEKGHDLLSKVTILknrLQSLEAIEKDFvkNKLNQD 424
Cdd:TIGR02169 188 RLDLIIDEKRQQLERLRREREKAER--------YQALLKEK--REYEGYELLKEKEAL---ERQKEAIERQL--ASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 425 SSKSTAALHQENNKIKELSQEVENLKLKLKDMKaiEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKLA 504
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLG--EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 505 -EKTESSHEQwLFRRLQEEEAKSGHLSREVDALKEkihEYMATEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTK 583
Cdd:TIGR02169 331 iDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKE---ELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
....
gi 1720388026 584 ELER 587
Cdd:TIGR02169 407 ELDR 410
|
|
| CortBP2 |
pfam09727 |
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ... |
16-62 |
3.33e-05 |
|
Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.
Pssm-ID: 462860 [Multi-domain] Cd Length: 187 Bit Score: 45.67 E-value: 3.33e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720388026 16 RLKKLIDQETASQEKKEQEKEKRIKTLKEELTKLKSFALMVVDEQQR 62
Cdd:pfam09727 141 RLKQELEQEKAQQKRLEKELKKLLEKLEEELSKQKQIALLLVKERKR 187
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
38-589 |
3.81e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 38 RIKTLKEELTKLKSFALMVVD--EQQRLTAQLALQRQKIQALTTSAKETQgkLALAEARAQEEEQKATRLEKELQtqtte 115
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDarEQIELLEPIRELAERYAAARERLAELE--YLRAALRLWFAQRRLELLEAELE----- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 116 fhqnqdkimakltnedsqnrQLRQKLAALSRQIDELEETnrsLRKAEEELQDIKDKINkgeyGNSGimDEVDELRKrvlD 195
Cdd:COG4913 299 --------------------ELRAELARLEAELERLEAR---LDALREELDELEAQIR----GNGG--DRLEQLER---E 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 196 MEGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITA-LEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSE 274
Cdd:COG4913 347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAlLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 275 ELESLNAR--------IKELEAIESRLEKTEITLK--DDLTKLKTL----------------TVMLVDE-------RKTM 321
Cdd:COG4913 427 EIASLERRksniparlLALRDALAEALGLDEAELPfvGELIEVRPEeerwrgaiervlggfaLTLLVPPehyaaalRWVN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 322 SEKLK---QTEdKLQSTTSQLQAEQNKVTTVTEKL--------------------------IEETKRALKSKT------- 365
Cdd:COG4913 507 RLHLRgrlVYE-RVRTGLPDPERPRLDPDSLAGKLdfkphpfrawleaelgrrfdyvcvdsPEELRRHPRAITragqvkg 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 366 ---------------------DAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDfvknklnQD 424
Cdd:COG4913 586 ngtrhekddrrrirsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEY-------SW 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 425 SSKSTAALHQEnnkIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYK-L 503
Cdd:COG4913 659 DEIDVASAERE---IAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQdR 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 504 AEKTESSHEQWLFRRLQE----------EEAKSGHLSREVDALKEKIHEymATEDLIchlqgdhSLLQKKLNQQENRNRD 573
Cdd:COG4913 736 LEAAEDLARLELRALLEErfaaalgdavERELRENLEERIDALRARLNR--AEEELE-------RAMRAFNREWPAETAD 806
|
650
....*....|....*.
gi 1720388026 574 LGREIENLTKELERYR 589
Cdd:COG4913 807 LDADLESLPEYLALLD 822
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
38-518 |
4.61e-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: 47.42 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 38 RIKTLKEELTKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLalaEARAQEEEQKATRLEKELQTqttefh 117
Cdd:pfam15921 462 KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI---EATNAEITKLRSRVDLKLQE------ 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 118 qnqdkiMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIkdkinKGEYGNS--GIMDEVDELRKRVLD 195
Cdd:pfam15921 533 ------LQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQL-----VGQHGRTagAMQVEKAQLEKEIND 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 196 --MEGKDEELI--KMEEQCRDLNKRLEketvqskDFKLEVDKL----SVRITALEKLEDALDK-------SKQECYSLKC 260
Cdd:pfam15921 602 rrLELQEFKILkdKKDAKIRELEARVS-------DLELEKVKLvnagSERLRAVKDIKQERDQllnevktSRNELNSLSE 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 261 NLEKEKMTTKQLSEELESLNARIK-ELEAIESRLEKTEITLKD-----------DLTKLKTLT------------VMLVD 316
Cdd:pfam15921 675 DYEVLKRNFRNKSEEMETTTNKLKmQLKSAQSELEQTRNTLKSmegsdghamkvAMGMQKQITakrgqidalqskIQFLE 754
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 317 ERKTMSEK----LKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKG 392
Cdd:pfam15921 755 EAMTNANKekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQES 834
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 393 HDLLSKVTILKNRLQSLEAIEKDFVKNKL-----------NQDSSKSTAA-LHQENNKIKELSQE-VENLKLKLKDMKAI 459
Cdd:pfam15921 835 VRLKLQHTLDVKELQGPGYTSNSSMKPRLlqpasftrthsNVPSSQSTASfLSHHSRKTNALKEDpTRDLKQLLQELRSV 914
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720388026 460 -----EDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKLaeKTESSHEQWLFRR 518
Cdd:pfam15921 915 ineepTVQLSKAEDKGRAPSLGALDDRVRDCIIESSLRSDICHSSSNSL--QTEGSKSSETCSR 976
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
44-363 |
5.35e-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: 47.25 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 44 EELTKLKSfalMVVDEQQRLTAQ--LALQ-RQKIQALttsaKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQ 120
Cdd:COG3096 389 EEVDSLKS---QLADYQQALDVQqtRAIQyQQAVQAL----EKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELE 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 121 DKimakLTNEDSQNRQLRQKLAALSRQIDELEeTNRSLRKAEEELQDIKDKINkgeygnsgIMDEVDELRKRVLDMEGKD 200
Cdd:COG3096 462 QK----LSVADAARRQFEKAYELVCKIAGEVE-RSQAWQTARELLRRYRSQQA--------LAQRLQQLRAQLAELEQRL 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 201 EELIKMEEQCRDLNKRLEKEtVQSKDfklevdklsvritALEKLEDALDKSKQECYSLKCNLEKEKMTTKQlseELESLN 280
Cdd:COG3096 529 RQQQNAERLLEEFCQRIGQQ-LDAAE-------------ELEELLAELEAQLEELEEQAAEAVEQRSELRQ---QLEQLR 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 281 ARIKELEAIESRLekteITLKDDLTKLktltvmlvderktmSEKLKQTEDKLQSTTSQLQ--AEQNKVTTVTEKLIEETK 358
Cdd:COG3096 592 ARIKELAARAPAW----LAAQDALERL--------------REQSGEALADSQEVTAAMQqlLEREREATVERDELAARK 653
|
....*
gi 1720388026 359 RALKS 363
Cdd:COG3096 654 QALES 658
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
131-345 |
6.04e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 131 DSQNRQLRQKLAALSRQIDELEETnrsLRKAEEELQDIKDKINKGEygnsgimDEVDELRKRvldMEGKDEELIKMEEQC 210
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAE---LDALQAELEELNEEYNELQ-------AELEALQAE---IDKLQAEIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 211 RDLNKRLEKETVQSKDFKLEVDKLSV------------RITALEKLEDALDKSKQECYSLKCNLEKEKmttKQLSEELES 278
Cdd:COG3883 82 EERREELGERARALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKK---AELEAKLAE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720388026 279 LNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNK 345
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
122-514 |
8.22e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.97 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 122 KIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEE-LQDIKDKINKGEY-----GNSGIMDEVDELRKRVLD 195
Cdd:TIGR01612 483 KDIDENSKQDNTVKLILMRMKDFKDIIDFMELYKPDEVPSKNIiGFDIDQNIKAKLYkeieaGLKESYELAKNWKKLIHE 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 196 ----MEGKDEELIKMEEQCRDL-NKRLE--KETVQSKDFKLEVDklsvritalEKLEDALDKSK--QECYSLKCNLEKE- 265
Cdd:TIGR01612 563 ikkeLEEENEDSIHLEKEIKDLfDKYLEidDEIIYINKLKLELK---------EKIKNISDKNEyiKKAIDLKKIIENNn 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 266 -------KMTTKQLSEELESLNariKELEAIESRLEKTeitLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQ 338
Cdd:TIGR01612 634 ayidelaKISPYQVPEHLKNKD---KIYSTIKSELSKI---YEDDIDALYNELSSIVKENAIDNTEDKAKLDDLKSKIDK 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 339 LQAEQNKVTTVTEKL----IEETKRALkSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNrlqslEAIEK 414
Cdd:TIGR01612 708 EYDKIQNMETATVELhlsnIENKKNEL-LDIIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAK-----EKDEL 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 415 DFVKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKaqFLSQELEHa 494
Cdd:TIGR01612 782 NKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDK--FINFENNC- 858
|
410 420
....*....|....*....|
gi 1720388026 495 kmelakyklAEKTESSHEQW 514
Cdd:TIGR01612 859 ---------KEKIDSEHEQF 869
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
108-460 |
8.29e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 108 ELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNR----SLRKAEEELQDIKDkinkgEYGN--SG 181
Cdd:PRK01156 406 AIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcGTTLGEEKSNHIIN-----HYNEkkSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 182 IMDEVDELRKRVLDMEGKDEELIKMEEQCRDLN-KRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKC 260
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEiNKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKL 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 261 NLEKEKMTtkqlseELESLNARIK--ELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQ 338
Cdd:PRK01156 561 EDLDSKRT------SWLNALAVISliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNK 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 339 LqaeqnkvttvteKLIEETKRA---LKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVtilknrlqsleaiEKD 415
Cdd:PRK01156 635 Y------------NEIQENKILiekLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKS-------------RKA 689
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1720388026 416 FVKNKLNQDSSKSTAALHQENNKikELSQEVENLKLKLKDMKAIE 460
Cdd:PRK01156 690 LDDAKANRARLESTIEILRTRIN--ELSDRINDINETLESMKKIK 732
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
51-217 |
9.17e-05 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 46.39 E-value: 9.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 51 SFALMVVDeqQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMA---KL 127
Cdd:COG5283 2 QVILGAVD--KPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQagiDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 128 TNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINK-GEYGNSGI-------------MDEVDELR--K 191
Cdd:COG5283 80 RQLSAAQRRLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQRlAGAGAAAAaigaalaasvkpaIDFEDAMAdvA 159
|
170 180
....*....|....*....|....*.
gi 1720388026 192 RVLDMEGKDEELIKMEEQCRDLNKRL 217
Cdd:COG5283 160 ATVDLDKSSEQFKALGKQARELSAQT 185
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
38-301 |
1.02e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 38 RIKTLKEELTKLKsfalMVVDEQQRLTAQLALQRQKIqalttSAKETQGKLALAEARAQEEE-----QKATRLEKELQTQ 112
Cdd:PRK03918 474 KERKLRKELRELE----KVLKKESELIKLKELAEQLK-----ELEEKLKKYNLEELEKKAEEyeklkEKLIKLKGEIKSL 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 113 TTEFHQNQDkIMAKLTNEDSQNRQLRQKLAALSRQI--------DELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMD 184
Cdd:PRK03918 545 KKELEKLEE-LKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLKELEPFYNEYLELKDAEKELEREEKELKK 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 185 EVDELRKRVLDMEGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEvdKLSVRITALEKLEDALDKSKQECYSLKCNLEK 264
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL--ELSRELAGLRAELEELEKRREEIKKTLEKLKE 701
|
250 260 270
....*....|....*....|....*....|....*..
gi 1720388026 265 EKMTTKQLSEELESLNARIKELEAIESRLEKTEITLK 301
Cdd:PRK03918 702 ELEEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
36-604 |
1.09e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.12 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 36 EKRIKTLKEELTKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSA----KETQGKLALAEARAQEEEQKATRLEKELQT 111
Cdd:pfam02463 267 LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDeeklKESEKEKKKAEKELKKEKEEIEELEKELKE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 112 QTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRK 191
Cdd:pfam02463 347 LEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 192 RVLDMEGKDEELIkmEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQ 271
Cdd:pfam02463 427 EELEILEEEEESI--ELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESK 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 272 LSEELESLNARIKELEAIesRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDklqsttsqlqAEQNKVTTVTE 351
Cdd:pfam02463 505 ARSGLKVLLALIKDGVGG--RIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVE----------ERQKLVRALTE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 352 KLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEE-EKGHDLLSKVTILKNRLQSLEAIEKDFVKNKLNQDSSKSTA 430
Cdd:pfam02463 573 LPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKaTLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGV 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 431 ALHQENNKIKELSQEVENLKLKLkdmKAIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKLAEKtess 510
Cdd:pfam02463 653 SLEEGLAEKSEVKASLSELTKEL---LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLAD---- 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 511 heqwlfrRLQEEEAKSghlSREVDALKEKIHEYMATEDLICHLQGDHSLLQKKLNQQENRNRDLGREIENLTKELERyRH 590
Cdd:pfam02463 726 -------RVQEAQDKI---NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEK-EE 794
|
570
....*....|....
gi 1720388026 591 FSKSLRPSLNERRI 604
Cdd:pfam02463 795 KLKAQEEELRALEE 808
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
87-591 |
1.10e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.98 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 87 KLALAEARAQEEEQKATRLEKELQTQTT--EFHQNQDKIMAKltnedsqnrqlrqKLAALSRQIDELEETNRSLR--KAE 162
Cdd:PRK04778 38 KQELENLPVNDELEKVKKLNLTGQSEEKfeEWRQKWDEIVTN-------------SLPDIEEQLFEAEELNDKFRfrKAK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 163 EELQDIKDKINKGEygnsgimDEVDELRKRVLDMEGKDEELIKMEEQCRDLNKRLEKeTVQSKDFKLEVdklsvritALE 242
Cdd:PRK04778 105 HEINEIESLLDLIE-------EDIEQILEELQELLESEEKNREEVEQLKDLYRELRK-SLLANRFSFGP--------ALD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 243 KLEDALDKSKQEcYSLKCNLEKE------KMTTKQLSEELESLNARIKELEAIesrLEKTEITLKDDLTKLKTltvmlvD 316
Cdd:PRK04778 169 ELEKQLENLEEE-FSQFVELTESgdyveaREILDQLEEELAALEQIMEEIPEL---LKELQTELPDQLQELKA------G 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 317 ERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKL-IEETKRALKSKTDAEEKMYS-----------VTKERDDLRNK 384
Cdd:PRK04778 239 YRELVEEGYHLDHLDIEKEIQDLKEQIDENLALLEELdLDEAEEKNEEIQERIDQLYDilerevkarkyVEKNSDTLPDF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 385 LKAEEEKGHDLLSKVTILK-------NRLQSLEAIEKDFvkNKLNQDSSKSTAALHqenNKIKELSQEVENLKLKLKDMK 457
Cdd:PRK04778 319 LEHAKEQNKELKEEIDRVKqsytlneSELESVRQLEKQL--ESLEKQYDEITERIA---EQEIAYSELQEELEEILKQLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 458 AIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKL--------AEKTESSHE-QWLFRRLQEEEAKSGH 528
Cdd:PRK04778 394 EIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSNLpglpedylEMFFEVSDEiEALAEELEEKPINMEA 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720388026 529 LSREVDALKEKIHE-YMATEDLIchlqgDHSLLQKKLNQQENRNRDLGREIEN-LTKELERYRHF 591
Cdd:PRK04778 474 VNRLLEEATEDVETlEEETEELV-----ENATLTEQLIQYANRYRSDNEEVAEaLNEAERLFREY 533
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
131-296 |
1.13e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 131 DSQNRQLRQKLAALSRQIDELEET----NRSLRKAEEELQDIKDKINKGEygnsgimDEVDELRKRVLDMEGKDEELIKM 206
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDElaalEARLEAAKTELEDLEKEIKRLE-------LEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 207 EEQcRDLNKRLEKEtvqskdfKLEVDKLSVRI----TALEKLEDALDKSKQECYSLKCNLEKEKmttKQLSEELESLNAR 282
Cdd:COG1579 89 KEY-EALQKEIESL-------KRRISDLEDEIlelmERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAE 157
|
170
....*....|....
gi 1720388026 283 IKELEAIESRLEKT 296
Cdd:COG1579 158 LEELEAEREELAAK 171
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
94-513 |
1.45e-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: 45.77 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 94 RAQEEEQK-ATRLEKELQTQTTEFHQNQDKimakltNEDSQNRQLRQKLAALSRQIdeLEETNRSLRKAEEEL-QDIKDK 171
Cdd:NF033838 51 SGNESQKEhAKEVESHLEKILSEIQKSLDK------RKHTQNVALNKKLSDIKTEY--LYELNVLKEKSEAELtSKTKKE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 172 INKGeygNSGIMDEVDELRKRVLDMEGKDEELIKMEEQCRDLNKRlEKETVQSKDFKLEVDKLSVRITalekledaldKS 251
Cdd:NF033838 123 LDAA---FEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRR-NYPTNTYKTLELEIAESDVEVK----------KA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 252 KQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDL-TKLKTLTVMLVD--ERKTMSEKLKQ- 327
Cdd:NF033838 189 ELELVKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRAdAKLKEAVEKNVAtsEQDKPKRRAKRg 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 328 ------TEDKlqsttSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKerddlrnklKAEEEKGHDLLSKVTI 401
Cdd:NF033838 269 vlgepaTPDK-----KENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKK---------KAKDQKEEDRRNYPTN 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 402 LKNRLQsLEAIEKDFVKNKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEyetlERRYANER 481
Cdd:NF033838 335 TYKTLE-LEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEE----AKRKAAEE 409
|
410 420 430
....*....|....*....|....*....|..
gi 1720388026 482 DKAQFLSQELEHAKMELAKYKLAEKTESSHEQ 513
Cdd:NF033838 410 DKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQ 441
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
58-353 |
1.46e-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: 45.67 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 58 DEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQ- 136
Cdd:pfam15964 325 EAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGAt 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 137 ---LRQKLAALSRQIDELEETNRSLRKAEEELQ---------------DIKDKINKGEYGNSGIMDEVDELRKRVL-DME 197
Cdd:pfam15964 405 mlaLSQNVAQLEAQVEKVTREKNSLVSQLEEAQkqlasqemdvtkvcgEMRYQLNQTKMKKDEAEKEHREYRTKTGrQLE 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 198 GKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSvriTALEKLEDALDKSKQECYSLKCNLEKE-KMTTKQLSEEL 276
Cdd:pfam15964 485 IKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLT---ELLGESEHQLHLTRLEKESIQQSFSNEaKAQALQAQQRE 561
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720388026 277 ESLNARIKELEAiesRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKL 353
Cdd:pfam15964 562 QELTQKMQQMEA---QHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQKSRSEVEQLSQEKEYLQDRLEKL 635
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
89-308 |
2.09e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 89 ALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKltneDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDI 168
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEEL----NEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 169 KDKINKGEYGNSGIMDEVDELrkrvldMEGKDEElikmeeqcrDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDAL 248
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVL------LGSESFS---------DFLDRLSALSKIADADADLLEELKADKAELEAKKAEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 249 DKSKQECYSLKcnlekekmttKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLK 308
Cdd:COG3883 153 EAKLAELEALK----------AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
87-500 |
2.11e-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: 45.20 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 87 KLALAEARAQEEEQKATRLEKELQTQTTEFHQNQdkimaKLTNEDSQNRQLRQKLAALSRQIDELEetnRSLRKAEEELQ 166
Cdd:pfam10174 186 RIAEAEMQLGHLEVLLDQKEKENIHLREELHRRN-----QLQPDPAKTKALQTVIEMKDTKISSLE---RNIRDLEDEVQ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 167 DIKDKINKGEYGNSGIMDEVDELRKRVLDMEGK----DEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALE 242
Cdd:pfam10174 258 MLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKidqlKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 243 KLEDALdksKQECYSLKCNL-EKEKM---TTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDER 318
Cdd:pfam10174 338 QRAAIL---QTEVDALRLRLeEKESFlnkKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKD 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 319 KTMSEkLKQTEDKLQSTTSQlqaEQNKVTTVTEKLIEETK--RALKSKTDAEEKMYsvTKERDDLRNKLKaeeekghDLL 396
Cdd:pfam10174 415 KQLAG-LKERVKSLQTDSSN---TDTALTTLEEALSEKERiiERLKEQREREDRER--LEELESLKKENK-------DLK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 397 SKVTILKNRLQSLEAIEKDFVKNKLNQDSSKStaalhQENNKIKELSQEVENlklKLKDMKAIEDDLMKTEdEYETLERR 476
Cdd:pfam10174 482 EKVSALQPELTEKESSLIDLKEHASSLASSGL-----KKDSKLKSLEIAVEQ---KKEECSKLENQLKKAH-NAEEAVRT 552
|
410 420
....*....|....*....|....
gi 1720388026 477 YANERDKAQFLSQELEHAKMELAK 500
Cdd:pfam10174 553 NPEINDRIRLLEQEVARYKEESGK 576
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
83-241 |
2.15e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 83 ETQGKLALAEARaQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAE 162
Cdd:PRK12704 52 EAIKKEALLEAK-EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 163 EELQDIKDKINKGEYGNSGImdEVDELRKRVLDmegkdeeliKMEEQCRD----LNKRLEKETvqskdfKLEVDKLSVRI 238
Cdd:PRK12704 131 EELEELIEEQLQELERISGL--TAEEAKEILLE---------KVEEEARHeaavLIKEIEEEA------KEEADKKAKEI 193
|
...
gi 1720388026 239 TAL 241
Cdd:PRK12704 194 LAQ 196
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
58-304 |
2.71e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 58 DEQQRLTAQ--LALQ-RQKIQALTtSAKETQGKLAL---------AEARAQEEEQKATRLEKELQTQTTEFHQNQ----- 120
Cdd:PRK04863 401 DYQQALDVQqtRAIQyQQAVQALE-RAKQLCGLPDLtadnaedwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQfeqay 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 121 ---DKIMAKLTNEDSQN------------RQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNsgimDE 185
Cdd:PRK04863 480 qlvRKIAGEVSRSEAWDvarellrrlreqRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE----DE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 186 VDELRkrvldmEGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRIT-------ALEKLED---ALDKSKQEC 255
Cdd:PRK04863 556 LEQLQ------EELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPawlaaqdALARLREqsgEEFEDSQDV 629
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1720388026 256 YSLKCN-LEKEKMTTK---QLSEELESLNARIKELEAIESRLEKTEITLKDDL 304
Cdd:PRK04863 630 TEYMQQlLERERELTVerdELAARKQALDEEIERLSQPGGSEDPRLNALAERF 682
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
38-223 |
2.72e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 38 RIKTLKEELTKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQtqtTEFH 117
Cdd:COG1196 645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERL---EEEL 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 118 QNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVLDME 197
Cdd:COG1196 722 EEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVNLLAIEEYEELEERYDFLS 801
|
170 180
....*....|....*....|....*.
gi 1720388026 198 GKDEELIKMEEQCRDLNKRLEKETVQ 223
Cdd:COG1196 802 EQREDLEEARETLEEAIEEIDRETRE 827
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
41-387 |
2.74e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.83 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 41 TLKEELTKLKSFALMVVDEQQRLTAQLALQRQKIQALttSAKETQGKLALAEARaqEEEQKATRLEKELQTQTTE-FHQN 119
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKA--SREETFARTALKNAR--LDLRRLFDEKQSEKDKKNKaLAER 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 120 QDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKA-----EEELQD----IKDKINKGEYGNSGIMDEVDELR 190
Cdd:pfam12128 677 KDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAywqvvEGALDAqlalLKAAIAARRSGAKAELKALETWY 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 191 KRVLDMEGKDEE-LIKMEEQCRDLNKRLEKetvqskdfkLEVDKLSVRitalekledALDKSKQECYSLkcnlEKEKMTT 269
Cdd:pfam12128 757 KRDLASLGVDPDvIAKLKREIRTLERKIER---------IAVRRQEVL---------RYFDWYQETWLQ----RRPRLAT 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 270 kqlseeleslnarikELEAIESRLEKteitLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTV 349
Cdd:pfam12128 815 ---------------QLSNIERAISE----LQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATL 875
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1720388026 350 TE--------KLIEETKRA---LKSKTDAEekMYSVTKERDDLRNKLKA 387
Cdd:pfam12128 876 KEdanseqaqGSIGERLAQledLKLKRDYL--SESVKKYVEHFKNVIAD 922
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
18-209 |
3.00e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 18 KKLIDQETASQEKKEQEKEKRIKTLKEELTKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQE 97
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 98 EEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEy 177
Cdd:COG4942 130 DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL- 208
|
170 180 190
....*....|....*....|....*....|..
gi 1720388026 178 gnSGIMDEVDELRKRVLDMEGKDEELIKMEEQ 209
Cdd:COG4942 209 --AELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
56-157 |
3.22e-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: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 56 VVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNR 135
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
90 100
....*....|....*....|..
gi 1720388026 136 QLRQKLAALSRQIDELEETNRS 157
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPA 245
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
82-633 |
3.41e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 82 KETQGKLALAEARAQEEEQkatrLEKELQTQTTEFHQNQDKIMAKLTNEdsqNRQLRQKLAALSRQIDELEETNRSLRKA 161
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTL----CTPCMPDTYHERKQVLEKELKHLREA---LQQTQQSHAYLTQKREAQEEQLKKQQLL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 162 EEELQDIKDKINkgEYGNSGIMDEVDELRKRVLDMEGKDEELIKMEEQCRDLNKRL-EKETVQSKDFKLEVDKLSVRiTA 240
Cdd:TIGR00618 263 KQLRARIEELRA--QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELqSKMRSRAKLLMKRAAHVKQQ-SS 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 241 LEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELEsLNARIKELEAIESRLEKTEITLKDDLTKLKTLtVMLVDERKT 320
Cdd:TIGR00618 340 IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT-LTQHIHTLQQQKTTLTQKLQSLCKELDILQRE-QATIDTRTS 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 321 MSEKLKQtedKLQSTTSQLQAEQnKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERD----DLRNKLKAEEEKGhdll 396
Cdd:TIGR00618 418 AFRDLQG---QLAHAKKQQELQQ-RYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREqqlqTKEQIHLQETRKK---- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 397 skvTILKNRLQSLEAIEKDFvknklnqdsSKSTAALHQEnnkikelSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERR 476
Cdd:TIGR00618 490 ---AVVLARLLELQEEPCPL---------CGSCIHPNPA-------RQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQ 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 477 YANERDKAQFLSQELEHAKMELAkyKLAEKTESSHE-------------QWLFRRLQEEEAKSGHLSREVDALKEKIHEY 543
Cdd:TIGR00618 551 LTSERKQRASLKEQMQEIQQSFS--ILTQCDNRSKEdipnlqnitvrlqDLTEKLSEAEDMLACEQHALLRKLQPEQDLQ 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 544 mateDLICHLQGDHSLLQKKLNQqenrnrdLGREIENLTKELERYRHF-SKSLRPSLNERRISDPQVFSKEVQTEAADSE 622
Cdd:TIGR00618 629 ----DVRLHLQQCSQELALKLTA-------LHALQLTLTQERVREHALsIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697
|
570
....*....|.
gi 1720388026 623 PPDYKSLIPLE 633
Cdd:TIGR00618 698 MLAQCQTLLRE 708
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
158-307 |
3.66e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 158 LRKAEEELQDIKDKINKgeygnsgimdEVDELRKRVLdMEGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVR 237
Cdd:PRK12704 33 IKEAEEEAKRILEEAKK----------EAEAIKKEAL-LEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720388026 238 ITALEKLEDALDKSKQECYSLKCNLEK-----EKMTTKQLsEELESLNARIKElEAIESRLEKTEITLKDDLTKL 307
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKkeeelEELIEEQL-QELERISGLTAE-EAKEILLEKVEEEARHEAAVL 174
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
185-371 |
3.75e-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: 42.99 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 185 EVDELRKRVLDMEgkdEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSvriTALEKLEDALDKSKqecyslkcnlek 264
Cdd:COG1579 18 ELDRLEHRLKELP---AELAELEDELAALEARLEAAKTELEDLEKEIKRLE---LEIEEVEARIKKYE------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 265 EKMTTKQLSEELESLNariKELEAIESRLEKTEITLKDdltklktltvmLVDERKTMSEKLKQTEDKLQSTTSQLQAEQN 344
Cdd:COG1579 80 EQLGNVRNNKEYEALQ---KEIESLKRRISDLEDEILE-----------LMERIEELEEELAELEAELAELEAELEEKKA 145
|
170 180
....*....|....*....|....*..
gi 1720388026 345 KVTTVTEKLIEETKRALKSKTDAEEKM 371
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAKI 172
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
130-366 |
4.04e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 130 EDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKinKGEYGNSGIMDEVDELRKRVLDMEGKDEELIKMEEQ 209
Cdd:PRK05771 41 SNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVK--SLEELIKDVEEELEKIEKEIKELEEEISELENEIKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 210 CRDLNKRLEKetvqSKDFKLEVDKL-----------SVRITALEKLEDALDKSKQECYS--------------------- 257
Cdd:PRK05771 119 LEQEIERLEP----WGNFDLDLSLLlgfkyvsvfvgTVPEDKLEELKLESDVENVEYIStdkgyvyvvvvvlkelsdeve 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 258 ---LKCNLEKEKM-TTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVD---ERKTMSEKLKQTEd 330
Cdd:PRK05771 195 eelKKLGFERLELeEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEielERAEALSKFLKTD- 273
|
250 260 270
....*....|....*....|....*....|....*.
gi 1720388026 331 klqsTTSQLQAeqnkvtTVTEKLIEETKRALKSKTD 366
Cdd:PRK05771 274 ----KTFAIEG------WVPEDRVKKLKELIDKATG 299
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
96-424 |
4.90e-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: 43.91 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 96 QEEEQKATRLEKELQT---QTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEEL---QDIK 169
Cdd:pfam05622 172 EEELKKANALRGQLETykrQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRETNEELrcaQLQQ 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 170 DKINKGEYGNSGIMDEVDELRKRVLDMEGKdEELIKMEEQcrdlNKRL-EKETVQSKDfklevdklsvRITALEKLedal 248
Cdd:pfam05622 252 AELSQADALLSPSSDPGDNLAAEIMPAEIR-EKLIRLQHE----NKMLrLGQEGSYRE----------RLTELQQL---- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 249 dkskqecyslkcnLEKEKMTTKQLSEELESLNARIKELEAiesRLEKTEITLKDDLTKLKTlTVMLVDERKTMSEKLKQT 328
Cdd:pfam05622 313 -------------LEDANRRKNELETQNRLANQRILELQQ---QVEELQKALQEQGSKAED-SSLLKQKLEEHLEKLHEA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 329 EDKLQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTD----AEE--KMY-----SVTKERDDLRNKLKAEEekghdlls 397
Cdd:pfam05622 376 QSELQKKKEQIEELEPKQDSNLAQKIDELQEALRKKDEdmkaMEEryKKYvekakSVIKTLDPKQNPASPPE-------- 447
|
330 340 350
....*....|....*....|....*....|.
gi 1720388026 398 kVTILKNRLQ----SLEAIEKDFVKNKLNQD 424
Cdd:pfam05622 448 -IQALKNQLLekdkKIEHLERDFEKSKLQRE 477
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
17-474 |
5.27e-04 |
|
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: 44.01 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 17 LKKLIDQETASQEKKEQEKEKRIKTLKEELTKlksfalmvvDEQQRLTAQLALQRQKiQALTTSAKETQGKLALAEARAQ 96
Cdd:pfam01576 332 LKKALEEETRSHEAQLQEMRQKHTQALEELTE---------QLEQAKRNKANLEKAK-QALESENAELQAELRTLQQAKQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 97 EEEQKATRLEKELQtqttefhqnqdKIMAKLTNEDSQNRQLRQKLAALSrqiDELEETNRSLRKAEEELQDIKDKINKGE 176
Cdd:pfam01576 402 DSEHKRKKLEGQLQ-----------ELQARLSESERQRAELAEKLSKLQ---SELESVSSLLNEAEGKNIKLSKDVSSLE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 177 YGNSGIMDEVDELRKRVLDMEGKdeeLIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKledaldksKQECY 256
Cdd:pfam01576 468 SQLQDTQELLQEETRQKLNLSTR---LRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKK--------KLEED 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 257 SLkcNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDltkLKTLTVMLVDERKTMSeklkqTEDKLQSTT 336
Cdd:pfam01576 537 AG--TLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQE---LDDLLVDLDHQRQLVS-----NLEKKQKKF 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 337 SQLQAEQNkvtTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEkghdllskvtilKNRLQSLEAieKDF 416
Cdd:pfam01576 607 DQMLAEEK---AISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELER------------TNKQLRAEM--EDL 669
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720388026 417 VKNKlnQDSSKStaaLHQENNKIKELSQEVENLKLKLKDMkaiEDDLMKTEDEYETLE 474
Cdd:pfam01576 670 VSSK--DDVGKN---VHELERSKRALEQQVEEMKTQLEEL---EDELQATEDAKLRLE 719
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
60-346 |
5.49e-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: 43.99 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 60 QQRLTAQ-LALQRQK--IQALTTSAKETQGKL-----ALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNED 131
Cdd:pfam18971 562 ENKLTAKgLSLQEANklIKDFLSSNKELAGKAlnfnkAVAEAKSTGNYDEVKKAQKDLEKSLRKREHLEKEVEKKLESKS 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 132 SQNRQLRQKLAALSrQIDEL-----EETNR---------SLRKAEEELQDIKDKINKGEYGNSGIMDEVDelrkrvldmE 197
Cdd:pfam18971 642 GNKNKMEAKAQANS-QKDEIfalinKEANRdaraiaytqNLKGIKRELSDKLEKISKDLKDFSKSFDEFK---------N 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 198 GKDEELIKMEEQCRDLNKRLeKETVQSKDFKLEVDKLSvriTALEKLEDALDKSKQECYSLKCNLE---KEKMTTKQLSE 274
Cdd:pfam18971 712 GKNKDFSKAEETLKALKGSV-KDLGINPEWISKVENLN---AALNEFKNGKNKDFSKVTQAKSDLEnsvKDVIINQKVTD 787
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720388026 275 ELESLNARIKELEAIE--SRLEKTeitlkddLTKLKTLTvmlvdeRKTMSEKLKQTEDKLQSTTSQL-QAEQNKV 346
Cdd:pfam18971 788 KVDNLNQAVSVAKAMGdfSRVEQV-------LADLKNFS------KEQLAQQAQKNEDFNTGKNSELyQSVKNSV 849
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
214-554 |
5.77e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 214 NKRLEKETVQSKDFKLEVDKLSVRITA-LEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESL-------NARIKE 285
Cdd:pfam07888 54 NRQREKEKERYKRDREQWERQRRELESrVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALlaqraahEARIRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 286 LEAIESRLEKTEITLKDDLTKLKTLTVMLV-------DERKTMSEKLKQTEDKLQSTTSQLQ------AEQNKVTTVTEK 352
Cdd:pfam07888 134 LEEDIKTLTQRVLERETELERMKERAKKAGaqrkeeeAERKQLQAKLQQTEEELRSLSKEFQelrnslAQRDTQVLQLQD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 353 LIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEkghdllsKVTILKNRLQSLEAIEkdfvknklnqdsSKSTAAL 432
Cdd:pfam07888 214 TITTLTQKLTTAHRKEAENEALLEELRSLQERLNASER-------KVEGLGEELSSMAAQR------------DRTQAEL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 433 HQENNKIKELSQEVENLKLKLKDMKAieddlmKTEDEYETLERRYANERDKAQFLSQEL---------EHAKMELAKYKL 503
Cdd:pfam07888 275 HQARLQAAQLTLQLADASLALREGRA------RWAQERETLQQSAEADKDRIEKLSAELqrleerlqeERMEREKLEVEL 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1720388026 504 AEKTESSHEQW--LFRRLQEEEAKSGHLSREVDALKEKIHEYMateDLICHLQ 554
Cdd:pfam07888 349 GREKDCNRVQLseSRRELQELKASLRVAQKEKEQLQAEKQELL---EYIRQLE 398
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
38-423 |
6.11e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 38 RIKTLKEELtklksfalmvvDEQQRLTAQLALQRQKIQALTTSAKETQGK-LALAEARAQEEEQKATRleKELQTQTTEf 116
Cdd:PRK04863 787 RIEQLRAER-----------EELAERYATLSFDVQKLQRLHQAFSRFIGShLAVAFEADPEAELRQLN--RRRVELERA- 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 117 hqnqdkimakLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEElqdikdkinkgeygnsGIMDEVDELRkrvldm 196
Cdd:PRK04863 853 ----------LADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADE----------------TLADRVEEIR------ 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 197 egkdEELIKMEEQCRDLNK------RLEKE--TVQSKDFKLEVDKLSVritalEKLEDALDKSKQECYSLKCNLEK---- 264
Cdd:PRK04863 901 ----EQLDEAEEAKRFVQQhgnalaQLEPIvsVLQSDPEQFEQLKQDY-----QQAQQTQRDAKQQAFALTEVVQRrahf 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 265 -----EKMTTKQlSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQL 339
Cdd:PRK04863 972 syedaAEMLAKN-SDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPA 1050
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 340 QAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTK-ERDDLRNKLKAEEEKGHDLLSKVTILKNRLQS-LEAIEKDFV 417
Cdd:PRK04863 1051 DSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEaEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAvLRLVKDNGV 1130
|
....*.
gi 1720388026 418 KNKLNQ 423
Cdd:PRK04863 1131 ERRLHR 1136
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
46-254 |
6.76e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 46 LTKLKSFALMVVDEQQRLTAQLALQRQKIQAL-------TTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQ 118
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELlaalglpPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 119 NQDKIMAKLTNEDS---------QNRQLRQKLAALSRQIDELEETNRSLRKA------EEELQDIKDKINKGEygnsgim 183
Cdd:COG4717 373 AALLAEAGVEDEEElraaleqaeEYQELKEELEELEEQLEELLGELEELLEAldeeelEEELEELEEELEELE------- 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720388026 184 DEVDELRKRVLDMEgkdEELIKMEEQCRDLNKRLEKETVQSKdFKLEVDKLSVRITALEKLEDALDKSKQE 254
Cdd:COG4717 446 EELEELREELAELE---AELEQLEEDGELAELLQELEELKAE-LRELAEEWAALKLALELLEEAREEYREE 512
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
61-537 |
6.95e-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: 43.50 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 61 QRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQT----------------------TEFHQ 118
Cdd:TIGR00606 325 QRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLeldgfergpfserqiknfhtlvIERQE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 119 NQDKIMAKLTNEDSQNRQLRQKLAA-----LSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRV 193
Cdd:TIGR00606 405 DEAKTAAQLCADLQSKERLKQEQADeirdeKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAE 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 194 LDM---------EGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSV-------RITALEKLEDALDKSKQECYS 257
Cdd:TIGR00606 485 RELskaeknsltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQmemltkdKMDKDEQIRKIKSRHSDELTS 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 258 ----------LKCNLEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKL--KTLTVMLVDERKTMSEKL 325
Cdd:TIGR00606 565 llgyfpnkkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYedKLFDVCGSQDEESDLERL 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 326 KQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETK-------RALKSK-------TDAEEKMYSVTKERDDLRNKLKAEEEK 391
Cdd:TIGR00606 645 KEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqRVFQTEaelqefiSDLQSKLRLAPDKLKSTESELKKKEKR 724
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 392 GHDLLSKVTILKNRLQSLEAIEKDFVK--NKLNQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDe 469
Cdd:TIGR00606 725 RDEMLGLAPGRQSIIDLKEKEIPELRNklQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKD- 803
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 470 yetLERRYANERDKAQFLSQELEHAKMELAKYKLAEK--TESSHEQWLFRRLQEEEAKSGHLSREVDALK 537
Cdd:TIGR00606 804 ---VERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHEldTVVSKIELNRKLIQDQQEQIQHLKSKTNELK 870
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
121-390 |
9.53e-04 |
|
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: 43.13 E-value: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 121 DKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELqdikdkinkgeygnSGIMDEVDELRKRVLDMEGKD 200
Cdd:pfam05911 562 SKEALDDQDTSSDSSELSEVLQQFSATCNDVLSGKADLEDFVLEL--------------SHILDWISNHCFSLLDVSSME 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 201 EELIKMEeqCRDLNKRLEKETVQSKDFKLEVDKLS--VRITALEKLEDALDKSKQ-ECYSLKCNLEKEKMTTKQLSEELE 277
Cdd:pfam05911 628 DEIKKHD--CIDKVTLSENKVAQVDNGCSEIDNLSsdPEIPSDGPLVSGSNDLKTeENKRLKEEFEQLKSEKENLEVELA 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 278 SLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEET 357
Cdd:pfam05911 706 SCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEAELNELRQKFEALEVELEEEK 785
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1720388026 358 K---RALKSKTDAEEKMYSVTKER------DDLRNKLKAEEE 390
Cdd:pfam05911 786 NcheELEAKCLELQEQLERNEKKEssncdaDQEDKKLQQEKE 827
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
38-209 |
9.55e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 38 RIKTLKEE--LTKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKAT--RLEKELQTQT 113
Cdd:COG3206 197 ALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 114 TEfhqnQDKIMAKLTNEDSQNRQLRQKLAALSRQIDelEETNRSLRKAEEELQDIKDKINKgeygnsgIMDEVDELRKRV 193
Cdd:COG3206 277 AE----LAELSARYTPNHPDVIALRAQIAALRAQLQ--QEAQRILASLEAELEALQAREAS-------LQAQLAQLEARL 343
|
170
....*....|....*.
gi 1720388026 194 LDMEGKDEELIKMEEQ 209
Cdd:COG3206 344 AELPELEAELRRLERE 359
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
136-615 |
1.26e-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: 42.37 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 136 QLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINKGEYGNSGIMDEVDELRKRVldmegkdeelikmeEQCRDLNK 215
Cdd:pfam05622 11 ELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQL--------------EQLQEENF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 216 RLEKetvQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLekekmttkqlsEELESLNARIKELEA-IESRLE 294
Cdd:pfam05622 77 RLET---ARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEM-----------DILRESSDKVKKLEAtVETYKK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 295 KTEitlkdDLTKLKTlTVMLVDERKTMSEKLK-QTEDKLQSTT---SQLQAEQNKVTTVTEKLIEETKRALKSKTD---A 367
Cdd:pfam05622 143 KLE-----DLGDLRR-QVKLLEERNAEYMQRTlQLEEELKKANalrGQLETYKRQVQELHGKLSEESKKADKLEFEykkL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 368 EEKMYSVTKERDDL---RNKLK-AEEE------KGHDLLSKVTILKNRLQSLEAIEKDFVKNKLnqdssKSTAALHQENN 437
Cdd:pfam05622 217 EEKLEALQKEKERLiieRDTLReTNEElrcaqlQQAELSQADALLSPSSDPGDNLAAEIMPAEI-----REKLIRLQHEN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 438 KIKELSQEvENLKLKLKDMKAIEDDLMKTEDEYETlERRYANERDKaqflsqELEHAKMELAKYKLAEKTESSHEQWLFR 517
Cdd:pfam05622 292 KMLRLGQE-GSYRERLTELQQLLEDANRRKNELET-QNRLANQRIL------ELQQQVEELQKALQEQGSKAEDSSLLKQ 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 518 RLQEEEAKSGHLSREVDALKEKIHEYMATEDLICHLQGDHslLQKKLNQQENRNRDLGreiENLTKELERYRHFSKSLRP 597
Cdd:pfam05622 364 KLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDE--LQEALRKKDEDMKAME---ERYKKYVEKAKSVIKTLDP 438
|
490
....*....|....*...
gi 1720388026 598 SLNERRISDPQVFSKEVQ 615
Cdd:pfam05622 439 KQNPASPPEIQALKNQLL 456
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
98-234 |
1.26e-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: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 98 EEQKATRLEKELQTQTTEFHQNQdkimAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQdikdkinkgey 177
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEE----RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLE----------- 447
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720388026 178 gnsgimDEVDELRKRVLDMEGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKL 234
Cdd:COG2433 448 ------RELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
96-460 |
1.43e-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: 42.73 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 96 QEEEQKATRLEKELQTQTTEFHQNQD--KIMAKLTNEDSQNRQLRQKLaalsRQIDELEETNRSLR-KAEEELQDIKDKI 172
Cdd:TIGR01612 1946 EKEPEIYTKIRDSYDTLLDIFKKSQDlhKKEQDTLNIIFENQQLYEKI----QASNELKDTLSDLKyKKEKILNDVKLLL 2021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 173 NKgeygnsgimdeVDELRKRVLDMEGKDEEL-IKMEEQCRDLNKRLEKET---VQSKDFKLEVDKLSVRITALEKLEDAL 248
Cdd:TIGR01612 2022 HK-----------FDELNKLSCDSQNYDTILeLSKQDKIKEKIDNYEKEKekfGIDFDVKAMEEKFDNDIKDIEKFENNY 2090
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 249 DKSKQECYSLKCNLEKEKMTTKQLSEELESLNARIKELEaiESRLEKTEitLKDDLTKLKTLTVMLvdERKTMSEKLKQT 328
Cdd:TIGR01612 2091 KHSEKDNHDFSEEKDNIIQSKKKLKELTEAFNTEIKIIE--DKIIEKND--LIDKLIEMRKECLLF--SYATLVETLKSK 2164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 329 edklQSTTSQLQAEQNKVTTVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVtilKNRLQS 408
Cdd:TIGR01612 2165 ----VINHSEFITSAAKFSKDFFEFIEDISDSLNDDIDALQIKYNLNQTKKHMISILADATKDHNNLIEKE---KEATKI 2237
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720388026 409 LEAIEKDFVKNKLNQDSSkstaALHQENNKI----KELSQEVENLKLKLKDMKAIE 460
Cdd:TIGR01612 2238 INNLTELFTIDFNNADAD----ILHNNKIQIiyfnSELHKSIESIKKLYKKINAFK 2289
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
38-174 |
1.47e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 38 RIKTLKEELTKLKsfalmvvDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQK---------ATRLEKE 108
Cdd:COG1579 25 RLKELPAELAELE-------DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeYEALQKE 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720388026 109 LQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINK 174
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
277-586 |
1.48e-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: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 277 ESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTvmlvDERKTMSEKLkQTEDKLQSTTSQLQAEQNKVTTVTEKLIEE 356
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLC----EEKNALQEQL-QAETELCAEAEEMRARLAARKQELEEILHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 357 TKRALKSKTDAEEKMYSVTKERD----DLRNKLKAEEEKGHDL-LSKVTI------LKNRLQSLEAIEKDFVKNK--LNQ 423
Cdd:pfam01576 80 LESRLEEEEERSQQLQNEKKKMQqhiqDLEEQLDEEEAARQKLqLEKVTTeakikkLEEDILLLEDQNSKLSKERklLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 424 DSSKSTAALHQENNKIKELSQevenLKLKLKDMKAIEDDLMKTED----EYETLERRYANERDKAQFLSQELEhAKMELA 499
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSK----LKNKHEAMISDLEERLKKEEkgrqELEKAKRKLEGESTDLQEQIAELQ-AQIAEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 500 KYKLAEKTESSheQWLFRRLQEEEAKSGHLSREVDALKEKIHEymatedlichLQGDHSLLQKKLNQQENRNRDLGREIE 579
Cdd:pfam01576 235 RAQLAKKEEEL--QAALARLEEETAQKNNALKKIRELEAQISE----------LQEDLESERAARNKAEKQRRDLGEELE 302
|
....*..
gi 1720388026 580 NLTKELE 586
Cdd:pfam01576 303 ALKTELE 309
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-658 |
1.58e-03 |
|
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: 42.35 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 355 EETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAIEKDFVKNKLnqdsskstaalHQ 434
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREEL-----------EE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 435 ENNKIKELSQEVENLKLKLKdmkAIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKLAEKTESSHEQW 514
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQ---ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 515 LFRRLQEEEAKSGHLSREVDALKEKIHEYMATEDLichLQGDHSLLQKKLNQQENRNRDLGREIENLTKELERYRHFSKS 594
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELES---LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720388026 595 LRpslNERRISDPQVFSKEVQTEAADSEPPD-YKSLIPLERAVINGQFYEENEDQDDDPNEEESV 658
Cdd:TIGR02168 398 LN---NEIERLEARLERLEDRRERLQQEIEElLKKLEEAELKELQAELEELEEELEELQEELERL 459
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
207-599 |
1.66e-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: 42.34 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 207 EEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEEleslnarikEL 286
Cdd:TIGR00606 233 LESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDE---------QL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 287 EAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKlkQTEDKLQSTTSQLQAEQNKVTTVTEKLiEETKRALKSKTD 366
Cdd:TIGR00606 304 NDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQE--KTELLVEQGRLQLQADRHQEHIRARDS-LIQSLATRLELD 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 367 AEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVT---ILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQENNKIKELS 443
Cdd:TIGR00606 381 GFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCadlQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVI 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 444 QEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKMELAKYKLAEKTESSHEQWLFRRLQEEE 523
Cdd:TIGR00606 461 KELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEML 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 524 AKS---------GHLSREVDALKEKIHEYMATEDLICHLQGdhslLQKKLNQQENRNRDLGREIENLTKELERYRHFSKS 594
Cdd:TIGR00606 541 TKDkmdkdeqirKIKSRHSDELTSLLGYFPNKKQLEDWLHS----KSKEINQTRDRLAKLNKELASLEQNKNHINNELES 616
|
....*
gi 1720388026 595 LRPSL 599
Cdd:TIGR00606 617 KEEQL 621
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
18-236 |
1.76e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 18 KKLIDQETASQEKKEQEKEKRIKTLKEELTKLKSfalmvvdEQQRLTAQLALQRQKIQALTTSAKetqgKLALAEARAQE 97
Cdd:PHA02562 201 NKNIEEQRKKNGENIARKQNKYDELVEEAKTIKA-------EIEELTDELLNLVMDIEDPSAALN----KLNTAAAKIKS 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 98 EEQKATRLEKELQ------TQTTEFHQNQDKImAKLTNedsQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDK 171
Cdd:PHA02562 270 KIEQFQKVIKMYEkggvcpTCTQQISEGPDRI-TKIKD---KLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNK 345
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720388026 172 INKGEYGNSGIMDEVDELRKrvlDMEGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSV 236
Cdd:PHA02562 346 ISTNKQSLITLVDKAKKVKA---AIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGI 407
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
142-306 |
1.81e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 142 AALSRQI-----DELEETNRSLRKAEEELQDIKDKINKGEygnsgimDEVDELRKRVLDMEG----KDEELIKMEEQCRD 212
Cdd:COG2433 380 EALEELIekelpEEEPEAEREKEHEERELTEEEEEIRRLE-------EQVERLEAEVEELEAeleeKDERIERLERELSE 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 213 LNKRLEKETVQSKdfklEVDKLSVRITALEKLedaldkskqecyslkcnLEKEKMTtkqlSEELESLNARIKELEAIESR 292
Cdd:COG2433 453 ARSEERREIRKDR----EISRLDREIERLERE-----------------LEEERER----IEELKRKLERLKELWKLEHS 507
|
170
....*....|....
gi 1720388026 293 LEKTEITLKDDLTK 306
Cdd:COG2433 508 GELVPVKVVEKFTK 521
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
135-384 |
1.82e-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: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 135 RQLRQKLAALSRQIDELEETNRSLRKAEEE---LQDIKDKINKGEyGNSGIMDEVDELRKRvLDMEGKDEELIKMEEQCR 211
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQielLEPIRELAERYA-AARERLAELEYLRAA-LRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 212 DLNKRLEKETVQSKDFKLEVDKLSVRitaLEKLEDALDKSKQEcyslkcNLEkekmttkQLSEELESLNARIKELEAIES 291
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREE---LDELEAQIRGNGGD------RLE-------QLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 292 RLEKTeitlkddltkLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKVTtvteklieetkRALKSKTDAEEKM 371
Cdd:COG4913 363 RLEAL----------LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA-----------EAEAALRDLRREL 421
|
250
....*....|...
gi 1720388026 372 YSVTKERDDLRNK 384
Cdd:COG4913 422 RELEAEIASLERR 434
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
206-469 |
1.88e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 206 MEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQEcyslkcnlEKEKMttKQLSEELESLNARIKE 285
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE--------LREEA--QELREKRDELNEKVKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 286 LEaiESRLEKTEI--TLKDDLTKLKTLTVMLVDER---KTMSEKLKQTEDKLQSTTSQLQAEQnkvttvteKLIEETKRa 360
Cdd:COG1340 76 LK--EERDELNEKlnELREELDELRKELAELNKAGgsiDKLRKEIERLEWRQQTEVLSPEEEK--------ELVEKIKE- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 361 LKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSL-----EAIEK-DFVK---NKLNQDSSKSTAA 431
Cdd:COG1340 145 LEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELheemiELYKEaDELRkeaDELHKEIVEAQEK 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 1720388026 432 LHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDE 469
Cdd:COG1340 225 ADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
105-471 |
1.98e-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: 42.35 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 105 LEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQ-----LRQKLAALSRQ--IDELEETNRslrkaeeeLQDIKDKINKgEY 177
Cdd:TIGR01612 639 LAKISPYQVPEHLKNKDKIYSTIKSELSKIYEddidaLYNELSSIVKEnaIDNTEDKAK--------LDDLKSKIDK-EY 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 178 GNSGIMdEVDELRKRVLDMEGKDEELIKM---------EEQCRDLNKRLEketvqskDFKLEVDKLSVRITALEKLEDAL 248
Cdd:TIGR01612 710 DKIQNM-ETATVELHLSNIENKKNELLDIiveikkhihGEINKDLNKILE-------DFKNKEKELSNKINDYAKEKDEL 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 249 DKSKQECYSLKC------------------NLEKEKMTTKQLSEELESLNARIKELEaiesrlekteiTLKDDLTKLKTL 310
Cdd:TIGR01612 782 NKYKSKISEIKNhyndqinidnikdedakqNYDKSKEYIKTISIKEDEIFKIINEMK-----------FMKDDFLNKVDK 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 311 TVMLVDERKtmsEKLKQTEDKLQSTTSQLQAE-QNKVTTVTEKLIEETKRALKSKTDAEEKMY---SVTKERDDLRNKLK 386
Cdd:TIGR01612 851 FINFENNCK---EKIDSEHEQFAELTNKIKAEiSDDKLNDYEKKFNDSKSLINEINKSIEEEYqniNTLKKVDEYIKICE 927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 387 AEEEKGHDLLSKVTILKNRL-------QSLEAIEKDF-------VKNKLNQ-DSSKSTAALHQENNKIKELSQEVENLKL 451
Cdd:TIGR01612 928 NTKESIEKFHNKQNILKEILnknidtiKESNLIEKSYkdkfdntLIDKINElDKAFKDASLNDYEAKNNELIKYFNDLKA 1007
|
410 420
....*....|....*....|
gi 1720388026 452 KLKDMKaiEDDLMKTEDEYE 471
Cdd:TIGR01612 1008 NLGKNK--ENMLYHQFDEKE 1025
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
61-191 |
2.13e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 61 QRLTAQLALQRQKIQALTTSAKETQGKLALAEA--------------RAQEEEQKATRLEKELQTQTTEFHQNQDKImaK 126
Cdd:PRK09039 63 AELADLLSLERQGNQDLQDSVANLRASLSAAEAersrlqallaelagAGAAAEGRAGELAQELDSEKQVSARALAQV--E 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720388026 127 LTNEdsQNRQLRQKLAALSRQIDELEETNRSlrkAEEELQDIkdkinkGEYGNSGIMDEVDELRK 191
Cdd:PRK09039 141 LLNQ--QIAALRRQLAALEAALDASEKRDRE---SQAKIADL------GRRLNVALAQRVQELNR 194
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
60-253 |
2.15e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 60 QQRL-TAQLALQ--RQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQ 136
Cdd:COG3206 188 RKELeEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 137 LRQKLAALSRQIDELE----ETNRSLRKAEEELQDIKDKINKgeygnsGIMDEVDELRKRVLDMEGKDEELIKMEEQCRD 212
Cdd:COG3206 268 LRAQLAELEAELAELSarytPNHPDVIALRAQIAALRAQLQQ------EAQRILASLEAELEALQAREASLQAQLAQLEA 341
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720388026 213 LNKRLEKETVQSKDFKLEVDklsvriTALEKLEDALDKSKQ 253
Cdd:COG3206 342 RLAELPELEAELRRLEREVE------VARELYESLLQRLEE 376
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
46-333 |
2.51e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.60 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 46 LTKLKSFALMVVD-----EQQRLT---AQLAL---------QRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLE-- 106
Cdd:COG0497 115 LSQLRELGELLVDihgqhEHQSLLdpdAQRELldafagleeLLEEYREAYRAWRALKKELEELRADEAERARELDLLRfq 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 107 -KELQTqttefhqnqdkimAKLT-NEDsqnrqlrqklaalsrqiDELEETNRSLRKAE---EELQDIKDKINKGEygnSG 181
Cdd:COG0497 195 lEELEA-------------AALQpGEE-----------------EELEEERRRLSNAEklrEALQEALEALSGGE---GG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 182 IMDEVDELRKRVLDMEGKDEELikmeeqcRDLNKRLEKETVQSKDFKLEVDKLSVRITA----LEKLEDALDkskqECYS 257
Cdd:COG0497 242 ALDLLGQALRALERLAEYDPSL-------AELAERLESALIELEEAASELRRYLDSLEFdperLEEVEERLA----LLRR 310
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720388026 258 LKcnlEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKL-KQTEDKLQ 333
Cdd:COG0497 311 LA---RKYGVTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLeKAVTAELA 384
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
39-197 |
3.21e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.05 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 39 IKTLKEELTKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSAKE--TQGKLALAEArAQEEEQKATRLEKELQTQTTEF 116
Cdd:pfam04012 31 IRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAalTKGNEELARE-ALAEKKSLEKQAEALETQLAQQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 117 HqnqdkimakltnedSQNRQLRQKLAALSRQIDELEETNRSLrKAEEELQDIKDKINK--GEYGNSGIMDEVDELRKRVL 194
Cdd:pfam04012 110 R--------------SAVEQLRKQLAALETKIQQLKAKKNLL-KARLKAAKAQEAVQTslGSLSTSSATDSFERIEEKIE 174
|
...
gi 1720388026 195 DME 197
Cdd:pfam04012 175 ERE 177
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
39-584 |
3.46e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.36 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 39 IKTLKEELTKLKSFALMVVDEQ-----QRLTAQLALQRQKIQALTTSAKETqgklalaEARAQEEEQKATRLEKELQTQT 113
Cdd:PTZ00440 690 IKNLKKELQNLLSLKENIIKKQlnnieQDISNSLNQYTIKYNDLKSSIEEY-------KEEEEKLEVYKHQIINRKNEFI 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 114 TEFHQNQDKIMA--KLTNEDSQNR-QLRQKLAALSRQIDELEEtnrSLRKAEEELQDIKDKINKGEYGNsgimDEVDELR 190
Cdd:PTZ00440 763 LHLYENDKDLPDgkNTYEEFLQYKdTILNKENKISNDINILKE---NKKNNQDLLNSYNILIQKLEAHT----EKNDEEL 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 191 KRVLDMEGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKlsvrITALEKLEDALDKSKqecySLKCNLEKEKMTTK 270
Cdd:PTZ00440 836 KQLLQKFPTEDENLNLKELEKEFNENNQIVDNIIKDIENMNKN----INIIKTLNIAINRSN----SNKQLVEHLLNNKI 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 271 QLSEELESLNARIKELEAIEsrlEKTEITLKDDLTKLKT-----LTVMLVDERKTMSEKLKQTEDKLQSTTsqlqaeQNK 345
Cdd:PTZ00440 908 DLKNKLEQHMKIINTDNIIQ---KNEKLNLLNNLNKEKEkiekqLSDTKINNLKMQIEKTLEYYDKSKENI------NGN 978
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 346 VTTVTEKLIEETK--RALKSKTDAEEKMYSV-TKERDDLRNKLKAE---------EEKGHDLLSKVtilKNRLQSLEAIe 413
Cdd:PTZ00440 979 DGTHLEKLDKEKDewEHFKSEIDKLNVNYNIlNKKIDDLIKKQHDDiielidkliKEKGKEIEEKV---DQYISLLEKM- 1054
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 414 KDFVKNK-LNQDSSKSTAALHQEN------------NKIKELSQEVENLKLKLKDMKAIEDDLM-KTEDEYET----LER 475
Cdd:PTZ00440 1055 KTKLSSFhFNIDIKKYKNPKIKEEiklleekveallKKIDENKNKLIEIKNKSHEHVVNADKEKnKQTEHYNKkkksLEK 1134
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 476 RYANERDkaqfLSQELEHAKMELAKYKLAEKTESSHEQWLF----RRLQEEEAKSGHLSREVDALKEKIHEYMAteDLIC 551
Cdd:PTZ00440 1135 IYKQMEK----TLKELENMNLEDITLNEVNEIEIEYERILIdhivEQINNEAKKSKTIMEEIESYKKDIDQVKK--NMSK 1208
|
570 580 590
....*....|....*....|....*....|...
gi 1720388026 552 HLQGDHSLLqkKLNQQENRNRDLGREIENLTKE 584
Cdd:PTZ00440 1209 ERNDHLTTF--EYNAYYDKATASYENIEELTTE 1239
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
39-306 |
3.59e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 39 IKTLKEELTKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKE---LQTQTTE 115
Cdd:COG4372 54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKErqdLEQQRKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 116 FHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAE--EELQDIKDKINKGEYGNSGIMDEVDELRKRV 193
Cdd:COG4372 134 LEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANRNAEKEEELAEAEKLIESLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 194 LDMEGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLS 273
Cdd:COG4372 214 RELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL 293
|
250 260 270
....*....|....*....|....*....|...
gi 1720388026 274 EELESLNARIKELEAIESRLEKTEITLKDDLTK 306
Cdd:COG4372 294 ELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
113-288 |
3.83e-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: 41.20 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 113 TTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEELQDIKDKINkgeygnsGIMDEVDELRK- 191
Cdd:pfam13166 278 DDEFTEFQNRLQKLIEKVESAISSLLAQLPAVSDLASLLSAFELDVEDIESEAEVLNSQLD-------GLRRALEAKRKd 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 192 --RVLDMEGKDEELIKMEEQCRDLNKRLEKETVQSKDFKLEVDKL--SVRITALEKLEDALDKSKQECYSLKCNLEKEKM 267
Cdd:pfam13166 351 pfKSIELDSVDAKIESINDLVASINELIAKHNEITDNFEEEKNKAkkKLRLHLVEEFKSEIDEYKDKYAGLEKAINSLEK 430
|
170 180
....*....|....*....|.
gi 1720388026 268 TTKQLSEELESLNARIKELEA 288
Cdd:pfam13166 431 EIKNLEAEIKKLREEIKELEA 451
|
|
| COG0610 |
COG0610 |
Type I site-specific restriction-modification system, R (restriction) subunit and related ... |
45-254 |
4.25e-03 |
|
Type I site-specific restriction-modification system, R (restriction) subunit and related helicases ... [Defense mechanisms];
Pssm-ID: 440375 [Multi-domain] Cd Length: 936 Bit Score: 41.01 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 45 ELTKLKSFALMVVDEQQRLTAQLALQRQKIQALTTSAKETQGKLALAEARAQEEE--QKATRLEKelqtqttefhqnqDK 122
Cdd:COG0610 735 ELSRLYNLLSPDDEFGDLELEKYRDDVSFYLALRAKLRKLGEKLDLKEYEEKIRQllDEAIDLER-------------KE 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 123 IMAKLTNEDSQNRQLRQKLAALsrqIDELEETNRSLRKAEEELQDIKDKINKGE--YGNSGIMDEVDELRKRVLDMEGKD 200
Cdd:COG0610 802 IKPRIKQNPVQYRKFSELLEEI---IEEYNNGALDADEVLEELEELAKEVKEEEerAEEEGLNEEELAFYDALAENLGDE 878
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720388026 201 eeliKMEEQCRDLNKRLEKETvqSKDFKlevDKLSVRITALEKLEDALDKSKQE 254
Cdd:COG0610 879 ----KLKELAKELDDLLKKNV--TVDWR---KRESVRAKLRDAIKRLLRKYGYP 923
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
94-174 |
4.57e-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: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 94 RAQEE-EQKATRLEKELQTQTTEFHQNQDKIMAKLTNEDSQNRQLRQKLAALSRQIDEL-EETNRSLRKAEEEL-QDIKD 170
Cdd:pfam03938 19 AAQAQlEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLqQKAQQELQKKQQELlQPIQD 98
|
....
gi 1720388026 171 KINK 174
Cdd:pfam03938 99 KINK 102
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
42-595 |
5.03e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 42 LKEELTKLKSFALMVVDEQQRLTAQLalqrQKIQALTTSAKETQGKLALAEARAQEEEQKATRLEKELQTQTTEFHQNQD 121
Cdd:pfam01576 389 LQAELRTLQQAKQDSEHKRKKLEGQL----QELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVS 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 122 KIMAKLTNEDSQ-NRQLRQKLAaLSRQIDELEETNRSLRKAEEELQDIKDKINKGEygnSGIMDEVDELRKRVLDMEGKD 200
Cdd:pfam01576 465 SLESQLQDTQELlQEETRQKLN-LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQL---STLQAQLSDMKKKLEEDAGTL 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 201 EELikmEEQCRDLNKRLEKETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQECYSLKCNLEKEKMTTKQLSEELESLN 280
Cdd:pfam01576 541 EAL---EEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAIS 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 281 ARIKEleaiesRLEKTEITLKDDLTKLKTLTVMLvderktmsEKLKQTEDKLQSTTSQLQAEQNKVTTVTEKLIEETKRA 360
Cdd:pfam01576 618 ARYAE------ERDRAEAEAREKETRALSLARAL--------EEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHEL 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 361 LKSKTDAEEKMYSVTKERDDLRNKLKAEEEkghdllSKVTILKNrLQSLEAIEKDFVKNKLNQDSSKSTAALHQENNKIK 440
Cdd:pfam01576 684 ERSKRALEQQVEEMKTQLEELEDELQATED------AKLRLEVN-MQALKAQFERDLQARDEQGEEKRRQLVKQVRELEA 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 441 ELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYAN-----ERDKAQF--LSQELEHAKME----LAKYKLAEKTES 509
Cdd:pfam01576 757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEavkqlKKLQAQMkdLQRELEEARASrdeiLAQSKESEKKLK 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 510 SHEQWLFrRLQEEEAKSGHLSREVDALKEKIHEYMAT---------------EDLICHLQGDHSLLQKKLNQQENRNRDL 574
Cdd:pfam01576 837 NLEAELL-QLQEDLAASERARRQAQQERDELADEIASgasgksalqdekrrlEARIAQLEEELEEEQSNTELLNDRLRKS 915
|
570 580
....*....|....*....|.
gi 1720388026 575 GREIENLTKELERYRHFSKSL 595
Cdd:pfam01576 916 TLQVEQLTTELAAERSTSQKS 936
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
355-437 |
5.22e-03 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 40.58 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 355 EETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKghDLLSKVTILKNRLQSLEAIEKDFVKNKLNQDSSKSTAALHQ 434
Cdd:PTZ00400 561 EKKKELVDAKNEAETLIYSVEKQLSDLKDKISDADKD--ELKQKITKLRSTLSSEDVDSIKDKTKQLQEASWKISQQAYK 638
|
...
gi 1720388026 435 ENN 437
Cdd:PTZ00400 639 QGN 641
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
46-279 |
5.56e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 46 LTKLKSFALMVVDeqQRLTAQLALQrQKIQALTTSAKETQGKLALA---EARAQEEEQKATRLEKELQTQTTEFHQNQDK 122
Cdd:PLN02939 147 LNQARLQALEDLE--KILTEKEALQ-GKINILEMRLSETDARIKLAaqeKIHVEILEEQLEKLRNELLIRGATEGLCVHS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 123 IMAKLTNEDSQNRQLRQKLAALSRQIDELEETNRSLRKAEEE-------LQDIKDKINKGEYGNSGI--------MDEVD 187
Cdd:PLN02939 224 LSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKErslldasLRELESKFIVAQEDVSKLsplqydcwWEKVE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 188 ELRKRVLDMEGKDEELIKMEEQCRDLNKRLEK------ETVQSKDFKLEVDKLSVRITAlekLEDALDKSKQECYSlkcN 261
Cdd:PLN02939 304 NLQDLLDRATNQVEKAALVLDQNQDLRDKVDKleaslkEANVSKFSSYKVELLQQKLKL---LEERLQASDHEIHS---Y 377
|
250
....*....|....*...
gi 1720388026 262 LEKEKMTTKQLSEELESL 279
Cdd:PLN02939 378 IQLYQESIKEFQDTLSKL 395
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
136-512 |
5.70e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.80 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 136 QLRQKLAALSRQI--------DELEETNRSLRKAEEELQDIK----DKINKGEYGNSGIMDEVDELRKRVLDMEGKDEE- 202
Cdd:PTZ00108 1003 KLERELARLSNKVrfikhvinGELVITNAKKKDLVKELKKLGyvrfKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEEl 1082
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 203 --------LIKM------EEQCRDLNKRLEkETVQSKDFKLEVDKLSVRITALEKLEDALDKSKQEcyslkcnLEKEKMT 268
Cdd:PTZ00108 1083 gaavsydyLLSMpiwsltKEKVEKLNAELE-KKEKELEKLKNTTPKDMWLEDLDKFEEALEEQEEV-------EEKEIAK 1154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 269 TKQLS--EELESLNARIKELEAIESRLEKTEITLKDDLTKLKTLTVMLVDERKTMSEKLKQTEDKLQSTTSQLQAEQNKV 346
Cdd:PTZ00108 1155 EQRLKskTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTK 1234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 347 ttvtEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHdlLSKVTILKNRLQSLEAIEKDFvknklnqdSS 426
Cdd:PTZ00108 1235 ----PKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKR--VSAVQYSPPPPSKRPDGESNG--------GS 1300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 427 KSTAALHQENNKIKELSQEVENLKLKLKDmKAIEDDLMKTEDEYETLERRYANERDKAQFLSQELEhakmELAKYKLAEK 506
Cdd:PTZ00108 1301 KPSSPTKKKVKKRLEGSLAALKKKKKSEK-KTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSS----EDDDDSEVDD 1375
|
....*.
gi 1720388026 507 TESSHE 512
Cdd:PTZ00108 1376 SEDEDD 1381
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
348-589 |
9.25e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 348 TVTEKLIEETKRALKSKTDAEEKMYSVTKERDDLRNKLKAEEEKGHDLLSKVTILKNRLQSLEAiekdfVKNKLNQDSSK 427
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELRE-----KRDELNEKVKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 428 STAALHQENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANER----------DKAQFLSQELEHAKME 497
Cdd:COG1340 76 LKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVlspeeekelvEKIKELEKELEKAKKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 498 L-AKYKLAEKTESSHE-----QWLFRRLQEEEAKSGHLSREVDALKEKIHEYMATEDLichLQGDHSLLQKKLNQQENRN 571
Cdd:COG1340 156 LeKNEKLKELRAELKElrkeaEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADE---LHKEIVEAQEKADELHEEI 232
|
250
....*....|....*...
gi 1720388026 572 RDLGREIENLTKELERYR 589
Cdd:COG1340 233 IELQKELRELRKELKKLR 250
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
422-541 |
9.35e-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: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 422 NQDSSKSTAALHQENNKIKELSQEVENLKLKLKDMkaiEDDLMKTEDEYETLERRYANERDKAQFLSQELEHAKME-LAK 500
Cdd:pfam17060 132 NLKPQESPETPRRINRKYKSLELRVESMKDELEFK---DETIMEKDRELTELTSTISKLKDKYDFLSREFEFYKQHhEHG 208
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1720388026 501 YKLAEKTESSHE---QWLFRRLQEEEAKSGHLSREVDALKEKIH 541
Cdd:pfam17060 209 GNNSIKTATKHEfiiSELKRKLQEQNRLIRILQEQIQFDPGALH 252
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
262-513 |
9.65e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.89 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 262 LEKEKMTTKQLSEELESLNARIKELEAIESRLEKTEITLKDDLTKLKTltvmlvdERKTMSEKLKQTEDKLQSTTSQ--L 339
Cdd:PLN02939 116 QTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILT-------EKEALQGKINILEMRLSETDARikL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 340 QAEQNKVTTVTEKLIEETKRALKSKTDAEEK-MYSVTKERDDLRNK---LKAEEEKGHDLLSKVTILKNRLQSLEAiEKD 415
Cdd:PLN02939 189 AAQEKIHVEILEEQLEKLRNELLIRGATEGLcVHSLSKELDVLKEEnmlLKDDIQFLKAELIEVAETEERVFKLEK-ERS 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720388026 416 FVKNKLNQDSSKSTAAlhqENNKIKELSQEVENLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSQELEHA- 494
Cdd:PLN02939 268 LLDASLRELESKFIVA---QEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEAn 344
|
250 260
....*....|....*....|....*....
gi 1720388026 495 -------KMELAKYK---LAEKTESSHEQ 513
Cdd:PLN02939 345 vskfssyKVELLQQKlklLEERLQASDHE 373
|
|
| |
