|
Name |
Accession |
Description |
Interval |
E-value |
| FYVE_EEA1 |
cd15730 |
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ... |
1389-1451 |
1.92e-41 |
|
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed endosome-associated protein p162, or zinc finger FYVE domain-containing protein 2, is an essential component of the endosomal fusion machinery and required for the fusion and maturation of early endosomes in endocytosis. It forms a parallel coiled-coil homodimer in cells. EEA1 serves as the p97 ATPase substrate and the p97 ATPase may regulate the size of early endosomes by governing the oligomeric state of EEA1. It can interact with the GTP-bound form of Rab22a and be involved in endosomal membrane trafficking. EEA1 also functions as an obligate scaffold for angiotensin II-induced Akt activation in early endosomes. It can be phosphorylated by p38 mitogen-activated protein kinase (MAPK) and further regulate mu opioid receptor endocytosis. EEA1 consists of an N-terminal C2H2 Zn2+ finger, four long heptad repeats, and a C-terminal region containing a calmodulin binding (IQ) motif, a Rab5 interaction site, and a FYVE domain. This model corresponds to the FYVE domain that is responsible for binding phosphatidyl inositol-3-phosphate (PtdIns3P or PI3P) on the membrane.
Pssm-ID: 277269 [Multi-domain] Cd Length: 63 Bit Score: 146.00 E-value: 1.92e-41
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967300 1389 RKWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDACFNDL 1451
Cdd:cd15730 1 RKWADDEEVQNCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDACFDDL 63
|
|
| FYVE |
pfam01363 |
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ... |
1390-1452 |
3.75e-28 |
|
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.
Pssm-ID: 426221 [Multi-domain] Cd Length: 68 Bit Score: 108.24 E-value: 3.75e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568967300 1390 KWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTP---SSKKPVRVCDACFNDLQ 1452
Cdd:pfam01363 2 VWVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLpelGSNKPVRVCDACYDTLQ 67
|
|
| FYVE |
smart00064 |
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ... |
1388-1453 |
1.47e-27 |
|
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.
Pssm-ID: 214499 [Multi-domain] Cd Length: 68 Bit Score: 106.75 E-value: 1.47e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568967300 1388 NRKWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSS--KKPVRVCDACFNDLQG 1453
Cdd:smart00064 1 RPHWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENLNG 68
|
|
| FYVE_RUFY1_like |
cd15721 |
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ... |
1391-1448 |
8.04e-25 |
|
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1 and RUFY2. RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. Both RUFY1 and RUFY2 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.
Pssm-ID: 277261 [Multi-domain] Cd Length: 58 Bit Score: 98.61 E-value: 8.04e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568967300 1391 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDACF 1448
Cdd:cd15721 1 WADDKEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
542-1376 |
4.60e-23 |
|
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: 107.06 E-value: 4.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 542 ATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLlEKEREDLYAKIQAGEgetavLNQLQEKNHALQQQLTQ 621
Cdd:TIGR02168 177 TERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKEL-KAELRELELALLVLR-----LEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 622 LTEKLKNQSESHKQAE---ENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLsaea 698
Cdd:TIGR02168 251 AEEELEELTAELQELEeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE---- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 699 akaaqraDLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLE 778
Cdd:TIGR02168 327 -------ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 779 ADALEVKASKEQALQSLQQQRQLSTDL-----ELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVV 853
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 854 LKQEFEKLSQ--DSKTQHKELGDRMQAAVTELTAVKAQK---DALLAELSTTKEKLSK-------------VSDSLKNSK 915
Cdd:TIGR02168 480 AERELAQLQArlDSLERLQENLEGFSEGVKALLKNQSGLsgiLGVLSELISVDEGYEAaieaalggrlqavVVENLNAAK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 916 SEFE--KENQKGKAAVLDLEKACKElkhQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNtlkqke 993
Cdd:TIGR02168 560 KAIAflKQNELGRVTFLPLDSIKGT---EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDD------ 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 994 kdeqqLQGTINQLKQSAEQKKkqIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQL 1073
Cdd:TIGR02168 631 -----LDNALELAKKLRPGYR--IVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAEL 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1074 QSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQignqnksIQELQAAKASLEQDSAKKEALLKEQSKALEDAQRE 1153
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-------VEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1154 KSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQesikEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKE 1233
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE----EAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1234 SQQLMreqvkkeeEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQT 1313
Cdd:TIGR02168 853 DIESL--------AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568967300 1314 DDLRGEIAVLEATVQNNQDERRALLERCLKG-EGEIEKLQTKALELQRKLDNTTAAVQELGREN 1376
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSLTLEEaEALENKIEDDEEEARRRLKRLENKIKELGPVN 988
|
|
| FYVE_PKHF |
cd15717 |
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ... |
1391-1448 |
4.38e-22 |
|
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), and similar proteins; This family includes protein containing both PH and FYVE domains 1 (phafin-1) and 2 (phafin-2). Phafin-1 is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway. Phafin-2 is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.
Pssm-ID: 277257 [Multi-domain] Cd Length: 61 Bit Score: 90.89 E-value: 4.38e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1391 WAEDNEVQNCMSCGKC-FSVTVRRHHCRQCGNIFCAECSTKNALTPS-SKKPVRVCDACF 1448
Cdd:cd15717 2 WVPDSEAPVCMHCKKTkFTAINRRHHCRKCGAVVCGACSSKKFLLPHqSSKPLRVCDTCY 61
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
285-1112 |
1.03e-21 |
|
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: 102.83 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 285 ERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLE 364
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 365 EKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQR 444
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 445 EEKEQHGLQLQGEVSQLHCKLLETERQLGEAhgrlkeQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKekvtnstELQHQ 524
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEA------ELKELQAELEELEEELEELQEELERLEEALE-------ELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 525 LEkskqqhqeqqalqqsataKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKERED-------LYAKIQA 597
Cdd:TIGR02168 470 LE------------------EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvLSELISV 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 598 GEG-ETAVLNQLQEknhALQQQLTqlteklknqseshkqaeENLHDQVQEQKAHLRAAQDRVLSLETSV-------SELS 669
Cdd:TIGR02168 532 DEGyEAAIEAALGG---RLQAVVV-----------------ENLNAAKKAIAFLKQNELGRVTFLPLDSikgteiqGNDR 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 670 SQLNESKEKVSQLDIQIKAKTEL--LLSAEAAKAAQRADlqnhLDTAQHALQDKQQELNKVSVQLDQLTAKF-----QEK 742
Cdd:TIGR02168 592 EILKNIEGFLGVAKDLVKFDPKLrkALSYLLGGVLVVDD----LDNALELAKKLRPGYRIVTLDGDLVRPGGvitggSAK 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 743 QEHCIqleshlkdhkekhLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEV 822
Cdd:TIGR02168 668 TNSSI-------------LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 823 VSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGD---RMQAAVTELTAVKAQKDALLAELST 899
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEleaQIEQLKEELKALREALDELRAELTL 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 900 TKEKLSKVSDSLKNSKSEFEkenqkgkaavldlekACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVK 979
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIA---------------ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 980 GEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSAL 1059
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAL 959
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1060 QSNYEKCQADLKQLQSDLYGKESEL----LATRQDLKSVEEK---LTLAQEDLISNRNQI 1112
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKIKELgpvnLAAIEEYEELKERydfLTAQKEDLTEAKETL 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
423-1230 |
1.09e-20 |
|
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: 99.36 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 423 LREVESTRQHLKVEVKQ---LQQQREEKEQHGLQLQG-EVSQLHCKLLETERQLGEAHGRLKEqrqlSSEKLMEKEQQVA 498
Cdd:TIGR02168 195 LNELERQLKSLERQAEKaerYKELKAELRELELALLVlRLEELREELEELQEELKEAEEELEE----LTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 499 DLQLKLSRLEEQLkekvtnsTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGK 578
Cdd:TIGR02168 271 ELRLEVSELEEEI-------EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 579 ESVSLLEKEREDLYAKIQAGEgetAVLNQLQEKNHALQQQLTQLTEKLKnqseSHKQAEENLHDQVQEQKAHLRAAQDRV 658
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELE---AELEELESRLEELEEQLETLRSKVA----QLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 659 LSLETSVSELSSQLNESKEKVSQLDIQIKAKTElllsaeaakaaqrADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAK 738
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELEEEL-------------EELQEELERLEEALEELREELEEAEQALDAAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 739 FQEKQEHCIQLESHLKDHKEKHLS---LEQKVEDLEGHIKKLeADALEVKASKEQALQSLQQQRQLstDLELRNAELSR- 814
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFSEGvkaLLKNQSGLSGILGVL-SELISVDEGYEAAIEAALGGRLQ--AVVVENLNAAKk 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 815 --ELQEQEEVVSCT--KLDLQNKSEILENIKQTLTKKEEENVVLKQefekLSQDSKTQHKELGDRMQ--AAVTELTAVKA 888
Cdd:TIGR02168 561 aiAFLKQNELGRVTflPLDSIKGTEIQGNDREILKNIEGFLGVAKD----LVKFDPKLRKALSYLLGgvLVVDDLDNALE 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 889 QKDALLAELS--TTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELK---HQLQVQAESALKEQEDLKKSLEK 963
Cdd:TIGR02168 637 LAKKLRPGYRivTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEekiAELEKALAELRKELEELEEELEQ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 964 EKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKtvleNKLQQQSS 1043
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI----EELEAQIE 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1044 QAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQ 1123
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1124 AAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAE----MEEIKCRQEK---EITKLNEELKSHKQES 1196
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEElrekLAQLELRLEGlevRIDNLQERLSEEYSLT 952
|
810 820 830
....*....|....*....|....*....|....
gi 568967300 1197 IKEITNLKDAKQLLIQqklELQGRVDSLKAALEQ 1230
Cdd:TIGR02168 953 LEEAEALENKIEDDEE---EARRRLKRLENKIKE 983
|
|
| FYVE_like_SF |
cd00065 |
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ... |
1399-1448 |
1.02e-19 |
|
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.
Pssm-ID: 277249 [Multi-domain] Cd Length: 52 Bit Score: 83.74 E-value: 1.02e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568967300 1399 NCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSK--KPVRVCDACF 1448
Cdd:cd00065 1 RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSFGsgKPVRVCDSCY 52
|
|
| FYVE_LST2 |
cd15731 |
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ... |
1391-1449 |
2.34e-19 |
|
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; Lst2, also termed zinc finger FYVE domain-containing protein 28, is a monoubiquitinylated phosphoprotein that functions as a negative regulator of epidermal growth factor receptor (EGFR) signaling. Unlike other FYVE domain-containing proteins, Lst2 displays primarily non-endosomal localization. Its endosomal localization is regulated by monoubiquitinylation. Lst2 physically binds Trim3, also known as BERP or RNF22, which is a coordinator of endosomal trafficking and interacts with Hrs and a complex that biases cargo recycling.
Pssm-ID: 277270 [Multi-domain] Cd Length: 65 Bit Score: 83.16 E-value: 2.34e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1391 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSK--KPVRVCDACFN 1449
Cdd:cd15731 5 WVPDEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRYGqmKPVRVCNHCFM 65
|
|
| FYVE_ANFY1 |
cd15728 |
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ... |
1391-1451 |
7.81e-19 |
|
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar proteins; ANFY1, also termed ankyrin repeats hooked to a zinc finger motif (Ankhzn), is a novel cytoplasmic protein that belongs to a new group of double zinc finger proteins involved in vesicle or protein transport. It is ubiquitously expressed in a spatiotemporal-specific manner and is located on endosomes. ANFY1 contains an N-terminal coiled-coil region and a BTB/POZ domain, ankyrin repeats in the middle, and a C-terminal FYVE domain.
Pssm-ID: 277267 [Multi-domain] Cd Length: 63 Bit Score: 81.70 E-value: 7.81e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568967300 1391 WAEDNevqNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKnaLTPSSK----KPVRVCDACFNDL 1451
Cdd:cd15728 4 WADGD---YCYECGVKFGITTRKHHCRHCGRLLCSKCSTK--EVPIIKfdlnKPVRVCDVCFDVL 63
|
|
| FYVE_endofin |
cd15729 |
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ... |
1391-1451 |
8.29e-19 |
|
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE domain-containing protein 16 (ZFY16), or endosome-associated FYVE domain protein, is a FYVE domain-containing protein that is localized to EEA1-containing endosomes. It is regulated by phosphoinositol lipid and engaged in endosome-mediated receptor modulation. Endofin is involved in Bone morphogenetic protein (BMP) signaling through interacting with Smad1 preferentially and enhancing Smad1 phosphorylation and nuclear localization upon BMP stimulation. It also functions as a scaffold protein that brings Smad4 to the proximity of the receptor complex in Transforming growth factor (TGF)-beta signaling. Moreover, endofin is a novel tyrosine phosphorylation target downstream of epidermal growth factor receptor (EGFR) in EGF-signaling. In addition, endofin plays a role in endosomal trafficking by recruiting cytosolic TOM1, an important molecule for membrane recruitment of clathrin, onto endosomal membranes.
Pssm-ID: 277268 [Multi-domain] Cd Length: 68 Bit Score: 81.63 E-value: 8.29e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967300 1391 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAE-CSTKNALTPSSKKPVRVCDACFNDL 1451
Cdd:cd15729 7 WVPDSEAPNCMQCEVKFTFTKRRHHCRACGKVLCSAcCSLKARLEYLDNKEARVCVPCYQTL 68
|
|
| FYVE_WDFY3 |
cd15719 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ... |
1391-1451 |
1.09e-18 |
|
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar proteins; WDFY3, also termed autophagy-linked FYVE protein (Alfy), is a ubiquitously expressed phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein required for selective macroautophagic degradation of aggregated proteins. It regulates the protein degradation through the direct interaction with the autophagy protein Atg5. Moreover, WDFY3 acts as a scaffold that bridges its cargo to the macroautophagic machinery via the creation of a greater complex with Atg12, Atg16L, and LC3. It also functionally associates with sequestosome-1/p62 (SQSTM1) in osteoclasts. WDFY3 shuttles between the nucleus and cytoplasm. It predominantly localizes to the nucleus and nuclear membrane under basal conditions, but is recruited to cytoplasmic ubiquitin-positive protein aggregates under stress conditions. WDFY3 contains a PH-BEACH domain assemblage, five WD40 repeats and a PtdIns3P-binding FYVE domain.
Pssm-ID: 277259 [Multi-domain] Cd Length: 65 Bit Score: 81.28 E-value: 1.09e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967300 1391 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSK--KPVRVCDACFNDL 1451
Cdd:cd15719 3 WVKDEGGDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFESEIRRLRisRPVRVCQACYNIL 65
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
488-1200 |
1.22e-18 |
|
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: 92.82 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 488 EKLMEKEQQVADLQLKLSRLEEQLKekvTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKI 567
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 568 QNLEALLQKGKESVSLLEKEREDLYAKIQA-GEGETavlNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEEnlhdQVQE 646
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQ---LRVKEKIGELEAEIASLERSIAEKERELEDAEE----RLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 647 QKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLdiqiKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELN 726
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL----KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 727 KVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLE 806
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 807 LRNAELSRELQEQEEVVSctkldlQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQ---HKELGDRMQAAVTEL 883
Cdd:TIGR02169 483 KELSKLQRELAEAEAQAR------ASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYAtaiEVAAGNRLNNVVVED 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 884 TAVKAQKDALLAE----------LSTTKEKLSKVSDSLKNSKS-------EFEKENQKGKAAVL-------DLEKACKEL 939
Cdd:TIGR02169 557 DAVAKEAIELLKRrkagratflpLNKMRDERRDLSILSEDGVIgfavdlvEFDPKYEPAFKYVFgdtlvveDIEAARRLM 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 940 --------------------------------KHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQN 987
Cdd:TIGR02169 637 gkyrmvtlegelfeksgamtggsraprggilfSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 988 TLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQ-ELAAEKGKLSALQSNYEKC 1066
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKlEEALNDLEARLSHSRIPEI 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1067 QADLKQLQSDLYGKESELLATRQDLKSVEEKLTLA-------QEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEAL 1139
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLekeiqelQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1140 LKEQSKALEDAQREKSVKEKELVAEKSKLAEMeEIKCRQEKEITKLNEELKSHKQESIKEI 1200
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLRELERKIEEL-EAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| FYVE_RUFY1 |
cd15758 |
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ... |
1391-1451 |
1.70e-18 |
|
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.
Pssm-ID: 277297 [Multi-domain] Cd Length: 71 Bit Score: 80.88 E-value: 1.70e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1391 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDACFNDL 1451
Cdd:cd15758 6 WLKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLL 66
|
|
| FYVE_Hrs |
cd15720 |
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ... |
1391-1451 |
4.43e-18 |
|
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) and similar proteins; Hrs, also termed protein pp110, is a tyrosine phosphorylated protein that plays an important role in the signaling pathway of HGF. It is localized to early endosomes and an essential component of the endosomal sorting and trafficking machinery. Hrs interacts with hypertonia-associated protein Trak1, a novel regulator of endosome-to-lysosome trafficking. It can also forms an Hrs/actinin-4/BERP/myosin V protein complex that is required for efficient transferrin receptor (TfR) recycling but not for epidermal growth factor receptor (EGFR) degradation. Moreover, Hrs, together with STAM proteins, STAM1 and STAM2, and EPs15, forms a multivalent ubiquitin-binding complex that sorts ubiquitinated proteins into the multivesicular body pathway, and plays a regulatory role in endocytosis/exocytosis. Furthermore, Hrs functions as an interactor of the neurofibromatosis 2 tumor suppressor protein schwannomin/merlin. It is also involved in the inhibition of citron kinase-mediated HIV-1 budding. Hrs contains a single ubiquitin-interacting motif (UIM) that is crucial for its function in receptor sorting, and a FYVE domain that harbors double Zn2+ binding sites.
Pssm-ID: 277260 [Multi-domain] Cd Length: 61 Bit Score: 79.35 E-value: 4.43e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967300 1391 WAEDNEvqnCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSS--KKPVRVCDACFNDL 1451
Cdd:cd15720 2 WKDGDE---CHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSSTIPKFgiEKEVRVCDPCYEKL 61
|
|
| FYVE_scVPS27p_like |
cd15760 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
1390-1448 |
5.12e-18 |
|
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and similar proteins; scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif.
Pssm-ID: 277299 [Multi-domain] Cd Length: 59 Bit Score: 79.26 E-value: 5.12e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967300 1390 KWAEDNEvqnCMSCGKCFSVTVRRHHCRQCGNIFCAECSTK----NALTPSSkKPVRVCDACF 1448
Cdd:cd15760 1 HWKPDSR---CDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRriplPHLGPLG-VPQRVCDRCF 59
|
|
| FYVE_MTMR4 |
cd15733 |
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ... |
1391-1448 |
5.82e-18 |
|
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also termed FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2), or zinc finger FYVE domain-containing protein 11, is an dual specificity protein phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). It is localizes to early endosomes, as well as to Rab11- and Sec15-positive recycling endosomes, and regulates sorting from early endosomes. Moreover, MTMR4 is preferentially associated with and dephosphorylated the activated regulatory Smad proteins (R-Smads) in cytoplasm to keep transforming growth factor (TGF) beta signaling in homeostasis. It also functions as an essential negative modulator for the homeostasis of bone morphogenetic protein (BMP)/decapentaplegic (Dpp) signaling. In addition, MTMR4 acts as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4) and may play a role in the biological process of muscle breakdown. MTMR4 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain.
Pssm-ID: 277272 [Multi-domain] Cd Length: 60 Bit Score: 79.01 E-value: 5.82e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1391 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSK--KPVRVCDACF 1448
Cdd:cd15733 1 WVPDHAASHCFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPDEQlyDPVRVCNSCY 60
|
|
| FYVE_PKHF2 |
cd15755 |
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ... |
1391-1451 |
2.97e-17 |
|
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar proteins; Phafin-2, also termed endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains (EAPF), or pleckstrin homology domain-containing family F member 2 (PKHF2), or PH domain-containing family F member 2, or PH and FYVE domain-containing protein 2, or zinc finger FYVE domain-containing protein 18, is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.
Pssm-ID: 277294 [Multi-domain] Cd Length: 64 Bit Score: 77.38 E-value: 2.97e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967300 1391 WAEDNEVQNCMSCGKC-FSVTVRRHHCRQCGNIFCAECSTKNALTPS-SKKPVRVCDACFNDL 1451
Cdd:cd15755 2 WVPDSEATVCMRCQKAkFTPVNRRHHCRKCGFVVCGPCSEKKFLLPSqSSKPVRVCDFCYDLL 64
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
285-818 |
3.52e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.68 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 285 ERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLE 364
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 365 EKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQR 444
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 445 EEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRL------KEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNS 518
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLerleeeLEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 519 TELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAG 598
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 599 EGETAVLNQLQEKN---------HALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELS 669
Cdd:COG1196 542 AALAAALQNIVVEDdevaaaaieYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 670 SQLNESKEKVSQLDIQIKAKT-ELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQ 748
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLaGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 749 LESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQE 818
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| FYVE_ZF21 |
cd15727 |
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ... |
1391-1447 |
1.30e-16 |
|
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ZF21 is phosphoinositide-binding protein that functions as a regulator of focal adhesions and cell movement through interaction with focal adhesion kinase. It can also bind to the cytoplasmic tail of membrane type 1 matrix metalloproteinase, a potent invasion-promoting protease, and play a key role in regulating multiple aspects of cancer cell migration and invasion. ZF21 contains a FYVE domain, which corresponds to this model.
Pssm-ID: 277266 [Multi-domain] Cd Length: 64 Bit Score: 75.49 E-value: 1.30e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 568967300 1391 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTP--SSKKPVRVCDAC 1447
Cdd:cd15727 4 WVPDKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVPLPrmCFVDPVRVCNEC 62
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
126-984 |
2.45e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 85.11 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 126 DITLLRQEVQDLQASLKEekwYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQMKDLFEQ 205
Cdd:TIGR02168 226 ELALLVLRLEELREELEE---LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 206 KAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTEllqrpgIEDVAVLKKELVQVQTLMDNMTLE 285
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE------LESLEAELEELEAELEELESRLEE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 286 RERESEKLKDECKKLQSEHAHLEATINQLRSELakgpqevavyvqeiQKLKGSINELTQKNQNLTEKLQKKDLdythlee 365
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARL--------------ERLEDRRERLQQEIEELLKKLEEAEL------- 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 366 khneesasrKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVEStrqhlKVEVKQLQQQRE 445
Cdd:TIGR02168 436 ---------KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-----RLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 446 EKEQHGLQlqgevsqlhcKLLETERQLGEAHGRLKEqrQLSSEKLMEKEQQVAdlqlklsrLEEQLKEKVTNSTElqhql 525
Cdd:TIGR02168 502 EGFSEGVK----------ALLKNQSGLSGILGVLSE--LISVDEGYEAAIEAA--------LGGRLQAVVVENLN----- 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 526 ekskqqhqeqqaLQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAG----EGE 601
Cdd:TIGR02168 557 ------------AAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsylLGG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 602 TAVLNQLQEKNHalqqqltQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQdrVLSLETSVSELSSQLNESKEKVSQ 681
Cdd:TIGR02168 625 VLVVDDLDNALE-------LAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAE 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 682 LDIQIKAKTELLlsaeaakaaqrADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHL 761
Cdd:TIGR02168 696 LEKALAELRKEL-----------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 762 SLEQKVEDLEGHIKKLEADALEVKASKEqalqslqqqrqlstDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIK 841
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIE--------------QLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 842 QTLTKKEEENVVLKQEFEKLSQD------SKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSK 915
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDieslaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967300 916 SEFEKE----NQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQ 984
Cdd:TIGR02168 911 SELRREleelREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
130-859 |
2.46e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.12 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 130 LRQEVQDLQASLKEEKWysEELKKELEKYQG----LQQQEAKSDGLVTDSSAELQALEQQLEEAQtenfniKQMKDLFEQ 205
Cdd:TIGR02169 216 LLKEKREYEGYELLKEK--EALERQKEAIERqlasLEEELEKLTEEISELEKRLEEIEQLLEELN------KKIKDLGEE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 206 KAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKtellqrpgiEDVAVLKKELVQVQtlmdnmtle 285
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL---------AEIEELEREIEEER--------- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 286 reRESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDL------- 358
Cdd:TIGR02169 350 --KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEeladlna 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 359 DYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVK 438
Cdd:TIGR02169 428 AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 439 QLQQQREEKEQHGLQLQGEVSQL------HCKLLET-------------------------ERQLGEAHG-RLKEQRQLS 486
Cdd:TIGR02169 508 GGRAVEEVLKASIQGVHGTVAQLgsvgerYATAIEVaagnrlnnvvveddavakeaiellkRRKAGRATFlPLNKMRDER 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 487 SEKLMEKEQQVADLQLKLSRLEEQLKEK---------VTNSTELQHQL--------------EKS------KQQHQEQQA 537
Cdd:TIGR02169 588 RDLSILSEDGVIGFAVDLVEFDPKYEPAfkyvfgdtlVVEDIEAARRLmgkyrmvtlegelfEKSgamtggSRAPRGGIL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 538 LQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEknhALQQ 617
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE---ELEE 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 618 QLTQLTEKLKNQSESHKQAEENLhDQVQEQKAHLRAAQDRVLS--LETSVSELSSQLNESKEKVSQLDIQIKAkTELLLS 695
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLRE-IEQKLN 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 696 AEAAKAAQRADLQNHLDTAQHALQDKQQELNKvsvQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIK 775
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK---EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 776 KLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTkLDLQNKSEILENIKQTLTKKEEENVVLK 855
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE-LSLEDVQAELQRVEEEIRALEPVNMLAI 978
|
....
gi 568967300 856 QEFE 859
Cdd:TIGR02169 979 QEYE 982
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
544-1340 |
2.91e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 84.73 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 544 AKLREAQNDLEQVLRQIG------------------DKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGE---- 601
Cdd:TIGR02169 170 RKKEKALEELEEVEENIErldliidekrqqlerlrrEREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQlasl 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 602 TAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRvlsLETSVSELSSQLNESKEKVSQ 681
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAS---LERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 682 LDIQIKAktelLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHL 761
Cdd:TIGR02169 327 LEAEIDK----LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 762 SLEQKVEDLEGHIKKLEADALEVKASKEQALQSLqqqrqlsTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIK 841
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKI-------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 842 QTLTKKEEENVVLKQEFEKL----------SQDSKTQHKELGDRMQ---AAVTELTAVKAQKDALLAELSTTKEKLSKVS 908
Cdd:TIGR02169 476 EEYDRVEKELSKLQRELAEAeaqaraseerVRGGRAVEEVLKASIQgvhGTVAQLGSVGERYATAIEVAAGNRLNNVVVE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 909 DSLKNSKS-EFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEK------------------EKETSQ 969
Cdd:TIGR02169 556 DDAVAKEAiELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafkyvfgdtlvvediEAARRL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 970 QLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLEN---KLQQQSSQAA 1046
Cdd:TIGR02169 636 MGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENrldELSQELSDAS 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1047 QELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKS-----IQE 1121
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsrIPE 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1122 LQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEikcrQEKEITKLNEELKSHKQESIKEIT 1201
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE----QIKSIEKEIENLNGKKEELEEELE 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1202 NLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAkLHSEIKEKEAGMKKHEENEAKL 1281
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA-LEEELSEIEDPKGEDEEIPEEE 950
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967300 1282 TmqvttlneNLGTVKKEWQSSQRRVSELE--------------KQTDDLRGEIAVLEAtvqnnqdERRALLER 1340
Cdd:TIGR02169 951 L--------SLEDVQAELQRVEEEIRALEpvnmlaiqeyeevlKRLDELKEKRAKLEE-------ERKAILER 1008
|
|
| FYVE_FYCO1 |
cd15726 |
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ... |
1391-1448 |
3.41e-16 |
|
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also termed zinc finger FYVE domain-containing protein 7, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that is associated with the exterior of autophagosomes and mediates microtubule plus-end-directed vesicle transport. It acts as an effector of GTP-bound Rab7, a GTPase that recruits FYCO1 to autophagosomes and has been implicated in autophagosome-lysosomal fusion. FYCO1 also interacts with two microtubule motor proteins, kinesin (KIF) 5B and KIF23, and thus functions as a platform for assembly of vesicle fusion and trafficking factors. FYCO1 contains an N-terminal alpha-helical RUN domain followed by a long central coiled-coil region, a FYVE domain and a GOLD (Golgi dynamics) domain in C-terminus.
Pssm-ID: 277265 [Multi-domain] Cd Length: 58 Bit Score: 74.13 E-value: 3.41e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568967300 1391 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDACF 1448
Cdd:cd15726 1 WQDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKACF 58
|
|
| FYVE_FGD6 |
cd15743 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ... |
1391-1448 |
3.51e-16 |
|
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar proteins; FGD6, also termed zinc finger FYVE domain-containing protein 24 is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) whose biological function remains unclear. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Moreover, the FYVE domain of FGD6 is a canonical FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site.
Pssm-ID: 277282 [Multi-domain] Cd Length: 61 Bit Score: 74.01 E-value: 3.51e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 568967300 1391 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNA-LTPSSKKPVRVCDACF 1448
Cdd:cd15743 3 WIPDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNKApLEYLKNKSARVCDECF 61
|
|
| FYVE_FGD1_2_4 |
cd15741 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ... |
1390-1451 |
7.85e-16 |
|
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia FGD1, FGD2, FGD4; This family represents a group of Rho GTPase cell division cycle 42 (Cdc42)-specific guanine nucleotide exchange factors (GEFs), including FYVE, RhoGEF and PH domain-containing protein FGD1, FGD2 and FGD4. FGD1, also termed faciogenital dysplasia 1 protein, or Rho/Rac guanine nucleotide exchange factor FGD1 (Rho/Rac GEF), or zinc finger FYVE domain-containing protein 3, is a central regulator of extracellular matrix remodeling and belongs to the DBL family of GEFs that regulate the activation of the Rho GTPases. FGD1 is encoded by gene FGD1. Disabling mutations in the FGD1 gene cause the human X-linked developmental disorder faciogenital dysplasia (FGDY, also known as Aarskog-Scott syndrome). FGD2, also termed zinc finger FYVE domain-containing protein 4, is expressed in antigen-presenting cells, including B lymphocytes, macrophages, and dendritic cells. It localizes to early endosomes and active membrane ruffles. It plays a role in leukocyte signaling and vesicle trafficking in cells specialized to present antigen in the immune system. FGD4, also termed actin filament-binding protein frabin, or FGD1-related F-actin-binding protein, or zinc finger FYVE domain-containing protein 6, functions as an F-actin-binding (FAB) protein showing significant homology to FGD1. It induces the formation of filopodia through the activation of Cdc42 in fibroblasts. Those FGD proteins possess a similar domain organization that contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus. However, each FGD has a unique N-terminal region that may directly or indirectly interact with F-actin. FGD1 and FGD4 have an N-terminal proline-rich domain (PRD) and an N-terminal F-actin binding (FAB) domain, respectively. This model corresponds to the FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site. FGD1 possesses a FYVE-like domain that lack the N-terminal WxxD motif. Moreover, FGD2 is the only known RhoGEF family member shown to have a functional FYVE domain and endosomal binding activity.
Pssm-ID: 277280 [Multi-domain] Cd Length: 65 Bit Score: 73.29 E-value: 7.85e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568967300 1390 KWAEDNEVQNCMSCGKCF-SVTVRRHHCRQCGNIFCAECSTKNA-LTPSSKKPVRVCDACFNDL 1451
Cdd:cd15741 2 RWVRDNEVTMCMRCKEPFnALTRRRHHCRACGYVVCWKCSDYKAtLEYDGNKLNRVCKHCYVIL 65
|
|
| FYVE_RBNS5 |
cd15716 |
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ... |
1391-1451 |
8.74e-16 |
|
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and similar proteins; Rbsn-5, also termed zinc finger FYVE domain-containing protein 20, is a novel Rab5 effector that is complexed to the Sec1-like protein VPS45 and recruited in a phosphatidylinositol-3-kinase-dependent fashion to early endosomes. It also binds to Rab4 and EHD1/RME-1, two regulators of the recycling route, and is involved in cargo recycling to the plasma membrane. Moreover, Rbsn-5 regulates endocytosis at the apical side of the wing epithelium and plays a role of the apical endocytic trafficking of Fmi in the establishment of planar cell polarity (PCP).
Pssm-ID: 277256 [Multi-domain] Cd Length: 61 Bit Score: 72.76 E-value: 8.74e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1391 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALtpsskkPVRVCDACFNDL 1451
Cdd:cd15716 4 WVNDSDVPFCPDCGKKFNLARRRHHCRLCGSIMCNKCSQFLPL------HIRCCHHCKDLL 58
|
|
| FYVE_MTMR3 |
cd15732 |
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ... |
1390-1448 |
1.17e-15 |
|
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also termed Myotubularin-related phosphatase 3, or FYVE domain-containing dual specificity protein phosphatase 1 (FYVE-DSP1), or zinc finger FYVE domain-containing protein 10, is a ubiquitously expressed phosphoinositide 3-phosphatase specific for phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and PIKfyve, which produces PtdIns(3,5)P2 from PtdIns3P. It regulates cell migration through modulating phosphatidylinositol 5-phosphate (PtdIns5P) levels. MTMR3 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain. Unlike conventional FYVE domains, the FYVE domain of MTMR3 neither confers endosomal localization nor binds to PtdIns3P. It is also not required for the enzyme activity of MTMR3. In contrast, the PH-G domain binds phosphoinositides.
Pssm-ID: 277271 [Multi-domain] Cd Length: 61 Bit Score: 72.62 E-value: 1.17e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1390 KWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSK--KPVRVCDACF 1448
Cdd:cd15732 1 RWVPDHLAASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLPVPSQQlfEPSRVCKSCF 61
|
|
| FYVE_RABE_unchar |
cd15739 |
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ... |
1390-1448 |
1.34e-15 |
|
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This family includes a group of uncharacterized rab GTPase-binding effector proteins found in bilateria. Although their biological functions remain unclear, they all contain a FYVE domain that harbors a putative phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding site.
Pssm-ID: 277278 [Multi-domain] Cd Length: 73 Bit Score: 72.76 E-value: 1.34e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 568967300 1390 KWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDACF 1448
Cdd:cd15739 3 RWQHEDDVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCH 61
|
|
| FYVE_ZFY26 |
cd15724 |
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ... |
1391-1449 |
2.55e-15 |
|
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed FYVE domain-containing centrosomal protein (FYVE-CENT), or spastizin, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that localizes to the centrosome and midbody. ZFY26 and its interacting partners TTC19 and KIF13A are required for cytokinesis. It also interacts with Beclin 1, a subunit of class III phosphatidylinositol 3-kinase complex, and may have potential implications for carcinogenesis. In addition, it has been considered as the causal agent of a rare form of hereditary spastic paraplegia. ZFY26 contains a FYVE domain that is important for targeting of FYVE-CENT to the midbody.
Pssm-ID: 277263 [Multi-domain] Cd Length: 61 Bit Score: 71.78 E-value: 2.55e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1391 WAEDNEVQNCMSC-GKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKK-PVRVCDACFN 1449
Cdd:cd15724 1 WVPDEAVSVCMVCqVERFSMFNRRHHCRRCGRVVCSSCSTKKMLVEGYREnPVRVCDQCYE 61
|
|
| FYVE_ZFYV1 |
cd15734 |
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ... |
1391-1448 |
2.63e-15 |
|
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar proteins; ZFYV1, also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYV1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by wortmannin, a PI3-kinase inhibitor. In addition to C-terminal tandem FYVE domain, ZFYV1 contains an N-terminal putative C2H2 type zinc finger and a possible nucleotide binding P-loop.
Pssm-ID: 277273 [Multi-domain] Cd Length: 61 Bit Score: 71.59 E-value: 2.63e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1391 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSS--KKPVRVCDACF 1448
Cdd:cd15734 2 WVPDSEIKECSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRgwDHPVRVCDPCA 61
|
|
| FYVE_PKHF1 |
cd15754 |
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ... |
1391-1451 |
3.51e-15 |
|
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar proteins; Phafin-1, also termed lysosome-associated apoptosis-inducing protein containing PH (pleckstrin homology) and FYVE domains (LAPF), or pleckstrin homology domain-containing family F member 1 (PKHF1), or PH domain-containing family F member 1, or apoptosis-inducing protein, or PH and FYVE domain-containing protein 1, or zinc finger FYVE domain-containing protein 15, is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway.
Pssm-ID: 277293 [Multi-domain] Cd Length: 64 Bit Score: 71.53 E-value: 3.51e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967300 1391 WAEDNEVQNCMSCGKC-FSVTVRRHHCRQCGNIFCAECSTKNALTPS-SKKPVRVCDACFNDL 1451
Cdd:cd15754 2 WIPDKATDICMRCTQTnFSLLTRRHHCRKCGFVVCHECSRQRFLIPRlSPKPVRVCSLCYRKL 64
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
806-1343 |
3.60e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 81.73 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 806 ELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTA 885
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 886 VKAQKDAllAELSTTKEKlsKVSDSLKNSKSEFEKENQKGKAAVLDLEKAcKELKHQLQVQ--AESALKEQEDLKKSLEK 963
Cdd:PTZ00121 1362 AEEKAEA--AEKKKEEAK--KKADAAKKKAEEKKKADEAKKKAEEDKKKA-DELKKAAAAKkkADEAKKKAEEKKKADEA 1436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 964 EKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQgtinQLKQSAEQKKKQiEALQGEVKNAVSQKTVLENKLQQQSS 1043
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD----EAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1044 QAAQELAAEKGKLSALQSNYEKCQADlkQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQElQ 1123
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKKAEEAKKAD--EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK-K 1588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1124 AAKASLEQDSAKKEALLKEQSKALEDAQREKsVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKeitnl 1203
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAK-IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK----- 1662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1204 kdAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTM 1283
Cdd:PTZ00121 1663 --AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1284 QVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEI-AVLEATVQNNQDERRALLERCLK 1343
Cdd:PTZ00121 1741 EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| FYVE_spVPS27p_like |
cd15735 |
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ... |
1394-1448 |
5.43e-15 |
|
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 (spVps27p) and similar proteins; spVps27p, also termed suppressor of ste12 deletion protein 4 (Sst4p), is a conserved homolog of budding Saccharomyces cerevisiae Vps27 and of mammalian Hrs. It functions as a downstream factor for phosphatidylinositol 3-kinase (PtdIns 3-kinase) in forespore membrane formation with normal morphology. It colocalizes and interacts with Hse1p, a homolog of Saccharomyces cerevisiae Hse1p and of mammalian STAM, to form a complex whose ubiquitin-interacting motifs (UIMs) are important for sporulation. spVps27p contains a VHS (Vps27p/Hrs/Stam) domain, a FYVE domain, and two UIMs.
Pssm-ID: 277274 [Multi-domain] Cd Length: 59 Bit Score: 70.64 E-value: 5.43e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568967300 1394 DNEVqnCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTP--SSKKPVRVCDACF 1448
Cdd:cd15735 5 DSDV--CMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPhfGINQPVRVCDGCY 59
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
651-1339 |
5.95e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.37 E-value: 5.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 651 LRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSV 730
Cdd:COG1196 181 LEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 731 QLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNA 810
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 811 ELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQK 890
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 891 DALLAELSTTKEKLSKvsdslknsKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQ 970
Cdd:COG1196 421 EELEELEEALAELEEE--------EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 971 LKIELNSVKGEVSQAQNTLKQKEKDEQQLqgtINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENkLQQQSSQAAQELA 1050
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAALLLAGLRG---LAGAVAVLIGVEAAYEAALEAALAAALQNIVVED-DEVAAAAIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1051 AEKGKLSALQSNYEKcQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRnqignqnksiqELQAAKASLE 1130
Cdd:COG1196 569 AKAGRATFLPLDKIR-ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT-----------LVAARLEAAL 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1131 QDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLL 1210
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1211 IQQKLELQgRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMkkheeneakltmqvttlnE 1290
Cdd:COG1196 717 LEEELEEE-ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI------------------E 777
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 568967300 1291 NLGTV----KKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQN-NQDERRALLE 1339
Cdd:COG1196 778 ALGPVnllaIEEYEELEERYDFLSEQREDLEEARETLEEAIEEiDRETRERFLE 831
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
130-778 |
9.04e-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: 80.10 E-value: 9.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 130 LRQEVQDLQASLKEEKWYSEELKKELEKYQG----LQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQMKDLFEQ 205
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKelyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 206 KAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRpgIEDVAVLKKELVQVQTLMDNMTLE 285
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL--ELQIASLNNEIERLEARLERLEDR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 286 RERESEKLKDECKKLQS-EHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLE 364
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 365 ---EKHNEESASRKTLQASLHQRDLDCQQLQARL-------TASESSLQ-RAQGELSEKAEAAQKLREELREVESTRQHL 433
Cdd:TIGR02168 496 rlqENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdegyeAAIEAALGgRLQAVVVENLNAAKKAIAFLKQNELGRVTF 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 434 KVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQL-------------------------------------GE-- 474
Cdd:TIGR02168 576 LPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsyllggvlvvddldnalelakklrpgyrivtldGDlv 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 475 -AHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDL 553
Cdd:TIGR02168 656 rPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 554 EQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGEtavLNQLQEKNHALQQQLTQLTEKLKNQSESH 633
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE---IEELEAQIEQLKEELKALREALDELRAEL 812
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 634 KQAEENLHDQVQ----------EQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQ 703
Cdd:TIGR02168 813 TLLNEEAANLRErleslerriaATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 704 RADLQN----------HLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQE----------------------------- 744
Cdd:TIGR02168 893 RSELEElseelrelesKRSELRRELEELREKLAQLELRLEGLEVRIDNLQErlseeysltleeaealenkieddeeearr 972
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 568967300 745 HCIQLESHLK--------------DHKEKHLSLEQKVEDLEGHIKKLE 778
Cdd:TIGR02168 973 RLKRLENKIKelgpvnlaaieeyeELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
131-719 |
1.24e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 131 RQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTEnFNIKQmkdlfeQKAAQL 210
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQ------AEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 211 ATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRpgIEDVAVLKKELVQVQtlmdnmtLERERES 290
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL--EEELEEAEEELEEAE-------AELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 291 EKLKDECKKLQSEHAHLEATINQLRSELakgpqevavyvQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEE 370
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEAL-----------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 371 SASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREE-KEQ 449
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 450 HGLQLQGEVSQLHCKLL----ETERQLGEAHGRLKEQRQLSSEKLmEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQL 525
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIgveaAYEAALEAALAAALQNIVVEDDEV-AAAAIEYLKAAKAGRATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 526 EKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDkdqkiqnlEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVL 605
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA--------ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 606 NQLQEKNHALQQQLtQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQ 685
Cdd:COG1196 665 GSRRELLAALLEAE-AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
570 580 590
....*....|....*....|....*....|....
gi 568967300 686 IKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQ 719
Cdd:COG1196 744 EEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
362-1098 |
2.49e-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: 78.62 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 362 HLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELS-EKAEAAQKLREELREVESTRQHLKVEVKQL 440
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQmERDAMADIRRRESQSQEDLRNQLQNTVHEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 441 QQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQ----QVADLQLKLSRLEEQLKEKVT 516
Cdd:pfam15921 155 EAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSmstmHFRSLGSAISKILRELDTEIS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 517 ----NSTELQHQLEKSKQqhqeqqalqqsataklrEAQNDLEQVLRQIGDKdqkiqnLEALLQKGKESVSLLEKEREDLY 592
Cdd:pfam15921 235 ylkgRIFPVEDQLEALKS-----------------ESQNKIELLLQQHQDR------IEQLISEHEVEITGLTEKASSAR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 593 AKIQAGEGETAVLN-QLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQ 671
Cdd:pfam15921 292 SQANSIQSQLEIIQeQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 672 LNESKEKVSQLDIQI-KAKTELLLSAEAAKAAQRADLQNHL--DTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQ 748
Cdd:pfam15921 372 SGNLDDQLQKLLADLhKREKELSLEKEQNKRLWDRDTGNSItiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMA 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 749 LESHLKDHKEKHLSLEQKVEDLEGHIKK----LEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSR-------ELQ 817
Cdd:pfam15921 452 AIQGKNESLEKVSSLTAQLESTKEMLRKvveeLTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsrvdlKLQ 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 818 EQEEVVScTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQ--------------DSKTQHKELGDRmQAAVTEL 883
Cdd:pfam15921 532 ELQHLKN-EGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagamqvEKAQLEKEINDR-RLELQEF 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 884 TAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEK 963
Cdd:pfam15921 610 KILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEE 689
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 964 EKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVK-------NAVSQKTVL-- 1034
Cdd:pfam15921 690 METTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQfleeamtNANKEKHFLke 769
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1035 -ENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQ-----SDLYGKESELLATRQDLKSVEEKL 1098
Cdd:pfam15921 770 eKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEvaldkASLQFAECQDIIQRQEQESVRLKL 839
|
|
| FYVE_RUFY2 |
cd15759 |
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ... |
1391-1447 |
2.52e-14 |
|
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions.
Pssm-ID: 277298 [Multi-domain] Cd Length: 71 Bit Score: 69.28 E-value: 2.52e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568967300 1391 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDAC 1447
Cdd:cd15759 4 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSC 60
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
990-1339 |
6.89e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.02 E-value: 6.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 990 KQKEKDEQQL---QGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKC 1066
Cdd:TIGR02168 172 ERRKETERKLertRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1067 QADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEA-LLKEQSK 1145
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAqLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1146 ALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEitklnEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLK 1225
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAEL-----EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1226 AALEQEKESQQlmreqvkkeeEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRR 1305
Cdd:TIGR02168 407 ARLERLEDRRE----------RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330 340 350
....*....|....*....|....*....|....
gi 568967300 1306 VSELEKQTDDLRGEIAVLEATVQNNQDERRALLE 1339
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
724-1380 |
8.13e-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: 77.03 E-value: 8.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 724 ELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKL-EADALEVKASKEQALQSLQQQRQLS 802
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 803 TDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKL---SQDSKTQHKELGDRMQAA 879
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLraeLEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 880 VTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQvQAESALKEQEDLKK 959
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW-KLEQLAADLSKYEQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 960 SLEKEKETSQQLKIELNSVKGEVSQAQNTLKQ--------------KEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVK 1025
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARAseervrggraveevLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1026 NAVsqktVLENKLqqqSSQAAQELAAEK--GKLSALQSNyekcqaDLKQLQSDL-YGKESELLATRQDLKSVEEKL---- 1098
Cdd:TIGR02169 550 NNV----VVEDDA---VAKEAIELLKRRkaGRATFLPLN------KMRDERRDLsILSEDGVIGFAVDLVEFDPKYepaf 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1099 ------TLAQEDLISNRNQIGnqnksiqelQAAKASLEQDsakkealLKEQSKALEDAQREKSVKEKELVAEKSKLAEME 1172
Cdd:TIGR02169 617 kyvfgdTLVVEDIEAARRLMG---------KYRMVTLEGE-------LFEKSGAMTGGSRAPRGGILFSRSEPAELQRLR 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1173 EIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIqqklELQGRVDSLKAALEQEKESQQLMReQVKKEEEKRKEE 1252
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG----EIEKEIEQLEQEEEKLKERLEELE-EDLSSLEQEIEN 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1253 FSEKEAKLHSEIKEKEAGMKKHEENEAKLTM-----QVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATV 1327
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEArlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 568967300 1328 QNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQ 1380
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
|
|
| FYVE2_Vac1p_like |
cd15737 |
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ... |
1390-1447 |
5.51e-13 |
|
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the second FYVE domain that is responsible for the ability of Pep7p to efficiently interact with Vac1p and Vps45p.
Pssm-ID: 277276 [Multi-domain] Cd Length: 83 Bit Score: 65.60 E-value: 5.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1390 KWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCA----ECSTK---NALTPSS-----------------KKPVRVCD 1445
Cdd:cd15737 1 PWEDDSSVTHCPICLRSFGLLLRKHHCRLCGKVVCDdrrtKCSTEvplDLLSSALpdlpfvfkepqsdipddTKSVRVCR 80
|
..
gi 568967300 1446 AC 1447
Cdd:cd15737 81 DC 82
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
263-966 |
5.55e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.33 E-value: 5.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 263 EDVAVLKKELVQVQTLMDNM-----TLERERESeklKDECKKLQSEHAHLEATINQLRSELAkgpqevavyVQEIQKLKG 337
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKrqqleRLRREREK---AERYQALLKEKREYEGYELLKEKEAL---------ERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 338 SINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQaslhqrDLDCQQLQARLTASESSLQRAQGELSEKAEAAQ 417
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 418 KLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQ-- 495
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlk 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 496 -QVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALL 574
Cdd:TIGR02169 399 rEINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 575 QKGKESVSLLEKEREDLYAKIQAGEGE-------TAVLNQLQEKNHALQQQLTQLTEK------------LKN------- 628
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARASEERvrggravEEVLKASIQGVHGTVAQLGSVGERyataievaagnrLNNvvvedda 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 629 ----------------------------QSESHKQAEENLHDQV--------QEQKAHLRAAQDRVL--SLET------- 663
Cdd:TIGR02169 559 vakeaiellkrrkagratflplnkmrdeRRDLSILSEDGVIGFAvdlvefdpKYEPAFKYVFGDTLVveDIEAarrlmgk 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 664 --------------------SVSELSSQLNESKEKVSQLdiQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQ 723
Cdd:TIGR02169 639 yrmvtlegelfeksgamtggSRAPRGGILFSRSEPAELQ--RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 724 ELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSlqqqrqlst 803
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--------- 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 804 DLELRNAELSRELQEQEEVVSctkldlqNKSEILENIKQTLTKKEEENVVLKQEFEKLSQ---DSKTQHKELGDR---MQ 877
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEVS-------RIEARLREIEQKLNRLTLEKEYLEKEIQELQEqriDLKEQIKSIEKEienLN 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 878 AAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESaLKEQEDL 957
Cdd:TIGR02169 861 GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE-LSEIEDP 939
|
....*....
gi 568967300 958 KKSLEKEKE 966
Cdd:TIGR02169 940 KGEDEEIPE 948
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
706-1380 |
5.77e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.94 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 706 DLQNHLDTAQHAL-----QDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEAD 780
Cdd:TIGR02168 217 ELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 781 ALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSctklDLQNKSEILENIKQTLTKKEEEnvvlkqeFEK 860
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA----ELEEKLEELKEELESLEAELEE-------LEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 861 LSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELK 940
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 941 HQLQVQAESALKEQEDLKKSLEKEKETSQQlkiELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQsAEQKKKQIEAL 1020
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQ---ALDAAERELAQLQARLDSLERLQENLEGFSEGVKA-LLKNQSGLSGI 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1021 QGEVKNAVS-----------------QKTVLENKLQQQSSQAAQElAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESE 1083
Cdd:TIGR02168 522 LGVLSELISvdegyeaaieaalggrlQAVVVENLNAAKKAIAFLK-QNELGRVTFLPLDSIKGTEIQGNDREILKNIEGF 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1084 LLATrQDLKSVEEKLTLAQEDL-----ISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLkeqskALEDAQREKSVKE 1158
Cdd:TIGR02168 601 LGVA-KDLVKFDPKLRKALSYLlggvlVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVI-----TGGSAKTNSSILE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1159 KelvaeKSKLAEMEEIKCRQEKEITKLNEELKSHKqesiKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLm 1238
Cdd:TIGR02168 675 R-----RREIEELEEKIEELEEKIAELEKALAELR----KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ- 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1239 REQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNEnlgtvkkEWQSSQRRVSELEKQTDDLRG 1318
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE-------ELKALREALDELRAELTLLNE 817
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967300 1319 EIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQ 1380
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
|
| FYVE_scVPS27p_Vac1p_like |
cd15736 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
1400-1448 |
7.31e-13 |
|
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; The family includes Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and protein VAC1 (Vac1p). scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The FYVE domain in both Vps27p and Vac1p harbors a zinc-binding site composed of seven Cysteines and one Histidine, which is different from that of other FYVE domain containing proteins.
Pssm-ID: 277275 [Multi-domain] Cd Length: 56 Bit Score: 64.51 E-value: 7.31e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568967300 1400 CMSCGKCFSVTVRRHHCRQCGNIFCAECSTKN------ALTPSSKKPVRVCDACF 1448
Cdd:cd15736 2 CHTCSRTFNLNIRAHHCRKCGKLFCRRHLPNMiplnlsAYDPRNGKWYRCCHSCF 56
|
|
| FYVE_FGD5 |
cd15742 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ... |
1397-1452 |
8.89e-13 |
|
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar proteins; FGD5, also termed zinc finger FYVE domain-containing protein 23, is an endothelial cell (EC)-specific guanine nucleotide exchange factor (GEF) that regulates endothelial adhesion, survival, and angiogenesis by modulating phosphatidylinositol 3-kinase signaling. It functions as a novel genetic regulator of vascular pruning by activation of endothelial cell-targeted apoptosis. FGD5 is a homologue of FGD1 and contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. The FYVE domain of FGD5 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.
Pssm-ID: 277281 [Multi-domain] Cd Length: 67 Bit Score: 64.57 E-value: 8.89e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568967300 1397 VQNCMSCGKCFSVTVRRHHCRQCGNIFCAECS-TKNALTPSSKKPVRVCDACFNDLQ 1452
Cdd:cd15742 9 VMMCMNCGSDFTLTLRRHHCHACGKIVCRNCSrNKYPLKYLKDRPAKVCDGCFAELR 65
|
|
| FYVE_PIKfyve_Fab1 |
cd15725 |
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ... |
1391-1448 |
2.11e-12 |
|
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, also termed FYVE finger-containing phosphoinositide kinase, or 1-phosphatidylinositol 3-phosphate 5-kinase, or phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase), is a phosphoinositide 5-kinase that forms a complex with its regulators, the scaffolding protein Vac14 and the lipid phosphatase Fig4. The complex is responsible for synthesizing phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2] from phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). Then phosphatidylinositol-5-phosphate (PtdIns5P) is generated directly from PtdIns(3,5)P2. PtdIns(3,5)P2 and PtdIns5P regulate endosomal trafficking and responses to extracellular stimuli. At this point, PIKfyve is vital in early embryonic development. Moreover, PIKfyve forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, which plays a role in receptor tyrosine kinase (RTK) degradation. The phosphorylation of PIKfyve by AKT can facilitate Epidermal growth factor receptor (EGFR) degradation. In addition, PIKfyve may participate in the regulation of the glutamate transporters EAAT2, EAAT3 and EAAT4, and the cystic fibrosis transmembrane conductance regulator (CFTR). It is also essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle. It can be activated by protein kinase B (PKB/Akt) and further up-regulates human ether-a-go-go (hERG) channels. This family also includes the yeast and plant orthologs of human PIKfyve, Fab1. PIKfyve and its orthologs share a similar architecture. They contain an N-terminal FYVE domain, a middle region related to the CCT/TCP-1/Cpn60 chaperonins that are involved in productive folding of actin and tubulin, a second middle domain that contains a number of conserved cysteine residues (CCR) unique to this family, and a C-terminal lipid kinase domain related to PtdInsP kinases.
Pssm-ID: 277264 [Multi-domain] Cd Length: 62 Bit Score: 63.50 E-value: 2.11e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1391 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKP--VRVCDACF 1448
Cdd:cd15725 2 WMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPgdLRVCTYCC 61
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
178-1161 |
2.36e-12 |
|
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: 72.13 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 178 ELQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELL 257
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 258 QRPG-IEDVAVLKKELVQVQTLMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLK 336
Cdd:pfam01576 86 EEEErSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 337 GSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAA 416
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 417 Q----KLREE----------LREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLET-ERQLGEAHGRLKE 481
Cdd:pfam01576 246 QaalaRLEEEtaqknnalkkIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTlDTTAAQQELRSKR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 482 QRQLSS-EKLMEKEQQVADLQlklsrLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQI 560
Cdd:pfam01576 326 EQEVTElKKALEEETRSHEAQ-----LQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 561 GDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGE----TAVLNQLQEKNHALQQQLTQLTEKLKNQSEshkqa 636
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSElesvSSLLNEAEGKNIKLSKDVSSLESQLQDTQE----- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 637 eenlhdQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADlqnhLDTAQH 716
Cdd:pfam01576 476 ------LLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT----LEALEE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 717 ALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQ 796
Cdd:pfam01576 546 GKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERD 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 797 QQRQLSTDLELRNAELSREL---QEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELG 873
Cdd:pfam01576 626 RAEAEAREKETRALSLARALeeaLEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELE 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 874 DRMQAAV-------TELTAVKAQKDA-LLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKhQLQV 945
Cdd:pfam01576 706 DELQATEdaklrleVNMQALKAQFERdLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLK-ELEA 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 946 QAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQ---SAEQKKKQIEA--- 1019
Cdd:pfam01576 785 QIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEdlaASERARRQAQQerd 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1020 -LQGEVKNAVSQKTVLEN---KLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESellaTRQDLKSVE 1095
Cdd:pfam01576 865 eLADEIASGASGKSALQDekrRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERS----TSQKSESAR 940
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568967300 1096 EKLTLAQEDLISNRNQIGNQNKSiqELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKEL 1161
Cdd:pfam01576 941 QQLERQNKELKAKLQEMEGTVKS--KFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKL 1004
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
408-1298 |
2.53e-12 |
|
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: 71.93 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 408 ELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSS 487
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 488 EKLMEKEQQVADLQLKLSRLEEQlkekvtnstelqhQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKI 567
Cdd:pfam02463 257 KQEIEKEEEKLAQVLKENKEEEK-------------EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 568 QNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLtqltEKLKNQSESHKQAEENLHDQVQEQ 647
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL----LAKKKLESERLSSAAKLKEEELEL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 648 KahlraaqdrvlsletsvSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNK 727
Cdd:pfam02463 400 K-----------------SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 728 VSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLEL 807
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 808 RNAELSRELQEQEEVVSCTKLD--LQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTA 885
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEERQklVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 886 VKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEK 965
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIK 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 966 ETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQA 1045
Cdd:pfam02463 703 KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREK 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1046 AQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLaqedlisnrnqigNQNKSIQELQAA 1125
Cdd:pfam02463 783 TEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEE-------------LALELKEEQKLE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1126 KASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITnlkd 1205
Cdd:pfam02463 850 KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE---- 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1206 aKQLLIQQKLELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQV 1285
Cdd:pfam02463 926 -EAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEK 1004
|
890
....*....|...
gi 568967300 1286 TTLNENLGTVKKE 1298
Cdd:pfam02463 1005 KKLIRAIIEETCQ 1017
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
337-1153 |
2.78e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.10 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 337 GSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARltASESSLQRAQ----GELSEK 412
Cdd:PTZ00121 1058 GKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEAR--KAEEAKKKAEdarkAEEARK 1135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 413 AEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLME 492
Cdd:PTZ00121 1136 AEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAE 1215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 493 KEQQVADlqlklsrleEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEA 572
Cdd:PTZ00121 1216 EARKAED---------AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 573 LLQKGKESVSLLEKEREDLYAKIQAGEGETAvlNQLQEKNHALQQQltqlTEKLKNQSESHKQAEENLHDQVQEQKAHLR 652
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKA--DEAKKKAEEAKKK----ADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 653 AAQDRVLSLETSVSELSSQLNESKEKVSQLDI--QIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSV 730
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 731 QLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLE--------QKVEDLEGHIK--KLEADALEVKASKEQALQSLQQQRQ 800
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEakkkaeeaKKADEAKKKAEeaKKKADEAKKAAEAKKKADEAKKAEE 1520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 801 LSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEIL----ENIKQTLTKKEEENvvlKQEFEKLSQDSKTQHKELGDRM 876
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELkkaeEKKKAEEAKKAEED---KNMALRKAEEAKKAEEARIEEV 1597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 877 QAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAA--VLDLEKACKELKHQLQVQAESALKEQ 954
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeeLKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 955 EDLKKSLEKEKETSQQLKIE------LNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEV--KN 1026
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEaeeakkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeeKK 1757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1027 AVSQKTVLENKLQQQSSQAAQELAAE--KGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTlaqED 1104
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAVIEEelDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAI---KE 1834
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 568967300 1105 LISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQRE 1153
Cdd:PTZ00121 1835 VADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEE 1883
|
|
| FYVE_MTMR_unchar |
cd15738 |
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ... |
1390-1448 |
2.91e-12 |
|
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from eumetazoa; This family includes a group of uncharacterized myotubularin-related proteins mainly found in eumetazoa. Although their biological functions remain unclear, they share similar domain architecture that consists of an N-terminal pleckstrin homology (PH) domain, a highly conserved region related to myotubularin proteins, a C-terminal FYVE domain. The model corresponds to the FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.
Pssm-ID: 277277 [Multi-domain] Cd Length: 61 Bit Score: 62.73 E-value: 2.91e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1390 KWAEDNEVQNCmSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPS--SKKPVRVCDACF 1448
Cdd:cd15738 2 DWKSFRNVTEC-SCSTPFDHFSKKHHCWRCGNVFCTRCIDKQRALPGhlSQRPVPVCRACY 61
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
811-1397 |
3.00e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 811 ELSRELQEQEEVVSCTKLD-LQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQ 889
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 890 KDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAvldlekacKELKHQLQVQAESALKEQEDLKKSLEKEKETSQ 969
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL--------AEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 970 QLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLE-NKLQQQSSQAAQE 1048
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1049 LAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKAS 1128
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1129 LEQDS---AKKEALLKEQSKALEDAQREKSVKEKELVAEKSK----LAEMEEIKCRQEKEITKLNEELKSHKQESIKEIT 1201
Cdd:TIGR02168 529 ISVDEgyeAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELgrvtFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1202 NLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMREQVKK--------EEEKRKEEFSEKEAKLHSEIKEKEAGMKK 1273
Cdd:TIGR02168 609 KFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1274 HEENEAKLTMQVTT-------LNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLK--- 1343
Cdd:TIGR02168 689 LEEKIAELEKALAElrkeleeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEElee 768
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568967300 1344 -----------GEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQIKHTQALNRKWAEDNEV 1397
Cdd:TIGR02168 769 rleeaeeelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
|
| FYVE_WDFY1_like |
cd15718 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ... |
1391-1448 |
6.59e-12 |
|
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and similar proteins; This family includes WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2. WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. Both WDFY1 and WDFY2 contain a FYVE domain and multiple WD-40 repeats.
Pssm-ID: 277258 [Multi-domain] Cd Length: 70 Bit Score: 62.34 E-value: 6.59e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1391 WAEDNevqNCMSCGKCF-----------SVTVRRHHCRQCGNIFCAECSTKNALTPSS--KKPVRVCDACF 1448
Cdd:cd15718 3 WAESD---NCQKCSRPFfwnfkqmwekkTLGVRQHHCRKCGKAVCDKCSSNRSTIPVMgfEFPVRVCNECY 70
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
742-1399 |
6.74e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 6.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 742 KQEHCIQLESHLKDHKEKHLSLEQKVEDL-EGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLelRNAELSRELQEQE 820
Cdd:PTZ00121 1135 KAEDARKAEEARKAEDAKRVEIARKAEDArKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDA--RKAEAARKAEEER 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 821 EVVSCTKLDLQNKSEILENIKQTLTKKEEENvvlKQEFEKLSQDSKtqhKELGDRMQAAVTELTAVKAQKDALLAELSTT 900
Cdd:PTZ00121 1213 KAEEARKAEDAKKAEAVKKAEEAKKDAEEAK---KAEEERNNEEIR---KFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 901 KEKlsKVSDSLKNSKSEFEKENQKGKAavlDLEKACKELKHQlqvqAESALKEQEDLKKSLEKEKETSQQLKIELNSVKG 980
Cdd:PTZ00121 1287 EEK--KKADEAKKAEEKKKADEAKKKA---EEAKKADEAKKK----AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 981 EVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQ 1060
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK 1437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1061 SNYE-KCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISN--RNQIGNQNKSIQEL-QAAKASLEQDSAKK 1136
Cdd:PTZ00121 1438 KKAEeAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADeaKKKAEEAKKKADEAkKAAEAKKKADEAKK 1517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1137 --EALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQK 1214
Cdd:PTZ00121 1518 aeEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1215 LELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEaKLHSEIKEKEAGMKKHEENEAKLTMQvttlnenlgt 1294
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK-KEAEEKKKAEELKKAEEENKIKAAEE---------- 1666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1295 vKKEWQSSQRRVSELEKQTDDLRGEiavLEATVQNNQDERRAllERCLKGEGEIEKlqtKALELQRKLDNTTAAVQELGR 1374
Cdd:PTZ00121 1667 -AKKAEEDKKKAEEAKKAEEDEKKA---AEALKKEAEEAKKA--EELKKKEAEEKK---KAEELKKAEEENKIKAEEAKK 1737
|
650 660
....*....|....*....|....*
gi 568967300 1375 ENQSlQIKHTQALNRKWAEDNEVQN 1399
Cdd:PTZ00121 1738 EAEE-DKKKAEEAKKDEEEKKKIAH 1761
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
117-622 |
8.13e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 8.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 117 EAGLALTRDDITLLRQEVQDLQASLKEEKWYSEELKKELEKYQG----LQQQEAKSDGLVTDSSAELQALEQQLEEAQTE 192
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAeeyeLLAELARLEQDIARLEERRRELEERLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 193 NFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRpgIEDVAVLKKEL 272
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA--LRAAAELAAQL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 273 VQVQTLMDNMTLERER-----------------ESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKL 335
Cdd:COG1196 403 EELEEAEEALLERLERleeeleeleealaeleeEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 336 KGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEA 415
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAA 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 416 AQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSS-------- 487
Cdd:COG1196 563 IEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAalrravtl 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 488 -EKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDL-EQVLRQIGDKDQ 565
Cdd:COG1196 643 aGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELaEAEEERLEEELE 722
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 568967300 566 KIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQL 622
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
477-1324 |
9.40e-12 |
|
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: 70.00 E-value: 9.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 477 GRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVtnstelqhqlEKSKQQHQEQQALQQSATAKLREAQNDLEQV 556
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLK----------EQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 557 LRqigdkdQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQA 636
Cdd:pfam02463 235 NE------ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 637 EENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQH 716
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 717 ALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQ 796
Cdd:pfam02463 389 AAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 797 QQRQLSTdlELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRM 876
Cdd:pfam02463 469 KSEDLLK--ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 877 QAAVTELTAVKAQKDALLaelstTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQED 956
Cdd:pfam02463 547 TAVIVEVSATADEVEERQ-----KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 957 LKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLEN 1036
Cdd:pfam02463 622 AKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1037 KLQQQSSQAAQE---LAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIG 1113
Cdd:pfam02463 702 KKKEQREKEELKklkLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEERE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1114 NQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKsvKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHK 1193
Cdd:pfam02463 782 KTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQL--LIEQEEKIKEEELEELALELKEEQKLEKLAEEELERL 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1194 QESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKEsQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKK 1273
Cdd:pfam02463 860 EEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEK-KELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE 938
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1274 HEENEAKLTMQVttLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLE 1324
Cdd:pfam02463 939 ELLLEEADEKEK--EENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKE 987
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
611-1213 |
3.73e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 67.74 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 611 KNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLD---IQIK 687
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNsdlSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 688 AKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKV 767
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 768 EDLEGHIKKLEADALEVKASKEQA---LQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTL 844
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQKNkslESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 845 TKKEEEnvvlkqefeklSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLaeLSTTKEKLSKVSDSLKNSKSEFEKENQK 924
Cdd:TIGR04523 270 SEKQKE-----------LEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNQISQNNKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 925 GKAAVLDLEKACKELKH------QLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQ 998
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNsesensEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 999 LQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQelaaEKGKLSALQSNYEKCQADLKQLQSDLY 1078
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES----LETQLKVLSRSINKIKQNLEQKQKELK 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1079 GKESELLA----------TRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQ-ELQAAKASLEQDSAKKEAL-------- 1139
Cdd:TIGR04523 493 SKEKELKKlneekkeleeKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEdELNKDDFELKKENLEKEIDeknkeiee 572
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568967300 1140 LKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQ 1213
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
758-1340 |
4.21e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 758 EKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEevvsctkldlqnkseiL 837
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE----------------L 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 838 ENIKQTLTKKEEENVVLKQEFEKLSQD---SKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNS 914
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDiarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 915 KSEFEKENQKGKAAVLDLEKACKELKhQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEK 994
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELE-ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 995 DEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQ 1074
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1075 SDLYGKESELLAtrqdlksVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREK 1154
Cdd:COG1196 516 LAGLRGLAGAVA-------VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAAL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1155 SVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKES 1234
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1235 QQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTD 1314
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
570 580
....*....|....*....|....*.
gi 568967300 1315 DLRGEIAVLEATVQNNQDERRALLER 1340
Cdd:COG1196 749 EEEALEELPEPPDLEELERELERLER 774
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
351-524 |
1.05e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 351 EKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDcqQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTR 430
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE--LLEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 431 --------QHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQL 502
Cdd:COG4913 333 rgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
170 180
....*....|....*....|..
gi 568967300 503 KLSRLEEQLKEKVTNSTELQHQ 524
Cdd:COG4913 413 ALRDLRRELRELEAEIASLERR 434
|
|
| FYVE_FGD3 |
cd15740 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ... |
1394-1448 |
3.80e-10 |
|
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar proteins; FGD3, also termed zinc finger FYVE domain-containing protein 5, is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) that undergoes the ubiquitin ligase SCFFWD1/beta-TrCP-mediated proteasomal degradation. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Due to this difference, FGD3 may play different roles from that of FGD1 to regulate cell morphology or motility. The FYVE domain of FGD3 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.
Pssm-ID: 277279 [Multi-domain] Cd Length: 54 Bit Score: 56.55 E-value: 3.80e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568967300 1394 DNEVQNCMSCGKCF-SVTVRRHHCRQCGNIFCAECStknALTPSSKKPVRVCDACF 1448
Cdd:cd15740 2 EKEKQTCKGCNESFnSITKRRHHCKQCGAVICGKCS---EFKDLASRHNRVCRDCF 54
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
289-779 |
4.53e-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: 64.27 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 289 ESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDL---DYTHLEE 365
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSlesQISELKK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 366 KHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQRE 445
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 446 EKEQHglQLQGEVSQLHCKLLETERQLGEahgrlkeqrqlSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQL 525
Cdd:TIGR04523 306 QDWNK--ELKSELKNQEKKLEEIQNQISQ-----------NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 526 EKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVL 605
Cdd:TIGR04523 373 EKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 606 NQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQ 685
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 686 IKAKTELLLSAEAAKAAQRADLQNhlDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQ 765
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDFELKK--ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEK 610
|
490
....*....|....
gi 568967300 766 KVEDLEGHIKKLEA 779
Cdd:TIGR04523 611 KISSLEKELEKAKK 624
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
281-1190 |
4.80e-10 |
|
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: 64.61 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 281 NMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDY 360
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 361 THLEEKHNEESASRKTLQASLHqrdldcQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQL 440
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKL------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 441 QQQREEKEQHGLQLQGEVSQLHCKLLETERQLgEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTE 520
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKR-EAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 521 LQHQLEKSKQQHqeqqalqqsatAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEG 600
Cdd:pfam02463 399 LKSEEEKEAQLL-----------LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 601 ETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEenlhdqvqeqkahlraaqdrvlsletSVSELSSQLNESKEKVS 680
Cdd:pfam02463 468 KKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESK--------------------------ARSGLKVLLALIKDGVG 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 681 QLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHciQLESHLKDHKEKH 760
Cdd:pfam02463 522 GRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPK--LKLPLKSIAVLEI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 761 LSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILEnI 840
Cdd:pfam02463 600 DPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE-I 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 841 KQTLTKKEEENVVLKQEFEKLSQDSKTQHKElgdrmqaavTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEK 920
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLEIKKKEQREK---------EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEE 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 921 ENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQ 1000
Cdd:pfam02463 750 EEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1001 GTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGK 1080
Cdd:pfam02463 830 IKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKL 909
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1081 ESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKE 1160
Cdd:pfam02463 910 NLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEER 989
|
890 900 910
....*....|....*....|....*....|
gi 568967300 1161 LVAEKSKLAEMEEIKCRQEKEITKLNEELK 1190
Cdd:pfam02463 990 YNKDELEKERLEEEKKKLIRAIIEETCQRL 1019
|
|
| FYVE_protrudin |
cd15723 |
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ... |
1399-1447 |
1.84e-09 |
|
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc finger FYVE domain-containing protein 27 (ZFY27 or ZFYVE27), is a FYVE domain-containing protein involved in transport of neuronal cargoes and implicated in the onset of hereditary spastic paraplegia (HSP). It is involved in neurite outgrowth through binding to spastin. Moreover, it functions as a key regulator of the Rab11-dependent membrane trafficking during neurite extension. It serves as an adaptor molecule that links its associated proteins, such as Rab11-GDP, VAP-A and -B, Surf4, and RTN3, to KIF5, a motor protein that mediates anterograde vesicular transport in neurons, and thus plays a key role in the maintenance of neuronal function. The FYVE domain of protrudin resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. In addition, unlike canonical FYVE domains that is located to early endosomes and specifically binds to phosphatidylinositol 3-phosphate (PtdIns3P or PI3P), the FYVE domain of protrudin is located to plasma membrane and preferentially binds phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2), and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). In addition to FYVE-related domain, protrudin also contains a Rab11-binding domain (RBD11), two hydrophobic domains, HP-1 and HP-2, an FFAT motif, and a coiled-coil domain.
Pssm-ID: 277262 [Multi-domain] Cd Length: 62 Bit Score: 55.20 E-value: 1.84e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568967300 1399 NCMSCGKCFSV-TVRRHHCRQCGNIFCAEC-------STKNALTPSSKK-PVRVCDAC 1447
Cdd:cd15723 1 NCTGCGASFSVlLKKRRSCNNCGNAFCSRCcskkvprSVMGATAPAAQReTVFVCSGC 58
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1071-1374 |
2.11e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1071 KQLQSDLYGKESELLATRqdLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDA 1150
Cdd:COG1196 216 RELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1151 QREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQ 1230
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1231 --EKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSE 1308
Cdd:COG1196 374 laEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568967300 1309 LEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGR 1374
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
268-691 |
5.35e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 268 LKKELVQVQTLMDNMTLERERESEKlKDECKKLQSEHAH-------LEATINQLRSELAKGPQEVAVYVQEIQKLKGSIN 340
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARET-RDEADEVLEEHEErreeletLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 341 ELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQ-------LQARLTASESSLQRAQGELSEKA 413
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAhneeaesLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 414 EAAQKLREELREVESTRQHLKVEVKQLQQ-------QREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLS 486
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRErfgdapvDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 487 SE-----------------KLMEKEQQVADLQLKLSRLEEQLkEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREA 549
Cdd:PRK02224 450 EAgkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEV-EEVEERLERAEDLVEAEDRIERLEERREDLEELIAER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 550 QNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQ----------LQEKNHALQQQL 619
Cdd:PRK02224 529 RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKErieslerirtLLAAIADAEDEI 608
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967300 620 TQLTEKLKNQSESHKQAEENLHDQvQEQKAHLRAAQDrvlslETSVSELSSQLNESKEKVSQLDIQIKAKTE 691
Cdd:PRK02224 609 ERLREKREALAELNDERRERLAEK-RERKRELEAEFD-----EARIEEAREDKERAEEYLEQVEEKLDELRE 674
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
770-1316 |
7.14e-09 |
|
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: 60.42 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 770 LEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEE 849
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 850 ENVVLKQEFEKlsqdsktqHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAV 929
Cdd:TIGR04523 202 LLSNLKKKIQK--------NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 930 LDLEKACKELKhQLQVQAESALKEQEDLKKslEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQS 1009
Cdd:TIGR04523 274 KELEQNNKKIK-ELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1010 AEQKKKQIEALQGEVKnavsQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQ 1089
Cdd:TIGR04523 351 LTNSESENSEKQRELE----EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1090 DLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLA 1169
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1170 EMEEIKCRQEKEITKLN---EELKSHKQESIKEITNLKD---------AKQLLIQQKLELQGRVDSLKAALEQEKESQQL 1237
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKekiEKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQEE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1238 MREQVKKEEEKRK------EEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEK 1311
Cdd:TIGR04523 587 KQELIDQKEKEKKdlikeiEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIK 666
|
....*
gi 568967300 1312 QTDDL 1316
Cdd:TIGR04523 667 KIKES 671
|
|
| FYVE_ZFY19 |
cd15749 |
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ... |
1399-1448 |
7.20e-09 |
|
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ZFY19, also termed mixed lineage leukemia (MLL) partner containing FYVE domain, is encoded by a novel gene, MLL partner containing FYVE domain (MPFYVE). The FYVE domain of ZFY19 resembles FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. The biological function of ZFY19 remains unclear.
Pssm-ID: 277288 [Multi-domain] Cd Length: 51 Bit Score: 52.89 E-value: 7.20e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1399 NCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPS-SKKPVRVCDACF 1448
Cdd:cd15749 1 RCFGCAAKFSLFKKECGCKNCGRSFCKGCLTFSAVVPRkGNQKQKVCKQCH 51
|
|
| FYVE_RUFY4 |
cd15745 |
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ... |
1400-1448 |
8.32e-09 |
|
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain. The FYVE domain of RUFY4 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue). The biological function of RUFY4 still remains unclear.
Pssm-ID: 277284 [Multi-domain] Cd Length: 52 Bit Score: 52.89 E-value: 8.32e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1400 CMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNAL--TPSSKKPVRVCDACF 1448
Cdd:cd15745 2 CAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVlsVPDTCIYLRVCKTCY 52
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
117-427 |
1.18e-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: 60.07 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 117 EAGLALTRDDITLLRQEVQDLQASLkeekwysEELKKELEKyqgLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNI 196
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKEL-------EELEEELEQ---LRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 197 KQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTEL-LQRPGIEDVAVLKKELVQV 275
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 276 QTLMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQK 355
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967300 356 KDLDYTHLEEKHNEESASRKTLQASLhqrdldcQQLQARLTASESSLQRAQGELSEKAEA-AQKLREELREVE 427
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRI-------DNLQERLSEEYSLTLEEAEALENKIEDdEEEARRRLKRLE 978
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1117-1387 |
1.23e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1117 KSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEikcrqekEITKLNEELkshkQES 1196
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-------ELEEAQAEE----YEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1197 IKEITNLKDAKQLLIQQKLELQGRvdslKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHS---EIKEKEAGMKK 1273
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEER----LEELEEELAELEEELEELEEELEELEEELEEAEEELEEaeaELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1274 HEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQT 1353
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270
....*....|....*....|....*....|....
gi 568967300 1354 KALELQRKLDNTTAAVQELGRENQSLQIKHTQAL 1387
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
718-1266 |
1.70e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 718 LQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQ---- 793
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyikl 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 794 --SLQQQRQLSTDLELRNAELSRELQEQEEVVSctklDLQNKSEILENIKQTLTKKEEENVVLKqEFEKLSQDSKTQHKE 871
Cdd:PRK03918 299 seFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 872 LgDRMQAAVTELTAVKAQKdaLLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKA---CKELKHQLQVQAE 948
Cdd:PRK03918 374 L-ERLKKRLTGLTPEKLEK--ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkCPVCGRELTEEHR 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 949 SALKEQ-----EDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQqLQGTINQLK----QSAEQKKKQIEA 1019
Cdd:PRK03918 451 KELLEEytaelKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLKkynlEELEKKAEEYEK 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1020 LQGE----------VKNAVSQKTVLENK---LQQQSSQAAQELAAEKGKLSALQ-SNYEKCQADLKQLQSdLYGKESELL 1085
Cdd:PRK03918 530 LKEKliklkgeiksLKKELEKLEELKKKlaeLEKKLDELEEELAELLKELEELGfESVEELEERLKELEP-FYNEYLELK 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1086 ATRQDLKSVEEKLTLAQEDLisnrnqignqNKSIQELQAAKASLEQDSAKKEALLKEQS-KALEDAQREKSVKEKELVAE 1164
Cdd:PRK03918 609 DAEKELEREEKELKKLEEEL----------DKAFEELAETEKRLEELRKELEELEKKYSeEEYEELREEYLELSRELAGL 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1165 KSKLaemeeikcrqekeitklnEELKSHKQESIKEITNLKDAKQLLIQQKLELQgrvdslkaALEQEKESQQLMREQVKK 1244
Cdd:PRK03918 679 RAEL------------------EELEKRREEIKKTLEKLKEELEEREKAKKELE--------KLEKALERVEELREKVKK 732
|
570 580
....*....|....*....|..
gi 568967300 1245 EEEKRKEEFSEKEAKLHSEIKE 1266
Cdd:PRK03918 733 YKALLKERALSKVGEIASEIFE 754
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
391-631 |
2.00e-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: 58.24 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 391 LQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETER 470
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 471 QLGEAHGRLKEQRqlsseklmekeQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQ 550
Cdd:COG4942 91 EIAELRAELEAQK-----------EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 551 NDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAV-LNQLQEKNHALQQQLTQLTEKLKNQ 629
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAeLAELQQEAEELEALIARLEAEAAAA 239
|
..
gi 568967300 630 SE 631
Cdd:COG4942 240 AE 241
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
130-753 |
2.80e-08 |
|
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: 58.59 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 130 LRQEVQDLQASLKE--------------EKWYSEELKKELEK-YQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENF 194
Cdd:pfam15921 108 LRQSVIDLQTKLQEmqmerdamadirrrESQSQEDLRNQLQNtVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 195 NIKQMKDLFEQKAAQ---------------LATEIADIKSKYDEEKS-----LRAAAEQKVTHLTEDLNKQTTVIQDLKT 254
Cdd:pfam15921 188 EIRSILVDFEEASGKkiyehdsmstmhfrsLGSAISKILRELDTEISylkgrIFPVEDQLEALKSESQNKIELLLQQHQD 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 255 ELLQRPGIEDVAV--LKKELVQVQTLMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEI 332
Cdd:pfam15921 268 RIEQLISEHEVEItgLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEEL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 333 QK-----------LKGSINELTQKNQNLTEKLQK------KDLDYTHLEEKHNEESASRKT--------LQASLHQRDLD 387
Cdd:pfam15921 348 EKqlvlanselteARTERDQFSQESGNLDDQLQKlladlhKREKELSLEKEQNKRLWDRDTgnsitidhLRRELDDRNME 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 388 CQQLQARLTASESslqRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGE---VSQLHCK 464
Cdd:pfam15921 428 VQRLEALLKAMKS---ECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSertVSDLTAS 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 465 LLETERQLGEAHGRLKEQRQLSSEKLME------KEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQ---QHQEQ 535
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSRVDLKLQElqhlknEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgQHGRT 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 536 QALQQSATAKLREAQNDLEQVLRQI----GDKDQKIQNLEALLQKGK-ESVSLLEKEREDLYAKIQAGEGETAVLNQLQE 610
Cdd:pfam15921 585 AGAMQVEKAQLEKEINDRRLELQEFkilkDKKDAKIRELEARVSDLElEKVKLVNAGSERLRAVKDIKQERDQLLNEVKT 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 611 KN---HALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIK 687
Cdd:pfam15921 665 SRnelNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQID 744
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568967300 688 A---KTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHL 753
Cdd:pfam15921 745 AlqsKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
351-1119 |
2.90e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 351 EKLQKKDLDYTHLEEKHNEESAsRKTLQASLHQRDLDCQQLQARLTASESSLQRaQGELSEKAEAAQKLRE-----ELRE 425
Cdd:PTZ00121 1118 EEAKKKAEDARKAEEARKAEDA-RKAEEARKAEDAKRVEIARKAEDARKAEEAR-KAEDAKKAEAARKAEEvrkaeELRK 1195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 426 VESTRQHLKV----EVKQLQQQREEKEQHGLQLQGEVSQLHCKllETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQ 501
Cdd:PTZ00121 1196 AEDARKAEAArkaeEERKAEEARKAEDAKKAEAVKKAEEAKKD--AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 502 LKLSRLEEQLK--EKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDK-DQKIQNLEALLQKGK 578
Cdd:PTZ00121 1274 AEEARKADELKkaEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKaEEAKKAAEAAKAEAE 1353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 579 ESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQqltqlTEKLKNQSESHKQAEENLHDQVQEQKahlRAAQDRV 658
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-----ADEAKKKAEEDKKKADELKKAAAAKK---KADEAKK 1425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 659 LSLETSVSELSSQLNESKEKVSQLDIQIK-AKTELLLSAEAAKAAQRADLQNHLDTAQHA--LQDKQQELNKVSVQLDQl 735
Cdd:PTZ00121 1426 KAEEKKKADEAKKKAEEAKKADEAKKKAEeAKKAEEAKKKAEEAKKADEAKKKAEEAKKAdeAKKKAEEAKKKADEAKK- 1504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 736 TAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADAL----EVKASKEQALQSLQQQRQLSTDLELRNAE 811
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkkaeELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 812 LSRELQEQ--EEVVSCTKLDLQNKSEIL-----ENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKEL--GDRMQAAVTE 882
Cdd:PTZ00121 1585 EAKKAEEAriEEVMKLYEEEKKMKAEEAkkaeeAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELkkAEEENKIKAA 1664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 883 LTAVKAQKDALLAE-LSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKAcKELKHQLQVQA----ESALKEQEDL 957
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-EELKKAEEENKikaeEAKKEAEEDK 1743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 958 KKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENK 1037
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVIND 1823
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1038 LQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQ----------EDLIS 1107
Cdd:PTZ00121 1824 SKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADeiekidkddiEREIP 1903
|
810
....*....|..
gi 568967300 1108 NRNQIGNQNKSI 1119
Cdd:PTZ00121 1904 NNNMAGKNNDII 1915
|
|
| FYVE_WDFY1 |
cd15756 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ... |
1390-1452 |
3.49e-08 |
|
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar proteins; WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. In addition to FYVE domain, WDFY1 harbors multiple WD-40 repeats.
Pssm-ID: 277295 [Multi-domain] Cd Length: 76 Bit Score: 51.99 E-value: 3.49e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568967300 1390 KWAEDNevqNCMSCGKCF-----------SVTVRRHHCRQCGNIFCAECSTKNALTP--SSKKPVRVCDACFNDLQ 1452
Cdd:cd15756 2 QWLESD---SCQKCEQPFfwnikqmwdtkTLGLRQHHCRKCGQAVCGKCSSKRSSYPimGFEFQVRVCDSCFETIK 74
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
124-778 |
3.90e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 124 RDDITLLRQEVQDLQASLKEEKwysEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQMKDLF 203
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETR---DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 204 EQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELlqrpgiedvAVLKKELVQVqtlmdnmt 283
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL---------AEAEAQARAS-------- 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 284 lerERESEKLKDECKKLQSEHAHLEATINQLRS---------ELAKGPQEVAVYVQEIQKLKGSINELTQKN-------- 346
Cdd:TIGR02169 503 ---EERVRGGRAVEEVLKASIQGVHGTVAQLGSvgeryataiEVAAGNRLNNVVVEDDAVAKEAIELLKRRKagratflp 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 347 -------QNLTEKLQKKD-----LDYTHLEEKHneESASRKTLQASLHQRDLDcqqlQARLTASESSLQRAQGELSEKAE 414
Cdd:TIGR02169 580 lnkmrdeRRDLSILSEDGvigfaVDLVEFDPKY--EPAFKYVFGDTLVVEDIE----AARRLMGKYRMVTLEGELFEKSG 653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 415 A--------------AQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLgeahGRLK 480
Cdd:TIGR02169 654 AmtggsraprggilfSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI----EQLE 729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 481 EQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLekskqqhqeqqalqqsatAKLREAQNDLEQVLRQi 560
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL------------------HKLEEALNDLEARLSH- 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 561 gdkdQKIQNLEALLQKgkesvslLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENL 640
Cdd:TIGR02169 791 ----SRIPEIQAELSK-------LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL 859
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 641 HDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDI---QIKAKTELLLSAEAAKAAQRADLQNHLDTAQHA 717
Cdd:TIGR02169 860 NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERkieELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568967300 718 LQDKQQELNKVSVqLDQLTAKFQEKQEHCIQLES--------------HLKDHKEKHLSLEQKVEDLEGHIKKLE 778
Cdd:TIGR02169 940 KGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPvnmlaiqeyeevlkRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
966-1189 |
4.68e-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: 57.08 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 966 ETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAvsqktvlenklqqqssqa 1045
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1046 AQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKES----ELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQE 1121
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1122 LQAAKASLEQDSAKKEALLKEQS---KALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEEL 1189
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEeerAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| FYVE_RUFY3 |
cd15744 |
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ... |
1400-1448 |
5.67e-08 |
|
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).
Pssm-ID: 277283 [Multi-domain] Cd Length: 52 Bit Score: 50.49 E-value: 5.67e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1400 CMSCGKCFSVTVR-RHHCRQCGNIFCAECSTKNALTPSS-KKPVRVCDACF 1448
Cdd:cd15744 2 CSLCQEDFASLALpKHNCYNCGGTFCDACSSNELPLPSSiYEPARVCDVCY 52
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
308-513 |
6.02e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 57.61 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 308 EATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQnlteklqkkdldythleekhneESASRKTLQASLHQRDLD 387
Cdd:PRK11281 79 KEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETL----------------------STLSLRQLESRLAQTLDQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 388 CQQLQARLTASESSL-------QRAQGELSEKAEAAQKLREELREVESTRQHLKVEvkqlQQQREEKEQHGLQLQGEVSQ 460
Cdd:PRK11281 137 LQNAQNDLAEYNSQLvslqtqpERAQAALYANSQRLQQIRNLLKGGKVGGKALRPS----QRVLLQAEQALLNAQNDLQR 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 461 lhcKLLETERQLGEAhgrLKEQRQLSSEKLMEKEQQVADLQ-------LKLSrlEEQLKE 513
Cdd:PRK11281 213 ---KSLEGNTQLQDL---LQKQRDYLTARIQRLEHQLQLLQeainskrLTLS--EKTVQE 264
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
815-1324 |
7.10e-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: 57.34 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 815 ELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLsqdsKTQHKELGDRMQAAVTELTAVKAQKDALL 894
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKIL----EQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 895 AELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKhQLQVQAESALKEQEDLKKSLEKEKETSQQLKIE 974
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELE-KLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 975 LNSVKGEVSQAQNTL---KQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVknavSQKTVLENKLQQQSSQAAQELAA 1051
Cdd:TIGR04523 189 IDKIKNKLLKLELLLsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI----NEKTTEISNTQTQLNQLKDEQNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1052 EKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQ------------DLKSVEEKLTLAQEDLISNRNQIGNQNKSI 1119
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkeqdwnkelksELKNQEKKLEEIQNQISQNNKIISQLNEQI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1120 QELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKE 1199
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1200 ITNLKDAKQLLIQQKLELQgrvDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENea 1279
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIK---DLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK-- 499
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 568967300 1280 KLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLE 1324
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
282-686 |
7.88e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 7.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 282 MTLERERESEKLKDECKKLQSEH-AHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDY 360
Cdd:PRK04863 244 MTLEAIRVTQSDRDLFKHLITEStNYVAADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 361 THLEEKHNEESASRKTLQASLHQR------DLDCQQLQARLTASESSLQRAQG---ELSEKAEAAQKlreelrEVESTRQ 431
Cdd:PRK04863 324 SDLEQDYQAASDHLNLVQTALRQQekieryQADLEELEERLEEQNEVVEEADEqqeENEARAEAAEE------EVDELKS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 432 HLkVEVKQ---LQQQREEKEQHGLQLQGEVSQLhCKLLE-TERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRL 507
Cdd:PRK04863 398 QL-ADYQQaldVQQTRAIQYQQAVQALERAKQL-CGLPDlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQF 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 508 EE--QLKEKVTNSTELQ--HQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSL 583
Cdd:PRK04863 476 EQayQLVRKIAGEVSRSeaWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDE 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 584 LEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAE---ENLHDQVQEQKAHLRAAQDRVLS 660
Cdd:PRK04863 556 LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQdalARLREQSGEEFEDSQDVTEYMQQ 635
|
410 420
....*....|....*....|....*.
gi 568967300 661 LETSVSELSSQLNESKEKVSQLDIQI 686
Cdd:PRK04863 636 LLERERELTVERDELAARKQALDEEI 661
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
477-1077 |
9.50e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 9.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 477 GRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKV-TNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQ 555
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEeKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 556 VLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQagEGETAVLNQLQEKNHALqqqltqlteklkNQSESHKQ 635
Cdd:PRK02224 242 VLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVR--DLRERLEELEEERDDLL------------AEAGLDDA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 636 AEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTElllsaeaakaaQRADLQNHLDTAQ 715
Cdd:PRK02224 308 DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE-----------EAAELESELEEAR 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 716 HALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKL-----EADAL-------- 782
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTArerveEAEALleagkcpe 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 783 ---EVKASKEQALQSLQQQRQLSTDLELRNAELSRE-----------LQEQEEVVSCTKLDLQNKSEILENIKQTLTKKE 848
Cdd:PRK02224 457 cgqPVEGSPHVETIEEDRERVEELEAELEDLEEEVEeveerleraedLVEAEDRIERLEERREDLEELIAERRETIEEKR 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 849 EENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDAlLAELSTTKEKLSKVSDSLknsksefekenqkgkAA 928
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSK-LAELKERIESLERIRTLL---------------AA 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 929 VLDLEKACKELKHQLQvqaesALKEQEDLKKSLEKEK-ETSQQLKIELNSVKgeVSQAQNTLKQKEKDEQQLQGTINQLk 1007
Cdd:PRK02224 601 IADAEDEIERLREKRE-----ALAELNDERRERLAEKrERKRELEAEFDEAR--IEEAREDKERAEEYLEQVEEKLDEL- 672
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1008 qsaEQKKKQIEALQGEVKNAVSQKTVLENKLqqqssqaaQELAAEKGKLSALQSNYEKCQADLKQLQSDL 1077
Cdd:PRK02224 673 ---REERDDLQAEIGAVENELEELEELRERR--------EALENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
171-1105 |
1.14e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 56.98 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 171 LVTDSSAELQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRaAAEQKVTHLTEDLNKQTTVIQ 250
Cdd:TIGR00606 194 VRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLK-NRLKEIEHNLSKIMKLDNEIK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 251 DLKTELLQRPGIEDVAVLKKELVQVQTlmdnmtlerereSEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQ 330
Cdd:TIGR00606 273 ALKSRKKQMEKDNSELELKMEKVFQGT------------DEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQ 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 331 EIQKLKGSINELTQKNQNLTEKLQKKDLDY----THLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTAseSSLQRAQ 406
Cdd:TIGR00606 341 EKTELLVEQGRLQLQADRHQEHIRARDSLIqslaTRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAA--QLCADLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 407 GELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQG---EVSQLHCKLLETERQLGEAHGRLKEQR 483
Cdd:TIGR00606 419 SKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGssdRILELDQELRKAERELSKAEKNSLTET 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 484 QLSSEKLMEKEQqvADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREaqndleqVLRQIGDK 563
Cdd:TIGR00606 499 LKKEVKSLQNEK--ADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDE-------LTSLLGYF 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 564 DQKIQnLEALLQKGKESVSLLEKEREDLYAKIQAGEGETavlNQLQEKNHALQQQLTQLTEKLKN--QSESHKQAEENLH 641
Cdd:TIGR00606 570 PNKKQ-LEDWLHSKSKEINQTRDRLAKLNKELASLEQNK---NHINNELESKEEQLSSYEDKLFDvcGSQDEESDLERLK 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 642 DQVQEQKAHlRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSaeaakaaqraDLQNHLDTAQHALQDK 721
Cdd:TIGR00606 646 EEIEKSSKQ-RAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFIS----------DLQSKLRLAPDKLKST 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 722 QQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEAdALEVKASKEQALQSLQQQRQL 801
Cdd:TIGR00606 715 ESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET-LLGTIMPEEESAKVCLTDVTI 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 802 STDLELRNAELSRELQEQeevvsCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELgDRMQAAVT 881
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQ-----AAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI-QHLKSKTN 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 882 ELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSL 961
Cdd:TIGR00606 868 ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK 947
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 962 EKEKETSQQLKIELNSVKgevSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQ 1041
Cdd:TIGR00606 948 EKVKNIHGYMKDIENKIQ---DGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLR 1024
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568967300 1042 SSQA-----AQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQdlKSVEEKLTLAQEDL 1105
Cdd:TIGR00606 1025 KRENelkevEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQ--KGYEKEIKHFKKEL 1091
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
123-573 |
1.28e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 123 TRDDITLLRQEVQDLQASLKEEKWYSEELKKEL-EKYQGLQQQEAKSDGLVTDS---SAELQALEQQLEEAQTENFNIKQ 198
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVrDLRERLEELEEERDDLLAEAgldDADAEAVEARREELEDRDEELRD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 199 mkDLFEQKAAQ---------LATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELlqRPGIEDVAVLK 269
Cdd:PRK02224 329 --RLEECRVAAqahneeaesLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI--EELRERFGDAP 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 270 KELVQVQTLMDNMTLERERESEKLKDECKKLQSehahLEATINQLRSELAKG-------PQEVAVYVQEIQKLKGSINEL 342
Cdd:PRK02224 405 VDLGNAEDFLEELREERDELREREAELEATLRT----ARERVEEAEALLEAGkcpecgqPVEGSPHVETIEEDRERVEEL 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 343 TQKNQNLTEKLQKKDLDYTHLE-----EKHNEESASRKTL--------QASLHQRDLDCQQLQARLTASESSLQRAQGEL 409
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEdlveaEDRIERLEERREDleeliaerRETIEEKRERAEELRERAAELEAEAEEKREAA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 410 SEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREekeqhglqlqgevsqlhckLLETERQLGEAHGRLKEQRQLSSEK 489
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKLAELKERIESLERIRT-------------------LLAAIADAEDEIERLREKREALAEL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 490 LMEKEQQVADLQLKLSRLEEQLKEKvtnstelqhQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQN 569
Cdd:PRK02224 622 NDERRERLAEKRERKRELEAEFDEA---------RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
....
gi 568967300 570 LEAL 573
Cdd:PRK02224 693 LEEL 696
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
120-597 |
1.59e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 120 LALTRDDITLLRQEVQDLQASLKEEKwysEELKKELEKYQGLQQQEAKSDGlvtdssAELQALEQQLEEAQTEnfnikqm 199
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLE---ARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERE------- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 200 KDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQR--PGIEDVAVLKKELVQVQT 277
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAlrDLRRELRELEAEIASLER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 278 LMDNMTLERERESEKLKDECK-------------KLQSEHAH----LEATINQLRSELAKGPQ---EVAVYVQEIqKLKG 337
Cdd:COG4913 434 RKSNIPARLLALRDALAEALGldeaelpfvgeliEVRPEEERwrgaIERVLGGFALTLLVPPEhyaAALRWVNRL-HLRG 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 338 SINelTQKNQNLTEKLQKKDLDYTHLEEKHN-EESASRKTLQASLHQR-DLDC----QQLQ--------ARLTASESSL- 402
Cdd:COG4913 513 RLV--YERVRTGLPDPERPRLDPDSLAGKLDfKPHPFRAWLEAELGRRfDYVCvdspEELRrhpraitrAGQVKGNGTRh 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 403 ---------------QRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVsqlhcKLLE 467
Cdd:COG4913 591 ekddrrrirsryvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVAS 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 468 TERQLGEAHGRLKEQRQlSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLR 547
Cdd:COG4913 666 AEREIAELEAELERLDA-SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 568967300 548 EAQN-DLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQA 597
Cdd:COG4913 745 LELRaLLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
754-1290 |
2.11e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 754 KDHKEKHLSLEQKVEDLEGhikkleadalEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEvvscTKLDLQNK 833
Cdd:PRK03918 178 IERLEKFIKRTENIEELIK----------EKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 834 SEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGD--RMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSL 911
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 912 KNSKSEFEKENQKgKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQ 991
Cdd:PRK03918 324 NGIEERIKELEEK-EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 992 KEKDEQQLQGTINQLKQSAEQKKKQIEALQG-EVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADL 1070
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKaKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1071 KQLQSDLyGKESELLATRQ---DLKSVEEKLT-LAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEAL---LKEQ 1143
Cdd:PRK03918 483 RELEKVL-KKESELIKLKElaeQLKELEEKLKkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELkkkLAEL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1144 SKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDS 1223
Cdd:PRK03918 562 EKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568967300 1224 LKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNE 1290
Cdd:PRK03918 642 LEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
177-679 |
2.49e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 177 AELQALEQQLEEAQTENFNIKQMKDLFEQKAAQlaTEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTEL 256
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 257 LQRPGiEDVAVLKKELVQVQTLMDnmtlERERESEKLKDECKKLQSEHAHLEATINQLRSELAkgpqevavyvQEIQKLK 336
Cdd:COG4913 333 RGNGG-DRLEQLEREIERLERELE----ERERRRARLEALLAALGLPLPASAEEFAALRAEAA----------ALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 337 GSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQ-RDLDCQQLQArltaSESSLQRAqGEL---SEK 412
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAlRDALAEALGL----DEAELPFV-GELievRPE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 413 AEA-------------------AQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQ------------------LQ 455
Cdd:COG4913 473 EERwrgaiervlggfaltllvpPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDpdslagkldfkphpfrawLE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 456 GEVSQ---LHCklLETERQL---------------GEAHGRLKEQRQLSS---------EKLMEKEQQVADLQLKLSRLE 508
Cdd:COG4913 553 AELGRrfdYVC--VDSPEELrrhpraitragqvkgNGTRHEKDDRRRIRSryvlgfdnrAKLAALEAELAELEEELAEAE 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 509 EQLKEkvtnSTELQHQLEKSKqqhqeqqaLQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEAllqkGKESVSLLEKER 588
Cdd:COG4913 631 ERLEA----LEAELDALQERR--------EALQRLAEYSWDEIDVASAEREIAELEAELERLDA----SSDDLAALEEQL 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 589 EDLYAKIQAGEGEtavLNQLQEKNHALQQQLTQLTEKLKnqsESHKQAEENLHDQVQEQKAHL-----RAAQDRVL---- 659
Cdd:COG4913 695 EELEAELEELEEE---LDELKGEIGRLEKELEQAEEELD---ELQDRLEAAEDLARLELRALLeerfaAALGDAVErelr 768
|
570 580
....*....|....*....|.
gi 568967300 660 -SLETSVSELSSQLNESKEKV 679
Cdd:COG4913 769 eNLEERIDALRARLNRAEEEL 789
|
|
| FYVE_CARP |
cd15750 |
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ... |
1399-1447 |
4.12e-07 |
|
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 are a novel group of caspase regulators by the presence of a FYVE-type zinc finger domain. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains.
Pssm-ID: 277289 [Multi-domain] Cd Length: 47 Bit Score: 47.74 E-value: 4.12e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568967300 1399 NCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKnaltpsSKKPVRVCDAC 1447
Cdd:cd15750 2 PCESCGAKFSVFKRKRTCADCKRYFCSNCLSK------EERGRRRCRRC 44
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
943-1170 |
6.10e-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: 53.61 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 943 LQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQG 1022
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1023 EVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYE---KCQADLKQLQSDLYGKESELLATRQDLKSVEEKLT 1099
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLdavRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1100 LAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAE 1170
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
205-449 |
7.41e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 205 QKAAQLATEIAD------IKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKtellQRPGIEDVAVLKKELVQVQTl 278
Cdd:COG3206 148 ELAAAVANALAEayleqnLELRREEARKALEFLEEQLPELRKELEEAEAALEEFR----QKNGLVDLSEEAKLLLQQLS- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 279 mdnmTLEREREseklkdeckKLQSEHAHLEATINQLRSELAKGPQEVAVYVQ--EIQKLKGSINELTQKNQNLTEKLQKK 356
Cdd:COG3206 223 ----ELESQLA---------EARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPN 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 357 DLDYTHLEEKHNE-ESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKV 435
Cdd:COG3206 290 HPDVIALRAQIAAlRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
250
....*....|....
gi 568967300 436 EVKQLQQQREEKEQ 449
Cdd:COG3206 370 LLQRLEEARLAEAL 383
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
902-1385 |
7.46e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 902 EKLSKVSDSLKNSKSEFEKENQKGKaavlDLEKACKELKHQLQvQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGE 981
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEKEKELE-EVLREINEISSELPELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 982 VSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAaqELAAEKGKLSALQS 1061
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE--EYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1062 NYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLisnrnqignqnKSIQELQAAKASLEQDSAKKEALLK 1141
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH-----------ELYEEAKAKKEELERLKKRLTGLTP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1142 EQSKA-LEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNE----------ELKSHKQESI-----KEITNLKD 1205
Cdd:PRK03918 387 EKLEKeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrELTEEHRKELleeytAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1206 AKQLLIQQKLELQGRVDSLKAALEQEKESQQLMR-----EQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAK 1280
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIKLKElaeqlKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1281 LTMQVTTLNENLGTVKKEWQSSQRRVSELEKQ--------TDDLRGEIAVLEA------TVQNNQDERRALLERclkgeg 1346
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLDELEEELAELLKEleelgfesVEELEERLKELEPfyneylELKDAEKELEREEKE------ 620
|
490 500 510
....*....|....*....|....*....|....*....
gi 568967300 1347 eIEKLQTKALELQRKLDNTTAAVQELGRENQSLQIKHTQ 1385
Cdd:PRK03918 621 -LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
904-1380 |
1.82e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 904 LSKVSDSLKNSKSEFEKENQKGKAAVL-DLEKACKELKHQL---QVQAESALKEQEDLKKSLEKEKETSQqlkiELNSVK 979
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLnGLESELAELDEEIeryEEQREQARETRDEADEVLEEHEERRE----ELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 980 GEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVK-NAVSQKTVLENK--LQQQSSQAAQELAAEKGKL 1056
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlDDADAEAVEARReeLEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1057 SALQSNYEKCQADLKQLQSDLYGK-------ESELLATRQDLKSVEEKLTLAQEDLISNRN-------QIGNQNKSIQEL 1122
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELreeaaelESELEEAREAVEDRREEIEELEEEIEELRErfgdapvDLGNAEDFLEEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1123 QAAKASLEQDSAKKEALLKEQSKALEDAQR---EKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKE 1199
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEEAEAlleAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEER 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1200 ITNLKDAKqlliqqklELQGRVDSLKaalEQEKESQQLM--REQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEEN 1277
Cdd:PRK02224 498 LERAEDLV--------EAEDRIERLE---ERREDLEELIaeRRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1278 EAKLTMQVTTLNENLGTVKKEWQsSQRRVSELEKQTDDLRGEIAVLE---ATVQNNQDERRALL----ERCLKGEGE--- 1347
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERIE-SLERIRTLLAAIADAEDEIERLRekrEALAELNDERRERLaekrERKRELEAEfde 645
|
490 500 510
....*....|....*....|....*....|....*
gi 568967300 1348 --IEKLQTKALELQRKLDNTTAAVQELGRENQSLQ 1380
Cdd:PRK02224 646 arIEEAREDKERAEEYLEQVEEKLDELREERDDLQ 680
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
249-771 |
2.12e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 249 IQDLKTELLQRPGIED-VAVLKKELVQVQTLMDNMTLERERESEKLkDECKKLQSEHAHLEATINQLRSELAKGPQEVAV 327
Cdd:PRK03918 178 IERLEKFIKRTENIEElIKEKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 328 YVQEIQKLKGSINELTQKnqnlTEKLQKKDLDYTHLEEKHNEESASRKtLQASLHQRDLDCQQLQARLTASESSLQRAQG 407
Cdd:PRK03918 257 LEEKIRELEERIEELKKE----IEELEEKVKELKELKEKAEEYIKLSE-FYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 408 ELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEqhglQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSS 487
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE----ELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 488 EKLMEK----EQQVADLQLKLSRLEEQLKEKVTNSTELQHQ-----LEKSKQQHQEQQALQQSATAKLREAQNDLEQV-- 556
Cdd:PRK03918 408 SKITARigelKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELek 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 557 -------LRQIGDKDQKIQNLEALLQK-GKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKN 628
Cdd:PRK03918 488 vlkkeseLIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 629 QSESHKQAEENLH-------DQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDiQIKAKTELLLSAEAAKA 701
Cdd:PRK03918 568 LEEELAELLKELEelgfesvEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELD-KAFEELAETEKRLEELR 646
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 702 AQRADLQNHLDTAQHalQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLE 771
Cdd:PRK03918 647 KELEELEKKYSEEEY--EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
333-1339 |
2.30e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.48 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 333 QKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEK 412
Cdd:pfam01576 22 QKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 413 AEAAQKLREELREVESTRQHLKVE-------VKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQL 485
Cdd:pfam01576 102 QQHIQDLEEQLDEEEAARQKLQLEkvtteakIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 486 SS----------EKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQ 555
Cdd:pfam01576 182 KNkheamisdleERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 556 VLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGE-------TAVLNQLQEKNhalQQQLTQLTEKLKN 628
Cdd:pfam01576 262 ALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEledtldtTAAQQELRSKR---EQEVTELKKALEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 629 QSESHK-----------QAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLneskEKVSQLDIQIKAKTELLLSAE 697
Cdd:pfam01576 339 ETRSHEaqlqemrqkhtQALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL----RTLQQAKQDSEHKRKKLEGQL 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 698 AAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKE-------KHLSLEQKVEDL 770
Cdd:pfam01576 415 QELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQEllqeetrQKLNLSTRLRQL 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 771 EGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEE 850
Cdd:pfam01576 495 EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKT 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 851 NVVLKQEFEKLSQDSktqhkelgDRMQAAVTELTAVKAQKDALLAELSTtkeklskVSDSLKNSKSEFEKENQKGKAAVL 930
Cdd:pfam01576 575 KNRLQQELDDLLVDL--------DHQRQLVSNLEKKQKKFDQMLAEEKA-------ISARYAEERDRAEAEAREKETRAL 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 931 DLEKACKELKhqlqvqaeSALKEQEDLKKSLEKEKEtsqqlkiELNSVKGEVSqaqntlkqkeKDEQQLQGTINQLKQSA 1010
Cdd:pfam01576 640 SLARALEEAL--------EAKEELERTNKQLRAEME-------DLVSSKDDVG----------KNVHELERSKRALEQQV 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1011 EQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQD 1090
Cdd:pfam01576 695 EEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKK 774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1091 LKSVEEKLTLAQEDLISNRNQIGNQNKSIQ-ELQAAKASLEQDSAKKEALLKEQskaledaqREKSVKEKELVAEKSKLA 1169
Cdd:pfam01576 775 LELDLKELEAQIDAANKGREEAVKQLKKLQaQMKDLQRELEEARASRDEILAQS--------KESEKKLKNLEAELLQLQ 846
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1170 EMEEIKCRQEKEITKLNEELKshkqesiKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMreqvkkeeekr 1249
Cdd:pfam01576 847 EDLAASERARRQAQQERDELA-------DEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELL----------- 908
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1250 keefsekeaklhseikekeagmkkhEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQN 1329
Cdd:pfam01576 909 -------------------------NDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKS 963
|
1050
....*....|
gi 568967300 1330 NQDERRALLE 1339
Cdd:pfam01576 964 KFKSSIAALE 973
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
546-1105 |
2.35e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.21 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 546 LREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEK 625
Cdd:PRK01156 178 LRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 626 LKnQSESHKQAEENLHDQVQE-QKAHLRAAQDRVLSLETSVSE---LSSQLNESKEKVSQLDIQIKAKTELLlsaeaaka 701
Cdd:PRK01156 258 IK-TAESDLSMELEKNNYYKElEERHMKIINDPVYKNRNYINDyfkYKNDIENKKQILSNIDAEINKYHAII-------- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 702 AQRADLQNHLDTaqhaLQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADA 781
Cdd:PRK01156 329 KKLSVLQKDYND----YIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 782 LEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEE-----------VVSCTKLDLQNKSEILENIKQTLTKKEEE 850
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRnmemlngqsvcPVCGTTLGEEKSNHIINHYNEKKSRLEEK 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 851 NVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDslKNSKSEfEKENQKGKAAVL 930
Cdd:PRK01156 485 IREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKD--KHDKYE-EIKNRYKSLKLE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 931 DLEKACKELKHQLQVQA----ESALKEQEDLKKSLEKEKETSQQLKIELNSVKgevSQAQNTLKQKEKDEQQLQGTINQL 1006
Cdd:PRK01156 562 DLDSKRTSWLNALAVISlidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLNNKYNEI 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1007 kqsaEQKKKQIEALQGEVKNAVSQktvlenklQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLA 1086
Cdd:PRK01156 639 ----QENKILIEKLRGKIDNYKKQ--------IAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEI 706
|
570
....*....|....*....
gi 568967300 1087 TRQDLKSVEEKLTLAQEDL 1105
Cdd:PRK01156 707 LRTRINELSDRINDINETL 725
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
120-1026 |
2.42e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 52.28 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 120 LALTRDDITLLRQEVQDLQASLKEEKWYSeelKKELEKYQglqqqeaksdglvtdssaelqalEQQLEEAQTENFNIKQM 199
Cdd:pfam02463 178 LIEETENLAELIIDLEELKLQELKLKEQA---KKALEYYQ-----------------------LKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 200 KDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQrpgiedVAVLKKELVQVQTLM 279
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKL------LAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 280 DNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKgpqevavyVQEIQKLKGSINELTQKNQNLTEKLQKKDLD 359
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKE--------LEIKREAEEEEEEELEKLQEKLEQLEEELLA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 360 YTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLtasesslqrAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQ 439
Cdd:pfam02463 378 KKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL---------ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 440 LQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLsseklmekeQQVADLQLKLSRLEEQLKEKVTNST 519
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQK---------LEERSQKESKARSGLKVLLALIKDG 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 520 ELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGE 599
Cdd:pfam02463 520 VGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 600 GETAVLNQLQEKnhalqqqltqlteKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKV 679
Cdd:pfam02463 600 DPILNLAQLDKA-------------TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKA 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 680 SQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEK 759
Cdd:pfam02463 667 SLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKID 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 760 HLSLEQ---KVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEI 836
Cdd:pfam02463 747 EEEEEEeksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQ 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 837 LENIKQTLTKKEEENVVLKQEFEKLSQDSK-TQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSK 915
Cdd:pfam02463 827 EEKIKEEELEELALELKEEQKLEKLAEEELeRLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEES 906
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 916 SEFEKENQKGKAAVLDLEKACKELKHQLQVQAESaLKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKD 995
Cdd:pfam02463 907 QKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL-LLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEE 985
|
890 900 910
....*....|....*....|....*....|.
gi 568967300 996 EQQLQGTINQLKQSAEQKKKQIEALQGEVKN 1026
Cdd:pfam02463 986 KEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
295-527 |
2.67e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 295 DECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKkdldythLEEKHNEESASR 374
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-------LEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 375 KTLQASLHQRDldcQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQhglqL 454
Cdd:COG4942 93 AELRAELEAQK---EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA----L 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967300 455 QGEVSQLHCKLLETERQLGEAHGRLKEQRQlsseklmEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEK 527
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKA-------ERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
686-1282 |
3.04e-06 |
|
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: 52.03 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 686 IKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQ 765
Cdd:pfam05483 196 ILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 766 KV----EDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEE--------------VVSCTK 827
Cdd:pfam05483 276 KTklqdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAqmeelnkakaahsfVVTEFE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 828 LDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKeLGDRMQAAVTELTAVKAQKDALLAElsttKEKLSKV 907
Cdd:pfam05483 356 ATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTK-FKNNKEVELEELKKILAEDEKLLDE----KKQFEKI 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 908 SDSLKNSKSEFEKENQKGKAAVLDLEKACKELKhqlqVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQN 987
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKEIHDLEIQLTAIK----TSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQ 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 988 TLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQgevknavSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQ 1067
Cdd:pfam05483 507 EASDMTLELKKHQEDIINCKKQEERMLKQIENLE-------EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIE 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1068 ADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQ--ELQAAKASLEQDSAKKEAllkeqSK 1145
Cdd:pfam05483 580 YEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNayEIKVNKLELELASAKQKF-----EE 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1146 ALEDAQREKSVKEkelVAEKSKLAEMEEIKCRQEkEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLK 1225
Cdd:pfam05483 655 IIDNYQKEIEDKK---ISEEKLLEEVEKAKAIAD-EAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLY 730
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 568967300 1226 AALEQEKESqqlMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLT 1282
Cdd:pfam05483 731 KNKEQEQSS---AKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
117-529 |
3.15e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 117 EAGLALTRDDITLLRQEVQDLQ---ASLKEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTEN 193
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEekvKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 194 FNIKQMKDLFE----------------QKAAQLATEIADIKSKY-----DEEKSLRAAAEQKVTHLTEDLNKQTTVIQDL 252
Cdd:PRK03918 338 ERLEELKKKLKelekrleeleerhelyEEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 253 KTELLQRPgiEDVAVLKKELVQVQTLMDNMTLERERE-SEKLKDECKKLQSEHAHLEATINQLRSELAK------GPQEV 325
Cdd:PRK03918 418 KKEIKELK--KAIEELKKAKGKCPVCGRELTEEHRKElLEEYTAELKRIEKELKEIEEKERKLRKELRElekvlkKESEL 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 326 AVYVQEIQKLKGSINELTQKNqnlTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRdldcQQLQARLTASESSLQRA 405
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKKYN---LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL----EELKKKLAELEKKLDEL 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 406 QGELSE-KAEAAQKLREELREVESTRQHLK------VEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGR 478
Cdd:PRK03918 569 EEELAElLKELEELGFESVEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 568967300 479 LKEQRQLSSE--------KLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSK 529
Cdd:PRK03918 649 LEELEKKYSEeeyeelreEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
130-782 |
4.24e-06 |
|
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: 51.76 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 130 LRQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDS-SAELQALEQQLEEAQTENFNIKQMKDLFEQKAA 208
Cdd:pfam12128 306 LNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSwQSELENLEERLKALTGKHQDVTAKYNRRRSKIK 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 209 -QLATEIADIKSKYD---EEKSLRAAAEQKV-----THLTEDLNKQTTVIQDLKTELlqrpgIEDVAVLKKELVQVQtlm 279
Cdd:pfam12128 386 eQNNRDIAGIKDKLAkirEARDRQLAVAEDDlqaleSELREQLEAGKLEFNEEEYRL-----KSRLGELKLRLNQAT--- 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 280 dnMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKD-- 357
Cdd:pfam12128 458 --ATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAgt 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 358 -LDYTHLEEKHNEESASRKTLQASLHQRDLD----CQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTrqh 432
Cdd:pfam12128 536 lLHFLRKEAPDWEQSIGKVISPELLHRTDLDpevwDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEA--- 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 433 lkvevkqLQQQREEKEQhglqLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQqvadLQLKLSR-LEEQL 511
Cdd:pfam12128 613 -------LQSAREKQAA----AEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQS----EKDKKNKaLAERK 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 512 KEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLrqIGDKDQKIQNLEALLQKGKESVSLLEKEREDL 591
Cdd:pfam12128 678 DSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVV--EGALDAQLALLKAAIAARRSGAKAELKALETW 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 592 YAKIQAGEGETavlnqlQEKNHALQQQLTQLTEKLKNqSESHKQAEENLHDQVQEQ-KAHLRAAQDRVLSLETSVSELSS 670
Cdd:pfam12128 756 YKRDLASLGVD------PDVIAKLKREIRTLERKIER-IAVRRQEVLRYFDWYQETwLQRRPRLATQLSNIERAISELQQ 828
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 671 QLNeskekvsqldiQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVsvQLDQLTAKFQEKQEHCI-QL 749
Cdd:pfam12128 829 QLA-----------RLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATL--KEDANSEQAQGSIGERLaQL 895
|
650 660 670
....*....|....*....|....*....|...
gi 568967300 750 ESHLKDHKEKHLSLEQKVEDLEGHIKKLEADAL 782
Cdd:pfam12128 896 EDLKLKRDYLSESVKKYVEHFKNVIADHSGSGL 928
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
731-1230 |
5.15e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 731 QLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNA 810
Cdd:PRK02224 238 EADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 811 ELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMqaavTELTAVKAQK 890
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRR----EEIEELEEEI 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 891 DALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAE----------------SALKEQ 954
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvETIEED 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 955 EDLKKSLEKEKEtsqQLKIELNSVKGEVSQAQnTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVL 1034
Cdd:PRK02224 474 RERVEELEAELE---DLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1035 EnklqqqssqaaQELAAEKGKLSALQSNYEKCQADLKQLQSDLygkeSELLATRQDLKSVEEKLTLAQEdlisNRNQIGN 1114
Cdd:PRK02224 550 E-----------AEAEEKREAAAEAEEEAEEAREEVAELNSKL----AELKERIESLERIRTLLAAIAD----AEDEIER 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1115 QNKSIQELQA----AKASLEQDSAKKEALLKE-QSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEEL 1189
Cdd:PRK02224 611 LREKREALAElndeRRERLAEKRERKRELEAEfDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL 690
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 568967300 1190 KSHK--QESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQ 1230
Cdd:PRK02224 691 EELEelRERREALENRVEALEALYDEAEELESMYGDLRAELRQ 733
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
223-434 |
6.36e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 223 EEKSLRAAAEQKVTHLtEDLNKQTTVIQDLK--TELLQ--RPGIEDVAVLKKELVQVQTLMDNMTLER-ERESEKLKDEC 297
Cdd:COG4913 219 EEPDTFEAADALVEHF-DDLERAHEALEDAReqIELLEpiRELAERYAAARERLAELEYLRAALRLWFaQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 298 KKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGS-INELTQKNQNLTEKLQKKDLDYTHLEEKhneesASRKT 376
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEAL-----LAALG 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 377 LQASLHQRDLD--CQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLK 434
Cdd:COG4913 373 LPLPASAEEFAalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| PTZ00303 |
PTZ00303 |
phosphatidylinositol kinase; Provisional |
1367-1452 |
6.41e-06 |
|
phosphatidylinositol kinase; Provisional
Pssm-ID: 140324 [Multi-domain] Cd Length: 1374 Bit Score: 51.24 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1367 AAVQELGRENQSLQIKHTQAL-NRKWAEDNEVQN-CMSCGKCF-----SVTVRRHHCRQCGNIFCAECSTKNA------- 1432
Cdd:PTZ00303 428 ATVGGVAEENELNTFGLTKLLhNPSWQKDDESSDsCPSCGRAFislsrPLGTRAHHCRSCGIRLCVFCITKRAhysfakl 507
|
90 100
....*....|....*....|...
gi 568967300 1433 LTPSSKKPVR---VCDACFNDLQ 1452
Cdd:PTZ00303 508 AKPGSSDEAEerlVCDTCYKEYE 530
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
507-1230 |
6.60e-06 |
|
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: 50.89 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 507 LEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGD-KDQKIQNLEALLQKGKESVSLLE 585
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADiRRRESQSQEDLRNQLQNTVHELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 586 KEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENL------------HDQVQEQKAHLRA 653
Cdd:pfam15921 156 AAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMstmhfrslgsaiSKILRELDTEISY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 654 AQDRVLSLETSVSELSSqlnESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQD-----KQQELNKV 728
Cdd:pfam15921 236 LKGRIFPVEDQLEALKS---ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSqleiiQEQARNQN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 729 SVQLDQLTakfqEKQEHCIQLESHLKDHKEKHlslEQKVEDLEGHIKKLEADALEVKASKEQALQSL----QQQRQLSTD 804
Cdd:pfam15921 313 SMYMRQLS----DLESTVSQLRSELREAKRMY---EDKIEELEKQLVLANSELTEARTERDQFSQESgnldDQLQKLLAD 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 805 LELRNAELSRELQEQEEVVSctkLDLQNkSEILENIKQTLTKKEEEnvvlKQEFEKLSQDSKTQHKELGDRMQAAVTELT 884
Cdd:pfam15921 386 LHKREKELSLEKEQNKRLWD---RDTGN-SITIDHLRRELDDRNME----VQRLEALLKAMKSECQGQMERQMAAIQGKN 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 885 AVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQkgkaAVLDLEKACKELKHQLQVQAE--SALKEQEDLK---- 958
Cdd:pfam15921 458 ESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSER----TVSDLTASLQEKERAIEATNAeiTKLRSRVDLKlqel 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 959 KSLEKEKETSQQLKIELNSVKGEVSQAQNT---LKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLE 1035
Cdd:pfam15921 534 QHLKNEGDHLRNVQTECEALKLQMAEKDKVieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILK 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1036 NKLQQ---QSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYgkeSELLATRQDLKSVEEKLTLAQEDLISNRNQI 1112
Cdd:pfam15921 614 DKKDAkirELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLL---NEVKTSRNELNSLSEDYEVLKRNFRNKSEEM 690
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1113 -GNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDA---QREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEE 1188
Cdd:pfam15921 691 eTTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAmgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEE 770
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 568967300 1189 LKSHKQE---SIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQ 1230
Cdd:pfam15921 771 KNKLSQElstVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
408-654 |
7.60e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 408 ELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHgLQLQGEVSQLhcklleteRQLGEAHGRLKEQR--QL 485
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERY-AAARERLAEL--------EYLRAALRLWFAQRrlEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 486 SSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKqqhqeqqalqqsaTAKLREAQNDLEQVLRQIGDKDQ 565
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG-------------GDRLEQLEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 566 KIQNLEALLQKGKESVSLLEKEREDLYAKIQA-GEGETAVLNQLQEKNHALQQQLTQLTEK---LKNQSESHKQAEENLH 641
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRAEAAAlLEALEEELEALEEALAEAEAALRDLRRElreLEAEIASLERRKSNIP 439
|
250
....*....|...
gi 568967300 642 DQVQEQKAHLRAA 654
Cdd:COG4913 440 ARLLALRDALAEA 452
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
150-760 |
8.76e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 50.35 E-value: 8.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 150 ELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQ----------TENFNIKQMKDLFEQKAAQLATEIADIKS 219
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALqqtqqshaylTQKREAQEEQLKKQQLLKQLRARIEELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 220 KYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRPGIEDVAVLKKELVQVQTLmdnmtLERERESEKLKDECKK 299
Cdd:TIGR00618 275 QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH-----VKQQSSIEEQRRLLQT 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 300 LQSEHAHLEATINQLRSELAKGPQEVAVyVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQA 379
Cdd:TIGR00618 350 LHSQEIHIRDAHEVATSIREISCQQHTL-TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAH 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 380 SLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVEstrqhlkvEVKQLQQQREEKEQHGLQLQGEVS 459
Cdd:TIGR00618 429 AKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ--------TKEQIHLQETRKKAVVLARLLELQ 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 460 QLHCKLLETERQLgEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQ 539
Cdd:TIGR00618 501 EEPCPLCGSCIHP-NPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 540 QSATAKLREAQNDLEQVL----RQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAV----LNQLQEK 611
Cdd:TIGR00618 580 NRSKEDIPNLQNITVRLQdlteKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALhalqLTLTQER 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 612 NHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTE 691
Cdd:TIGR00618 660 VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARED 739
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568967300 692 LLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKH 760
Cdd:TIGR00618 740 ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEI 808
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
130-585 |
1.05e-05 |
|
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: 50.07 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 130 LRQEVQDLQ---ASLKEEKwysEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQMKDLFEQK 206
Cdd:pfam05622 12 LAQRCHELDqqvSLLQEEK---NSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 207 AAQLATEIADIKSKYDEEKSLRAAAEQ------KVTHLTEDLNKQTTVIQDLKTELlqrpgiEDVAVLKKelvQVQTLMD 280
Cdd:pfam05622 89 CEELEKEVLELQHRNEELTSLAEEAQAlkdemdILRESSDKVKKLEATVETYKKKL------EDLGDLRR---QVKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 281 NMTLERERESEkLKDECKKLQSEHAHLEAtinqlrselakgpqevavYVQEIQKLKGSINELTQKNQNLteklqkkDLDY 360
Cdd:pfam05622 160 RNAEYMQRTLQ-LEEELKKANALRGQLET------------------YKRQVQELHGKLSEESKKADKL-------EFEY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 361 THLEEKHNEESASRKTLqasLHQRD--------LDCQQLQARltasesSLQRAQGELSEKAEAAQKLREELR--EVESTR 430
Cdd:pfam05622 214 KKLEEKLEALQKEKERL---IIERDtlretneeLRCAQLQQA------ELSQADALLSPSSDPGDNLAAEIMpaEIREKL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 431 QHLKVEVKQLQQQREEKEQHglqlqgevsqlhcKLLETERQLGEAHGR---LKEQRQLSSEKLMEKEQQVADLQLKLSRL 507
Cdd:pfam05622 285 IRLQHENKMLRLGQEGSYRE-------------RLTELQQLLEDANRRkneLETQNRLANQRILELQQQVEELQKALQEQ 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568967300 508 EEQLKEKVTNSTELQHQLEKSKQQHQEQQalqqsataKLREAQNDLEQVLRQigDKDQKIQNLEALLQKGKESVSLLE 585
Cdd:pfam05622 352 GSKAEDSSLLKQKLEEHLEKLHEAQSELQ--------KKKEQIEELEPKQDS--NLAQKIDELQEALRKKDEDMKAME 419
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
642-1191 |
1.05e-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: 50.17 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 642 DQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLlsaeAAKAAQRADLQNHLDTAQHALQDK 721
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELC----AEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 722 QQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQqrql 801
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKL---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 802 stdLELRNAELSRELQEQEEVV-SCTKLDLQNKSEILEnIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDrMQAAV 880
Cdd:pfam01576 157 ---LEERISEFTSNLAEEEEKAkSLSKLKNKHEAMISD-LEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAE-LQAQI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 881 TELTAVKAQKD-------ALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQV-------- 945
Cdd:pfam01576 232 AELRAQLAKKEeelqaalARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEAlkteledt 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 946 -------QAESALKEQE--DLKKSLEKEKETSQQlkiELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQ 1016
Cdd:pfam01576 312 ldttaaqQELRSKREQEvtELKKALEEETRSHEA---QLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1017 ieaLQGEVKNAVSQKTVLEN---KLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKS 1093
Cdd:pfam01576 389 ---LQAELRTLQQAKQDSEHkrkKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1094 VEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEE 1173
Cdd:pfam01576 466 LESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEE 545
|
570
....*....|....*...
gi 568967300 1174 IKCRQEKEITKLNEELKS 1191
Cdd:pfam01576 546 GKKRLQRELEALTQQLEE 563
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
982-1230 |
1.06e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 982 VSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSqaaqELAAEKGKLSALQS 1061
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ----ELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1062 NYEKCQADLKQLQSDLygkeSELLATRQDLKSVEE-KLTLAQEDLisnrnqignqnksiqelqaakasleQDSAKKEALL 1140
Cdd:COG4942 91 EIAELRAELEAQKEEL----AELLRALYRLGRQPPlALLLSPEDF-------------------------LDAVRRLQYL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1141 KEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGR 1220
Cdd:COG4942 142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
250
....*....|
gi 568967300 1221 VDSLKAALEQ 1230
Cdd:COG4942 222 AEELEALIAR 231
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1049-1302 |
1.36e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1049 LAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKAS 1128
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1129 LEQDSAKKEALLKEQSKAledAQREKSVKEKELVAEKSKLAEMEeikcrqekeitKLNEELKSHKQESIKEITNLKDAKQ 1208
Cdd:COG4942 95 LRAELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAV-----------RRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1209 LLIQQKLELQGRVDSLKAALEQEKESQQLMReqvkkeeeKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTL 1288
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALE--------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|....
gi 568967300 1289 NENLGTVKKEWQSS 1302
Cdd:COG4942 233 EAEAAAAAERTPAA 246
|
|
| FYVE_WDFY2 |
cd15757 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); WDFY2, also ... |
1409-1447 |
1.43e-05 |
|
FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. WDFY2 contains WD40 motifs and a FYVE domain.
Pssm-ID: 277296 [Multi-domain] Cd Length: 70 Bit Score: 44.29 E-value: 1.43e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 568967300 1409 VTVRRHHCRQCGNIFCAECSTKNALTP--SSKKPVRVCDAC 1447
Cdd:cd15757 29 IGLRQHHCRKCGKAVCGKCSSKRSTIPlmGFEFEVRVCDSC 69
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
117-668 |
1.87e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 117 EAGLALTRDDITLLRQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEaqtenfni 196
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE-------- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 197 kqmkdlfeqkaaqLATEIADIKSKYDEEKSLRAAAEQKVThLTEDLNKQTTVIQDLKTELlqrpgiedvAVLKKELVQVQ 276
Cdd:PRK03918 271 -------------LKKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRL---------SRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 277 TLMDNMTlERERESEKLKDECKKLQSEHAHLEA------TINQLRSELAKGPQEVAVYvqEIQKLKGSINELTQKNQNLT 350
Cdd:PRK03918 328 ERIKELE-EKEERLEELKKKLKELEKRLEELEErhelyeEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 351 EKLQKKDLDYTHLEEKHNEESASRKTLQAS-----LHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELRE 425
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 426 VESTRQH------LKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEqrqlSSEKLMEKEQQVAD 499
Cdd:PRK03918 485 LEKVLKKeselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK----ELEKLEELKKKLAE 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 500 LQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKE 579
Cdd:PRK03918 561 LEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 580 SVSLLEKEREDLYAKIQAGEGEtavlnQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLhDQVQEQKAHLRAAQDRVL 659
Cdd:PRK03918 641 RLEELRKELEELEKKYSEEEYE-----ELREEYLELSRELAGLRAELEELEKRREEIKKTL-EKLKEELEEREKAKKELE 714
|
....*....
gi 568967300 660 SLETSVSEL 668
Cdd:PRK03918 715 KLEKALERV 723
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
978-1396 |
1.94e-05 |
|
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: 49.45 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 978 VKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLS 1057
Cdd:pfam12128 239 IRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1058 ALQSNYEKCQADLKQLQSD----LYGKESELLATRQDLKSVEEKLTLaqedlisnrnQIGNQNKSIQELQAAKASLEQDS 1133
Cdd:pfam12128 319 KDRSELEALEDQHGAFLDAdietAAADQEQLPSWQSELENLEERLKA----------LTGKHQDVTAKYNRRRSKIKEQN 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1134 AKK-EALLKEQSKALEDAQREKSVKEKELVAEKSKL------------AEMEEIKCRQEKEITKLN-----EELKSHKQE 1195
Cdd:pfam12128 389 NRDiAGIKDKLAKIREARDRQLAVAEDDLQALESELreqleagklefnEEEYRLKSRLGELKLRLNqatatPELLLQLEN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1196 SIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHE 1275
Cdd:pfam12128 469 FDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWE 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1276 ENEAKLTMQVTTLNENLGTVKKEWQSSQRR-------------VSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCL 1342
Cdd:pfam12128 549 QSIGKVISPELLHRTDLDPEVWDGSVGGELnlygvkldlkridVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLV 628
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 568967300 1343 KGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQIKHTQALNRKWAEDNE 1396
Cdd:pfam12128 629 QANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANE 682
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
486-688 |
2.07e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 486 SSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQ 565
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 566 KIQNLEALLQK--------GKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLtEKLKNQSESHKQAE 637
Cdd:COG4942 98 ELEAQKEELAEllralyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL-AALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568967300 638 ENLHDQVQEQKAHLRAAQDR----VLSLETSVSELSSQLNESKEKVSQLDIQIKA 688
Cdd:COG4942 177 EALLAELEEERAALEALKAErqklLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
590-1327 |
2.12e-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: 49.35 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 590 DLYAKIQAGEGETAVLNQLQEKNHA---LQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVS 666
Cdd:pfam15921 62 DSPRKIIAYPGKEHIERVLEEYSHQvkdLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 667 ELSSQLNESkekVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHldtaqhalQDKQQELNKVSVQLDQLTAK--FQEKQE 744
Cdd:pfam15921 142 DLRNQLQNT---VHELEAAKCLKEDMLEDSNTQIEQLRKMMLSH--------EGVLQEIRSILVDFEEASGKkiYEHDSM 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 745 HCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELS-RELQEQEEVV 823
Cdd:pfam15921 211 STMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEiTGLTEKASSA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 824 SCTKLDLQNKSEILENIKQT--------LTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLA 895
Cdd:pfam15921 291 RSQANSIQSQLEIIQEQARNqnsmymrqLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 896 ELSTTKEKLSKVSDSLKNSKSEFEKENQKGK------------------------AAVLDLEKACKELKHQLQVQAESAL 951
Cdd:pfam15921 371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKrlwdrdtgnsitidhlrrelddrnMEVQRLEALLKAMKSECQGQMERQM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 952 KEQEDLKKSLEKEKETSQQL---KIELNSVKGEVSQAQNTLKQKEKdeqqlqgTINQLKQSAEQKKKQIEALQGEVknav 1028
Cdd:pfam15921 451 AAIQGKNESLEKVSSLTAQLestKEMLRKVVEELTAKKMTLESSER-------TVSDLTASLQEKERAIEATNAEI---- 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1029 sqktvleNKLQQQSSQAAQELAAEKGKLSALQSNYEKCQAdlkqLQSDLYGKESELLATRQDLKSVEEkltlaqedlisn 1108
Cdd:pfam15921 520 -------TKLRSRVDLKLQELQHLKNEGDHLRNVQTECEA----LKLQMAEKDKVIEILRQQIENMTQ------------ 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1109 rnQIGNQNKSIQELQAAKASLEQDSAKKEALLKEqSKALEDAQ----REKSVKEKELVAEKSKLAEMEEIKCRQEKEITK 1184
Cdd:pfam15921 577 --LVGQHGRTAGAMQVEKAQLEKEINDRRLELQE-FKILKDKKdakiRELEARVSDLELEKVKLVNAGSERLRAVKDIKQ 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1185 LNEELKSHKQESIKEITNLKDAKQLL---IQQKLE--------LQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEF 1253
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNSLSEDYEVLkrnFRNKSEemetttnkLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1254 SEKEAK------LHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATV 1327
Cdd:pfam15921 734 KQITAKrgqidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1121-1386 |
2.31e-05 |
|
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: 49.28 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1121 ELQAAKASLEQDSAKKEALlKEQSKALEDAQREKSVKEKElvAEKSKLAEMEEIKCRQEKEITKLNEELkshkQESIKEI 1200
Cdd:TIGR02168 197 ELERQLKSLERQAEKAERY-KELKAELRELELALLVLRLE--ELREELEELQEELKEAEEELEELTAEL----QELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1201 TNLKDAKQLLIQQKLELQGRVDSLKAalEQEKESQQLMReqvkkeeekrkeeFSEKEAKLHSEIKEKEAGMKKHEENEAK 1280
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALAN--EISRLEQQKQI-------------LRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1281 LTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKALELQR 1360
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260
....*....|....*....|....*.
gi 568967300 1361 KLDNTTAAVQELGRENQSLQIKHTQA 1386
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQA 440
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1081-1380 |
2.40e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1081 ESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQdsaKKEALLKEQSKALEDAQREKSVKEKE 1160
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKE---KREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1161 LVAEKSKLAEMEEIKCRQEKEITKLNEELKshkqESIKEITNLKDAKQLLIQQKL-ELQGRVDSLKAALEqEKESQQLMR 1239
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLE----ELNKKIKDLGEEEQLRVKEKIgELEAEIASLERSIA-EKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1240 EQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGE 1319
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1320 IAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQ 1380
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
517-1098 |
2.45e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 517 NSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIG-------DKDQKIQNLEALLQKGKESVSLLEKERE 589
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINeisselpELREELEKLEKEVKELEELKEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 590 DLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLhdqvqEQKAHLRAAQDRVLSLETSVSELS 669
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI-----KLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 670 SQLNESKEKVSQLDIQIKAKTELLLSAEAakaaqradlqnhldtaqhaLQDKQQELNKVSVQLDQLTAKFQEKQEHCIQL 749
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKE-------------------LEKRLEELEERHELYEEAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 750 ESHLKDHKEKHL-SLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRElqEQEEVVSCTKL 828
Cdd:PRK03918 382 TGLTPEKLEKELeELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE--HRKELLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 829 DLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKtqHKELGDRMQAAVTELTAVKAQK-DALLAELSTTKEKLSKV 907
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK--LKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 908 SDSLKNSKSEFEKENQ-KGKAAVL-----DLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSqqlkIELNSVKGE 981
Cdd:PRK03918 538 KGEIKSLKKELEKLEElKKKLAELekkldELEEELAELLKELEELGFESVEELEERLKELEPFYNEY----LELKDAEKE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 982 VSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEvknaVSQKTvlENKLQQQSSQAAQELAAEKGKLSALQS 1061
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK----YSEEE--YEELREEYLELSRELAGLRAELEELEK 687
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 568967300 1062 NYEKCQADLKQLQSDL-----YGKESELLA-TRQDLKSVEEKL 1098
Cdd:PRK03918 688 RREEIKKTLEKLKEELeerekAKKELEKLEkALERVEELREKV 730
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
370-515 |
2.82e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 48.92 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 370 ESASRKTLQASLHQRDLDcqQLQARLTASE---SSLQRAQGELSEkaEAAQKLREELREVESTRQHLKvevkqlQQQREE 446
Cdd:COG0542 397 EAAARVRMEIDSKPEELD--ELERRLEQLEiekEALKKEQDEASF--ERLAELRDELAELEEELEALK------ARWEAE 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 447 KE--QHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSE--------------------KLMEKEQQvadlqlKL 504
Cdd:COG0542 467 KEliEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREevteediaevvsrwtgipvgKLLEGERE------KL 540
|
170
....*....|.
gi 568967300 505 SRLEEQLKEKV 515
Cdd:COG0542 541 LNLEEELHERV 551
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
396-783 |
2.82e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 396 TASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQqREEKEQHGLQLQGEVSQLHCKLLETERQLGEA 475
Cdd:PRK04863 289 LELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASD-HLNLVQTALRQQEKIERYQADLEELEERLEEQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 476 HGRLK---EQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQH---QLEKSKQQHQEQQALQQSATAKLREA 549
Cdd:PRK04863 368 NEVVEeadEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQavqALERAKQLCGLPDLTADNAEDWLEEF 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 550 QNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEK-----EREDLY----AKIQAGEGETAVLNQLQ---------EK 611
Cdd:PRK04863 448 QAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagevSRSEAWdvarELLRRLREQRHLAEQLQqlrmrlselEQ 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 612 NHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAhlraaqdRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTE 691
Cdd:PRK04863 528 RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEA-------RLESLSESVSEARERRMALRQQLEQLQARIQRLAA 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 692 LllsaeaakaaqradlqnhlDTAQHALQDKqqelnkvsvqLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLE 771
Cdd:PRK04863 601 R-------------------APAWLAAQDA----------LARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELA 651
|
410
....*....|..
gi 568967300 772 GHIKKLEADALE 783
Cdd:PRK04863 652 ARKQALDEEIER 663
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
280-575 |
3.12e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.58 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 280 DNMTLERERESEKLKDECKKLQSEhahleatinQLRSElakgpqEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDld 359
Cdd:pfam17380 340 ERMAMERERELERIRQEERKRELE---------RIRQE------EIAMEISRMRELERLQMERQQKNERVRQELEAAR-- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 360 ythlEEKHNEESASRKTLQASLHQRDLDCQQLQARltasesslqraQGELSEKAEAAQKLREELREVESTRQHlkvEVKQ 439
Cdd:pfam17380 403 ----KVKILEEERQRKIQQQKVEMEQIRAEQEEAR-----------QREVRRLEEERAREMERVRLEEQERQQ---QVER 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 440 LQQQREEKEQHGLQLQGEvsqlhckllETERQLGEahgrlKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNST 519
Cdd:pfam17380 465 LRQQEEERKRKKLELEKE---------KRDRKRAE-----EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIY 530
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568967300 520 ELQH----QLEKSKQQHQEQQALQQSATAKLREAQNDLE------QVLRQIGDKDQKIQNLEALLQ 575
Cdd:pfam17380 531 EEERrreaEEERRKQQEMEERRRIQEQMRKATEERSRLEamererEMMRQIVESEKARAEYEATTP 596
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
389-1010 |
3.36e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.81 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 389 QQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLET 468
Cdd:TIGR00618 166 KELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 469 ERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLRE 548
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 549 AQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKN 628
Cdd:TIGR00618 326 LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 629 QSESHKQAEENLHDQV-QEQKAHLRA---AQDRVLSLETSVSELSSQ--------LNESKEKVSQLDIQIKAKTELLLSA 696
Cdd:TIGR00618 406 QREQATIDTRTSAFRDlQGQLAHAKKqqeLQQRYAELCAAAITCTAQceklekihLQESAQSLKEREQQLQTKEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 697 EAAKAAQRADLQNH-----------LDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQE-----HCIQLESHLKDHKEKH 760
Cdd:TIGR00618 486 TRKKAVVLARLLELqeepcplcgscIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEedvyhQLTSERKQRASLKEQM 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 761 LSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVScTKLDLQNKSEILENI 840
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQD-VRLHLQQCSQELALK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 841 KQTLTKKEEEnvVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEK 920
Cdd:TIGR00618 645 LTALHALQLT--LTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 921 ENQKGKAAVLDLE---KACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVsqaQNTLKQKEKDEQ 997
Cdd:TIGR00618 723 IENASSSLGSDLAareDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEI---QFFNRLREEDTH 799
|
650
....*....|...
gi 568967300 998 QLQGTINQLKQSA 1010
Cdd:TIGR00618 800 LLKTLEAEIGQEI 812
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
124-680 |
3.61e-05 |
|
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: 48.48 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 124 RDDITLLRQEVQDLQASLKEEKwysEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQMKDLF 203
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENK---KNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 204 EQKAAQLATEIADIKSKYDEEKSLRAAA---EQKVTHLTEDLNKQTTVIQDLKTELLQRPgiEDVAVLKKELVQVQTLMD 280
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNKSLESQIselKKQNNQLKDNIEKKQQEINEKTTEISNTQ--TQLNQLKDEQNKIKKQLS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 281 NMTLERERESEKLKDECKKLQSEHAHLEA--------TINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEK 352
Cdd:TIGR04523 271 EKQKELEQNNKKIKELEKQLNQLKSEISDlnnqkeqdWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 353 LQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQH 432
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 433 LKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLqLKLSRLEEQLK 512
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL-KKLNEEKKELE 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 513 EKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQkIQNLEALLQKGKESVSLLEKEREDLY 592
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE-IDEKNKEIEELKQTQKSLKKKQEEKQ 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 593 AKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQL 672
Cdd:TIGR04523 589 ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKI 668
|
....*...
gi 568967300 673 NESKEKVS 680
Cdd:TIGR04523 669 KESKTKID 676
|
|
| FYVE1_Vac1p_like |
cd15761 |
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ... |
1391-1448 |
3.64e-05 |
|
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the first FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.
Pssm-ID: 277300 Cd Length: 76 Bit Score: 43.41 E-value: 3.64e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568967300 1391 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECST------KNA-LTPSSKKPVRVCDACF 1448
Cdd:cd15761 4 WKKPSGKSRCSECGKTLNKKNGIVNCRKCGELFCNEHCRnriklnNSAeYDPKNGKWCRCCEKCF 68
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
217-441 |
3.69e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 217 IKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRPG-----IEDVAVLKKELVQVQTLMDNMTLERERESE 291
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIArkqnkYDELVEEAKTIKAEIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 292 KLKDECKKLQSEHAHLEATINQLRSELA--KGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNE 369
Cdd:PHA02562 252 DPSAALNKLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDE 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568967300 370 ESASRKT---LQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQ 441
Cdd:PHA02562 332 FNEQSKKlleLKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRG 406
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
179-576 |
4.43e-05 |
|
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: 47.97 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 179 LQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIK---SKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTE 255
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKeelRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 256 LLQRpgiedvavlKKELVQVQTLMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKL 335
Cdd:pfam07888 127 HEAR---------IRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 336 KGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQAslhqrdldcqqLQARLTASEsslqraqgelsekaEA 415
Cdd:pfam07888 198 RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRS-----------LQERLNASE--------------RK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 416 AQKLREELREVESTRQHLKVEVKQLQQQreekeqhglqlqgeVSQLHCKLLETERQLGEAHGRLKEQR---QLSSEKLME 492
Cdd:pfam07888 253 VEGLGEELSSMAAQRDRTQAELHQARLQ--------------AAQLTLQLADASLALREGRARWAQERetlQQSAEADKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 493 K-EQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLE 571
Cdd:pfam07888 319 RiEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLE 398
|
....*
gi 568967300 572 ALLQK 576
Cdd:pfam07888 399 QRLET 403
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
371-576 |
4.81e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 371 SASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQH 450
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 451 GLQLQGEVSQLHCKLLETERQ-------LGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQH 523
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568967300 524 QLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQK 576
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
981-1227 |
5.13e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 981 EVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAvsqktvlenklqqqssqaAQELAAEKGKLSALQ 1060
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL------------------QAEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1061 SNYEKCQADLKQLQSDLYgkesellaTRQDLKSVEEKLTLAQ--EDLISNRNQI----GNQNKSIQELQAAKASLEQDSA 1134
Cdd:COG3883 79 AEIEERREELGERARALY--------RSGGSVSYLDVLLGSEsfSDFLDRLSALskiaDADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1135 KKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQK 1214
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250
....*....|...
gi 568967300 1215 LELQGRVDSLKAA 1227
Cdd:COG3883 231 AAAAAAAAAAAAA 243
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
541-769 |
5.88e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 541 SATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQ--KGKESVSLLEKEREDLYAKIQAGEGEtavLNQLQEKNHALQQQ 618
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQ---LAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 619 LTQLTEKLKNQSESHKQAEENlhDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEA 698
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967300 699 AKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEhciQLESHLKDHKEKHLSLEQKVED 769
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE---LYESLLQRLEEARLAEALTVGN 387
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
812-1027 |
7.55e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 812 LSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQ---DSKTQHKELGDRMQAAVTELTAVKA 888
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriaALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 889 QKDALLAELSTTKEKLSKVSDSL-KNSKSEFEKE--NQKGKAAVLDLEKACKELKHQLQVQAE---SALKEQEDLKKSLE 962
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALyRLGRQPPLALllSPEDFLDAVRRLQYLKYLAPARREQAEelrADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568967300 963 KEKETSQQLKIELNSVKGEVSQAQN----TLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNA 1027
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAerqkLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
909-1364 |
7.87e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 909 DSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAEsALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQN- 987
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 988 --TLKQKEKDEQQLQGTINQLKQsAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEkgkLSALQSNYEK 1065
Cdd:COG4717 128 lpLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1066 CQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQ-EDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQS 1144
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAAlEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1145 KALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAkqllIQQKLELQGRVDSL 1224
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR----IEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1225 KAALEQEKESQQlmREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEE--NEAKLTMQVTTLNENLGTVKKEWQSS 1302
Cdd:COG4717 360 EEELQLEELEQE--IAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEEL 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967300 1303 QRRVSELEKQTDDLRGEIAVLEATVQNnqderrallercLKGEGEIEKLQTKALELQRKLDN 1364
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQ------------LEEDGELAELLQELEELKAELRE 487
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
482-691 |
1.03e-04 |
|
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: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 482 QRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIG 561
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 562 DKDQKIQNLEALLqkgkESVSLlekerEDLYAKIQAgegetavLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLH 641
Cdd:COG3883 97 RSGGSVSYLDVLL----GSESF-----SDFLDRLSA-------LSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568967300 642 DQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTE 691
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
283-522 |
1.03e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 283 TLERERES-----EKLKDECKKLQSEHAHLEATINQ-LRSELAKGP-QEVAVYVQEIQKLKGSINELTQKNQNLTEKLQK 355
Cdd:PRK04863 790 QLRAEREElaeryATLSFDVQKLQRLHQAFSRFIGShLAVAFEADPeAELRQLNRRRVELERALADHESQEQQQRSQLEQ 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 356 ---------------KDLDYTHLEEKHNE--------ESASR------------KTLQASLHQRDLDCQQLQARLTASES 400
Cdd:PRK04863 870 akeglsalnrllprlNLLADETLADRVEEireqldeaEEAKRfvqqhgnalaqlEPIVSVLQSDPEQFEQLKQDYQQAQQ 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 401 SLQR----------------------AQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEV 458
Cdd:PRK04863 950 TQRDakqqafaltevvqrrahfsyedAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY 1029
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967300 459 SQLHCKLLETERQLGE--------AHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQ 522
Cdd:PRK04863 1030 DAKRQMLQELKQELQDlgvpadsgAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLE 1101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
546-1080 |
1.06e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 546 LREAQNDLEQVLRQIgDKDQKIQNLEALLQKGKESVSLLEKEREdlYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEK 625
Cdd:COG4913 237 LERAHEALEDAREQI-ELLEPIRELAERYAAARERLAELEYLRA--ALRLWFAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 626 LKNQSESHKQAEENLHDQVQEQKAhlraaqDRVLSLETSVSELSSQLNESKEKVSQLDiqikaktELLLSAEAAKAAQRA 705
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERELEERERRRARLE-------ALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 706 DLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVED----LEGHIKKLEADA 781
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAlrdaLAEALGLDEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 782 ------LEVKASKEQ--------------------ALQSLQQQRQLSTDLELR-NAELSRELQEQEEVVSCTKLDLQNKS 834
Cdd:COG4913 461 pfvgelIEVRPEEERwrgaiervlggfaltllvppEHYAAALRWVNRLHLRGRlVYERVRTGLPDPERPRLDPDSLAGKL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 835 EILEN-----IKQTLTKKEE----ENVvlkQEFEK---------LSQDSKTQHkELGDRMQAA---VTELTAvKAQKDAL 893
Cdd:COG4913 541 DFKPHpfrawLEAELGRRFDyvcvDSP---EELRRhpraitragQVKGNGTRH-EKDDRRRIRsryVLGFDN-RAKLAAL 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 894 LAELSTTKEKLSKVSDSLKNSKSEfEKENQKGKAAVLDLEKACKElkhqlQVQAESALKEQEDLKKSLEKEKETSQQLKi 973
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAE-LDALQERREALQRLAEYSWD-----EIDVASAEREIAELEAELERLDASSDDLA- 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 974 elnSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEK 1053
Cdd:COG4913 689 ---ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVER 765
|
570 580
....*....|....*....|....*..
gi 568967300 1054 GKLSALQSNYEKCQADLKQLQSDLYGK 1080
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERA 792
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
856-1362 |
1.10e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 856 QEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDA--LLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLE 933
Cdd:PRK02224 165 EEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 934 K---------ACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGE----------VSQAQNTLkqkEK 994
Cdd:PRK02224 245 EheerreeleTLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREEL---ED 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 995 DEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENK---LQQQSSQAAQELAAEKGKLSALQSNYEKCQA--- 1068
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEaaeLESELEEAREAVEDRREEIEELEEEIEELRErfg 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1069 ----DLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNR---------------------NQIGNQNKSIQELQ 1123
Cdd:PRK02224 402 dapvDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpvegsphvETIEEDRERVEELE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1124 AAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKsKLAEMEEIKCRQEKEITKLNE---ELKSHKQESIKEI 1200
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEE-LIAERRETIEEKRERAEELREraaELEAEAEEKREAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1201 TNLKDAKQLLIQQKLELQGRVDSLKAALEQ-EKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEK-EAGMKKHEENE 1278
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKLAELKERIESlERIRTLLAAIADAEDEIERLREKREALAELNDERRERlAEKRERKRELE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1279 AKLT-MQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQ---DERRALLERCLKGE---GEIEKL 1351
Cdd:PRK02224 641 AEFDeARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEelrERREALENRVEALEalyDEAEEL 720
|
570
....*....|.
gi 568967300 1352 QTKALELQRKL 1362
Cdd:PRK02224 721 ESMYGDLRAEL 731
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
479-690 |
1.20e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 479 LKEQRQLSSEKLMEKEQQVADLQLK--LSRLEEQLKEKVTNSTELQHQLEKSKqqhqeqqalqqsatAKLREAQNDLEQV 556
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEAR--------------AELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 557 LRQIGDKDQKIQNLEA--LLQKGKESVSLLEKEREDLYAKIQAGEGE-TAVLNQLQEKNHALQQQLTQLTEKLKNQSESH 633
Cdd:COG3206 246 RAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDvIALRAQIAALRAQLQQEAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 634 KQAEENLHDQVQEQKAHLR---AAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKT 690
Cdd:COG3206 326 QAREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYESLLQRLEEARLAEALTV 385
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
323-857 |
1.41e-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: 46.35 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 323 QEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDldythleeKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSL 402
Cdd:pfam10174 185 RRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRN--------QLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 403 Q--RAQGELSekaeaAQKLREELREVESTRQH---LKVEVKQLQQQREEKEQHGLQLQGEvsqlhcklLETerqLGEAHG 477
Cdd:pfam10174 257 QmlKTNGLLH-----TEDREEEIKQMEVYKSHskfMKNKIDQLKQELSKKESELLALQTK--------LET---LTNQNS 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 478 RLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKskqqhqeQQALQQSATAKLREAQNDLEQVL 557
Cdd:pfam10174 321 DCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQD-------LTEEKSTLAGEIRDLKDMLDVKE 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 558 RQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQ-LQEKN---HALQQQLTQLTEKLKNQSESH 633
Cdd:pfam10174 394 RKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEaLSEKEriiERLKEQREREDRERLEELESL 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 634 KQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTE---------LLLSAEAAKAAQR 704
Cdd:pfam10174 474 KKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEecsklenqlKKAHNAEEAVRTN 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 705 ADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQE-------KQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKL 777
Cdd:pfam10174 554 PEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREvenekndKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKK 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 778 EADALEvKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQE 857
Cdd:pfam10174 634 GAQLLE-EARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQE 712
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
944-1217 |
1.54e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 944 QVQAESALKEQEDLKKSLEKEKETSQQlkielnsvkgevSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGE 1023
Cdd:PRK11281 28 RAASNGDLPTEADVQAQLDALNKQKLL------------EAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1024 VKNAVSQKTVLENKLQQQSSQAAQELAaekgkLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQE 1103
Cdd:PRK11281 96 LRQAQAELEALKDDNDEETRETLSTLS-----LRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1104 DLISNRNQIGNQNKS--------IQELQAAKASLEQDSAKKEALLK--EQSKALEDAQReksvkekELVAEKSKlaemee 1173
Cdd:PRK11281 171 RLQQIRNLLKGGKVGgkalrpsqRVLLQAEQALLNAQNDLQRKSLEgnTQLQDLLQKQR-------DYLTARIQ------ 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568967300 1174 ikcRQEKEITKL----NEELKSHKQESIKEITNLKDAKQL----LIQQKLEL 1217
Cdd:PRK11281 238 ---RLEHQLQLLqeaiNSKRLTLSEKTVQEAQSQDEAARIqanpLVAQELEI 286
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
374-682 |
1.65e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.48 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 374 RKTLQASLHQRDlDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELrevESTRQHLKVEVKQLQQQreEKEQHglq 453
Cdd:COG3096 281 RELSERALELRR-ELFGARRQLAEEQYRLVEMARELEELSARESDLEQDY---QAASDHLNLVQTALRQQ--EKIER--- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 454 LQGEVSQLHCKLLETERQLGEAHgrlkEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSteLQHQ-----LEKS 528
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAA----EQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRA--IQYQqavqaLEKA 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 529 KQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEK-----EREDLY----------- 592
Cdd:COG3096 426 RALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKiagevERSQAWqtarellrryr 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 593 -AKIQAGEGET--AVLNQLqEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELS 669
Cdd:COG3096 506 sQQALAQRLQQlrAQLAEL-EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELR 584
|
330
....*....|...
gi 568967300 670 SQLNESKEKVSQL 682
Cdd:COG3096 585 QQLEQLRARIKEL 597
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
436-1023 |
1.76e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.25 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 436 EVKQLQQQREEKEQHGLQLQGEVSQLHCKL----LETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQL 511
Cdd:pfam05483 170 KTKKYEYEREETRQVYMDLNNNIEKMILAFeelrVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 512 KEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQN-------LEALLQKGKESVSLL 584
Cdd:pfam05483 250 TEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRsmstqkaLEEDLQIATKTICQL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 585 EKEREDLYAKI-QAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLET 663
Cdd:pfam05483 330 TEEKEAQMEELnKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 664 SVSELSSQ--LNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQE 741
Cdd:pfam05483 410 LKKILAEDekLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 742 KQEHCIQLESHLKDhkekhlsLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEE 821
Cdd:pfam05483 490 LTAHCDKLLLENKE-------LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGD 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 822 VVSCT--KLDLQNKSEILENIKQTLTKKEEENVV--LKQEFEKLSQDSKTQHKE---LGDRMQAAVTELTAVKAQKDALL 894
Cdd:pfam05483 563 EVKCKldKSEENARSIEYEVLKKEKQMKILENKCnnLKKQIENKNKNIEELHQEnkaLKKKGSAENKQLNAYEIKVNKLE 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 895 AELSTTKEKLSKVSDslkNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIE 974
Cdd:pfam05483 643 LELASAKQKFEEIID---NYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKI 719
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 568967300 975 LNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGE 1023
Cdd:pfam05483 720 IEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEE 768
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
552-1173 |
1.76e-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: 46.37 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 552 DLEQVLRQIGDKDQKIQNLEallQKGKESVSLLEKEReDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNqse 631
Cdd:pfam12128 197 DVKSMIVAILEDDGVVPPKS---RLNRQQVEHWIRDI-QAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKS--- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 632 sHKQAEENLHDQVQEQKAHLRaaqDRVLSLETSVSELSSQLNESKekvSQLDIQIKAKTELLLSAEAAKAAQRADLQNHL 711
Cdd:pfam12128 270 -DETLIASRQEERQETSAELN---QLLRTLDDQWKEKRDELNGEL---SAADAAVAKDRSELEALEDQHGAFLDADIETA 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 712 DTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLS-LEQKVEDLEGHIKKLEA------DALEv 784
Cdd:pfam12128 343 AADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAgIKDKLAKIREARDRQLAvaeddlQALE- 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 785 KASKEQALQSLQQQRQLSTDLELRNAELsRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQD 864
Cdd:pfam12128 422 SELREQLEAGKLEFNEEEYRLKSRLGEL-KLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKR 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 865 SKTQHKELGD---RMQAAVTELTAVKAQKDA----LLAELSTT----KEKLSKVSDSLKNSKS----EFEKENQKGKAAV 929
Cdd:pfam12128 501 RDQASEALRQasrRLEERQSALDELELQLFPqagtLLHFLRKEapdwEQSIGKVISPELLHRTdldpEVWDGSVGGELNL 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 930 LDLEKACKELKHQLQVQAESALKEQED-LKKSLEKEKETSQQLKIELNSVKGEVSQAQ-------NTLKQKEKDEQQLQG 1001
Cdd:pfam12128 581 YGVKLDLKRIDVPEWAASEEELRERLDkAEEALQSAREKQAAAEEQLVQANGELEKASreetfarTALKNARLDLRRLFD 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1002 TINQLK-QSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQEL-------------------AAEKGKLSALQS 1061
Cdd:pfam12128 661 EKQSEKdKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKreartekqaywqvvegaldAQLALLKAAIAA 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1062 NYEKCQADLKQLQS----DLYGK---ESELLATRQDLKSVEEKLTLAQED---------------LISNRN---QIGNQN 1116
Cdd:pfam12128 741 RRSGAKAELKALETwykrDLASLgvdPDVIAKLKREIRTLERKIERIAVRrqevlryfdwyqetwLQRRPRlatQLSNIE 820
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 568967300 1117 KSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEE 1173
Cdd:pfam12128 821 RAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKE 877
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
128-637 |
2.09e-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: 46.12 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 128 TLLRQEVQDLQASlKEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQMKDLFEQKA 207
Cdd:TIGR00618 349 TLHSQEIHIRDAH-EVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 208 AQLATEIADIKSKY------DEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRPGIEDVAVLKKELVQV------ 275
Cdd:TIGR00618 428 HAKKQQELQQRYAElcaaaiTCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEepcplc 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 276 -QTLMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQ 354
Cdd:TIGR00618 508 gSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 355 K----KDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTR 430
Cdd:TIGR00618 588 NlqniTVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSI 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 431 QHLKVEVKQLQQQREEKEQHGLQ----LQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSR 506
Cdd:TIGR00618 668 RVLPKELLASRQLALQKMQSEKEqltyWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKE 747
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 507 LEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKI-QNLEALLQKGKESVSLLE 585
Cdd:TIGR00618 748 LMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIgQEIPSDEDILNLQCETLV 827
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 568967300 586 KEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAE 637
Cdd:TIGR00618 828 QEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
586-1375 |
2.19e-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: 46.19 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 586 KEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEK-LKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETS 664
Cdd:TIGR00606 255 KEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 665 VSELSSQLNESKEKVSQLdiQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQE 744
Cdd:TIGR00606 335 RRLLNQEKTELLVEQGRL--QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 745 HCIQLESHLKDHKEKHLSLEQKVEDLeGHIKKLEADALEVKAS------KEQALQSLQQQRQLSTDLELRNAELSRELQE 818
Cdd:TIGR00606 413 LCADLQSKERLKQEQADEIRDEKKGL-GRTIELKKEILEKKQEelkfviKELQQLEGSSDRILELDQELRKAERELSKAE 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 819 QEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEklsqdSKTQHKELGDRMQAAVTELTAVKAQKDALLAELS 898
Cdd:TIGR00606 492 KNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTT-----TRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 899 ---TTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKkslekEKETSQQLKIEL 975
Cdd:TIGR00606 567 gyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLF-----DVCGSQDEESDL 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 976 NSVKGEvsqaqntLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLE---NKLQQQSSQAAQELAAE 1052
Cdd:TIGR00606 642 ERLKEE-------IEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQefiSDLQSKLRLAPDKLKST 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1053 KGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKsiqELQAAKASLEQD 1132
Cdd:TIGR00606 715 ESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMP---EEESAKVCLTDV 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1133 SAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQ 1212
Cdd:TIGR00606 792 TIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKS 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1213 QKLELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEaKLTMQVTTLNENL 1292
Cdd:TIGR00606 872 EKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK-KAQDKVNDIKEKV 950
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1293 GTVKKEWQSSQRRVSE-LEKQTDDLRGEIAVLEATVQNNQDERRALLE--RCLKGEGEIEKLQTKALELQRKLDNTTAAV 1369
Cdd:TIGR00606 951 KNIHGYMKDIENKIQDgKDDYLKQKETELNTVNAQLEECEKHQEKINEdmRLMRQDIDTQKIQERWLQDNLTLRKRENEL 1030
|
....*.
gi 568967300 1370 QELGRE 1375
Cdd:TIGR00606 1031 KEVEEE 1036
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
414-658 |
2.26e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 414 EAAQKLREELREVESTRQhlkvEVKQLQQQREekeqhglqlqgevsqlhckLLETERQLGEAHGRLKEQRQLSSEklMEK 493
Cdd:COG4913 225 EAADALVEHFDDLERAHE----ALEDAREQIE-------------------LLEPIRELAERYAAARERLAELEY--LRA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 494 EQQVADLQLKLSRLEEQLkekvtnsTELQHQLEKSKQQHQEQQALQQSATAKLREaqndLEQVLRQIGdkDQKIQNLEAL 573
Cdd:COG4913 280 ALRLWFAQRRLELLEAEL-------EELRAELARLEAELERLEARLDALREELDE----LEAQIRGNG--GDRLEQLERE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 574 LQKGKESVSLLEKEREDLYAKIQA----GEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENL---HDQVQE 646
Cdd:COG4913 347 IERLERELEERERRRARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLrreLRELEA 426
|
250
....*....|..
gi 568967300 647 QKAHLRAAQDRV 658
Cdd:COG4913 427 EIASLERRKSNI 438
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
118-356 |
2.40e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 118 AGLALTRDDITLLRQEVQDLQASLKEEKwysEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQtenfniK 197
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELE---KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE------A 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 198 QMKDLfEQKAAQLATEIADIKSKYdeEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRPGIEDVAVLKKELVQVQT 277
Cdd:COG4942 84 ELAEL-EKEIAELRAELEAQKEEL--AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568967300 278 LMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKK 356
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
916-1384 |
2.49e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.87 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 916 SEFEKENQKGKAAVLDLEKACKELK---HQLQVQAESA-LKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQ 991
Cdd:pfam05483 172 KKYEYEREETRQVYMDLNNNIEKMIlafEELRVQAENArLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 992 KEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKgklsALQSNYEKCQADLK 1071
Cdd:pfam05483 252 KENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQK----ALEEDLQIATKTIC 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1072 QLQSDLYGKESELLATRQDLKSVEEKL---TLAQEDLISNRNQIGNQNKSIQELQAAKasleqdsakkealLKEQSKALE 1148
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSFVVTEFeatTCSLEELLRTEQQRLEKNEDQLKIITME-------------LQKKSSELE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1149 DAQREKSVKEKELVAEKSKLAEMEEIkCRQEKEITKLNEELKSHKQESI-------KEITNLKDAKQLLIQQKLELQGRV 1221
Cdd:pfam05483 395 EMTKFKNNKEVELEELKKILAEDEKL-LDEKKQFEKIAEELKGKEQELIfllqareKEIHDLEIQLTAIKTSEEHYLKEV 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1222 DSLKAALEQEKeSQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQS 1301
Cdd:pfam05483 474 EDLKTELEKEK-LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELES 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1302 SQRrvsELEKQTDDLRGEIavleatvQNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQI 1381
Cdd:pfam05483 553 VRE---EFIQKGDEVKCKL-------DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
...
gi 568967300 1382 KHT 1384
Cdd:pfam05483 623 KGS 625
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
329-649 |
2.55e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 45.06 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 329 VQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQrdldcqqLQARLTASESSLQRAQGE 408
Cdd:pfam19220 40 LRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAK-------LEAALREAEAAKEELRIE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 409 LSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSE 488
Cdd:pfam19220 113 LRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 489 ---KLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQS----ATAKLREAQNDLEQVLRQIG 561
Cdd:pfam19220 193 ltrRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMkleaLTARAAATEQLLAEARNQLR 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 562 DKDQKIQNLEALLQKG-------KESVSLLEKEREDLYAKIQ------------------AGEGETAVLNQLQEKNHALQ 616
Cdd:pfam19220 273 DRDEAIRAAERRLKEAsierdtlERRLAGLEADLERRTQQFQemqraraeleeraemltkALAAKDAALERAEERIASLS 352
|
330 340 350
....*....|....*....|....*....|...
gi 568967300 617 QQLTQLTEKLKNQSESHKQAEENLHDQVQEQKA 649
Cdd:pfam19220 353 DRIAELTKRFEVERAALEQANRRLKEELQRERA 385
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
177-610 |
2.92e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 177 AELQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAE-----QKVTHLTEDLNKQTTVIQD 251
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 252 LKTELLQ-RPGIEDVAVLKKELVQVQTLMDNmtlERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQ 330
Cdd:COG4717 151 LEERLEElRELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 331 EIQKLKGSINELTQKNQNLTEKLQKKD---------------------------------LDYTHLEEKHNEESASRKTL 377
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLLLIaaallallglggsllsliltiagvlflvlgllaLLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 378 QASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQhlkvevkQLQQQREEKEQHGLQLQGE 457
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE-------ELQLEELEQEIAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 458 VsqlhckllETERQLGEAHGRLKEQRQLsseklmEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEkskqqhqeqqa 537
Cdd:COG4717 381 V--------EDEEELRAALEQAEEYQEL------KEELEELEEQLEELLGELEELLEALDEEELEEELE----------- 435
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967300 538 lqqSATAKLREAQNDLEQVLRQIGDKDQKIQNLEallqkGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQE 610
Cdd:COG4717 436 ---ELEEELEELEEELEELREELAELEAELEQLE-----EDGELAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
333-762 |
3.00e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 333 QKLKGSINELTQKNQNLTEKLQKKDlDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASE--SSLQRAQGELS 410
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 411 EKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKL 490
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 491 MEKEQQVADLQLKLSR--LEEQLKEK-----------------VTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQN 551
Cdd:COG4717 223 EELEEELEQLENELEAaaLEERLKEArlllliaaallallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 552 DLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQE--KNHALQQQLTQLTEKLKNQ 629
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 630 SESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNES--KEKVSQLDIQIKAKTELLLSAEAAKAAQRADL 707
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 568967300 708 QNHLDtaQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLS 762
Cdd:COG4717 463 EQLEE--DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
287-528 |
3.19e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 287 ERESEKLKDECKKLQSEHAHLEATINQLR--SELAKGPQEVAVYVQEIQKLKGSINELTQKN---QNLTEKLQKKDLDYT 361
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASSddlAALEEQLEELEAELE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 362 HLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVestRQHLKVEVKQLQ 441
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL---RENLEERIDALR 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 442 QQREEKEQHGLQLQGE-VSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQqvadlqlklsRLEEQLKEKVTNS-T 519
Cdd:COG4913 780 ARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYEE----------RFKELLNENSIEFvA 849
|
....*....
gi 568967300 520 ELQHQLEKS 528
Cdd:COG4913 850 DLLSKLRRA 858
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
714-966 |
3.25e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 714 AQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADalevkaskeqalq 793
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 794 slqqqrqlSTDLELRNAELSRELQEQEEVVsctkldlqnkSEILENIkQTLTKKEEENVVLKQEFEKLSQDSKTQHKELG 873
Cdd:COG4942 85 --------LAELEKEIAELRAELEAQKEEL----------AELLRAL-YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 874 DRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESAlKE 953
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA-EE 224
|
250
....*....|...
gi 568967300 954 QEDLKKSLEKEKE 966
Cdd:COG4942 225 LEALIARLEAEAA 237
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
834-1239 |
3.43e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 834 SEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQhKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKN 913
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEA-EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 914 SksEFEKENQKGKAAVLDLEKACKELKHQLQVQAEsALKEQEDLKKSLEKEKETSQQLKIELN-SVKGEVSQAQNTLKQK 992
Cdd:COG4717 128 L--PLYQELEALEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 993 EKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNY--------- 1063
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIagvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1064 -------------EKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLE 1130
Cdd:COG4717 285 llallflllarekASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1131 QDSAKKE--ALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEikcRQEKEITKLNEELKSHKQESIK-EITNLKDAK 1207
Cdd:COG4717 365 LEELEQEiaALLAEAGVEDEEELRAALEQAEEYQELKEELEELEE---QLEELLGELEELLEALDEEELEeELEELEEEL 441
|
410 420 430
....*....|....*....|....*....|..
gi 568967300 1208 QLLIQQKLELQGRVDSLKAALEQEKESQQLMR 1239
Cdd:COG4717 442 EELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
945-1151 |
3.58e-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: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 945 VQAESALKEQEDLKKSLEKEKETSQQlkiELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEV 1024
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQA---ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1025 KNAVS-------------------------QKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYG 1079
Cdd:COG3883 89 GERARalyrsggsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967300 1080 KESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQ 1151
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1121-1398 |
4.32e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1121 ELQAAKASLE---QDSAKKEALLKEQSKALEDAQREKSVKEK--ELVAEKSKlaemeeikcRQEKEITKLNEELKSHKQE 1195
Cdd:TIGR02169 171 KKEKALEELEeveENIERLDLIIDEKRQQLERLRREREKAERyqALLKEKRE---------YEGYELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1196 SIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHE 1275
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1276 ENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKA 1355
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568967300 1356 LELQRKLDNttaaVQELGRENQSLQIKHTQALNRKWAEDNEVQ 1398
Cdd:TIGR02169 402 NELKRELDR----LQEELQRLSEELADLNAAIAGIEAKINELE 440
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
719-1025 |
5.08e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.89 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 719 QDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDhkeKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQ 798
Cdd:PLN02939 45 QQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLR---TVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 799 RQLSTDLEL-------RNAELS---------RELQEQEEVVScTKLDLQNKSEILE------NIKQTLTKKEEENV-VLK 855
Cdd:PLN02939 122 GEQLSDFQLedlvgmiQNAEKNilllnqarlQALEDLEKILT-EKEALQGKINILEmrlsetDARIKLAAQEKIHVeILE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 856 QEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSlKNSKSEFEKENQKGKAAVLDLEka 935
Cdd:PLN02939 201 EQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAET-EERVFKLEKERSLLDASLRELE-- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 936 CKELKHQLQVQAESALKEQedlkkSLEKEKETSQQLkieLNSVKGEVSQAQNTLKQkekdEQQLQGTINQLKQSAEQKK- 1014
Cdd:PLN02939 278 SKFIVAQEDVSKLSPLQYD-----CWWEKVENLQDL---LDRATNQVEKAALVLDQ----NQDLRDKVDKLEASLKEANv 345
|
330
....*....|....*.
gi 568967300 1015 -----KQIEALQGEVK 1025
Cdd:PLN02939 346 skfssYKVELLQQKLK 361
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1002-1231 |
5.43e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1002 TINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQsdlygke 1081
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLE------- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1082 sellatrQDLKSVEEKLTLAQEDLISNRNQI-GNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKE 1160
Cdd:COG4913 309 -------AELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1161 LVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQE 1231
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| FYVE_CARP2 |
cd15770 |
FYVE-like domain found in caspase regulator CARP2 and similar proteins; CARP2, also termed E3 ... |
1398-1436 |
5.50e-04 |
|
FYVE-like domain found in caspase regulator CARP2 and similar proteins; CARP2, also termed E3 ubiquitin-protein ligase rififylin, or caspases-8 and -10-associated RING finger protein 2, or FYVE-RING finger protein Sakura (Fring), or RING finger and FYVE-like domain-containing protein 1, or RING finger protein 189, or RING finger protein 34-like, is a novel caspase regulator containing a FYVE-type zinc finger domain. It regulates the p53 signaling pathway through degrading 14-3-3 sigma and stabilizing MDM2. CARP2 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, CARP2 has an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus it belongs to a family of unique FYVE-type domains called FYVE-like domains. In addition to the N-terminal FYVE-like domain, CARP2 harbors a C-terminal RING domain.
Pssm-ID: 277309 Cd Length: 49 Bit Score: 39.06 E-value: 5.50e-04
10 20 30
....*....|....*....|....*....|....*....
gi 568967300 1398 QNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPS 1436
Cdd:cd15770 2 ISCKACGIRFASCARKHPCMDCKKNYCTACSSQAENGPS 40
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
464-1198 |
5.68e-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: 44.65 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 464 KLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLkekvtnstELQHQLEKSKQQHQEQQALQQSAT 543
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQL--------ESSREIVKSYENELDPLKNRLKEI 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 544 AKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSL-LEKEREDLY----AKIQAGEGETAVLNQLQEKNHALQQQ 618
Cdd:TIGR00606 258 EHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQgTDEQLNDLYhnhqRTVREKERELVDCQRELEKLNKERRL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 619 LTQLTEKLKNQseshkqaEENLHDQVQEQKAHLRAAQDRVLSLETSvSELSSqLNESKEKVSQLDIQIKAKTELLLSAEA 698
Cdd:TIGR00606 338 LNQEKTELLVE-------QGRLQLQADRHQEHIRARDSLIQSLATR-LELDG-FERGPFSERQIKNFHTLVIERQEDEAK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 699 AKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQE---HCIQLESHLKDHKEKHLSLEQKVEDLEGHIK 775
Cdd:TIGR00606 409 TAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEelkFVIKELQQLEGSSDRILELDQELRKAERELS 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 776 KLEADALEVKASKEQALQSLQQQRQLST--DLELRNAELSRELQEQEEVVSCTKldlqNKSEILENIKQTLTKKEEENVV 853
Cdd:TIGR00606 489 KAEKNSLTETLKKEVKSLQNEKADLDRKlrKLDQEMEQLNHHTTTRTQMEMLTK----DKMDKDEQIRKIKSRHSDELTS 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 854 LKQEFEKLSQDSKTQH------KELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKA 927
Cdd:TIGR00606 565 LLGYFPNKKQLEDWLHskskeiNQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERL 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 928 AVlDLEKACKELK-------------HQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEK 994
Cdd:TIGR00606 645 KE-EIEKSSKQRAmlagatavysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEK 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 995 DEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEK---------GKLSALQSNYEK 1065
Cdd:TIGR00606 724 RRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEEsakvcltdvTIMERFQMELKD 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1066 CQADLKQLQSDLYGKESELLAT--RQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLkEQ 1143
Cdd:TIGR00606 804 VERKIAQQAAKLQGSDLDRTVQqvNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNL-QR 882
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 568967300 1144 SKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIK 1198
Cdd:TIGR00606 883 RQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK 937
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
970-1194 |
6.26e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.44 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 970 QLKIELNSVKGEVSQ---AQNTLKQKEKDEQQLQgtinQLKQSAEQKKKQIEALQGEVKNavSQKTVLENK-------LQ 1039
Cdd:NF012221 1539 ESSQQADAVSKHAKQddaAQNALADKERAEADRQ----RLEQEKQQQLAAISGSQSQLES--TDQNALETNgqaqrdaIL 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1040 QQSSQAAQELAAEKGKLSAL--QSNYEKCQAD----------LKQLQSDLygkesellatrQDLKS-VEEKLTLAQEDLI 1106
Cdd:NF012221 1613 EESRAVTKELTTLAQGLDALdsQATYAGESGDqwrnpfagglLDRVQEQL-----------DDAKKiSGKQLADAKQRHV 1681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1107 SNRNQI-------------GNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEK-SKLAEME 1172
Cdd:NF012221 1682 DNQQKVkdavakseagvaqGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQdASAAENK 1761
|
250 260
....*....|....*....|..
gi 568967300 1173 EIKCRQEKEITKLNEELKSHKQ 1194
Cdd:NF012221 1762 ANQAQADAKGAKQDESDKPNRQ 1783
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
757-1399 |
6.66e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.58 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 757 KEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEI 836
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 837 LENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELtavkaQKDALLAELSTTKEKLSKVSDSLKNSKS 916
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL-----KSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 917 EFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDE 996
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 997 QQLQGTINQLKQSAEQKKKQIEALQGEVKnavsQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSD 1076
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKEELEILEEE----EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1077 LYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSV 1156
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1157 KEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQ 1236
Cdd:pfam02463 563 RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1237 LMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQS---SQRRVSELEKQT 1313
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRekeELKKLKLEAEEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1314 DDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQIKHTQALNRKWAE 1393
Cdd:pfam02463 723 LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE 802
|
....*.
gi 568967300 1394 DNEVQN 1399
Cdd:pfam02463 803 LRALEE 808
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
932-1105 |
7.00e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 932 LEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLK----IELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLK 1007
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEALLAALG 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1008 QSAEQKKKQIEALQGEVKNAVSQktvlenkLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQS--DLYgkESELL 1085
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEA-------LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrkSNI--PARLL 443
|
170 180
....*....|....*....|
gi 568967300 1086 ATRQDLksvEEKLTLAQEDL 1105
Cdd:COG4913 444 ALRDAL---AEALGLDEAEL 460
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
408-1033 |
7.17e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 408 ELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSS 487
Cdd:PRK01156 160 EINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 488 EKlmekeQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKI 567
Cdd:PRK01156 240 AL-----NELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQIL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 568 QNLEALLQKGKESV---SLLEKEREDLYAKIQAGEGETAVLNQLQEkNHALQQQLTQLTEKLKNQSESHKQAEENLHDQV 644
Cdd:PRK01156 315 SNIDAEINKYHAIIkklSVLQKDYNDYIKKKSRYDDLNNQILELEG-YEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 645 QEQKAHLRAAQDRVLSLetsVSELSSQLNESKEKVSQLDIQIKAktelLLSAEAAKAAQRADLQNH-----------LDT 713
Cdd:PRK01156 394 SEILKIQEIDPDAIKKE---LNEINVKLQDISSKVSSLNQRIRA----LRENLDELSRNMEMLNGQsvcpvcgttlgEEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 714 AQHALQDKQQELNKVSVQLDQL---TAKFQEKQEHCIQLESHLKDHK-EKHLSLEQKVEDLEGHIKKLEADALEVKaske 789
Cdd:PRK01156 467 SNHIINHYNEKKSRLEEKIREIeieVKDIDEKIVDLKKRKEYLESEEiNKSINEYNKIESARADLEDIKIKINELK---- 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 790 qalqslqqqrqlstdlelrNAELSRElQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVvlkqefEKLSQDSKTQH 869
Cdd:PRK01156 543 -------------------DKHDKYE-EIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETN------RSRSNEIKKQL 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 870 KELGDRMQAAVTELTAVKaqkdallaelSTTKEKLSKVSDSLKNSKSEFeKENQKGKAAVLDLEKACKELKHQLQvQAES 949
Cdd:PRK01156 597 NDLESRLQEIEIGFPDDK----------SYIDKSIREIENEANNLNNKY-NEIQENKILIEKLRGKIDNYKKQIA-EIDS 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 950 ALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQ--GEVKNA 1027
Cdd:PRK01156 665 IIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGdlKRLREA 744
|
....*.
gi 568967300 1028 VSQKTV 1033
Cdd:PRK01156 745 FDKSGV 750
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
617-1266 |
7.49e-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: 44.19 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 617 QQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLD-IQIKAKTELLLS 695
Cdd:TIGR00618 204 QLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEeLRAQEAVLEETQ 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 696 AEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIK 775
Cdd:TIGR00618 284 ERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEV 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 776 KLEADALEVKAsKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDL-QNKSEILENIKQTLTKKEEENVVL 854
Cdd:TIGR00618 364 ATSIREISCQQ-HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSaFRDLQGQLAHAKKQQELQQRYAEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 855 KQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKEN------------ 922
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCihpnparqdidn 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 923 --------QKGKAAVLDLEKACKELKHQLQvqaeSALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLK--QK 992
Cdd:TIGR00618 523 pgpltrrmQRGEQTYAQLETSEEDVYHQLT----SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVrlQD 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 993 EKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQAdLKQ 1072
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEL-LAS 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1073 LQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISnrnqIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQR 1152
Cdd:TIGR00618 678 RQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETH----IEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1153 EK--------SVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSL 1224
Cdd:TIGR00618 754 TVlkarteahFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQF 833
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 568967300 1225 KAALEQEKESQQLMREQVKK--EEEKRKEEFSEKEAKLHSEIKE 1266
Cdd:TIGR00618 834 LSRLEEKSATLGEITHQLLKyeECSKQLAQLTQEQAKIIQLSDK 877
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
957-1379 |
8.15e-04 |
|
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: 43.86 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 957 LKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLEN 1036
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1037 KLQQQSSQAAQELAAEKgKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQN 1116
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLES-QISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNN 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1117 KSIQELqaaKASLEQDSAKKEALLKE-QSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQE 1195
Cdd:TIGR04523 281 KKIKEL---EKQLNQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1196 SIKEITNLKDAKQLLIQQKLELQGRVDSLKaaleqekesqqlmreqvkkeeekrkeefsekeaKLHSEIKEKEAGMKKHE 1275
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKENQSYKQEIK---------------------------------NLESQINDLESKIQNQE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1276 ENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKA 1355
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL 484
|
410 420
....*....|....*....|....
gi 568967300 1356 LELQRKLDNTTAAVQELGRENQSL 1379
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEEKKEL 508
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1125-1282 |
8.78e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1125 AKASLEQDSAKKEALL---KEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEIT 1201
Cdd:PRK12704 45 EEAKKEAEAIKKEALLeakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1202 NL----KDAKQLLIQQKLELQgRVdslkAALEQEKESQQLMReqvkkeeekrkeefsekeaKLHSEIKEKEAGMKKHEEN 1277
Cdd:PRK12704 125 ELekkeEELEELIEEQLQELE-RI----SGLTAEEAKEILLE-------------------KVEEEARHEAAVLIKEIEE 180
|
....*
gi 568967300 1278 EAKLT 1282
Cdd:PRK12704 181 EAKEE 185
|
|
| FYVE_CARP1 |
cd15769 |
FYVE-like domain found in caspase regulator CARP1 and similar proteins; CARP1, also termed E3 ... |
1400-1447 |
9.14e-04 |
|
FYVE-like domain found in caspase regulator CARP1 and similar proteins; CARP1, also termed E3 ubiquitin-protein ligase RNF34, or caspases-8 and -10-associated RING finger protein 1, or FYVE-RING finger protein Momo, or RING finger homologous to inhibitor of apoptosis protein (RFI), or RING finger protein 34, or RING finger protein RIFF, is a nuclear protein that functions as a specific E3 ubiquitin ligase for the transcriptional coactivator PGC-1alpha, a master regulator of energy metabolism and adaptive thermogenesis in the brown fat cell, and negatively regulates brown fat cell metabolism. It is preferentially expressed in esophageal, gastric and colorectal cancers, suggesting a possible association with the development of the digestive tract cancers. It regulates the p53 signaling pathway through degrading 14-3-3 sigma and stabilizing MDM2. CARP1 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, CARP1 has an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus it belongs to a family of unique FYVE-type domains called FYVE-like domains. In addition to the N-terminal FYVE-like domain, CARP1 harbors a C-terminal RING domain.
Pssm-ID: 277308 Cd Length: 47 Bit Score: 38.43 E-value: 9.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 568967300 1400 CMSCGKCFSVTVRRHHCRQCGNIFCAECSTknaltpsSKKPVRVCDAC 1447
Cdd:cd15769 4 CKACGLAFSVFRKKHVCCDCKKDFCSVCSV-------LQENLRRCSTC 44
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
134-621 |
9.55e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 134 VQDLQASLK--EEKwysEELKKELEKyqgLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQMKDLfEQKAAQLA 211
Cdd:PRK11281 62 QQDLEQTLAllDKI---DRQKEETEQ---LKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLRQL-ESRLAQTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 212 TEIADIkskydeEKSLRAAAEQKVTHLTEDLNKQTTViqdlkTELLQRpgiedvavlkkeLVQVQTLMDNMTLERERESE 291
Cdd:PRK11281 135 DQLQNA------QNDLAEYNSQLVSLQTQPERAQAAL-----YANSQR------------LQQIRNLLKGGKVGGKALRP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 292 KLKDeckKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLdythleekhneeS 371
Cdd:PRK11281 192 SQRV---LLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRL------------T 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 372 ASRKTLQASLHQRDLdcQQLQA-RLTASESSLQRaqgELSEK-AEAAQKLReelrevESTRQHLKveVKQ-----LQQQR 444
Cdd:PRK11281 257 LSEKTVQEAQSQDEA--ARIQAnPLVAQELEINL---QLSQRlLKATEKLN------TLTQQNLR--VKNwldrlTQSER 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 445 EEKEQHGLqLQGevSQLHCKLLeterqlgeahgrLKEQRQLSSEKLMEK-EQQVADLQLKLSRLEEQlKEKVTNSTELQH 523
Cdd:PRK11281 324 NIKEQISV-LKG--SLLLSRIL------------YQQQQALPSADLIEGlADRIADLRLEQFEINQQ-RDALFQPDAYID 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 524 QLEKSkqqhqeqqaLQQSATAKLREAQNDLEQVLRQIgdKDQKIQNLEALLQkgkESVSLlekeredlyakiqagegeta 603
Cdd:PRK11281 388 KLEAG---------HKSEVTDEVRDALLQLLDERREL--LDQLNKQLNNQLN---LAINL-------------------- 433
|
490 500
....*....|....*....|
gi 568967300 604 VLN--QLQEKNHALQQQLTQ 621
Cdd:PRK11281 434 QLNqqQLLSVSDSLQSTLTQ 453
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
408-651 |
9.87e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.53 E-value: 9.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 408 ELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQlQGEVSQLhckllETERQLGEAHGRLKEQRQLSS 487
Cdd:COG0497 159 EYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQ-PGEEEEL-----EEERRRLSNAEKLREALQEAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 488 EKLMEKEQQVADLqlkLSRLEEQLKEKVTNSTELQHQLEkskqqhqeqqaLQQSATAKLREAQNDLEQVLRQI------- 560
Cdd:COG0497 233 EALSGGEGGALDL---LGQALRALERLAEYDPSLAELAE-----------RLESALIELEEAASELRRYLDSLefdperl 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 561 GDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLknqSESHKQAEENL 640
Cdd:COG0497 299 EEVEERLALLRRLARKYGVTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKL---SAARKKAAKKL 375
|
250
....*....|.
gi 568967300 641 HDQVQEQKAHL 651
Cdd:COG0497 376 EKAVTAELADL 386
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
602-815 |
1.05e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 602 TAVLNQLQEKNHALQQQLTQLTEKLKNQseshKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQ 681
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 682 LDIQIKAKTELLLSAEAAKAAQR--------------ADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCI 747
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568967300 748 QLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRE 815
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
949-1227 |
1.41e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.53 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 949 SALKEQEDLKKSLEKEKETSQQLKIELNSVK-------GEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEAlq 1021
Cdd:COG5022 814 SYLACIIKLQKTIKREKKLRETEEVEFSLKAevliqkfGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDV-- 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1022 GEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKC--QADLKQLQSDLYGKESELlatrQDLKSVEEKLT 1099
Cdd:COG5022 892 KSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLlnNIDLEEGPSIEYVKLPEL----NKLHEVESKLK 967
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1100 LAQED----LISNRNQIGNQNKSIQELQAAKASLEQDSAKKEAlLKEQSKALEDAQREKSVKE------KELVAEKSKLA 1169
Cdd:COG5022 968 ETSEEyedlLKKSTILVREGNKANSELKNFKKELAELSKQYGA-LQESTKQLKELPVEVAELQsaskiiSSESTELSILK 1046
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568967300 1170 EMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAA 1227
Cdd:COG5022 1047 PLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVT 1104
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1120-1213 |
1.48e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1120 QELQAAKASLEQDSAKKEALLKEQSKALEdaQREKSVKEK--ELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESI 1197
Cdd:PRK12704 64 EEIHKLRNEFEKELRERRNELQKLEKRLL--QKEENLDRKleLLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQL 141
|
90 100
....*....|....*....|.
gi 568967300 1198 KE---ITNL--KDAKQLLIQQ 1213
Cdd:PRK12704 142 QElerISGLtaEEAKEILLEK 162
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
932-1229 |
1.54e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 932 LEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAE 1011
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1012 QKKKQIEALQGEVKNAVSQKTVLE---NKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATR 1088
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1089 QD--LKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKS 1166
Cdd:COG4372 185 LDelLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967300 1167 KLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALE 1229
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
117-423 |
1.60e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 117 EAGLALTRDDITLLRQEVQDLQAslkEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDS-SAELQALEQQLEEAQTENFN 195
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHES---QEQQQRSQLEQAKEGLSALNRLLPRLNLLADETlADRVEEIREQLDEAEEAKRF 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 196 IKQMKDLFEQKAAQLAT------EIADIKSKYDEEKSLRAAAEQKVTHLtedlnkqttviqdlkTELLQRpgiedVAVLK 269
Cdd:PRK04863 913 VQQHGNALAQLEPIVSVlqsdpeQFEQLKQDYQQAQQTQRDAKQQAFAL---------------TEVVQR-----RAHFS 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 270 KElvqvqtlmdnmtlERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNL 349
Cdd:PRK04863 973 YE-------------DAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568967300 350 TEKLQkkDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREEL 423
Cdd:PRK04863 1040 KQELQ--DLGVPADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
333-635 |
1.89e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 333 QKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEK 412
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 413 AEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLME 492
Cdd:COG4372 100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 493 KEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEA 572
Cdd:COG4372 180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967300 573 LLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQ 635
Cdd:COG4372 260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
867-1089 |
1.94e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 867 TQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQ 946
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 947 AES--------ALKEQEDLKKSLEKEKETSQQLKIELNSVKgEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIE 1018
Cdd:COG3883 96 YRSggsvsyldVLLGSESFSDFLDRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1019 ALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQ 1089
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
805-1199 |
1.95e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 805 LELRNAELSRELQEQEEVVSCTKLdLQNKSEILENIKQT-LTKKEEENVVLKQEFEKLsqdsKTQHKELgdrmQAAVTEL 883
Cdd:COG5022 824 KTIKREKKLRETEEVEFSLKAEVL-IQKFGRSLKAKKRFsLLKKETIYLQSAQRVELA----ERQLQEL----KIDVKSI 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 884 TAVK---AQKDALLAEL-STTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKE-QEDLK 958
Cdd:COG5022 895 SSLKlvnLELESEIIELkKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKEtSEEYE 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 959 KSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQlqgtinqlKQSAEQKKKQIEALQGEVKNAVSQKTVLENKL 1038
Cdd:COG5022 975 DLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQES--------TKQLKELPVEVAELQSASKIISSESTELSILK 1046
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1039 QQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQsdlygkESELLATRQDLKSVEEK-LTLAQEDLISNRNQIGN--- 1114
Cdd:COG5022 1047 PLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQ------LYQLESTENLLKTINVKdLEVTNRNLVKPANVLQFiva 1120
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1115 QNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKeITKLNEELKSHKQ 1194
Cdd:COG5022 1121 QMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSA-LYDEKSKLSSSEV 1199
|
....*
gi 568967300 1195 ESIKE 1199
Cdd:COG5022 1200 NDLKN 1204
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
174-365 |
2.00e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 174 DSSAELQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLK 253
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 254 TEL------LQRPGIEDVAVLK------KELVQVQTLMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKG 321
Cdd:COG4942 104 EELaellraLYRLGRQPPLALLlspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568967300 322 PQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEE 365
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1115-1325 |
2.00e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1115 QNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAeksklaemeeikcrQEKEITKLNEELKSHKQ 1194
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA--------------LARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1195 ESIKEITNLKDAKQLLIQQKLEL---------QGRVDSLKAALEQEKESQQLM-----------REQVKKEEEKRKEEFS 1254
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELaellralyrLGRQPPLALLLSPEDFLDAVRrlqylkylapaRREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967300 1255 EKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEA 1325
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
120-529 |
2.25e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 120 LALTRDDITLLRQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQM 199
Cdd:TIGR00618 440 AELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQD 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 200 KDL----------FEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRPGIEDvaVLK 269
Cdd:TIGR00618 520 IDNpgpltrrmqrGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV--RLQ 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 270 KELVQVQTLMDNMTLERERESEKLKDECKKLQ---------SEHAHLEATINQLRSELAKGPQ-EVAVYVQEIQKLKGSI 339
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQPEQDLQDvrlhlqqcsQELALKLTALHALQLTLTQERVrEHALSIRVLPKELLAS 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 340 NELT-QKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQK 418
Cdd:TIGR00618 678 RQLAlQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 419 LREELREVESTRQHLKVEV-KQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQV 497
Cdd:TIGR00618 758 ARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL 837
|
410 420 430
....*....|....*....|....*....|..
gi 568967300 498 ADLQLKLSRLEEQLKEKVTNSTELQHQLEKSK 529
Cdd:TIGR00618 838 EEKSATLGEITHQLLKYEECSKQLAQLTQEQA 869
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
920-1269 |
2.27e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 920 KENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQL 999
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1000 QGTINQLKQSAEQKKKQIEALQGEVKNAvsqktvlenklqqqssqaAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYG 1079
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEEL------------------QEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1080 KESELLATRQDLKSVEEKLTLAQEDLiSNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEK 1159
Cdd:COG4372 148 REEELKELEEQLESLQEELAALEQEL-QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1160 ELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMR 1239
Cdd:COG4372 227 LEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAA 306
|
330 340 350
....*....|....*....|....*....|
gi 568967300 1240 EQVKKEEEKRKEEFSEKEAKLHSEIKEKEA 1269
Cdd:COG4372 307 LSLIGALEDALLAALLELAKKLELALAILL 336
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
937-1154 |
2.34e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 937 KELKHQLQVQ------AESALKEQEDLKKSLEK---EKETSQQLKI-----ELNSVKGEVSQAQNTLKQKEKDEQQLQGT 1002
Cdd:PHA02562 177 RELNQQIQTLdmkidhIQQQIKTYNKNIEEQRKkngENIARKQNKYdelveEAKTIKAEIEELTDELLNLVMDIEDPSAA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1003 INQLKQSAEQKKKQIEALQGEVKnaVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKcqadLKQLQSDLYGKES 1082
Cdd:PHA02562 257 LNKLNTAAAKIKSKIEQFQKVIK--MYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEK----LDTAIDELEEIMD 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967300 1083 ELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREK 1154
Cdd:PHA02562 331 EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
391-526 |
2.38e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 391 LQARLTASESSLQRAQGELsekAEAAQKLREElrevESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETER 470
Cdd:PRK09039 44 LSREISGKDSALDRLNSQI---AELADLLSLE----RQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568967300 471 QLGEAHGRLKEQRQLSSEKLMEKE---QQVADLQLKLSRLEEQLKEKVTNSTELQHQLE 526
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVEllnQQIAALRRQLAALEAALDASEKRDRESQAKIA 175
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
389-605 |
2.50e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 389 QQLQARLTASESSLQ--RAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQL--HCK 464
Cdd:COG3206 185 PELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqSPV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 465 LLETERQLGEAHGRLKEQRQlsseKLMEKEQQVADLQLKLSRLEEQLKEKVTNS-TELQHQLEKSKQQHqeqqalqqsat 543
Cdd:COG3206 265 IQQLRAQLAELEAELAELSA----RYTPNHPDVIALRAQIAALRAQLQQEAQRIlASLEAELEALQARE----------- 329
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967300 544 AKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVL 605
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVI 391
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
283-663 |
2.65e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 283 TLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTH 362
Cdd:COG4717 106 ELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQ 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 363 LEEKHNEE----SASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELsEKAEAAQKLREELR--EVESTRQHLKVE 436
Cdd:COG4717 186 LSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-EAAALEERLKEARLllLIAAALLALLGL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 437 VKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVT 516
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 517 NSTELQHQLEKSKQQHQ--EQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAK 594
Cdd:COG4717 345 RIEELQELLREAEELEEelQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568967300 595 IQAGEGETAvLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEE-----NLHDQVQEQKAHLRAAQDRVLSLET 663
Cdd:COG4717 425 LDEEELEEE-LEELEEELEELEEELEELREELAELEAELEQLEEdgelaELLQELEELKAELRELAEEWAALKL 497
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1119-1335 |
2.93e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1119 IQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQEsiK 1198
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL--L 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1199 EITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMReqvkkeeekrkeEFSEKEAKLHSEIKEKEAGMKKHEENe 1278
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE------------ELEAELAELQEELEELLEQLSLATEE- 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568967300 1279 akltmQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERR 1335
Cdd:COG4717 193 -----ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
129-688 |
3.18e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 129 LLRQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQ-MKDL--FEQ 205
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSaLNELssLED 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 206 KAAQLATEIADIKSKydeeKSLRAAAEQKVTHLTEDLNKQTTviqdlKTELLQRPGIEDVAVLKKELVQVQTLMDNMTLE 285
Cdd:PRK01156 250 MKNRYESEIKTAESD----LSMELEKNNYYKELEERHMKIIN-----DPVYKNRNYINDYFKYKNDIENKKQILSNIDAE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 286 RERESEKLKdECKKLQSEHAHLEAT------INQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNL----TEKLQK 355
Cdd:PRK01156 321 INKYHAIIK-KLSVLQKDYNDYIKKksryddLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMsafiSEILKI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 356 KDLDYTHLEEKHNEesasrktLQASLHQRDLDCQQLQARLTASESSLQraqgELSEKAE----------AAQKLREElrE 425
Cdd:PRK01156 400 QEIDPDAIKKELNE-------INVKLQDISSKVSSLNQRIRALRENLD----ELSRNMEmlngqsvcpvCGTTLGEE--K 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 426 VESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLhcKLLETERQLGEAHGRLKEQRQLSS-----EKLMEKEQQVADL 500
Cdd:PRK01156 467 SNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDL--KKRKEYLESEEINKSINEYNKIESaradlEDIKIKINELKDK 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 501 QLKLSRLEEQLkekvtNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQ-NLEALLQKGKE 579
Cdd:PRK01156 545 HDKYEEIKNRY-----KSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEiGFPDDKSYIDK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 580 SVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEE------NLHDQVQEQKAHLRA 653
Cdd:PRK01156 620 SIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDiednlkKSRKALDDAKANRAR 699
|
570 580 590
....*....|....*....|....*....|....*
gi 568967300 654 AQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKA 688
Cdd:PRK01156 700 LESTIEILRTRINELSDRINDINETLESMKKIKKA 734
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
408-516 |
3.42e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 408 ELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEK-EQHGLQLQGEVSQLHCKLlETERQLGEAHGRLKEQRQLS 486
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAElRDELAELEEELEALKARW-EAEKELIEEIQELKEELEQR 483
|
90 100 110
....*....|....*....|....*....|
gi 568967300 487 SEKLMEKEQQVADLQLKLSRLEEQLKEKVT 516
Cdd:COG0542 484 YGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
993-1203 |
3.67e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 993 EKDEQQLQGTINQLKQSAEQKkkqIEALQGEVKNAVSQKTVLENKLQqqssqaaqELAAEKGKLSALQSNYEKCQA---- 1068
Cdd:COG4913 591 EKDDRRRIRSRYVLGFDNRAK---LAALEAELAELEEELAEAEERLE--------ALEAELDALQERREALQRLAEyswd 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1069 --DLKQLQSDLYGKESE---LLATRQDLKSVEEKLTLAQEDLISNRNQIGnqnksiqELQAAKASLEQDSAKKEALLKEQ 1143
Cdd:COG4913 660 eiDVASAEREIAELEAElerLDASSDDLAALEEQLEELEAELEELEEELD-------ELKGEIGRLEKELEQAEEELDEL 732
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1144 SKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNL 1203
Cdd:COG4913 733 QDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
390-972 |
4.03e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.65 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 390 QLQARLTASESSLQRAQGELSEKAEAaqkLREELREVESTRQHLKVEVKQLQQQREEKEQhGLQLQGEVSQLHCKLLETE 469
Cdd:pfam05557 13 QLQNEKKQMELEHKRARIELEKKASA---LKRQLDRESDRNQELQKRIRLLEKREAEAEE-ALREQAELNRLKKKYLEAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 470 RQLGEAhgrlKEQRQLS-SEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHqeqqalqqsatAKLRE 548
Cdd:pfam05557 89 NKKLNE----KESQLADaREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKA-----------SEAEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 549 AQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKERE------DLYAKIQAGEGETAVLNQLQEKNHALQQQLTQL 622
Cdd:pfam05557 154 LRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSelaripELEKELERLREHNKHLNENIENKLLLKEEVEDL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 623 TEKLKNQSESHKQA---EENLHDQVQEQKAHLRAAQDRVLSLETSVSelssqLNESKEKVSQLDIQIKAKTELLLSAEAA 699
Cdd:pfam05557 234 KRKLEREEKYREEAatlELEKEKLEQELQSWVKLAQDTGLNLRSPED-----LSRRIEQLQQREIVLKEENSSLTSSARQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 700 KAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKF----QEKQEHCIQLESHLKDHKEKHLS--LEQKVEDLEGH 773
Cdd:pfam05557 309 LEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltKERDGYRAILESYDKELTMSNYSpqLLERIEEAEDM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 774 IKKLEADALEVKASKEQALQSLQQQRQLSTDLElRNAELSRELQEQEEVVSCtkldlqnkSEILENIKQtltkkeeENVV 853
Cdd:pfam05557 389 TQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLE-RELQALRQQESLADPSYS--------KEEVDSLRR-------KLET 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 854 LKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAqkdallaeLSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLE 933
Cdd:pfam05557 453 LELERQRLREQKNELEMELERRCLQGDYDPKKTKV--------LHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLE 524
|
570 580 590
....*....|....*....|....*....|....*....
gi 568967300 934 KACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLK 972
Cdd:pfam05557 525 DDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLK 563
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
520-943 |
4.09e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 520 ELQHQLEKSKQQHQEqqalqqSATAKLreAQNDLEQVLRQIGDKDQKIQNLEAllqkgkesvslLEKEREDLYAKIQAGE 599
Cdd:PRK11281 40 DVQAQLDALNKQKLL------EAEDKL--VQQDLEQTLALLDKIDRQKEETEQ-----------LKQQLAQAPAKLRQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 600 GEtavLNQLQEKNHALQQQ------LTQLTEKLknqseshkqaeENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLN 673
Cdd:PRK11281 101 AE---LEALKDDNDEETREtlstlsLRQLESRL-----------AQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 674 ESKEKVSQLDIQIKaktelllSAEAAKAAQRADLQNHLDTAQHALQDK----QQELNKVSVQLDQLTAKFQEKQEHCIQL 749
Cdd:PRK11281 167 ANSQRLQQIRNLLK-------GGKVGGKALRPSQRVLLQAEQALLNAQndlqRKSLEGNTQLQDLLQKQRDYLTARIQRL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 750 ESHLKDHKE----KHLSL-EQKVEdleghikklEADALEVKASkeqalqsLQQQRQLSTDLElRNAELSRELQEQ-EEVV 823
Cdd:PRK11281 240 EHQLQLLQEainsKRLTLsEKTVQ---------EAQSQDEAAR-------IQANPLVAQELE-INLQLSQRLLKAtEKLN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 824 SCTKLDLQNKSeILENIKQTLTKKEEENVVLK----------QEFEKLSQDSKTqhKELGDRMQAAVTELTAVKAQKDAl 893
Cdd:PRK11281 303 TLTQQNLRVKN-WLDRLTQSERNIKEQISVLKgslllsrilyQQQQALPSADLI--EGLADRIADLRLEQFEINQQRDA- 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 568967300 894 LAELSTTKEKLskvsdsLKNSKSEFEKENqkgKAAVLDLEKACKELKHQL 943
Cdd:PRK11281 379 LFQPDAYIDKL------EAGHKSEVTDEV---RDALLQLLDERRELLDQL 419
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
949-1182 |
4.19e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 949 SALKEQEDLKKSLEKE-KETSQQLKIELNSVKGEVSQAQNTLKQKEK----DEQQLQGTINQLKQSAEQKKKQIEALQGE 1023
Cdd:PHA02562 163 SVLSEMDKLNKDKIRElNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKkngeNIARKQNKYDELVEEAKTIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1024 VKNAVSQKTVLENKLQQQSSQAAQeLAAEKGKLSALQSNYEK---CQADLKQLqSDLYGKESELLATRQDLKSVEEKLTL 1100
Cdd:PHA02562 243 LLNLVMDIEDPSAALNKLNTAAAK-IKSKIEQFQKVIKMYEKggvCPTCTQQI-SEGPDRITKIKDKLKELQHSLEKLDT 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1101 AQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEK 1180
Cdd:PHA02562 321 AIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVK 400
|
..
gi 568967300 1181 EI 1182
Cdd:PHA02562 401 EK 402
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
656-839 |
4.48e-03 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 41.38 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 656 DRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRAD---LQNHLdtaQHALQDKQQElnKVSVQl 732
Cdd:pfam09726 395 DALVRLEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQEndlLQTKL---HNAVSAKQKD--KQTVQ- 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 733 dQLTAKFQEKQEHCIQLESHLKDHK----------------------EKHLSLEQKVEDLEGHIKKLEadaLEVKASKEQ 790
Cdd:pfam09726 469 -QLEKRLKAEQEARASAEKQLAEEKkrkkeeeataaravalaaasrgECTESLKQRKRELESEIKKLT---HDIKLKEEQ 544
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568967300 791 ALqslqqqrqlstDLELRNAELS--RELQEQEEVVSCTKLDLQNKSEILEN 839
Cdd:pfam09726 545 IR-----------ELEIKVQELRkyKESEKDTEVLMSALSAMQDKNQHLEN 584
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
143-691 |
4.61e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 143 EEKWYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQAlEQQLEEAQTENFNIKQMKDLFEQKA--AQLATEIADIKSK 220
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKKADAAKKKAeeAKKAAEAAKAEAE 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 221 YDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRpgiedVAVLKKELVQVQTLMDNmtLERERESEKLKDECKKL 300
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-----ADEAKKKAEEDKKKADE--LKKAAAAKKKADEAKKK 1426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 301 QSEHAHLEATinQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQnlTEKLQKKDLDYTHLEE-KHNEESASRKTLQA 379
Cdd:PTZ00121 1427 AEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK--ADEAKKKAEEAKKADEaKKKAEEAKKKADEA 1502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 380 SLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKlREELREVESTRQHLKV----EVKQLQQQREEKEQHGLQLQ 455
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK-AEEKKKADELKKAEELkkaeEKKKAEEAKKAEEDKNMALR 1581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 456 GevsqlhcklleterqlGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQ 535
Cdd:PTZ00121 1582 K----------------AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 536 QALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHAL 615
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568967300 616 QQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTE 691
Cdd:PTZ00121 1726 EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
429-687 |
4.96e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 429 TRQHLKVEVKQLQQQRE-EKEQHGLQLQGEVSQLHCKLLETERQLGEAhgrLKEQRQLSSEKLMEKEQQVADLQLKLSRL 507
Cdd:PRK11281 37 TEADVQAQLDALNKQKLlEAEDKLVQQDLEQTLALLDKIDRQKEETEQ---LKQQLAQAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 508 EEQLKEKVTNsTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKE 587
Cdd:PRK11281 114 TRETLSTLSL-RQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 588 REDLY--------AKIQAGEGETAVLNQLQ-----------EKNHALQQQLTQLTEKL--KNQSESHKQAEenlhdQVQE 646
Cdd:PRK11281 193 QRVLLqaeqallnAQNDLQRKSLEGNTQLQdllqkqrdyltARIQRLEHQLQLLQEAInsKRLTLSEKTVQ-----EAQS 267
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568967300 647 QKAHLRAAQDRVLSLETSVS-ELSSQLNESKEKVSQL---DIQIK 687
Cdd:PRK11281 268 QDEAARIQANPLVAQELEINlQLSQRLLKATEKLNTLtqqNLRVK 312
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
289-591 |
5.49e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 289 ESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHN 368
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 369 EESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVEstRQHLKVEVKQLQQQREEKE 448
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS--EAEAEQALDELLKEANRNA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 449 QHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKS 528
Cdd:COG4372 197 EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEE 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967300 529 KQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDL 591
Cdd:COG4372 277 ELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1204-1394 |
5.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1204 KDAKQLLIQQKLELQGRVDSLKAALEQ-EKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENE---A 1279
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEAlEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSddlA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1280 KLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEI----AVLEATVQNNQDERRALLERCLKGEGEIEKLQTKA 1355
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdelqDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180 190
....*....|....*....|....*....|....*....
gi 568967300 1356 LELQRKLDnttAAVQELGRENQSLqIKHTQALNRKWAED 1394
Cdd:COG4913 769 ENLEERID---ALRARLNRAEEEL-ERAMRAFNREWPAE 803
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1048-1161 |
5.77e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.87 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1048 ELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLisnrNQIgnQNKSIQELQAAKA 1127
Cdd:TIGR04320 248 PIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKEL----ANA--QAQALQTAQNNLA 321
|
90 100 110
....*....|....*....|....*....|....
gi 568967300 1128 SLEQDSAKKEALLKEQSKALEDAQREKSVKEKEL 1161
Cdd:TIGR04320 322 TAQAALANAEARLAKAKEALANLNADLAKKQAAL 355
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1262-1379 |
7.00e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1262 SEIKEKEAGmKKHEENEAKLTMQVTTLNENLGTVKKewqsSQRRVSELEKQTDDLRGEIAVLEATVQNNQDE---RRALL 1338
Cdd:COG2433 383 EELIEKELP-EEEPEAEREKEHEERELTEEEEEIRR----LEEQVERLEAEVEELEAELEEKDERIERLERElseARSEE 457
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 568967300 1339 ERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSL 1379
Cdd:COG2433 458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
622-822 |
7.24e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 622 LTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRV---------LSLETSVSELSSQLNESKEKVSQLDIQIKAKTEL 692
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALeefrqknglVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 693 LLSAEAAKAAQRADLQNHLDTAqhALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKV-EDLE 771
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIlASLE 319
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568967300 772 GHIKKLEADALEVKASKEQALQSLQQQRQLSTDLelrnAELSRELQEQEEV 822
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAEL----RRLEREVEVAREL 366
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
126-511 |
7.76e-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: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 126 DITLLRQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLE-----EAQTENFNIKQMK 200
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQedlesERAARNKAEKQRR 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 201 DLFEQKAAqLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRpgiedvavlkkelvQVQTLmd 280
Cdd:pfam01576 296 DLGEELEA-LKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQK--------------HTQAL-- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 281 nmtlereresEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDY 360
Cdd:pfam01576 359 ----------EELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQR 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 361 THLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQL 440
Cdd:pfam01576 429 AELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEE 508
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568967300 441 QQQREEKEQHGLQLQGEVSQLHCKL---LETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQL 511
Cdd:pfam01576 509 EEAKRNVERQLSTLQAQLSDMKKKLeedAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQEL 582
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
312-695 |
8.33e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.81 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 312 NQLRSEL-----AKGPQEVAVyvqeIQKLKGSINEL--TQKNQNLTEKLQKKDLDY----THLEEKHNEESASRKTLQAS 380
Cdd:PRK10929 26 KQITQELeqakaAKTPAQAEI----VEALQSALNWLeeRKGSLERAKQYQQVIDNFpklsAELRQQLNNERDEPRSVPPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 381 LHQRDLDCQQLQArltaseSSlqraqgELSEKAEAAQKLREELREVESTrqhlkveVKQLQQQREEkeqhglqlqgevsq 460
Cdd:PRK10929 102 MSTDALEQEILQV------SS------QLLEKSRQAQQEQDRAREISDS-------LSQLPQQQTE-------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 461 lhcklleTERQLGEAHGRLK---------EQRQLSSEKL-----------MEKEQQVADLQLKLSRLEEQLKEKVTNSTE 520
Cdd:PRK10929 149 -------ARRQLNEIERRLQtlgtpntplAQAQLTALQAesaalkalvdeLELAQLSANNRQELARLRSELAKKRSQQLD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 521 LQHQLEKSKQQHQEQQALQQS--ATAKLREAQNDLEQVlrqIGDKDQKIQNLEALLQKGKESVSLL-EKEREDLYAKIQA 597
Cdd:PRK10929 222 AYLQALRNQLNSQRQREAERAleSTELLAEQSGDLPKS---IVAQFKINRELSQALNQQAQRMDLIaSQQRQAASQTLQV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 598 GEgetaVLNQLQEKNH----------ALQQQLTQLTEKLKNQseshkQAEENLHdQVQEQKAHLRAAQDRVLSLETSVSE 667
Cdd:PRK10929 299 RQ----ALNTLREQSQwlgvsnalgeALRAQVARLPEMPKPQ-----QLDTEMA-QLRVQRLRYEDLLNKQPQLRQIRQA 368
|
410 420
....*....|....*....|....*...
gi 568967300 668 LSSQLNESKEKVsqLDIQIKAKTELLLS 695
Cdd:PRK10929 369 DGQPLTAEQNRI--LDAQLRTQRELLNS 394
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
104-441 |
8.85e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 104 AVHDAGNDSGhGGEAGLALTRDDITLLRQEVQDLQASLKEEKWYSEELKKELEKYQ----GLQQQEAKSDGLVTDSSAEL 179
Cdd:PRK02224 399 RFGDAPVDLG-NAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecGQPVEGSPHVETIEEDRERV 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 180 QALEQQLEEAQTENFNIKQMKDLFEQkAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTEllqr 259
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE---- 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 260 pgiedvAVLKKELVQvqtlmdnmtlERERESEKLKDECKKLQSEHAHLEATINQLRsELAKGPQEVAVYVQEIQKLKGSI 339
Cdd:PRK02224 553 ------AEEKREAAA----------EAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKR 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 340 NELTQKNQNLTEKLQKKDLDYTHLEEKHNE---ESASRKTLQASLHQRDLDcQQLQArLTASESSLQRAQGELSEKAEAA 416
Cdd:PRK02224 616 EALAELNDERRERLAEKRERKRELEAEFDEariEEAREDKERAEEYLEQVE-EKLDE-LREERDDLQAEIGAVENELEEL 693
|
330 340
....*....|....*....|....*...
gi 568967300 417 QKLREELREVESTRQHLKV---EVKQLQ 441
Cdd:PRK02224 694 EELRERREALENRVEALEAlydEAEELE 721
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
877-1017 |
9.23e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 877 QAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKackelkhQLQvQAESALKEQED 956
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEK-------RLL-QKEENLDRKLE 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967300 957 LkksLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLkqSAEQKKKQI 1017
Cdd:PRK12704 104 L---LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL--TAEEAKEIL 159
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1216-1399 |
9.71e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1216 ELQGRVDSLK----AAL------EQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQV 1285
Cdd:COG1196 197 ELERQLEPLErqaeKAEryrelkEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967300 1286 TTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNT 1365
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190
....*....|....*....|....*....|....
gi 568967300 1366 TAAVQELGRENQSLQIKHTQALNRKWAEDNEVQN 1399
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
|
| |
