|
Name |
Accession |
Description |
Interval |
E-value |
| FYVE_EEA1 |
cd15730 |
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ... |
1347-1409 |
1.87e-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: 1.87e-41
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50053824 1347 RKWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDACFNDL 1409
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: ... |
1348-1410 |
3.64e-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: 3.64e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50053824 1348 KWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTP---SSKKPVRVCDACFNDLQ 1410
Cdd:pfam01363 2 VWVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLpelGSNKPVRVCDACYDTLQ 67
|
|
| FYVE |
smart00064 |
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ... |
1346-1411 |
1.42e-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: 1.42e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50053824 1346 NRKWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSS--KKPVRVCDACFNDLQG 1411
Cdd:smart00064 1 RPHWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENLNG 68
|
|
| FYVE_RUFY1_like |
cd15721 |
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ... |
1349-1406 |
4.80e-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: 98.99 E-value: 4.80e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 50053824 1349 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDACF 1406
Cdd:cd15721 1 WADDKEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
500-1334 |
2.45e-22 |
|
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: 104.75 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 500 ATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLlEKEREDLYAKIQAGEgetavLNQLQEKNHALQQQLTQ 579
Cdd:TIGR02168 177 TERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKEL-KAELRELELALLVLR-----LEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 580 LTEKLKNQSESHKQAE---ENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLsaea 656
Cdd:TIGR02168 251 AEEELEELTAELQELEeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE---- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 657 akaaqraDLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLE 736
Cdd:TIGR02168 327 -------ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 737 ADALEVKASKEQALQSLQQQRQLSTDL-----ELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVV 811
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 812 LKQEFEKLSQ--DSKTQHKELGDRMQAAVTELTAVKAQKDA---LLAELSTTKEKLSK-------------VSDSLKNSK 873
Cdd:TIGR02168 480 AERELAQLQArlDSLERLQENLEGFSEGVKALLKNQSGLSGilgVLSELISVDEGYEAaieaalggrlqavVVENLNAAK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 874 SEFE--KENQKGKAAVLDLEKACKElkhQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNtlkqke 951
Cdd:TIGR02168 560 KAIAflKQNELGRVTFLPLDSIKGT---EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDD------ 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 952 kdeqqLQGTINQLKQSAEQKKkqIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQL 1031
Cdd:TIGR02168 631 -----LDNALELAKKLRPGYR--IVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAEL 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1032 QSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQignqnksIQELQAAKASLEQDSAKKEALLKEQSKALEDAQRE 1111
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-------VEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1112 KSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQesikEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKE 1191
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE----EAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1192 SQQLMreqvkkeeEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQT 1271
Cdd:TIGR02168 853 DIESL--------AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50053824 1272 DDLRGEIAVLEATVQNNQDERRALLERCLKG-EGEIEKLQTKALELQRKLDNTTAAVQELGREN 1334
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), ... |
1349-1406 |
4.26e-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: 4.26e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1349 WAEDNEVQNCMSCGKC-FSVTVRRHHCRQCGNIFCAECSTKNALTPS-SKKPVRVCDACF 1406
Cdd:cd15717 2 WVPDSEAPVCMHCKKTkFTAINRRHHCRKCGAVVCGACSSKKFLLPHqSSKPLRVCDTCY 61
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
243-1070 |
5.23e-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: 100.52 E-value: 5.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 243 ERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLE 322
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 323 EKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQR 402
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 403 EEKEQHGLQLQGEVSQLHCKLLETERQLGEAhgrlkeQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKekvtnstELQHQ 482
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEA------ELKELQAELEELEEELEELQEELERLEEALE-------ELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 483 LEkskqqhqeqqalqqsataKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKERED-------LYAKIQA 555
Cdd:TIGR02168 470 LE------------------EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvLSELISV 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 556 GEG-ETAVLNQLQEknhALQQQLTqlteklknqseshkqaeENLHDQVQEQKAHLRAAQDRVLSLETSV-------SELS 627
Cdd:TIGR02168 532 DEGyEAAIEAALGG---RLQAVVV-----------------ENLNAAKKAIAFLKQNELGRVTFLPLDSikgteiqGNDR 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 628 SQLNESKEKVSQLDIQIKAKTEL--LLSAEAAKAAQRADlqnhLDTAQHALQDKQQELNKVSVQLDQLTAKF-----QEK 700
Cdd:TIGR02168 592 EILKNIEGFLGVAKDLVKFDPKLrkALSYLLGGVLVVDD----LDNALELAKKLRPGYRIVTLDGDLVRPGGvitggSAK 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 701 QEHCIqleshlkdhkekhLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEV 780
Cdd:TIGR02168 668 TNSSI-------------LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 781 VSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSqdsktqhkelgDRMQAAVTELTAVKAQKDALLAELSTTKE 860
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE-----------EELAEAEAEIEELEAQIEQLKEELKALRE 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 861 KLSKVSDSLKNSKSEFeKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEV 940
Cdd:TIGR02168 804 ALDELRAELTLLNEEA-ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 941 SQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSN 1020
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENK 962
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 50053824 1021 YEKCQADLKQLQSDLYGKESEL----LATRQDLKSVEEK---LTLAQEDLISNRNQI 1070
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKELgpvnLAAIEEYEELKERydfLTAQKEDLTEAKETL 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
381-1188 |
4.11e-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: 97.43 E-value: 4.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 381 LREVESTRQHLKVEVKQ---LQQQREEKEQHGLQLQG-EVSQLHCKLLETERQLGEAHGRLKEqrqlSSEKLMEKEQQVA 456
Cdd:TIGR02168 195 LNELERQLKSLERQAEKaerYKELKAELRELELALLVlRLEELREELEELQEELKEAEEELEE----LTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 457 DLQLKLSRLEEQLkekvtnsTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGK 536
Cdd:TIGR02168 271 ELRLEVSELEEEI-------EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 537 ESVSLLEKEREDLYAKIQAGEgetAVLNQLQEKNHALQQQLTQLTEKLKnqseSHKQAEENLHDQVQEQKAHLRAAQDRV 616
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELE---AELEELESRLEELEEQLETLRSKVA----QLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 617 LSLETSVSELSSQLNESKEKVSQLDIQIKAKTElllsaeaakaaqrADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAK 696
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELEEEL-------------EELQEELERLEEALEELREELEEAEQALDAAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 697 FQEKQEHCIQLESHLKDHKEKHLS---LEQKVEDLEGHIKKLeADALEVKASKEQALQSLQQQRQLstDLELRNAELSR- 772
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFSEGvkaLLKNQSGLSGILGVL-SELISVDEGYEAAIEAALGGRLQ--AVVVENLNAAKk 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 773 --ELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVlkQEFEKLSQDSKTQHKELGDRMQ--AAVTELTAVKAQK 848
Cdd:TIGR02168 561 aiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFL--GVAKDLVKFDPKLRKALSYLLGgvLVVDDLDNALELA 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 849 DALLAELS--TTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELK---HQLQVQAESALKEQEDLKKSLEKEK 923
Cdd:TIGR02168 639 KKLRPGYRivTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEekiAELEKALAELRKELEELEEELEQLR 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 924 ETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKtvleNKLQQQSSQA 1003
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI----EELEAQIEQL 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1004 AQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAA 1083
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1084 KASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAE----MEEIKCRQEK---EITKLNEELKSHKQESIK 1156
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEElrekLAQLELRLEGlevRIDNLQERLSEEYSLTLE 954
|
810 820 830
....*....|....*....|....*....|..
gi 50053824 1157 EITNLKDAKQLLIQqklELQGRVDSLKAALEQ 1188
Cdd:TIGR02168 955 EAEALENKIEDDEE---EARRRLKRLENKIKE 983
|
|
| FYVE_like_SF |
cd00065 |
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ... |
1357-1406 |
9.94e-20 |
|
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: 9.94e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 50053824 1357 NCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSK--KPVRVCDACF 1406
Cdd:cd00065 1 RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSFGsgKPVRVCDSCY 52
|
|
| FYVE_LST2 |
cd15731 |
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ... |
1349-1407 |
2.27e-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: 2.27e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50053824 1349 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSK--KPVRVCDACFN 1407
Cdd:cd15731 5 WVPDEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRYGqmKPVRVCNHCFM 65
|
|
| FYVE_WDFY3 |
cd15719 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ... |
1349-1409 |
6.83e-19 |
|
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: 81.66 E-value: 6.83e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50053824 1349 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSK--KPVRVCDACFNDL 1409
Cdd:cd15719 3 WVKDEGGDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFESEIRRLRisRPVRVCQACYNIL 65
|
|
| FYVE_ANFY1 |
cd15728 |
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ... |
1349-1409 |
7.58e-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: 7.58e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50053824 1349 WAEDNevqNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKnaLTPSSK----KPVRVCDACFNDL 1409
Cdd:cd15728 4 WADGD---YCYECGVKFGITTRKHHCRHCGRLLCSKCSTK--EVPIIKfdlnKPVRVCDVCFDVL 63
|
|
| FYVE_endofin |
cd15729 |
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ... |
1349-1409 |
8.05e-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: 8.05e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50053824 1349 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAE-CSTKNALTPSSKKPVRVCDACFNDL 1409
Cdd:cd15729 7 WVPDSEAPNCMQCEVKFTFTKRRHHCRACGKVLCSAcCSLKARLEYLDNKEARVCVPCYQTL 68
|
|
| FYVE_RUFY1 |
cd15758 |
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ... |
1349-1409 |
1.28e-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: 81.26 E-value: 1.28e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50053824 1349 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDACFNDL 1409
Cdd:cd15758 6 WLKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLL 66
|
|
| FYVE_Hrs |
cd15720 |
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ... |
1349-1409 |
2.75e-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: 80.12 E-value: 2.75e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50053824 1349 WAEDNEvqnCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSS--KKPVRVCDACFNDL 1409
Cdd:cd15720 2 WKDGDE---CHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSSTIPKFgiEKEVRVCDPCYEKL 61
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
446-1158 |
4.96e-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: 90.51 E-value: 4.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 446 EKLMEKEQQVADLQLKLSRLEEQLKekvTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKI 525
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 526 QNLEALLQKGKESVSLLEKEREDLYAKIQA-GEGETavlNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEEnlhdQVQE 604
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQ---LRVKEKIGELEAEIASLERSIAEKERELEDAEE----RLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 605 QKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLdiqiKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELN 684
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL----KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 685 KVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLE 764
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 765 LRNAELSRELQEQEEVVSctkldlQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQ---HKELGDRMQAAVTEL 841
Cdd:TIGR02169 483 KELSKLQRELAEAEAQAR------ASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYAtaiEVAAGNRLNNVVVED 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 842 TAVKAQKDALLAE----------LSTTKEKLSKVSDSLKNSKS-------EFEKENQKGKAAVL-------DLEKACKEL 897
Cdd:TIGR02169 557 DAVAKEAIELLKRrkagratflpLNKMRDERRDLSILSEDGVIgfavdlvEFDPKYEPAFKYVFgdtlvveDIEAARRLM 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 898 --------------------------------KHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQN 945
Cdd:TIGR02169 637 gkyrmvtlegelfeksgamtggsraprggilfSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 946 TLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQ-ELAAEKGKLSALQSNYEKC 1024
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKlEEALNDLEARLSHSRIPEI 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1025 QADLKQLQSDLYGKESELLATRQDLKSVEEKLTLA-------QEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEAL 1097
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLekeiqelQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50053824 1098 LKEQSKALEDAQREKSVKEKELVAEKSKLAEMeEIKCRQEKEITKLNEELKSHKQESIKEI 1158
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLRELERKIEEL-EAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| FYVE_scVPS27p_like |
cd15760 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
1348-1406 |
4.97e-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: 4.97e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50053824 1348 KWAEDNEvqnCMSCGKCFSVTVRRHHCRQCGNIFCAECSTK----NALTPSSkKPVRVCDACF 1406
Cdd:cd15760 1 HWKPDSR---CDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRriplPHLGPLG-VPQRVCDRCF 59
|
|
| FYVE_MTMR4 |
cd15733 |
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ... |
1349-1406 |
5.65e-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: 5.65e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1349 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSK--KPVRVCDACF 1406
Cdd:cd15733 1 WVPDHAASHCFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPDEQlyDPVRVCNSCY 60
|
|
| FYVE_PKHF2 |
cd15755 |
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ... |
1349-1409 |
2.88e-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: 2.88e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50053824 1349 WAEDNEVQNCMSCGKC-FSVTVRRHHCRQCGNIFCAECSTKNALTPS-SKKPVRVCDACFNDL 1409
Cdd:cd15755 2 WVPDSEATVCMRCQKAkFTPVNRRHHCRKCGFVVCGPCSEKKFLLPSqSSKPVRVCDFCYDLL 64
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
243-776 |
7.34e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.53 E-value: 7.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 243 ERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLE 322
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 323 EKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQR 402
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 403 EEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRL------KEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNS 476
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLerleeeLEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 477 TELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAG 556
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 557 EGETAVLNQLQEKN---------HALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELS 627
Cdd:COG1196 542 AALAAALQNIVVEDdevaaaaieYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 628 SQLNESKEKVSQLDIQIKAKT-ELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQ 706
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLaGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 707 LESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQE 776
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| FYVE_ZF21 |
cd15727 |
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ... |
1349-1405 |
1.27e-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: 1.27e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 50053824 1349 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTP--SSKKPVRVCDAC 1405
Cdd:cd15727 4 WVPDKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVPLPrmCFVDPVRVCNEC 62
|
|
| FYVE_FYCO1 |
cd15726 |
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ... |
1349-1406 |
3.31e-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: 3.31e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 50053824 1349 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDACF 1406
Cdd:cd15726 1 WQDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKACF 58
|
|
| FYVE_FGD6 |
cd15743 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ... |
1349-1406 |
3.40e-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: 3.40e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 50053824 1349 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNA-LTPSSKKPVRVCDACF 1406
Cdd:cd15743 3 WIPDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNKApLEYLKNKSARVCDECF 61
|
|
| FYVE_FGD1_2_4 |
cd15741 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ... |
1348-1409 |
7.62e-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: 7.62e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50053824 1348 KWAEDNEVQNCMSCGKCF-SVTVRRHHCRQCGNIFCAECSTKNA-LTPSSKKPVRVCDACFNDL 1409
Cdd:cd15741 2 RWVRDNEVTMCMRCKEPFnALTRRRHHCRACGYVVCWKCSDYKAtLEYDGNKLNRVCKHCYVIL 65
|
|
| FYVE_RBNS5 |
cd15716 |
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ... |
1349-1409 |
8.48e-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: 8.48e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50053824 1349 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALtpsskkPVRVCDACFNDL 1409
Cdd:cd15716 4 WVNDSDVPFCPDCGKKFNLARRRHHCRLCGSIMCNKCSQFLPL------HIRCCHHCKDLL 58
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
511-1298 |
1.08e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.81 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 511 LEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGE----TAVLNQLQEKNHALQQQLTQLTEKLKN 586
Cdd:TIGR02169 197 RQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQlaslEEELEKLTEEISELEKRLEEIEQLLEE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 587 QSESHKQAEENLHDQVQEQKAHLRAAQDRvlsLETSVSELSSQLNESKEKVSQLDIQIKAktelLLSAEAAKAAQRADLQ 666
Cdd:TIGR02169 277 LNKKIKDLGEEEQLRVKEKIGELEAEIAS---LERSIAEKERELEDAEERLAKLEAEIDK----LLAEIEELEREIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 667 NHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASK 746
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 747 EQALQSLqqqrqlsTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKL------- 819
Cdd:TIGR02169 430 AGIEAKI-------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAeaqaras 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 820 ---SQDSKTQHKELGDRMQ---AAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKS-EFEKENQKGKAAVLDLEK 892
Cdd:TIGR02169 503 eerVRGGRAVEEVLKASIQgvhGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAiELLKRRKAGRATFLPLNK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 893 ACKELKHQLQVQAESALKEQEDLKKSLEK------------------EKETSQQLKIELNSVKGEVSQAQNTLKQKEKDE 954
Cdd:TIGR02169 583 MRDERRDLSILSEDGVIGFAVDLVEFDPKyepafkyvfgdtlvvediEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAP 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 955 QQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLEN---KLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQL 1031
Cdd:TIGR02169 663 RGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1032 QSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKS-----IQELQAAKASLEQDSAKKEALLKEQSKALE 1106
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLN 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1107 DAQREKSVKEKELVAEKSKLAEMEEikcrQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAAL 1186
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKE----QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1187 EQEKESQQLMREQVKKEEEKRKEEFSEKEAkLHSEIKEKEAGMKKHEENEAKLTmqvttlneNLGTVKKEWQSSQRRVSE 1266
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLEA-LEEELSEIEDPKGEDEEIPEEEL--------SLEDVQAELQRVEEEIRA 969
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 50053824 1267 LE--------------KQTDDLRGEIAVLEAtvqnnqdERRALLER 1298
Cdd:TIGR02169 970 LEpvnmlaiqeyeevlKRLDELKEKRAKLEE-------ERKAILER 1008
|
|
| FYVE_MTMR3 |
cd15732 |
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ... |
1348-1406 |
1.14e-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: 1.14e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50053824 1348 KWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSK--KPVRVCDACF 1406
Cdd:cd15732 1 RWVPDHLAASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLPVPSQQlfEPSRVCKSCF 61
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
88-817 |
1.28e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.81 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 88 LRQEVQDLQASLKEEKWysEELKKELEKYQG----LQQQEAKSDGLVTDSSAELQALEQQLEEAQtenfniKQMKDLFEQ 163
Cdd:TIGR02169 216 LLKEKREYEGYELLKEK--EALERQKEAIERqlasLEEELEKLTEEISELEKRLEEIEQLLEELN------KKIKDLGEE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 164 KAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKtellqrpgiEDVAVLKKELVQVQtlmdnmtle 243
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL---------AEIEELEREIEEER--------- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 244 reRESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDL------- 316
Cdd:TIGR02169 350 --KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEeladlna 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 317 DYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVK 396
Cdd:TIGR02169 428 AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 397 QLQQQREEKEQHGLQLQGEVSQL------HCKLLET-------------------------ERQLGEAHG-RLKEQRQLS 444
Cdd:TIGR02169 508 GGRAVEEVLKASIQGVHGTVAQLgsvgerYATAIEVaagnrlnnvvveddavakeaiellkRRKAGRATFlPLNKMRDER 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 445 SEKLMEKEQQVADLQLKLSRLEEQLKEK---------VTNSTELQHQL--------------EKS------KQQHQEQQA 495
Cdd:TIGR02169 588 RDLSILSEDGVIGFAVDLVEFDPKYEPAfkyvfgdtlVVEDIEAARRLmgkyrmvtlegelfEKSgamtggSRAPRGGIL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 496 LQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEknhALQQ 575
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE---ELEE 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 576 QLTQLTEKLKNQSESHKQAEENLhDQVQEQKAHLRAAQDRVLS--LETSVSELSSQLNESKEKVSQLDIQIKAkTELLLS 653
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLRE-IEQKLN 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 654 AEAAKAAQRADLQNHLDTAQHALQDKQQELNKvsvQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIK 733
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK---EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 734 KLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTkLDLQNKSEILENIKQTLTKKEEENVVLK 813
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE-LSLEDVQAELQRVEEEIRALEPVNMLAI 978
|
....
gi 50053824 814 QEFE 817
Cdd:TIGR02169 979 QEYE 982
|
|
| FYVE_RABE_unchar |
cd15739 |
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ... |
1348-1406 |
1.30e-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: 1.30e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 50053824 1348 KWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDACF 1406
Cdd:cd15739 3 RWQHEDDVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCH 61
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
84-942 |
1.32e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 82.80 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 84 DITLLRQEVQDLQASLKEekwYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQMKDLFEQ 163
Cdd:TIGR02168 226 ELALLVLRLEELREELEE---LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 164 KAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTEllqrpgIEDVAVLKKELVQVQTLMDNMTLE 243
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE------LESLEAELEELEAELEELESRLEE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 244 RERESEKLKDECKKLQSEHAHLEATINQLRSELakgpqevavyvqeiQKLKGSINELTQKNQNLTEKLQKKDLdythlee 323
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARL--------------ERLEDRRERLQQEIEELLKKLEEAEL------- 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 324 khneesasrKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVEStrqhlKVEVKQLQQQRE 403
Cdd:TIGR02168 436 ---------KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-----RLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 404 EKEQHGLQlqgevsqlhcKLLETERQLGEAHGRLKEqrQLSSEKLMEKEQQVAdlqlklsrLEEQLKEKVTNSTElqhql 483
Cdd:TIGR02168 502 EGFSEGVK----------ALLKNQSGLSGILGVLSE--LISVDEGYEAAIEAA--------LGGRLQAVVVENLN----- 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 484 ekskqqhqeqqaLQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAG----EGE 559
Cdd:TIGR02168 557 ------------AAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsylLGG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 560 TAVLNQLQEKNHalqqqltQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQdrVLSLETSVSELSSQLNESKEKVSQ 639
Cdd:TIGR02168 625 VLVVDDLDNALE-------LAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAE 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 640 LDIQIKAKTELLlsaeaakaaqrADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHL 719
Cdd:TIGR02168 696 LEKALAELRKEL-----------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 720 SLEQKVEDLEGHIKKLEADALEVKASKEqalqslqqqrqlstDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIK 799
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIE--------------QLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 800 QTLTKKEEENVVLKQEFEKLSQD------SKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSK 873
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDieslaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50053824 874 SEFEKE----NQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQ 942
Cdd:TIGR02168 911 SELRREleelREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| FYVE_ZFY26 |
cd15724 |
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ... |
1349-1407 |
2.48e-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: 2.48e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50053824 1349 WAEDNEVQNCMSC-GKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKK-PVRVCDACFN 1407
Cdd:cd15724 1 WVPDEAVSVCMVCqVERFSMFNRRHHCRRCGRVVCSSCSTKKMLVEGYREnPVRVCDQCYE 61
|
|
| FYVE_ZFYV1 |
cd15734 |
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ... |
1349-1406 |
2.55e-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: 2.55e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1349 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSS--KKPVRVCDACF 1406
Cdd:cd15734 2 WVPDSEIKECSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRgwDHPVRVCDPCA 61
|
|
| FYVE_PKHF1 |
cd15754 |
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ... |
1349-1409 |
3.41e-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: 3.41e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50053824 1349 WAEDNEVQNCMSCGKC-FSVTVRRHHCRQCGNIFCAECSTKNALTPS-SKKPVRVCDACFNDL 1409
Cdd:cd15754 2 WIPDKATDICMRCTQTnFSLLTRRHHCRKCGFVVCHECSRQRFLIPRlSPKPVRVCSLCYRKL 64
|
|
| FYVE_spVPS27p_like |
cd15735 |
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ... |
1352-1406 |
5.27e-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: 5.27e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 50053824 1352 DNEVqnCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTP--SSKKPVRVCDACF 1406
Cdd:cd15735 5 DSDV--CMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPhfGINQPVRVCDGCY 59
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
764-1301 |
8.39e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.19 E-value: 8.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 764 ELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTA 843
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 844 VKAQKDAllAELSTTKEKlsKVSDSLKNSKSEFEKENQKGKAAVLDLEKAcKELKHQLQVQ--AESALKEQEDLKKSLEK 921
Cdd:PTZ00121 1362 AEEKAEA--AEKKKEEAK--KKADAAKKKAEEKKKADEAKKKAEEDKKKA-DELKKAAAAKkkADEAKKKAEEKKKADEA 1436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 922 EKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQgtinQLKQSAEQKKKQiEALQGEVKNAVSQKTVLENKLQQQSS 1001
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD----EAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1002 QAAQELAAEKGKLSALQSNYEKCQADlkQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQElQ 1081
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKKAEEAKKAD--EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK-K 1588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1082 AAKASLEQDSAKKEALLKEQSKALEDAQREKsVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKeitnl 1161
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAK-IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK----- 1662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1162 kdAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTM 1241
Cdd:PTZ00121 1663 --AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50053824 1242 QVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEI-AVLEATVQNNQDERRALLERCLK 1301
Cdd:PTZ00121 1741 EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
609-1297 |
1.59e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.21 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 609 LRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSV 688
Cdd:COG1196 181 LEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 689 QLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNA 768
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 769 ELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQK 848
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 849 DALLAELSTTKEKLSKvsdslknsKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQ 928
Cdd:COG1196 421 EELEELEEALAELEEE--------EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 929 LKIELNSVKGEVSQAQNTLKQKEKDEQQLqgtINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENkLQQQSSQAAQELA 1008
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAALLLAGLRG---LAGAVAVLIGVEAAYEAALEAALAAALQNIVVED-DEVAAAAIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1009 AEKGKLSALQSNYEKcQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRnqignqnksiqELQAAKASLE 1088
Cdd:COG1196 569 AKAGRATFLPLDKIR-ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT-----------LVAARLEAAL 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1089 QDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLL 1168
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1169 IQQKLELQgRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMkkheeneakltmqvttlnE 1248
Cdd:COG1196 717 LEEELEEE-ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI------------------E 777
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 50053824 1249 NLGTV----KKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQN-NQDERRALLE 1297
Cdd:COG1196 778 ALGPVnllaIEEYEELEERYDFLSEQREDLEEARETLEEAIEEiDRETRERFLE 831
|
|
| FYVE_RUFY2 |
cd15759 |
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ... |
1349-1405 |
1.97e-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: 1.97e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 50053824 1349 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDAC 1405
Cdd:cd15759 4 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSC 60
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
238-549 |
3.12e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.17 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 238 DNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQE--------------IQKLKGSINELTQK 303
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEleelsrqisalrkdLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 304 NQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELRE 383
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 384 VESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHckllETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLS 463
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE----ELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 464 RLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLrqigdkDQKIQNLEALLQKGKESVSLLE 543
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA------EALENKIEDDEEEARRRLKRLE 978
|
....*.
gi 50053824 544 KEREDL 549
Cdd:TIGR02168 979 NKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
89-677 |
3.26e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.05 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 89 RQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTEnFNIKQmkdlfeQKAAQL 168
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQ------AEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 169 ATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRpgIEDVAVLKKELVQVQtlmdnmtLERERES 248
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL--EEELEEAEEELEEAE-------AELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 249 EKLKDECKKLQSEHAHLEATINQLRSELakgpqevavyvQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEE 328
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEAL-----------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 329 SASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREE-KEQ 407
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 408 HGLQLQGEVSQLHCKLL----ETERQLGEAHGRLKEQRQLSSEKLmEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQL 483
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIgveaAYEAALEAALAAALQNIVVEDDEV-AAAAIEYLKAAKAGRATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 484 EKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDkdqkiqnlEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVL 563
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA--------ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 564 NQLQEKNHALQQQLtQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQ 643
Cdd:COG1196 665 GSRRELLAALLEAE-AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
570 580 590
....*....|....*....|....*....|....
gi 50053824 644 IKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQ 677
Cdd:COG1196 744 EEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-736 |
3.89e-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: 77.79 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 88 LRQEVQDLQASLKEEKWYSEELKKELEKYQG----LQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQMKDLFEQ 163
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKelyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 164 KAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRpgIEDVAVLKKELVQVQTLMDNMTLE 243
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL--ELQIASLNNEIERLEARLERLEDR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 244 RERESEKLKDECKKLQS-EHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLE 322
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 323 ---EKHNEESASRKTLQASLHQRDLDCQQLQARL-------TASESSLQ-RAQGELSEKAEAAQKLREELREVESTRQHL 391
Cdd:TIGR02168 496 rlqENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdegyeAAIEAALGgRLQAVVVENLNAAKKAIAFLKQNELGRVTF 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 392 KVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQL-------------------------------------GE-- 432
Cdd:TIGR02168 576 LPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsyllggvlvvddldnalelakklrpgyrivtldGDlv 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 433 -AHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDL 511
Cdd:TIGR02168 656 rPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 512 EQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGEtavLNQLQEKNHALQQQLTQLTEKLKNQSESH 591
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE---IEELEAQIEQLKEELKALREALDELRAEL 812
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 592 KQAEENLHDQVQ----------EQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQ 661
Cdd:TIGR02168 813 TLLNEEAANLRErleslerriaATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 662 RADLQN----------HLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQE----------------------------- 702
Cdd:TIGR02168 893 RSELEElseelrelesKRSELRRELEELREKLAQLELRLEGLEVRIDNLQErlseeysltleeaealenkieddeeearr 972
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 50053824 703 HCIQLESHLK--------------DHKEKHLSLEQKVEDLEGHIKKLE 736
Cdd:TIGR02168 973 RLKRLENKIKelgpvnlaaieeyeELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
320-1056 |
6.73e-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: 77.08 E-value: 6.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 320 HLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELS-EKAEAAQKLREELREVESTRQHLKVEVKQL 398
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQmERDAMADIRRRESQSQEDLRNQLQNTVHEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 399 QQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQ----QVADLQLKLSRLEEQLKEKVT 474
Cdd:pfam15921 155 EAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSmstmHFRSLGSAISKILRELDTEIS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 475 ----NSTELQHQLEKSKQqhqeqqalqqsataklrEAQNDLEQVLRQIGDK-DQKIQNLEALLQKGKESVSLLEKEREDL 549
Cdd:pfam15921 235 ylkgRIFPVEDQLEALKS-----------------ESQNKIELLLQQHQDRiEQLISEHEVEITGLTEKASSARSQANSI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 550 YAKIQAgegetaVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQ 629
Cdd:pfam15921 298 QSQLEI------IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 630 LNESKEKVSQLDIQI-KAKTELLLSAEAAKAAQRADLQNHL--DTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQ 706
Cdd:pfam15921 372 SGNLDDQLQKLLADLhKREKELSLEKEQNKRLWDRDTGNSItiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMA 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 707 LESHLKDHKEKHLSLEQKVEDLEGHIKK----LEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSR-------ELQ 775
Cdd:pfam15921 452 AIQGKNESLEKVSSLTAQLESTKEMLRKvveeLTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsrvdlKLQ 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 776 EQEEVVScTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQ--------------DSKTQHKELGDRmQAAVTEL 841
Cdd:pfam15921 532 ELQHLKN-EGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagamqvEKAQLEKEINDR-RLELQEF 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 842 TAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEK 921
Cdd:pfam15921 610 KILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEE 689
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 922 EKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVK-------NAVSQKTVL-- 992
Cdd:pfam15921 690 METTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQfleeamtNANKEKHFLke 769
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 993 -ENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQ-----SDLYGKESELLATRQDLKSVEEKL 1056
Cdd:pfam15921 770 eKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEvaldkASLQFAECQDIIQRQEQESVRLKL 839
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
948-1297 |
1.52e-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: 75.86 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 948 KQKEKDEQQL---QGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKC 1024
Cdd:TIGR02168 172 ERRKETERKLertRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1025 QADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEA-LLKEQSK 1103
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAqLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1104 ALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEitklnEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLK 1183
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAEL-----EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1184 AALEQEKESQQlmreqvkkeeEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRR 1263
Cdd:TIGR02168 407 ARLERLEDRRE----------RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330 340 350
....*....|....*....|....*....|....
gi 50053824 1264 VSELEKQTDDLRGEIAVLEATVQNNQDERRALLE 1297
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
682-1338 |
2.76e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.10 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 682 ELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKL-EADALEVKASKEQALQSLQQQRQLS 760
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 761 TDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLS---QDSKTQHKELGDRMQAA 837
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRaelEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 838 VTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQvQAESALKEQEDLKK 917
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW-KLEQLAADLSKYEQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 918 SLEKEKETSQQLKIELNSVKGEVSQAQNTLKQ--------------KEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVK 983
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARAseervrggraveevLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 984 NAVsqktVLENKLqqqSSQAAQELAAEK--GKLSALQSNyekcqaDLKQLQSDL-YGKESELLATRQDLKSVEEKL---- 1056
Cdd:TIGR02169 550 NNV----VVEDDA---VAKEAIELLKRRkaGRATFLPLN------KMRDERRDLsILSEDGVIGFAVDLVEFDPKYepaf 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1057 ------TLAQEDLISNRNQIGnqnksiqelQAAKASLEQDsakkealLKEQSKALEDAQREKSVKEKELVAEKSKLAEME 1130
Cdd:TIGR02169 617 kyvfgdTLVVEDIEAARRLMG---------KYRMVTLEGE-------LFEKSGAMTGGSRAPRGGILFSRSEPAELQRLR 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1131 EIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIqqklELQGRVDSLKAALEQEKESQQLMReQVKKEEEKRKEE 1210
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG----EIEKEIEQLEQEEEKLKERLEELE-EDLSSLEQEIEN 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1211 FSEKEAKLHSEIKEKEAGMKKHEENEAKLTM-----QVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATV 1285
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEArlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 50053824 1286 QNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQ 1338
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
|
|
| FYVE2_Vac1p_like |
cd15737 |
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ... |
1348-1405 |
5.35e-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: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1348 KWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCA----ECSTK---NALTPSS-----------------KKPVRVCD 1403
Cdd:cd15737 1 PWEDDSSVTHCPICLRSFGLLLRKHHCRLCGKVVCDdrrtKCSTEvplDLLSSALpdlpfvfkepqsdipddTKSVRVCR 80
|
..
gi 50053824 1404 AC 1405
Cdd:cd15737 81 DC 82
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
833-1153 |
6.95e-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: 73.95 E-value: 6.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 833 RMQAAVTELTAVKAQK---DALLAELSTTKEKLSK-VSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKhQLQVQAESA 908
Cdd:TIGR02169 171 KKEKALEELEEVEENIerlDLIIDEKRQQLERLRReREKAERYQALLKEKREYEGYELLKEKEALERQKE-AIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 909 LKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQ-AQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVS 987
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 988 QKtvleNKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNR 1067
Cdd:TIGR02169 330 EI----DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1068 NQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEEL 1147
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
....*.
gi 50053824 1148 KSHKQE 1153
Cdd:TIGR02169 486 SKLQRE 491
|
|
| FYVE_scVPS27p_Vac1p_like |
cd15736 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
1358-1406 |
7.09e-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: 7.09e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 50053824 1358 CMSCGKCFSVTVRRHHCRQCGNIFCAECSTKN------ALTPSSKKPVRVCDACF 1406
Cdd:cd15736 2 CHTCSRTFNLNIRAHHCRKCGKLFCRRHLPNMiplnlsAYDPRNGKWYRCCHSCF 56
|
|
| FYVE_FGD5 |
cd15742 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ... |
1355-1410 |
8.63e-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: 8.63e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 50053824 1355 VQNCMSCGKCFSVTVRRHHCRQCGNIFCAECS-TKNALTPSSKKPVRVCDACFNDLQ 1410
Cdd:cd15742 9 VMMCMNCGSDFTLTLRRHHCHACGKIVCRNCSrNKYPLKYLKDRPAKVCDGCFAELR 65
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
664-1338 |
1.82e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 664 DLQNHLDTAQHAL-----QDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEAD 738
Cdd:TIGR02168 217 ELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 739 ALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSctklDLQNKSEILENIKQTLTKKEEEnvvlkqeFEK 818
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA----ELEEKLEELKEELESLEAELEE-------LEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 819 LSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELK 898
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 899 HQLQVQAESALKEQEDLKKSLEKEKETSQQlkiELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQsAEQKKKQIEAL 978
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQ---ALDAAERELAQLQARLDSLERLQENLEGFSEGVKA-LLKNQSGLSGI 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 979 QGEVKNAVS-----------------QKTVLENKLQQQSSQAAQElAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESE 1041
Cdd:TIGR02168 522 LGVLSELISvdegyeaaieaalggrlQAVVVENLNAAKKAIAFLK-QNELGRVTFLPLDSIKGTEIQGNDREILKNIEGF 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1042 LLATrQDLKSVEEKLTLAQEDL-----ISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLkeqskALEDAQREKSVKE 1116
Cdd:TIGR02168 601 LGVA-KDLVKFDPKLRKALSYLlggvlVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVI-----TGGSAKTNSSILE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1117 KelvaeKSKLAEMEEIKCRQEKEITKLNEELKSHKqesiKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLm 1196
Cdd:TIGR02168 675 R-----RREIEELEEKIEELEEKIAELEKALAELR----KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ- 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1197 REQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNEnlgtvkkEWQSSQRRVSELEKQTDDLRG 1276
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE-------ELKALREALDELRAELTLLNE 817
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50053824 1277 EIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQ 1338
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
|
| FYVE_PIKfyve_Fab1 |
cd15725 |
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ... |
1349-1406 |
2.05e-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: 2.05e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1349 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKP--VRVCDACF 1406
Cdd:cd15725 2 WMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPgdLRVCTYCC 61
|
|
| FYVE_MTMR_unchar |
cd15738 |
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ... |
1348-1406 |
2.83e-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: 2.83e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50053824 1348 KWAEDNEVQNCmSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPS--SKKPVRVCDACF 1406
Cdd:cd15738 2 DWKSFRNVTEC-SCSTPFDHFSKKHHCWRCGNVFCTRCIDKQRALPGhlSQRPVPVCRACY 61
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
221-924 |
2.86e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.64 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 221 EDVAVLKKELVQVQTLMDNM-----TLERERESeklKDECKKLQSEHAHLEATINQLRSELAkgpqevavyVQEIQKLKG 295
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKrqqleRLRREREK---AERYQALLKEKREYEGYELLKEKEAL---------ERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 296 SINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQaslhqrDLDCQQLQARLTASESSLQRAQGELSEKAEAAQ 375
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 376 KLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQ-- 453
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlk 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 454 -QVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALL 532
Cdd:TIGR02169 399 rEINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 533 QKGKESVSLLEKEREDLYAKIQAGEGE-------TAVLNQLQEKNHALQQQLTQLTEK------------LKN------- 586
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARASEERvrggravEEVLKASIQGVHGTVAQLGSVGERyataievaagnrLNNvvvedda 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 587 ----------------------------QSESHKQAEENLHDQV--------QEQKAHLRAAQDRVL--SLET------- 621
Cdd:TIGR02169 559 vakeaiellkrrkagratflplnkmrdeRRDLSILSEDGVIGFAvdlvefdpKYEPAFKYVFGDTLVveDIEAarrlmgk 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 622 --------------------SVSELSSQLNESKEKVSQLdiQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQ 681
Cdd:TIGR02169 639 yrmvtlegelfeksgamtggSRAPRGGILFSRSEPAELQ--RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 682 ELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSlqqqrqlst 761
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--------- 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 762 DLELRNAELSRELQEQEEVVSctkldlqNKSEILENIKQTLTKKEEENVVLKQEFEKLSQ---DSKTQHKELGDR---MQ 835
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEVS-------RIEARLREIEQKLNRLTLEKEYLEKEIQELQEqriDLKEQIKSIEKEienLN 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 836 AAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESaLKEQEDL 915
Cdd:TIGR02169 861 GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE-LSEIEDP 939
|
....*....
gi 50053824 916 KKSLEKEKE 924
Cdd:TIGR02169 940 KGEDEEIPE 948
|
|
| FYVE_WDFY1_like |
cd15718 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ... |
1349-1406 |
6.39e-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: 6.39e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50053824 1349 WAEDNevqNCMSCGKCF-----------SVTVRRHHCRQCGNIFCAECSTKNALTPSS--KKPVRVCDACF 1406
Cdd:cd15718 3 WAESD---NCQKCSRPFfwnfkqmwekkTLGVRQHHCRKCGKAVCDKCSSNRSTIPVMgfEFPVRVCNECY 70
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
295-1111 |
7.01e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.56 E-value: 7.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 295 GSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARltASESSLQRAQ----GELSEK 370
Cdd:PTZ00121 1058 GKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEAR--KAEEAKKKAEdarkAEEARK 1135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 371 AEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLME 450
Cdd:PTZ00121 1136 AEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAE 1215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 451 KEQQVADlqlklsrleEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEA 530
Cdd:PTZ00121 1216 EARKAED---------AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 531 LLQKGKESVSLLEKEREDLYAKIQAGEGETAvlNQLQEKNHALQQQltqlTEKLKNQSESHKQAEENLHDQVQEQKAHLR 610
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKA--DEAKKKAEEAKKK----ADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 611 AAQDRVLSLETSVSELSSQLNESKEKVSQLDI--QIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSV 688
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 689 QLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLE--------QKVEDLEGHIK--KLEADALEVKASKEQALQSLQQQRQ 758
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEakkkaeeaKKADEAKKKAEeaKKKADEAKKAAEAKKKADEAKKAEE 1520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 759 LSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEIL----ENIKQTLTKKEEENvvlKQEFEKLSQDSKTQHKELGDRM 834
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELkkaeEKKKAEEAKKAEED---KNMALRKAEEAKKAEEARIEEV 1597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 835 QAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAA--VLDLEKACKELKHQLQVQAESALKEQ 912
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeeLKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 913 EDLKKSLEKEKETSQQLKIE------LNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEV--KN 984
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEaeeakkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeeKK 1757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 985 AVSQKTVLENKLQQQSSQAAQELAAE--KGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTlaqED 1062
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAVIEEelDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAI---KE 1834
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 50053824 1063 LISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQRE 1111
Cdd:PTZ00121 1835 VADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEE 1883
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
769-1355 |
7.22e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 7.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 769 ELSRELQEQEEVVSCTKLD-LQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQ 847
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 848 KDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAvldlekacKELKHQLQVQAESALKEQEDLKKSLEKEKETSQ 927
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL--------AEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 928 QLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLE-NKLQQQSSQAAQE 1006
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1007 LAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKAS 1086
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1087 LEQDS---AKKEALLKEQSKALEDAQREKSVKEKELVAEKSK----LAEMEEIKCRQEKEITKLNEELKSHKQESIKEIT 1159
Cdd:TIGR02168 529 ISVDEgyeAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELgrvtFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1160 NLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMREQVKK--------EEEKRKEEFSEKEAKLHSEIKEKEAGMKK 1231
Cdd:TIGR02168 609 KFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1232 HEENEAKLTMQVTT-------LNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLK--- 1301
Cdd:TIGR02168 689 LEEKIAELEKALAElrkeleeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEElee 768
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50053824 1302 -----------GEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQIKHTQALNRKWAEDNEV 1355
Cdd:TIGR02168 769 rleeaeeelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
136-1119 |
1.09e-11 |
|
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: 69.82 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 136 ELQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELL 215
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 216 QRPG-IEDVAVLKKELVQVQTLMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLK 294
Cdd:pfam01576 86 EEEErSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 295 GSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAA 374
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 375 Q----KLREE----------LREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLET-ERQLGEAHGRLKE 439
Cdd:pfam01576 246 QaalaRLEEEtaqknnalkkIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTlDTTAAQQELRSKR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 440 QRQLSS-EKLMEKEQQVADLQlklsrLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQI 518
Cdd:pfam01576 326 EQEVTElKKALEEETRSHEAQ-----LQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 519 GDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGE----TAVLNQLQEKNHALQQQLTQLTEKLKNQSEshkqa 594
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSElesvSSLLNEAEGKNIKLSKDVSSLESQLQDTQE----- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 595 eenlhdQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADlqnhLDTAQH 674
Cdd:pfam01576 476 ------LLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT----LEALEE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 675 ALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQ 754
Cdd:pfam01576 546 GKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERD 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 755 QQRQLSTDLELRNAELSREL---QEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELG 831
Cdd:pfam01576 626 RAEAEAREKETRALSLARALeeaLEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELE 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 832 DRMQAAV-------TELTAVKAQKDA-LLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKhQLQV 903
Cdd:pfam01576 706 DELQATEdaklrleVNMQALKAQFERdLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLK-ELEA 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 904 QAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQ---SAEQKKKQIEA--- 977
Cdd:pfam01576 785 QIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEdlaASERARRQAQQerd 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 978 -LQGEVKNAVSQKTVLEN---KLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESellaTRQDLKSVE 1053
Cdd:pfam01576 865 eLADEIASGASGKSALQDekrRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERS----TSQKSESAR 940
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50053824 1054 EKLTLAQEDLISNRNQIGNQNKSiqELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKEL 1119
Cdd:pfam01576 941 QQLERQNKELKAKLQEMEGTVKS--KFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKL 1004
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
700-1357 |
1.68e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 700 KQEHCIQLESHLKDHKEKHLSLEQKVEDL-EGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLelRNAELSRELQEQE 778
Cdd:PTZ00121 1135 KAEDARKAEEARKAEDAKRVEIARKAEDArKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDA--RKAEAARKAEEER 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 779 EVVSCTKLDLQNKSEILENIKQTLTKKEEENvvlKQEFEKLSQDSKtqhKELGDRMQAAVTELTAVKAQKDALLAELSTT 858
Cdd:PTZ00121 1213 KAEEARKAEDAKKAEAVKKAEEAKKDAEEAK---KAEEERNNEEIR---KFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 859 KEKlsKVSDSLKNSKSEFEKENQKGKAavlDLEKACKELKHQlqvqAESALKEQEDLKKSLEKEKETSQQLKIELNSVKG 938
Cdd:PTZ00121 1287 EEK--KKADEAKKAEEKKKADEAKKKA---EEAKKADEAKKK----AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 939 EVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQ 1018
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK 1437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1019 SNYE-KCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISN--RNQIGNQNKSIQEL-QAAKASLEQDSAKK 1094
Cdd:PTZ00121 1438 KKAEeAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADeaKKKAEEAKKKADEAkKAAEAKKKADEAKK 1517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1095 --EALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQK 1172
Cdd:PTZ00121 1518 aeEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1173 LELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEaKLHSEIKEKEAGMKKHEENEAKLTMQvttlnenlgt 1252
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK-KEAEEKKKAEELKKAEEENKIKAAEE---------- 1666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1253 vKKEWQSSQRRVSELEKQTDDLRGEiavLEATVQNNQDERRAllERCLKGEGEIEKlqtKALELQRKLDNTTAAVQELGR 1332
Cdd:PTZ00121 1667 -AKKAEEDKKKAEEAKKAEEDEKKA---AEALKKEAEEAKKA--EELKKKEAEEKK---KAEELKKAEEENKIKAEEAKK 1737
|
650 660
....*....|....*....|....*
gi 50053824 1333 ENQSlQIKHTQALNRKWAEDNEVQN 1357
Cdd:PTZ00121 1738 EAEE-DKKKAEEAKKDEEEKKKIAH 1761
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
366-1256 |
1.72e-11 |
|
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: 69.23 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 366 ELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSS 445
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 446 EKLMEKEQQVADLQLKLSRLEEQlkekvtnstelqhQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKI 525
Cdd:pfam02463 257 KQEIEKEEEKLAQVLKENKEEEK-------------EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 526 QNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLtqltEKLKNQSESHKQAEENLHDQVQEQ 605
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL----LAKKKLESERLSSAAKLKEEELEL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 606 KahlraaqdrvlsletsvSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNK 685
Cdd:pfam02463 400 K-----------------SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 686 VSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLEL 765
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 766 RNAELSRELQEQEEVVSCTKLD--LQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTA 843
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEERQklVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 844 VKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEK 923
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIK 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 924 ETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQA 1003
Cdd:pfam02463 703 KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREK 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1004 AQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLaqedlisnrnqigNQNKSIQELQAA 1083
Cdd:pfam02463 783 TEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEE-------------LALELKEEQKLE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1084 KASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITnlkd 1163
Cdd:pfam02463 850 KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE---- 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1164 aKQLLIQQKLELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQV 1243
Cdd:pfam02463 926 -EAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEK 1004
|
890
....*....|...
gi 50053824 1244 TTLNENLGTVKKE 1256
Cdd:pfam02463 1005 KKLIRAIIEETCQ 1017
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
75-580 |
1.86e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 75 EAGLALTRDDITLLRQEVQDLQASLKEEKWYSEELKKELEKYQG----LQQQEAKSDGLVTDSSAELQALEQQLEEAQTE 150
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAeeyeLLAELARLEQDIARLEERRRELEERLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 151 NFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRpgIEDVAVLKKEL 230
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA--LRAAAELAAQL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 231 VQVQTLMDNMTLERER-----------------ESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKL 293
Cdd:COG1196 403 EELEEAEEALLERLERleeeleeleealaeleeEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 294 KGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEA 373
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAA 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 374 AQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSS-------- 445
Cdd:COG1196 563 IEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAalrravtl 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 446 -EKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDL-EQVLRQIGDKDQ 523
Cdd:COG1196 643 aGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELaEAEEERLEEELE 722
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 50053824 524 KIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQL 580
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 ... |
435-1282 |
6.45e-11 |
|
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: 67.30 E-value: 6.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 435 GRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVtnstelqhqlEKSKQQHQEQQALQQSATAKLREAQNDLEQV 514
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLK----------EQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 515 LRqigdkdQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQA 594
Cdd:pfam02463 235 NE------ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 595 EENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQH 674
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 675 ALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQ 754
Cdd:pfam02463 389 AAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 755 QQRQLSTdlELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRM 834
Cdd:pfam02463 469 KSEDLLK--ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 835 QAAVTELTAVKAQKDALLaelstTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQED 914
Cdd:pfam02463 547 TAVIVEVSATADEVEERQ-----KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 915 LKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLEN 994
Cdd:pfam02463 622 AKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 995 KLQQQSSQAAQE---LAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIG 1071
Cdd:pfam02463 702 KKKEQREKEELKklkLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEERE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1072 NQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKsvKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHK 1151
Cdd:pfam02463 782 KTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQL--LIEQEEKIKEEELEELALELKEEQKLEKLAEEELERL 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1152 QESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKEsQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKK 1231
Cdd:pfam02463 860 EEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEK-KELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE 938
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 50053824 1232 HEENEAKLTMQVttLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLE 1282
Cdd:pfam02463 939 ELLLEEADEKEK--EENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKE 987
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
716-1298 |
9.48e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 9.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 716 EKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEevvsctkldlqnkseiL 795
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE----------------L 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 796 ENIKQTLTKKEEENVVLKQEFEKLSQD---SKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNS 872
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDiarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 873 KSEFEKENQKGKAAVLDLEKACKELKhQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEK 952
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELE-ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 953 DEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQ 1032
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1033 SDLYGKESELLAtrqdlksVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREK 1112
Cdd:COG1196 516 LAGLRGLAGAVA-------VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAAL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1113 SVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKES 1192
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1193 QQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTD 1272
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
570 580
....*....|....*....|....*.
gi 50053824 1273 DLRGEIAVLEATVQNNQDERRALLER 1298
Cdd:COG1196 749 EEEALEELPEPPDLEELERELERLER 774
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
309-482 |
1.55e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 309 EKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDcqQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTR 388
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE--LLEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 389 --------QHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQL 460
Cdd:COG4913 333 rgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
170 180
....*....|....*....|..
gi 50053824 461 KLSRLEEQLKEKVTNSTELQHQ 482
Cdd:COG4913 413 ALRDLRRELRELEAEIASLERR 434
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
569-1171 |
2.90e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.04 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 569 KNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLD---IQIK 645
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNsdlSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 646 AKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKV 725
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 726 EDLEGHIKKLEADALEVKASKEQA---LQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTL 802
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQKNkslESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 803 TKKEEEnvvlkqefeklSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLaeLSTTKEKLSKVSDSLKNSKSEFEKENQK 882
Cdd:TIGR04523 270 SEKQKE-----------LEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNQISQNNKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 883 GKAAVLDLEKACKELKH------QLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQ 956
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNsesensEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 957 LQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQelaaEKGKLSALQSNYEKCQADLKQLQSDLY 1036
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES----LETQLKVLSRSINKIKQNLEQKQKELK 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1037 GKESELLA----------TRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQ-ELQAAKASLEQDSAKKEAL-------- 1097
Cdd:TIGR04523 493 SKEKELKKlneekkeleeKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEdELNKDDFELKKENLEKEIDeknkeiee 572
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50053824 1098 LKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQ 1171
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| FYVE_FGD3 |
cd15740 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ... |
1352-1406 |
3.01e-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: 56.93 E-value: 3.01e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 50053824 1352 DNEVQNCMSCGKCF-SVTVRRHHCRQCGNIFCAECStknALTPSSKKPVRVCDACF 1406
Cdd:cd15740 2 EKEKQTCKGCNESFnSITKRRHHCKQCGAVICGKCS---EFKDLASRHNRVCRDCF 54
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
247-737 |
1.68e-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: 62.35 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 247 ESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDL---DYTHLEE 323
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSlesQISELKK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 324 KHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQRE 403
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 404 EKEQHglQLQGEVSQLHCKLLETERQLGEahgrlkeqrqlSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQL 483
Cdd:TIGR04523 306 QDWNK--ELKSELKNQEKKLEEIQNQISQ-----------NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 484 EKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVL 563
Cdd:TIGR04523 373 EKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 564 NQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQ 643
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 644 IKAKTELLLSAEAAKAAQRADLQNhlDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQ 723
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDFELKK--ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEK 610
|
490
....*....|....
gi 50053824 724 KVEDLEGHIKKLEA 737
Cdd:TIGR04523 611 KISSLEKELEKAKK 624
|
|
| FYVE_protrudin |
cd15723 |
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ... |
1357-1405 |
1.79e-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: 1.79e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 50053824 1357 NCMSCGKCFSV-TVRRHHCRQCGNIFCAEC-------STKNALTPSSKK-PVRVCDAC 1405
Cdd:cd15723 1 NCTGCGASFSVlLKKRRSCNNCGNAFCSRCcskkvprSVMGATAPAAQReTVFVCSGC 58
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1029-1332 |
3.63e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1029 KQLQSDLYGKESELLATRqdLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDA 1108
Cdd:COG1196 216 RELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1109 QREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQ 1188
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1189 --EKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSE 1266
Cdd:COG1196 374 laEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50053824 1267 LEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGR 1332
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
239-1148 |
4.11e-09 |
|
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: 61.53 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 239 NMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDY 318
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 319 THLEEKHNEESASRKTLQASLHqrdldcQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQL 398
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKL------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 399 QQQREEKEQHGLQLQGEVSQLHCKLLETERQLgEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTE 478
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKR-EAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 479 LQHQLEKSKQQHqeqqalqqsatAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEG 558
Cdd:pfam02463 399 LKSEEEKEAQLL-----------LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 559 ETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEenlhdqvqeqkahlraaqdrvlsletSVSELSSQLNESKEKVS 638
Cdd:pfam02463 468 KKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESK--------------------------ARSGLKVLLALIKDGVG 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 639 QLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHciQLESHLKDHKEKH 718
Cdd:pfam02463 522 GRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPK--LKLPLKSIAVLEI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 719 LSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILEnI 798
Cdd:pfam02463 600 DPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE-I 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 799 KQTLTKKEEENVVLKQEFEKLSQDSKTQHKElgdrmqaavTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEK 878
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLEIKKKEQREK---------EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEE 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 879 ENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQ 958
Cdd:pfam02463 750 EEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 959 GTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGK 1038
Cdd:pfam02463 830 IKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKL 909
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1039 ESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKE 1118
Cdd:pfam02463 910 NLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEER 989
|
890 900 910
....*....|....*....|....*....|
gi 50053824 1119 LVAEKSKLAEMEEIKCRQEKEITKLNEELK 1148
Cdd:pfam02463 990 YNKDELEKERLEEEKKKLIRAIIEETCQRL 1019
|
|
| FYVE_RUFY4 |
cd15745 |
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ... |
1358-1406 |
4.15e-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: 53.66 E-value: 4.15e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 50053824 1358 CMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNAL--TPSSKKPVRVCDACF 1406
Cdd:cd15745 2 CAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVlsVPDTCIYLRVCKTCY 52
|
|
| FYVE_ZFY19 |
cd15749 |
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ... |
1357-1406 |
5.31e-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: 53.28 E-value: 5.31e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 50053824 1357 NCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPS-SKKPVRVCDACF 1406
Cdd:cd15749 1 RCFGCAAKFSLFKKECGCKNCGRSFCKGCLTFSAVVPRkGNQKQKVCKQCH 51
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
226-649 |
1.00e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 226 LKKELVQVQTLMDNMTLERERESEKlKDECKKLQSEHAH-------LEATINQLRSELAKGPQEVAVYVQEIQKLKGSIN 298
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARET-RDEADEVLEEHEErreeletLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 299 ELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQ-------LQARLTASESSLQRAQGELSEKA 371
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAhneeaesLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 372 EAAQKLREELREVESTRQHLKVEVKQLQQ-------QREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLS 444
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRErfgdapvDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 445 SE-----------------KLMEKEQQVADLQLKLSRLEEQLkEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREA 507
Cdd:PRK02224 450 EAgkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEV-EEVEERLERAEDLVEAEDRIERLEERREDLEELIAER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 508 QNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQ----------LQEKNHALQQQL 577
Cdd:PRK02224 529 RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKErieslerirtLLAAIADAEDEI 608
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50053824 578 TQLTEKLKNQSESHKQAEENLHDQvQEQKAHLRAAQDrvlslETSVSELSSQLNESKEKVSQLDIQIKAKTE 649
Cdd:PRK02224 609 ERLREKREALAELNDERRERLAEK-RERKRELEAEFD-----EARIEEAREDKERAEEYLEQVEEKLDELRE 674
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1075-1345 |
2.04e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1075 KSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEikcrqekEITKLNEELkshkQES 1154
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-------ELEEAQAEE----YEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1155 IKEITNLKDAKQLLIQQKLELQGRvdslKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHS---EIKEKEAGMKK 1231
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEER----LEELEEELAELEEELEELEEELEELEEELEEAEEELEEaeaELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1232 HEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQT 1311
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270
....*....|....*....|....*....|....
gi 50053824 1312 KALELQRKLDNTTAAVQELGRENQSLQIKHTQAL 1345
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
75-385 |
2.39e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 75 EAGLALTRDDITLLRQEVQDLQASLkeekwysEELKKELEKyqgLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNI 154
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKEL-------EELEEELEQ---LRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 155 KQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTEL-LQRPGIEDVAVLKKELVQV 233
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 234 QTLMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQK 313
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50053824 314 KDLDYTHLEEKHNEESASRKTLQASLhqrdldcQQLQARLTASESSLQRAQGELSEKAEA-AQKLREELREVE 385
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRI-------DNLQERLSEEYSLTLEEAEALENKIEDdEEEARRRLKRLE 978
|
|
| FYVE_WDFY1 |
cd15756 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ... |
1348-1410 |
2.84e-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: 2.84e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50053824 1348 KWAEDNevqNCMSCGKCF-----------SVTVRRHHCRQCGNIFCAECSTKNALTP--SSKKPVRVCDACFNDLQ 1410
Cdd:cd15756 2 QWLESD---SCQKCEQPFfwnikqmwdtkTLGLRQHHCRKCGQAVCGKCSSKRSSYPimGFEFQVRVCDSCFETIK 74
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
728-1274 |
3.41e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.11 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 728 LEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEE 807
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 808 ENVVLKQEFEKlsqdsktqHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAV 887
Cdd:TIGR04523 202 LLSNLKKKIQK--------NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 888 LDLEKACKELKhQLQVQAESALKEQEDLKKslEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQS 967
Cdd:TIGR04523 274 KELEQNNKKIK-ELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 968 AEQKKKQIEALQGEVKnavsQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQ 1047
Cdd:TIGR04523 351 LTNSESENSEKQRELE----EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1048 DLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLA 1127
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1128 EMEEIKCRQEKEITKLNE---ELKSHKQESIKEITNLKD---------AKQLLIQQKLELQGRVDSLKAALEQEKESQQL 1195
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEkieKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQEE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1196 MREQVKKEEEKRK------EEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEK 1269
Cdd:TIGR04523 587 KQELIDQKEKEKKdlikeiEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIK 666
|
....*
gi 50053824 1270 QTDDL 1274
Cdd:TIGR04523 667 KIKES 671
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
349-589 |
3.70e-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: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 349 LQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETER 428
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 429 QLGEAHGRLKEQRqlsseklmekeQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQ 508
Cdd:COG4942 91 EIAELRAELEAQK-----------EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 509 NDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAV-LNQLQEKNHALQQQLTQLTEKLKNQ 587
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAeLAELQQEAEELEALIARLEAEAAAA 239
|
..
gi 50053824 588 SE 589
Cdd:COG4942 240 AE 241
|
|
| FYVE_RUFY3 |
cd15744 |
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ... |
1358-1406 |
3.76e-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: 50.88 E-value: 3.76e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 50053824 1358 CMSCGKCFSVTVR-RHHCRQCGNIFCAECSTKNALTPSS-KKPVRVCDACF 1406
Cdd:cd15744 2 CSLCQEDFASLALpKHNCYNCGGTFCDACSSNELPLPSSiYEPARVCDVCY 52
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
676-1224 |
6.48e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 676 LQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQ---- 751
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyikl 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 752 --SLQQQRQLSTDLELRNAELSRELQEQEEVVSctklDLQNKSEILENIKQTLTKKEEENVVLKqEFEKLSQDSKTQHKE 829
Cdd:PRK03918 299 seFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 830 LgDRMQAAVTELTAVKAQKdaLLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKA---CKELKHQLQVQAE 906
Cdd:PRK03918 374 L-ERLKKRLTGLTPEKLEK--ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkCPVCGRELTEEHR 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 907 SALKEQ-----EDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQqLQGTINQLK----QSAEQKKKQIEA 977
Cdd:PRK03918 451 KELLEEytaelKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLKkynlEELEKKAEEYEK 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 978 LQGEVKNAVSQKTVLENKLQqqssqaaqELAAEKGKLSALQSNYEKCQADLKQLQSDLygkESELLATRQDLKSVEEKLT 1057
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELE--------KLEELKKKLAELEKKLDELEEELAELLKEL---EELGFESVEELEERLKELE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1058 LAQEDLISNRNQIGNQNKSIQELQAAKASLEQ---DSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKC 1134
Cdd:PRK03918 599 PFYNEYLELKDAEKELEREEKELKKLEEELDKafeELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGL 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1135 RQEKEitklneELKSHKQESIKEITNLKDAKQLLIQQKLELQgrvdslkaALEQEKESQQLMREQVKKEEEKRKEEFSEK 1214
Cdd:PRK03918 679 RAELE------ELEKRREEIKKTLEKLKEELEEREKAKKELE--------KLEKALERVEELREKVKKYKALLKERALSK 744
|
570
....*....|
gi 50053824 1215 EAKLHSEIKE 1224
Cdd:PRK03918 745 VGEIASEIFE 754
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
366-1077 |
6.96e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 6.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 366 ELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLH-CKLLETERQLGEAHGRLKEQRQLS 444
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEdAKKAEAVKKAEEAKKDAEEAKKAE 1246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 445 SEKLME--KEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSA--TAKLREAQNDLEQVLRQIGD 520
Cdd:PTZ00121 1247 EERNNEeiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEE 1326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 521 KDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLH- 599
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKk 1406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 600 -DQVQEQKAHLRAAQD-RVLSLETSVSELSSQLNESKEKVSQLDIQIK-AKTELLLSAEAAKAAQRADLQNHLDTAQHA- 675
Cdd:PTZ00121 1407 aDELKKAAAAKKKADEaKKKAEEKKKADEAKKKAEEAKKADEAKKKAEeAKKAEEAKKKAEEAKKADEAKKKAEEAKKAd 1486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 676 -LQDKQQELNKVSVQLDQlTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADAL----EVKASKEQAL 750
Cdd:PTZ00121 1487 eAKKKAEEAKKKADEAKK-AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkkaeELKKAEEKKK 1565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 751 QSLQQQRQLSTDLELRNAELSRELQEQ--EEVVSCTKLDLQNKSEIL-----ENIKQTLTKKEEENVVLKQEFEKLSQDS 823
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEAriEEVMKLYEEEKKMKAEEAkkaeeAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 824 KTQHKEL--GDRMQAAVTELTAVKAQKDALLAE-LSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKAcKELKHQ 900
Cdd:PTZ00121 1646 KKKAEELkkAEEENKIKAAEEAKKAEEDKKKAEeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-EELKKA 1724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 901 LQVQA----ESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIE 976
Cdd:PTZ00121 1725 EEENKikaeEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF 1804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 977 ALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKL 1056
Cdd:PTZ00121 1805 DNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEI 1884
|
730 740 750
....*....|....*....|....*....|.
gi 50053824 1057 TLAQ----------EDLISNRNQIGNQNKSI 1077
Cdd:PTZ00121 1885 EEADeiekidkddiEREIPNNNMAGKNNDII 1915
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
266-471 |
8.08e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 57.23 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 266 EATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQnlteklqkkdldythleekhneESASRKTLQASLHQRDLD 345
Cdd:PRK11281 79 KEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETL----------------------STLSLRQLESRLAQTLDQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 346 CQQLQARLTASESSL-------QRAQGELSEKAEAAQKLREELREVESTRQHLKVEvkqlQQQREEKEQHGLQLQGEVSQ 418
Cdd:PRK11281 137 LQNAQNDLAEYNSQLvslqtqpERAQAALYANSQRLQQIRNLLKGGKVGGKALRPS----QRVLLQAEQALLNAQNDLQR 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 419 lhcKLLETERQLGEAhgrLKEQRQLSSEKLMEKEQQVADLQ-------LKLSrlEEQLKE 471
Cdd:PRK11281 213 ---KSLEGNTQLQDL---LQKQRDYLTARIQRLEHQLQLLQeainskrLTLS--EKTVQE 264
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
88-711 |
8.32e-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: 57.05 E-value: 8.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 88 LRQEVQDLQASLKE--------------EKWYSEELKKELEK-YQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENF 152
Cdd:pfam15921 108 LRQSVIDLQTKLQEmqmerdamadirrrESQSQEDLRNQLQNtVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 153 NIKQMKDLFEQKAAQ---------------LATEIADIKSKYDEEKS-----LRAAAEQKVTHLTEDLNKQTTVIQDLKT 212
Cdd:pfam15921 188 EIRSILVDFEEASGKkiyehdsmstmhfrsLGSAISKILRELDTEISylkgrIFPVEDQLEALKSESQNKIELLLQQHQD 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 213 ELLQRPGIEDVAV--LKKELVQVQTLMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEI 290
Cdd:pfam15921 268 RIEQLISEHEVEItgLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEEL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 291 QK-----------LKGSINELTQKNQNLTEKLQK------KDLDYTHLEEKHNEESASRKT--------LQASLHQRDLD 345
Cdd:pfam15921 348 EKqlvlanselteARTERDQFSQESGNLDDQLQKlladlhKREKELSLEKEQNKRLWDRDTgnsitidhLRRELDDRNME 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 346 CQQLQARLTASESslqRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGE---VSQLHCK 422
Cdd:pfam15921 428 VQRLEALLKAMKS---ECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSertVSDLTAS 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 423 LLETERQLGEAHGRLKEQRQLSSEKLME------KEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQ---QHQEQ 493
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSRVDLKLQElqhlknEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgQHGRT 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 494 QALQQSATAKLREAQNDLEQVLRQI----GDKDQKIQNLEALLQKGK-ESVSLLEKEREDLYAKIQAGEGETAVLNQLQE 568
Cdd:pfam15921 585 AGAMQVEKAQLEKEINDRRLELQEFkilkDKKDAKIRELEARVSDLElEKVKLVNAGSERLRAVKDIKQERDQLLNEVKT 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 569 KN---HALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIK 645
Cdd:pfam15921 665 SRnelNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQID 744
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50053824 646 A---KTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHL 711
Cdd:pfam15921 745 AlqsKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
924-1147 |
9.21e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 924 ETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAvsqktvlenklqqqssqa 1003
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1004 AQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKES----ELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQE 1079
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50053824 1080 LQAAKASLEQDSAKKEALLKEQS---KALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEEL 1147
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEeerAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
82-736 |
1.34e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 82 RDDITLLRQEVQDLQASLKEEKwysEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQMKDLF 161
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETR---DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 162 EQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELlqrpgiedvAVLKKELVQVqtlmdnmt 241
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL---------AEAEAQARAS-------- 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 242 lerERESEKLKDECKKLQSEHAHLEATINQLRS---------ELAKGPQEVAVYVQEIQKLKGSINELTQKN-------- 304
Cdd:TIGR02169 503 ---EERVRGGRAVEEVLKASIQGVHGTVAQLGSvgeryataiEVAAGNRLNNVVVEDDAVAKEAIELLKRRKagratflp 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 305 -------QNLTEKLQKKD-----LDYTHLEEKHneESASRKTLQASLHQRDLDcqqlQARLTASESSLQRAQGELSEKAE 372
Cdd:TIGR02169 580 lnkmrdeRRDLSILSEDGvigfaVDLVEFDPKY--EPAFKYVFGDTLVVEDIE----AARRLMGKYRMVTLEGELFEKSG 653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 373 A--------------AQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLgeahGRLK 438
Cdd:TIGR02169 654 AmtggsraprggilfSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI----EQLE 729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 439 EQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLekskqqhqeqqalqqsatAKLREAQNDLEQVLRQi 518
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL------------------HKLEEALNDLEARLSH- 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 519 gdkdQKIQNLEALLQKgkesvslLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENL 598
Cdd:TIGR02169 791 ----SRIPEIQAELSK-------LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL 859
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 599 HDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDI---QIKAKTELLLSAEAAKAAQRADLQNHLDTAQHA 675
Cdd:TIGR02169 860 NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERkieELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50053824 676 LQDKQQELNKVSVqLDQLTAKFQEKQEHCIQLES--------------HLKDHKEKHLSLEQKVEDLEGHIKKLE 736
Cdd:TIGR02169 940 KGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPvnmlaiqeyeevlkRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
240-644 |
1.36e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.50 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 240 MTLERERESEKLKDECKKLQSEH-AHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDY 318
Cdd:PRK04863 244 MTLEAIRVTQSDRDLFKHLITEStNYVAADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 319 THLEEKHNEESASRKTLQASLHQR------DLDCQQLQARLTASESSLQRAQG---ELSEKAEAAQKlreelrEVESTRQ 389
Cdd:PRK04863 324 SDLEQDYQAASDHLNLVQTALRQQekieryQADLEELEERLEEQNEVVEEADEqqeENEARAEAAEE------EVDELKS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 390 HLkVEVKQ---LQQQREEKEQHGLQLQGEVSQLhCKLLE-TERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRL 465
Cdd:PRK04863 398 QL-ADYQQaldVQQTRAIQYQQAVQALERAKQL-CGLPDlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQF 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 466 EE--QLKEKVTNSTELQ--HQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSL 541
Cdd:PRK04863 476 EQayQLVRKIAGEVSRSeaWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDE 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 542 LEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAE---ENLHDQVQEQKAHLRAAQDRVLS 618
Cdd:PRK04863 556 LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQdalARLREQSGEEFEDSQDVTEYMQQ 635
|
410 420
....*....|....*....|....*.
gi 50053824 619 LETSVSELSSQLNESKEKVSQLDIQI 644
Cdd:PRK04863 636 LLERERELTVERDELAARKQALDEEI 661
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
435-1035 |
1.76e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 435 GRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKV-TNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQ 513
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEeKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 514 VLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQageGETAVLNQLQEKNhalqqqltqltEKLKNQSESHKQ 593
Cdd:PRK02224 242 VLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVR---DLRERLEELEEER-----------DDLLAEAGLDDA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 594 AEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTElllsaeaakaaQRADLQNHLDTAQ 673
Cdd:PRK02224 308 DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE-----------EAAELESELEEAR 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 674 HALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKL-----EADAL-------- 740
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTArerveEAEALleagkcpe 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 741 ---EVKASKEQALQSLQQQRQLSTDLELRNAELSRE-----------LQEQEEVVSCTKLDLQNKSEILENIKQTLTKKE 806
Cdd:PRK02224 457 cgqPVEGSPHVETIEEDRERVEELEAELEDLEEEVEeveerleraedLVEAEDRIERLEERREDLEELIAERRETIEEKR 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 807 EENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDAlLAELSTTKEKLSKVSDSLknsksefekenqkgkAA 886
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSK-LAELKERIESLERIRTLL---------------AA 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 887 VLDLEKACKELKHQLQvqaesALKEQEDLKKSLEKEK-ETSQQLKIELNSVKgeVSQAQNTLKQKEKDEQQLQGTINQLk 965
Cdd:PRK02224 601 IADAEDEIERLREKRE-----ALAELNDERRERLAEKrERKRELEAEFDEAR--IEEAREDKERAEEYLEQVEEKLDEL- 672
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 966 qsaEQKKKQIEALQGEVKNAVSQKTVLENKLqqqssqaaQELAAEKGKLSALQSNYEKCQADLKQLQSDL 1035
Cdd:PRK02224 673 ---REERDDLQAEIGAVENELEELEELRERR--------EALENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
81-531 |
2.31e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 81 TRDDITLLRQEVQDLQASLKEEKWYSEELKKEL-EKYQGLQQQEAKSDGLVTDS---SAELQALEQQLEEAQTENFNIKQ 156
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVrDLRERLEELEEERDDLLAEAgldDADAEAVEARREELEDRDEELRD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 157 MKD-------LFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELlqRPGIEDVAVLKKE 229
Cdd:PRK02224 329 RLEecrvaaqAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI--EELRERFGDAPVD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 230 LVQVQTLMDNMTLERERESEKLKDECKKLQSehahLEATINQLRSELAKG-------PQEVAVYVQEIQKLKGSINELTQ 302
Cdd:PRK02224 407 LGNAEDFLEELREERDELREREAELEATLRT----ARERVEEAEALLEAGkcpecgqPVEGSPHVETIEEDRERVEELEA 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 303 KNQNLTEKLQKKDLDYTHLE-----EKHNEESASRKTL--------QASLHQRDLDCQQLQARLTASESSLQRAQGELSE 369
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERAEdlveaEDRIERLEERREDleeliaerRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 370 KAEAAQKLREELREVESTRQHLKVEVKQLQQQREekeqhglqlqgevsqlhckLLETERQLGEAHGRLKEQRQLSSEKLM 449
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIESLERIRT-------------------LLAAIADAEDEIERLREKREALAELND 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 450 EKEQQVADLQLKLSRLEEQLKEKvtnstelqhQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLE 529
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDEA---------RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE 694
|
..
gi 50053824 530 AL 531
Cdd:PRK02224 695 EL 696
|
|
| FYVE_CARP |
cd15750 |
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ... |
1357-1405 |
2.43e-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: 48.51 E-value: 2.43e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 50053824 1357 NCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKnaltpsSKKPVRVCDAC 1405
Cdd:cd15750 2 PCESCGAKFSVFKRKRTCADCKRYFCSNCLSK------EERGRRRCRRC 44
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
773-1282 |
3.12e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.03 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 773 ELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLsqdsKTQHKELGDRMQAAVTELTAVKAQKDALL 852
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKIL----EQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 853 AELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKhQLQVQAESALKEQEDLKKSLEKEKETSQQLKIE 932
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELE-KLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 933 LNSVKGEVSQAQNTL---KQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVknavSQKTVLENKLQQQSSQAAQELAA 1009
Cdd:TIGR04523 189 IDKIKNKLLKLELLLsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI----NEKTTEISNTQTQLNQLKDEQNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1010 EKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQ------------DLKSVEEKLTLAQEDLISNRNQIGNQNKSI 1077
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkeqdwnkelksELKNQEKKLEEIQNQISQNNKIISQLNEQI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1078 QELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKE 1157
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1158 ITNLKDAKQLLIQQKLELQgrvDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENea 1237
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIK---DLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK-- 499
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 50053824 1238 KLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLE 1282
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
129-1063 |
4.12e-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: 55.05 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 129 LVTDSSAELQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRaAAEQKVTHLTEDLNKQTTVIQ 208
Cdd:TIGR00606 194 VRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLK-NRLKEIEHNLSKIMKLDNEIK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 209 DLKTELLQRPGIEDVAVLKKELVQVQTlmdnmtlerereSEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQ 288
Cdd:TIGR00606 273 ALKSRKKQMEKDNSELELKMEKVFQGT------------DEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQ 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 289 EIQKLKGSINELTQKNQNLTEKLQKKDLDY----THLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTAseSSLQRAQ 364
Cdd:TIGR00606 341 EKTELLVEQGRLQLQADRHQEHIRARDSLIqslaTRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAA--QLCADLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 365 GELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQG---EVSQLHCKLLETERQLGEAHGRLKEQR 441
Cdd:TIGR00606 419 SKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGssdRILELDQELRKAERELSKAEKNSLTET 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 442 QLSSEKLMEKEQqvADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREaqndleqVLRQIGDK 521
Cdd:TIGR00606 499 LKKEVKSLQNEK--ADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDE-------LTSLLGYF 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 522 DQKIQnLEALLQKGKESVSLLEKEREDLYAKIQAGEGETavlNQLQEKNHALQQQLTQLTEKLKN--QSESHKQAEENLH 599
Cdd:TIGR00606 570 PNKKQ-LEDWLHSKSKEINQTRDRLAKLNKELASLEQNK---NHINNELESKEEQLSSYEDKLFDvcGSQDEESDLERLK 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 600 DQVQEQKAHlRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSaeaakaaqraDLQNHLDTAQHALQDK 679
Cdd:TIGR00606 646 EEIEKSSKQ-RAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFIS----------DLQSKLRLAPDKLKST 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 680 QQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEAdALEVKASKEQALQSLQQQRQL 759
Cdd:TIGR00606 715 ESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET-LLGTIMPEEESAKVCLTDVTI 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 760 STDLELRNAELSRELQEQeevvsCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELgDRMQAAVT 839
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQ-----AAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI-QHLKSKTN 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 840 ELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSL 919
Cdd:TIGR00606 868 ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK 947
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 920 EKEKETSQQLKIELNSVKgevSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQ 999
Cdd:TIGR00606 948 EKVKNIHGYMKDIENKIQ---DGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLR 1024
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50053824 1000 SSQA-----AQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQdlKSVEEKLTLAQEDL 1063
Cdd:TIGR00606 1025 KRENelkevEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQ--KGYEKEIKHFKKEL 1091
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
78-555 |
4.32e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 78 LALTRDDITLLRQEVQDLQASLKEEKwysEELKKELEKYQGLQQQEAKSDGlvtdssAELQALEQQLEEAQTEnfnikqm 157
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLE---ARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERE------- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 158 KDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQR--PGIEDVAVLKKELVQVQT 235
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAlrDLRRELRELEAEIASLER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 236 LMDNMTLERERESEKLKDECK-------------KLQSEHAH----LEATINQLRSELAKGPQ---EVAVYVQEIqKLKG 295
Cdd:COG4913 434 RKSNIPARLLALRDALAEALGldeaelpfvgeliEVRPEEERwrgaIERVLGGFALTLLVPPEhyaAALRWVNRL-HLRG 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 296 SINelTQKNQNLTEKLQKKDLDYTHLEEKHN-EESASRKTLQASLHQR-DLDC----QQLQ--------ARLTASESSL- 360
Cdd:COG4913 513 RLV--YERVRTGLPDPERPRLDPDSLAGKLDfKPHPFRAWLEAELGRRfDYVCvdspEELRrhpraitrAGQVKGNGTRh 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 361 ---------------QRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVsqlhcKLLE 425
Cdd:COG4913 591 ekddrrrirsryvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVAS 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 426 TERQLGEAHGRLKEQRQlSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLR 505
Cdd:COG4913 666 AEREIAELEAELERLDA-SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 50053824 506 EAQN-DLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQA 555
Cdd:COG4913 745 LELRaLLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
712-1248 |
5.22e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 712 KDHKEKHLSLEQKVEDLEGhikkleadalEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEvvscTKLDLQNK 791
Cdd:PRK03918 178 IERLEKFIKRTENIEELIK----------EKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 792 SEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGD--RMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSL 869
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 870 KNSKSEFEKENQKgKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQ 949
Cdd:PRK03918 324 NGIEERIKELEEK-EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 950 KEKDEQQLQGTINQLKQSAEQKKKQIEALQG-EVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADL 1028
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKaKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1029 KQLQSDLyGKESELLATRQ---DLKSVEEKLT-LAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEAL---LKEQ 1101
Cdd:PRK03918 483 RELEKVL-KKESELIKLKElaeQLKELEEKLKkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELkkkLAEL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1102 SKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDS 1181
Cdd:PRK03918 562 EKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50053824 1182 LKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNE 1248
Cdd:PRK03918 642 LEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
135-637 |
7.11e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 135 AELQALEQQLEEAQTENFNIKQMKDLFEQKAAQlaTEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTEL 214
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 215 LQRPGiEDVAVLKKELVQVQTLMDnmtlERERESEKLKDECKKLQSEHAHLEATINQLRSELAkgpqevavyvQEIQKLK 294
Cdd:COG4913 333 RGNGG-DRLEQLEREIERLERELE----ERERRRARLEALLAALGLPLPASAEEFAALRAEAA----------ALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 295 GSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQ-RDLDCQQLQArltaSESSLQRAqGEL---SEK 370
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAlRDALAEALGL----DEAELPFV-GELievRPE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 371 AEA-------------------AQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQ------------------LQ 413
Cdd:COG4913 473 EERwrgaiervlggfaltllvpPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDpdslagkldfkphpfrawLE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 414 GEVSQ---LHCklLETERQL---------------GEAHGRLKEQRQLSS---------EKLMEKEQQVADLQLKLSRLE 466
Cdd:COG4913 553 AELGRrfdYVC--VDSPEELrrhpraitragqvkgNGTRHEKDDRRRIRSryvlgfdnrAKLAALEAELAELEEELAEAE 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 467 EQLKEkvtnSTELQHQLEKSKQQHQEQqalqqsatAKLREAQNDLEQVLRQIGDKDQKIQNLEAllqkGKESVSLLEKER 546
Cdd:COG4913 631 ERLEA----LEAELDALQERREALQRL--------AEYSWDEIDVASAEREIAELEAELERLDA----SSDDLAALEEQL 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 547 EDLYAKIQAGEGEtavLNQLQEKNHALQQQLTQLTEKLKnqsESHKQAEENLHDQVQEQKAHL-----RAAQDRVL---- 617
Cdd:COG4913 695 EELEAELEELEEE---LDELKGEIGRLEKELEQAEEELD---ELQDRLEAAEDLARLELRALLeerfaAALGDAVErelr 768
|
570 580
....*....|....*....|.
gi 50053824 618 -SLETSVSELSSQLNESKEKV 637
Cdd:COG4913 769 eNLEERIDALRARLNRAEEEL 789
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
905-1128 |
1.01e-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: 52.84 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 905 AESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKN 984
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 985 AVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYE---KCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQE 1061
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLdavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50053824 1062 DLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAE 1128
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
163-407 |
1.33e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 163 QKAAQLATEIAD------IKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKtellQRPGIEDVAVLKKELVQVQTl 236
Cdd:COG3206 148 ELAAAVANALAEayleqnLELRREEARKALEFLEEQLPELRKELEEAEAALEEFR----QKNGLVDLSEEAKLLLQQLS- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 237 mdnmTLEREREseklkdeckKLQSEHAHLEATINQLRSELAKGPQEVAVYVQ--EIQKLKGSINELTQKNQNLTEKLQKK 314
Cdd:COG3206 223 ----ELESQLA---------EARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPN 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 315 DLDYTHLEEKHNE-ESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKV 393
Cdd:COG3206 290 HPDVIALRAQIAAlRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
250
....*....|....
gi 50053824 394 EVKQLQQQREEKEQ 407
Cdd:COG3206 370 LLQRLEEARLAEAL 383
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
860-1343 |
2.25e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 860 EKLSKVSDSLKNSKSEFEKENQKGKaavlDLEKACKELKHQLQvQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGE 939
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEKEKELE-EVLREINEISSELPELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 940 VSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAaqELAAEKGKLSALQS 1019
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE--EYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1020 NYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLisnrnqignqnKSIQELQAAKASLEQDSAKKEALLK 1099
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH-----------ELYEEAKAKKEELERLKKRLTGLTP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1100 EQSKA-LEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKL---------------NEELKSHKQESIKEITNLKD 1163
Cdd:PRK03918 387 EKLEKeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcgreltEEHRKELLEEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1164 AKQLLIQQKLELQGRVDSLKAALEQEKESQQLMR-----EQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAK 1238
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIKLKElaeqlKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1239 LTMQVTTLNENLGTVKKEWQSSQRRVSELEKQ--------TDDLRGEIAVLEA------TVQNNQDERRALLERclkgeg 1304
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLDELEEELAELLKEleelgfesVEELEERLKELEPfyneylELKDAEKELEREEKE------ 620
|
490 500 510
....*....|....*....|....*....|....*....
gi 50053824 1305 eIEKLQTKALELQRKLDNTTAAVQELGRENQSLQIKHTQ 1343
Cdd:PRK03918 621 -LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
862-1338 |
3.83e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 862 LSKVSDSLKNSKSEFEKENQKGKAAVL-DLEKACKELKHQL---QVQAESALKEQEDLKKSLEKEKETSQqlkiELNSVK 937
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLnGLESELAELDEEIeryEEQREQARETRDEADEVLEEHEERRE----ELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 938 GEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVK-NAVSQKTVLENK--LQQQSSQAAQELAAEKGKL 1014
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlDDADAEAVEARReeLEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1015 SALQSNYEKCQADLKQLQSDLYGK-------ESELLATRQDLKSVEEKLTLAQEDLISNRN-------QIGNQNKSIQEL 1080
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELreeaaelESELEEAREAVEDRREEIEELEEEIEELRErfgdapvDLGNAEDFLEEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1081 QAAKASLEQDSAKKEALLKEQSKALEDAQR---EKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKE 1157
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEEAEAlleAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEER 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1158 ITNLKDAKqlliqqklELQGRVDSLKaalEQEKESQQLM--REQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEEN 1235
Cdd:PRK02224 498 LERAEDLV--------EAEDRIERLE---ERREDLEELIaeRRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1236 EAKLTMQVTTLNENLGTVKKEWQsSQRRVSELEKQTDDLRGEIAVLE---ATVQNNQDERRALL----ERCLKGEGE--- 1305
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERIE-SLERIRTLLAAIADAEDEIERLRekrEALAELNDERRERLaekrERKRELEAEfde 645
|
490 500 510
....*....|....*....|....*....|....*
gi 50053824 1306 --IEKLQTKALELQRKLDNTTAAVQELGRENQSLQ 1338
Cdd:PRK02224 646 arIEEAREDKERAEEYLEQVEEKLDELREERDDLQ 680
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
253-485 |
4.83e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 253 DECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKkdldythLEEKHNEESASR 332
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-------LEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 333 KTLQASLHQRDldcQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQhglqL 412
Cdd:COG4942 93 AELRAELEAQK---EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA----L 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50053824 413 QGEVSQLHCKLLETERQLGEAHGRLKEQRQlsseklmEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEK 485
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKA-------ERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
504-1063 |
5.04e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 504 LREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEK 583
Cdd:PRK01156 178 LRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 584 LKnQSESHKQAEENLHDQVQE-QKAHLRAAQDRVLSLETSVSE---LSSQLNESKEKVSQLDIQIKAKTELLlsaeaaka 659
Cdd:PRK01156 258 IK-TAESDLSMELEKNNYYKElEERHMKIINDPVYKNRNYINDyfkYKNDIENKKQILSNIDAEINKYHAII-------- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 660 AQRADLQNHLDTaqhaLQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADA 739
Cdd:PRK01156 329 KKLSVLQKDYND----YIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 740 LEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEE-----------VVSCTKLDLQNKSEILENIKQTLTKKEEE 808
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRnmemlngqsvcPVCGTTLGEEKSNHIINHYNEKKSRLEEK 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 809 NVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDslKNSKSEfEKENQKGKAAVL 888
Cdd:PRK01156 485 IREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKD--KHDKYE-EIKNRYKSLKLE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 889 DLEKACKELKHQLQVQA----ESALKEQEDLKKSLEKEKETSQQLKIELNSVKgevSQAQNTLKQKEKDEQQLQGTINQL 964
Cdd:PRK01156 562 DLDSKRTSWLNALAVISlidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLNNKYNEI 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 965 kqsaEQKKKQIEALQGEVKNAVSQktvlenklQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLA 1044
Cdd:PRK01156 639 ----QENKILIEKLRGKIDNYKKQ--------IAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEI 706
|
570
....*....|....*....
gi 50053824 1045 TRQDLKSVEEKLTLAQEDL 1063
Cdd:PRK01156 707 LRTRINELSDRINDINETL 725
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
969-1293 |
5.16e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 969 EQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQD 1048
Cdd:TIGR02169 194 DEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1049 LKSVEEKLtlaqEDLISNRnqignqnksIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAE 1128
Cdd:TIGR02169 274 LEELNKKI----KDLGEEE---------QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1129 MEEIKCRQEKEITKLNEELKSHKQE---SIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEqEKESQQLMREQVKKEEE 1205
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEEledLRAELEEVDKEFAETRDELKDYREKLEKLKREIN-ELKRELDRLQEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1206 KRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATV 1285
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
....*...
gi 50053824 1286 QNNQDERR 1293
Cdd:TIGR02169 500 RASEERVR 507
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
644-1240 |
5.75e-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: 50.88 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 644 IKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQ 723
Cdd:pfam05483 196 ILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 724 KV----EDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEE--------------VVSCTK 785
Cdd:pfam05483 276 KTklqdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAqmeelnkakaahsfVVTEFE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 786 LDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKeLGDRMQAAVTELTAVKAQKDALLAElsttKEKLSKV 865
Cdd:pfam05483 356 ATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTK-FKNNKEVELEELKKILAEDEKLLDE----KKQFEKI 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 866 SDSLKNSKSEFEKENQKGKAAVLDLEKACKELKhqlqVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQN 945
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKEIHDLEIQLTAIK----TSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQ 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 946 TLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQgevknavSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQ 1025
Cdd:pfam05483 507 EASDMTLELKKHQEDIINCKKQEERMLKQIENLE-------EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIE 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1026 ADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKAL 1105
Cdd:pfam05483 580 YEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNY 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1106 EDAQREKSVKEKELVAEKSKLAEMEEikcrqekEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAA 1185
Cdd:pfam05483 660 QKEIEDKKISEEKLLEEVEKAKAIAD-------EAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKN 732
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 50053824 1186 LEQEKESqqlMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLT 1240
Cdd:pfam05483 733 KEQEQSS---AKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| PTZ00303 |
PTZ00303 |
phosphatidylinositol kinase; Provisional |
1325-1410 |
6.20e-06 |
|
phosphatidylinositol kinase; Provisional
Pssm-ID: 140324 [Multi-domain] Cd Length: 1374 Bit Score: 51.24 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1325 AAVQELGRENQSLQIKHTQAL-NRKWAEDNEVQN-CMSCGKCF-----SVTVRRHHCRQCGNIFCAECSTKNA------- 1390
Cdd:PTZ00303 428 ATVGGVAEENELNTFGLTKLLhNPSWQKDDESSDsCPSCGRAFislsrPLGTRAHHCRSCGIRLCVFCITKRAhysfakl 507
|
90 100
....*....|....*....|...
gi 50053824 1391 LTPSSKKPVR---VCDACFNDLQ 1410
Cdd:PTZ00303 508 AKPGSSDEAEerlVCDTCYKEYE 530
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
227-729 |
6.32e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 227 KKELVQVQTLMDNMTLERERESEKLkDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKnqn 306
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE--- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 307 lTEKLQKKDLDYTHLEEKHNEESASRKtLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVES 386
Cdd:PRK03918 275 -IEELEEKVKELKELKEKAEEYIKLSE-FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 387 TRQHLKVEVKQLQQQREEKEqhglQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEK----EQQVADLQLKL 462
Cdd:PRK03918 353 RLEELEERHELYEEAKAKKE----ELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARigelKKEIKELKKAI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 463 SRLEEQLKEKVTNSTELQHQ-----LEKSKQQHQEQQALQQSATAKLREAQNDLEQV---------LRQIGDKDQKIQNL 528
Cdd:PRK03918 429 EELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELekvlkkeseLIKLKELAEQLKEL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 529 EALLQK-GKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLH-------D 600
Cdd:PRK03918 509 EEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfesvE 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 601 QVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDiQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHalQDKQ 680
Cdd:PRK03918 589 ELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELD-KAFEELAETEKRLEELRKELEELEKKYSEEEY--EELR 665
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 50053824 681 QELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLE 729
Cdd:PRK03918 666 EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
689-1188 |
7.81e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 689 QLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNA 768
Cdd:PRK02224 238 EADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 769 ELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMqaavTELTAVKAQK 848
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRR----EEIEELEEEI 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 849 DALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAE----------------SALKEQ 912
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvETIEED 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 913 EDLKKSLEKEKEtsqQLKIELNSVKGEVSQAQnTLKQKEKDEQQLqgtinqlkqsaEQKKKQIEALQGEVKNAVSQKTVL 992
Cdd:PRK02224 474 RERVEELEAELE---DLEEEVEEVEERLERAE-DLVEAEDRIERL-----------EERREDLEELIAERRETIEEKRER 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 993 ENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLygkeSELLATRQDLKSVEEKLTLAQEdlisNRNQIGN 1072
Cdd:PRK02224 539 AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL----AELKERIESLERIRTLLAAIAD----AEDEIER 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1073 QNKSIQELQA----AKASLEQDSAKKEALLKE-QSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEEL 1147
Cdd:PRK02224 611 LREKREALAElndeRRERLAEKRERKRELEAEfDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL 690
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 50053824 1148 KSHK--QESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQ 1188
Cdd:PRK02224 691 EELEelRERREALENRVEALEALYDEAEELESMYGDLRAELRQ 733
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
75-487 |
9.25e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 75 EAGLALTRDDITLLRQEVQDLQ---ASLKEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTEN 151
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEekvKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 152 FNIKQMKDLFE----------------QKAAQLATEIADIKSKY-----DEEKSLRAAAEQKVTHLTEDLNKQTTVIQDL 210
Cdd:PRK03918 338 ERLEELKKKLKelekrleeleerhelyEEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 211 KTELLQRPgiEDVAVLKKELVQVQTLMDNMTLE-RERESEKLKDECKKLQSEHAHLEATINQLRSELAK------GPQEV 283
Cdd:PRK03918 418 KKEIKELK--KAIEELKKAKGKCPVCGRELTEEhRKELLEEYTAELKRIEKELKEIEEKERKLRKELRElekvlkKESEL 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 284 AVYVQEIQKLKGSINELTQKNqnlTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRdldcQQLQARLTASESSLQRA 363
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKKYN---LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL----EELKKKLAELEKKLDEL 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 364 QGELSE-KAEAAQKLREELREVESTRQHLK------VEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGR 436
Cdd:PRK03918 569 EEELAElLKELEELGFESVEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 50053824 437 LKEQRQLSSE--------KLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSK 487
Cdd:PRK03918 649 LEELEKKYSEeeyeelreEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
88-740 |
1.09e-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: 50.22 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 88 LRQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDS-SAELQALEQQLEEAQTENFNIKQMKDLFEQKAA 166
Cdd:pfam12128 306 LNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSwQSELENLEERLKALTGKHQDVTAKYNRRRSKIK 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 167 -QLATEIADIKSKYD---EEKSLRAAAEQKV-----THLTEDLNKQTTVIQDLKTELlqrpgIEDVAVLKKELVQVQtlm 237
Cdd:pfam12128 386 eQNNRDIAGIKDKLAkirEARDRQLAVAEDDlqaleSELREQLEAGKLEFNEEEYRL-----KSRLGELKLRLNQAT--- 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 238 dnMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKD-- 315
Cdd:pfam12128 458 --ATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAgt 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 316 -LDYTHLEEKHNEESASRKTLQASLHQRDLD----CQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTrqh 390
Cdd:pfam12128 536 lLHFLRKEAPDWEQSIGKVISPELLHRTDLDpevwDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEA--- 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 391 lkvevkqLQQQREEKEQhglqLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQqvadLQLKLSR-LEEQL 469
Cdd:pfam12128 613 -------LQSAREKQAA----AEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQS----EKDKKNKaLAERK 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 470 KEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLrqIGDKDQKIQNLEALLQKGKESVSLLEKEREDL 549
Cdd:pfam12128 678 DSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVV--EGALDAQLALLKAAIAARRSGAKAELKALETW 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 550 YAKIQAGEGETavlnqlQEKNHALQQQLTQLTEKLKNqSESHKQAEENLHDQVQEQ-KAHLRAAQDRVLSLETSVSELSS 628
Cdd:pfam12128 756 YKRDLASLGVD------PDVIAKLKREIRTLERKIER-IAVRRQEVLRYFDWYQETwLQRRPRLATQLSNIERAISELQQ 828
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 629 QLNeskekvsqldiQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVsvQLDQLTAKFQEKQEHCI-QL 707
Cdd:pfam12128 829 QLA-----------RLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATL--KEDANSEQAQGSIGERLaQL 895
|
650 660 670
....*....|....*....|....*....|...
gi 50053824 708 ESHLKDHKEKHLSLEQKVEDLEGHIKKLEADAL 740
Cdd:pfam12128 896 EDLKLKRDYLSESVKKYVEHFKNVIADHSGSGL 928
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
291-1297 |
1.15e-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: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 291 QKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEK 370
Cdd:pfam01576 22 QKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 371 AEAAQKLREELREVESTRQHLKVE-------VKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQL 443
Cdd:pfam01576 102 QQHIQDLEEQLDEEEAARQKLQLEkvtteakIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 444 SS----------EKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQ 513
Cdd:pfam01576 182 KNkheamisdleERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 514 VLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGE-------TAVLNQLQEKNhalQQQLTQLTEKLKN 586
Cdd:pfam01576 262 ALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEledtldtTAAQQELRSKR---EQEVTELKKALEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 587 QSESHK-----------QAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLneskEKVSQLDIQIKAKTELLLSAE 655
Cdd:pfam01576 339 ETRSHEaqlqemrqkhtQALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL----RTLQQAKQDSEHKRKKLEGQL 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 656 AAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKL 735
Cdd:pfam01576 415 QELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQL 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 736 EADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQE 815
Cdd:pfam01576 495 EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKT 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 816 FEKLSQDSKTQHKELgDRMQAAVTELTAVKAQKDALLAELSTtkeklskVSDSLKNSKSEFEKENQKGKAAVLDLEKACK 895
Cdd:pfam01576 575 KNRLQQELDDLLVDL-DHQRQLVSNLEKKQKKFDQMLAEEKA-------ISARYAEERDRAEAEAREKETRALSLARALE 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 896 ELKhqlqvqaeSALKEQEDLKKSLEKEKEtsqqlkiELNSVKGEVSqaqntlkqkeKDEQQLQGTINQLKQSAEQKKKQI 975
Cdd:pfam01576 647 EAL--------EAKEELERTNKQLRAEME-------DLVSSKDDVG----------KNVHELERSKRALEQQVEEMKTQL 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 976 EALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEK 1055
Cdd:pfam01576 702 EELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKE 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1056 LTLAQEDLISNRNQIGNQNKSIQ-ELQAAKASLEQDSAKKEALLKEQskaledaqREKSVKEKELVAEKSKLAEMEEIKC 1134
Cdd:pfam01576 782 LEAQIDAANKGREEAVKQLKKLQaQMKDLQRELEEARASRDEILAQS--------KESEKKLKNLEAELLQLQEDLAASE 853
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1135 RQEKEITKLNEELKshkqesiKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMreqvkkeeekrkeefsek 1214
Cdd:pfam01576 854 RARRQAQQERDELA-------DEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELL------------------ 908
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1215 eaklhseikekeagmkkhEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRA 1294
Cdd:pfam01576 909 ------------------NDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIA 970
|
...
gi 50053824 1295 LLE 1297
Cdd:pfam01576 971 ALE 973
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
366-612 |
1.21e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 366 ELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHgLQLQGEVSQLhcklleteRQLGEAHGRLKEQR--QL 443
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERY-AAARERLAEL--------EYLRAALRLWFAQRrlEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 444 SSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKqqhqeqqalqqsaTAKLREAQNDLEQVLRQIGDKDQ 523
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG-------------GDRLEQLEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 524 KIQNLEALLQKGKESVSLLEKEREDLYAKIQA-GEGETAVLNQLQEKNHALQQQLTQLTEK---LKNQSESHKQAEENLH 599
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRAEAAAlLEALEEELEALEEALAEAEAALRDLRRElreLEAEIASLERRKSNIP 439
|
250
....*....|...
gi 50053824 600 DQVQEQKAHLRAA 612
Cdd:COG4913 440 ARLLALRDALAEA 452
|
|
| FYVE_WDFY2 |
cd15757 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); WDFY2, also ... |
1367-1405 |
1.23e-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: 1.23e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 50053824 1367 VTVRRHHCRQCGNIFCAECSTKNALTP--SSKKPVRVCDAC 1405
Cdd:cd15757 29 IGLRQHHCRKCGKAVCGKCSSKRSTIPlmGFEFEVRVCDSC 69
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
78-984 |
1.95e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.20 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 78 LALTRDDITLLRQEVQDLQASLKEEKWYSeelKKELEKYQglqqqeaksdglvtdssaelqalEQQLEEAQTENFNIKQM 157
Cdd:pfam02463 178 LIEETENLAELIIDLEELKLQELKLKEQA---KKALEYYQ-----------------------LKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 158 KDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQrpgiedVAVLKKELVQVQTLM 237
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKL------LAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 238 DNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKgpqevavyVQEIQKLKGSINELTQKNQNLTEKLQKKDLD 317
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKE--------LEIKREAEEEEEEELEKLQEKLEQLEEELLA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 318 YTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLtasesslqrAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQ 397
Cdd:pfam02463 378 KKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL---------ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 398 LQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLsseklmekeQQVADLQLKLSRLEEQLKEKVTNST 477
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQK---------LEERSQKESKARSGLKVLLALIKDG 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 478 ELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGE 557
Cdd:pfam02463 520 VGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 558 GETAVLNQLQEKnhalqqqltqlteKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKV 637
Cdd:pfam02463 600 DPILNLAQLDKA-------------TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKA 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 638 SQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEK 717
Cdd:pfam02463 667 SLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKID 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 718 HLSLEQ---KVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEI 794
Cdd:pfam02463 747 EEEEEEeksRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQ 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 795 LENIKQTLTKKEEENVVLKQEFEKLSQDSK-TQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSK 873
Cdd:pfam02463 827 EEKIKEEELEELALELKEEQKLEKLAEEELeRLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEES 906
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 874 SEFEKENQKGKAAVLDLEKACKELKHQLQVQAESaLKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKD 953
Cdd:pfam02463 907 QKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL-LLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEE 985
|
890 900 910
....*....|....*....|....*....|.
gi 50053824 954 EQQLQGTINQLKQSAEQKKKQIEALQGEVKN 984
Cdd:pfam02463 986 KEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
465-1188 |
1.98e-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: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 465 LEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGD-KDQKIQNLEALLQKGKESVSLLE 543
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADiRRRESQSQEDLRNQLQNTVHELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 544 KEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENL------------HDQVQEQKAHLRA 611
Cdd:pfam15921 156 AAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMstmhfrslgsaiSKILRELDTEISY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 612 AQDRVLSLETSVSELSSqlnESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQD-----KQQELNKV 686
Cdd:pfam15921 236 LKGRIFPVEDQLEALKS---ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSqleiiQEQARNQN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 687 SVQLDQLTakfqEKQEHCIQLESHLKDHKEKHlslEQKVEDLEGHIKKLEADALEVKASKEQALQSL----QQQRQLSTD 762
Cdd:pfam15921 313 SMYMRQLS----DLESTVSQLRSELREAKRMY---EDKIEELEKQLVLANSELTEARTERDQFSQESgnldDQLQKLLAD 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 763 LELRNAELSRELQEQEEVVSctkLDLQNkSEILENIKQTLTKKEEEnvvlKQEFEKLSQDSKTQHKELGDRMQAAVTELT 842
Cdd:pfam15921 386 LHKREKELSLEKEQNKRLWD---RDTGN-SITIDHLRRELDDRNME----VQRLEALLKAMKSECQGQMERQMAAIQGKN 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 843 AVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQkgkaAVLDLEKACKELKHQLQVQAE--SALKEQEDLK---- 916
Cdd:pfam15921 458 ESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSER----TVSDLTASLQEKERAIEATNAeiTKLRSRVDLKlqel 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 917 KSLEKEKETSQQLKIELNSVKGEVSQAQNT---LKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLE 993
Cdd:pfam15921 534 QHLKNEGDHLRNVQTECEALKLQMAEKDKVieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILK 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 994 NKLQQ---QSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYgkeSELLATRQDLKSVEEKLTLAQEDLISNRNQI 1070
Cdd:pfam15921 614 DKKDAkirELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLL---NEVKTSRNELNSLSEDYEVLKRNFRNKSEEM 690
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1071 -GNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDA---QREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEE 1146
Cdd:pfam15921 691 eTTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAmgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEE 770
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 50053824 1147 LKSHKQE---SIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQ 1188
Cdd:pfam15921 771 KNKLSQElstVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
108-718 |
2.17e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 108 ELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQ----------TENFNIKQMKDLFEQKAAQLATEIADIKS 177
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALqqtqqshaylTQKREAQEEQLKKQQLLKQLRARIEELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 178 KYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRPGIEDVAVLKKELVQVQTLmdnmtLERERESEKLKDECKK 257
Cdd:TIGR00618 275 QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH-----VKQQSSIEEQRRLLQT 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 258 LQSEHAHLEATINQLRSELAKGPQEVAVyVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQA 337
Cdd:TIGR00618 350 LHSQEIHIRDAHEVATSIREISCQQHTL-TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAH 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 338 SLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVEstrqhlkvEVKQLQQQREEKEQHGLQLQGEVS 417
Cdd:TIGR00618 429 AKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ--------TKEQIHLQETRKKAVVLARLLELQ 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 418 QLHCKLLETERQLgEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQ 497
Cdd:TIGR00618 501 EEPCPLCGSCIHP-NPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 498 QSATAKLREAQNDLEQVL----RQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAV----LNQLQEK 569
Cdd:TIGR00618 580 NRSKEDIPNLQNITVRLQdlteKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALhalqLTLTQER 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 570 NHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTE 649
Cdd:TIGR00618 660 VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARED 739
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50053824 650 LLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKH 718
Cdd:TIGR00618 740 ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEI 808
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1007-1260 |
2.42e-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: 48.22 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1007 LAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKAS 1086
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1087 LEQDSAKKEALLKEQSKAledAQREKSVKEKELVAEKSKLAEMEeikcrqekeitKLNEELKSHKQESIKEITNLKDAKQ 1166
Cdd:COG4942 95 LRAELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAV-----------RRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1167 LLIQQKLELQGRVDSLKAALEQEKESQQLMReqvkkeeeKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTL 1246
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALE--------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|....
gi 50053824 1247 NENLGTVKKEWQSS 1260
Cdd:COG4942 233 EAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
940-1188 |
2.46e-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: 48.22 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 940 VSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSqaaqELAAEKGKLSALQS 1019
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ----ELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1020 NYEKCQADLKQLQSDLygkeSELLATRQDLKSVEE-KLTLAQEDLisnrnqignqnksiqelqaakasleQDSAKKEALL 1098
Cdd:COG4942 91 EIAELRAELEAQKEEL----AELLRALYRLGRQPPlALLLSPEDF-------------------------LDAVRRLQYL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1099 KEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGR 1178
Cdd:COG4942 142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
250
....*....|
gi 50053824 1179 VDSLKAALEQ 1188
Cdd:COG4942 222 AEELEALIAR 231
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
82-543 |
2.67e-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: 48.53 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 82 RDDITLLRQEVQDLQASLKEEKwysEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQMKDLF 161
Cdd:pfam05622 9 KDELAQRCHELDQQVSLLQEEK---NSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 162 EQKAAQLATEIADIKSKYDEEKSLRAAAEQ------KVTHLTEDLNKQTTVIQDLKTELlqrpgiEDVAVLKKelvQVQT 235
Cdd:pfam05622 86 RIKCEELEKEVLELQHRNEELTSLAEEAQAlkdemdILRESSDKVKKLEATVETYKKKL------EDLGDLRR---QVKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 236 LMDNMTLERERESEkLKDECKKLQSEHAHLEAtinqlrselakgpqevavYVQEIQKLKGSINELTQKNQNLteklqkkD 315
Cdd:pfam05622 157 LEERNAEYMQRTLQ-LEEELKKANALRGQLET------------------YKRQVQELHGKLSEESKKADKL-------E 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 316 LDYTHLEEKHNEESASRKTLqasLHQRD--------LDCQQLQARltasesSLQRAQGELSEKAEAAQKLREELR--EVE 385
Cdd:pfam05622 211 FEYKKLEEKLEALQKEKERL---IIERDtlretneeLRCAQLQQA------ELSQADALLSPSSDPGDNLAAEIMpaEIR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 386 STRQHLKVEVKQLQQQREEKEQHglqlqgevsqlhcKLLETERQLGEAHGR---LKEQRQLSSEKLMEKEQQVADLQLKL 462
Cdd:pfam05622 282 EKLIRLQHENKMLRLGQEGSYRE-------------RLTELQQLLEDANRRkneLETQNRLANQRILELQQQVEELQKAL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 463 SRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQalqqsataKLREAQNDLEQVLRQigDKDQKIQNLEALLQKGKESVSLL 542
Cdd:pfam05622 349 QEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQ--------KKKEQIEELEPKQDS--NLAQKIDELQEALRKKDEDMKAM 418
|
.
gi 50053824 543 E 543
Cdd:pfam05622 419 E 419
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
600-1149 |
2.95e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 600 DQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLlsaeAAKAAQRADLQNHLDTAQHALQDK 679
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELC----AEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 680 QQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQqrql 759
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKL---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 760 stdLELRNAELSRELQEQEEVV-SCTKLDLQNKSEILEnIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDrMQAAV 838
Cdd:pfam01576 157 ---LEERISEFTSNLAEEEEKAkSLSKLKNKHEAMISD-LEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAE-LQAQI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 839 TELTAVKAQKD-------ALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQV-------- 903
Cdd:pfam01576 232 AELRAQLAKKEeelqaalARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEAlkteledt 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 904 -------QAESALKEQE--DLKKSLEKEKETSQQlkiELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQ 974
Cdd:pfam01576 312 ldttaaqQELRSKREQEvtELKKALEEETRSHEA---QLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 975 ieaLQGEVKNAVSQKTVLEN---KLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKS 1051
Cdd:pfam01576 389 ---LQAELRTLQQAKQDSEHkrkKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1052 VEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEE 1131
Cdd:pfam01576 466 LESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEE 545
|
570
....*....|....*...
gi 50053824 1132 IKCRQEKEITKLNEELKS 1149
Cdd:pfam01576 546 GKKRLQRELEALTQQLEE 563
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
936-1354 |
3.19e-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: 48.68 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 936 VKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLS 1015
Cdd:pfam12128 239 IRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1016 ALQSNYEKCQADLKQLQSD----LYGKESELLATRQDLKSVEEKLTLaqedlisnrnQIGNQNKSIQELQAAKASLEQDS 1091
Cdd:pfam12128 319 KDRSELEALEDQHGAFLDAdietAAADQEQLPSWQSELENLEERLKA----------LTGKHQDVTAKYNRRRSKIKEQN 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1092 AKK-EALLKEQSKALEDAQREKSVKEKELVAEKSKL------------AEMEEIKCRQEKEITKLN-----EELKSHKQE 1153
Cdd:pfam12128 389 NRDiAGIKDKLAKIREARDRQLAVAEDDLQALESELreqleagklefnEEEYRLKSRLGELKLRLNqatatPELLLQLEN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1154 SIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHE 1233
Cdd:pfam12128 469 FDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWE 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1234 ENEAKLTMQVTTLNENLGTVKKEWQSSQRR-------------VSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCL 1300
Cdd:pfam12128 549 QSIGKVISPELLHRTDLDPEVWDGSVGGELnlygvkldlkridVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLV 628
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 50053824 1301 KGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQIKHTQALNRKWAEDNE 1354
Cdd:pfam12128 629 QANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANE 682
|
|
| FYVE1_Vac1p_like |
cd15761 |
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ... |
1349-1406 |
3.53e-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: 3.53e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50053824 1349 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECST------KNA-LTPSSKKPVRVCDACF 1406
Cdd:cd15761 4 WKKPSGKSRCSECGKTLNKKNGIVNCRKCGELFCNEHCRnriklnNSAeYDPKNGKWCRCCEKCF 68
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1039-1338 |
3.73e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1039 ESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQdsaKKEALLKEQSKALEDAQREKSVKEKE 1118
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKE---KREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1119 LVAEKSKLAEMEEIKCRQEKEITKLNEELKshkqESIKEITNLKDAKQLLIQQKL-ELQGRVDSLKAALEqEKESQQLMR 1197
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLE----ELNKKIKDLGEEEQLRVKEKIgELEAEIASLERSIA-EKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1198 EQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGE 1277
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50053824 1278 IAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQ 1338
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
328-473 |
3.76e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 48.15 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 328 ESASRKTLQASLHQRDLDcqQLQARLTASE---SSLQRAQGELSEkaEAAQKLREELREVESTRQHLKvevkqlQQQREE 404
Cdd:COG0542 397 EAAARVRMEIDSKPEELD--ELERRLEQLEiekEALKKEQDEASF--ERLAELRDELAELEEELEALK------ARWEAE 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 405 KE--QHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSE--------------------KLMEKEQQvadlqlKL 462
Cdd:COG0542 467 KEliEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREevteediaevvsrwtgipvgKLLEGERE------KL 540
|
170
....*....|.
gi 50053824 463 SRLEEQLKEKV 473
Cdd:COG0542 541 LNLEEELHERV 551
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1079-1344 |
3.80e-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: 48.51 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1079 ELQAAKASLEQDSAKKEALlKEQSKALEDAQREKSVKEKElvAEKSKLAEMEEIKCRQEKEITKLNEELkshkQESIKEI 1158
Cdd:TIGR02168 197 ELERQLKSLERQAEKAERY-KELKAELRELELALLVLRLE--ELREELEELQEELKEAEEELEELTAEL----QELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1159 TNLKDAKQLLIQQKLELQGRVDSLKAalEQEKESQQLMReqvkkeeekrkeeFSEKEAKLHSEIKEKEAGMKKHEENEAK 1238
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALAN--EISRLEQQKQI-------------LRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1239 LTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKALELQR 1318
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260
....*....|....*....|....*.
gi 50053824 1319 KLDNTTAAVQELGRENQSLQIKHTQA 1344
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQA 440
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
444-646 |
3.81e-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: 47.84 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 444 SSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQ 523
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 524 KIQNLEALLQK--------GKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLtEKLKNQSESHKQAE 595
Cdd:COG4942 98 ELEAQKEELAEllralyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL-AALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 50053824 596 ENLHDQVQEQKAHLRAAQDR----VLSLETSVSELSSQLNESKEKVSQLDIQIKA 646
Cdd:COG4942 177 EALLAELEEERAALEALKAErqklLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
354-741 |
4.16e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 354 TASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQqREEKEQHGLQLQGEVSQLHCKLLETERQLGEA 433
Cdd:PRK04863 289 LELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASD-HLNLVQTALRQQEKIERYQADLEELEERLEEQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 434 HGRLK---EQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQH---QLEKSKQQHQEQQALQQSATAKLREA 507
Cdd:PRK04863 368 NEVVEeadEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQavqALERAKQLCGLPDLTADNAEDWLEEF 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 508 QNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEK-----EREDLY----AKIQAGEGETAVLNQLQ---------EK 569
Cdd:PRK04863 448 QAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagevSRSEAWdvarELLRRLREQRHLAEQLQqlrmrlselEQ 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 570 NHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAhlraaqdRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTE 649
Cdd:PRK04863 528 RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEA-------RLESLSESVSEARERRMALRQQLEQLQARIQRLAA 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 650 LllsaeaakaaqradlqnhlDTAQHALQDKqqelnkvsvqLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLE 729
Cdd:PRK04863 601 R-------------------APAWLAAQDA----------LARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELA 651
|
410
....*....|..
gi 50053824 730 GHIKKLEADALE 741
Cdd:PRK04863 652 ARKQALDEEIER 663
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
175-399 |
4.85e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 175 IKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRPG-----IEDVAVLKKELVQVQTLMDNMTLERERESE 249
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIArkqnkYDELVEEAKTIKAEIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 250 KLKDECKKLQSEHAHLEATINQLRSELA--KGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNE 327
Cdd:PHA02562 252 DPSAALNKLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDE 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50053824 328 ESASRKT---LQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQ 399
Cdd:PHA02562 332 FNEQSKKlleLKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRG 406
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
548-1285 |
5.70e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 548 DLYAKIQAGEGETAVLNQLQEKNHA---LQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVS 624
Cdd:pfam15921 62 DSPRKIIAYPGKEHIERVLEEYSHQvkdLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 625 ELSSQLNESkekVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHldtaqhalQDKQQELNKVSVQLDQLTAK--FQEKQE 702
Cdd:pfam15921 142 DLRNQLQNT---VHELEAAKCLKEDMLEDSNTQIEQLRKMMLSH--------EGVLQEIRSILVDFEEASGKkiYEHDSM 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 703 HCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELS-RELQEQEEVV 781
Cdd:pfam15921 211 STMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEiTGLTEKASSA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 782 SCTKLDLQNKSEILENIKQT--------LTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLA 853
Cdd:pfam15921 291 RSQANSIQSQLEIIQEQARNqnsmymrqLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 854 ELSTTKEKLSKVSDSLKNSKSEFEKENQKGK------------------------AAVLDLEKACKELKHQLQVQAESAL 909
Cdd:pfam15921 371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKrlwdrdtgnsitidhlrrelddrnMEVQRLEALLKAMKSECQGQMERQM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 910 KEQEDLKKSLEKEKETSQQL---KIELNSVKGEVSQAQNTLKQKEKdeqqlqgTINQLKQSAEQKKKQIEALQGEVknav 986
Cdd:pfam15921 451 AAIQGKNESLEKVSSLTAQLestKEMLRKVVEELTAKKMTLESSER-------TVSDLTASLQEKERAIEATNAEI---- 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 987 sqktvleNKLQQQSSQAAQELAAEKGKLSALQSNYEKCQAdlkqLQSDLYGKESELLATRQDLKSVEEkltlaqedlisn 1066
Cdd:pfam15921 520 -------TKLRSRVDLKLQELQHLKNEGDHLRNVQTECEA----LKLQMAEKDKVIEILRQQIENMTQ------------ 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1067 rnQIGNQNKSIQELQAAKASLEQDSAKKEALLKEqSKALEDAQ----REKSVKEKELVAEKSKLAEMEEIKCRQEKEITK 1142
Cdd:pfam15921 577 --LVGQHGRTAGAMQVEKAQLEKEINDRRLELQE-FKILKDKKdakiRELEARVSDLELEKVKLVNAGSERLRAVKDIKQ 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1143 LNEELKSHKQESIKEITNLKDAKQLL---IQQKLE--------LQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEF 1211
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNSLSEDYEVLkrnFRNKSEemetttnkLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1212 SEKEAK------LHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATV 1285
Cdd:pfam15921 734 KQITAKrgqidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
75-626 |
5.73e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 75 EAGLALTRDDITLLRQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEaqtenfni 154
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE-------- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 155 kqmkdlfeqkaaqLATEIADIKSKYDEEKSLRAAAEQKVThLTEDLNKQTTVIQDLKTELlqrpgiedvAVLKKELVQVQ 234
Cdd:PRK03918 271 -------------LKKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRL---------SRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 235 TLMDNMTlERERESEKLKDECKKLQSEHAHLEA------TINQLRSELAKGPQEVAVYvqEIQKLKGSINELTQKNQNLT 308
Cdd:PRK03918 328 ERIKELE-EKEERLEELKKKLKELEKRLEELEErhelyeEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 309 EKLQKKDLDYTHLEEKHNEESASRKTLQAS-----LHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELRE 383
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 384 VESTRQH------LKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEqrqlSSEKLMEKEQQVAD 457
Cdd:PRK03918 485 LEKVLKKeselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK----ELEKLEELKKKLAE 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 458 LQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKE 537
Cdd:PRK03918 561 LEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 538 SVSLLEKEREDLYAKIQAGEGEtavlnQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLhDQVQEQKAHLRAAQDRVL 617
Cdd:PRK03918 641 RLEELRKELEELEKKYSEEEYE-----ELREEYLELSRELAGLRAELEELEKRREEIKKTL-EKLKEELEEREKAKKELE 714
|
....*....
gi 50053824 618 SLETSVSEL 626
Cdd:PRK03918 715 KLEKALERV 723
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
238-533 |
6.00e-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: 47.43 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 238 DNMTLERERESEKLKDECKKLQSEhahleatinQLRSElakgpqEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDld 317
Cdd:pfam17380 340 ERMAMERERELERIRQEERKRELE---------RIRQE------EIAMEISRMRELERLQMERQQKNERVRQELEAAR-- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 318 ythlEEKHNEESASRKTLQASLHQRDLDCQQLQARltasesslqraQGELSEKAEAAQKLREELREVESTRQHlkvEVKQ 397
Cdd:pfam17380 403 ----KVKILEEERQRKIQQQKVEMEQIRAEQEEAR-----------QREVRRLEEERAREMERVRLEEQERQQ---QVER 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 398 LQQQREEKEQHGLQLQGEvsqlhckllETERQLGEahgrlKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNST 477
Cdd:pfam17380 465 LRQQEEERKRKKLELEKE---------KRDRKRAE-----EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIY 530
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50053824 478 ELQH----QLEKSKQQHQEQQALQQSATAKLREAQNDLE------QVLRQIGDKDQKIQNLEALLQ 533
Cdd:pfam17380 531 EEERrreaEEERRKQQEMEERRRIQEQMRKATEERSRLEamererEMMRQIVESEKARAEYEATTP 596
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
475-1043 |
6.78e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 475 NSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIG-------DKDQKIQNLEALLQKGKESVSLLEKERE 547
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINeisselpELREELEKLEKEVKELEELKEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 548 DLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLhdqvqEQKAHLRAAQDRVLSLETSVSELS 627
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI-----KLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 628 SQLNESKEKVSQLDIQIKAKTELLLSAEAakaaqradlqnhldtaqhaLQDKQQELNKVSVQLDQLTAKFQEKQEHCIQL 707
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKE-------------------LEKRLEELEERHELYEEAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 708 ESHLKDHKEKHL-SLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRElqEQEEVVSCTKL 786
Cdd:PRK03918 382 TGLTPEKLEKELeELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE--HRKELLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 787 DLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKtqHKELGDRMQAAVTELTAVKAQK-DALLAELSTTKEKLSKV 865
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK--LKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 866 SDSLKNSKSEFEKENQ-KGKAAVL-----DLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSqqlkIELNSVKGE 939
Cdd:PRK03918 538 KGEIKSLKKELEKLEElKKKLAELekkldELEEELAELLKELEELGFESVEELEERLKELEPFYNEY----LELKDAEKE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 940 VSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEvknaVSQKTvlENKLQQQSSQAAQELAAEKGKLSALQS 1019
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK----YSEEE--YEELREEYLELSRELAGLRAELEELEK 687
|
570 580
....*....|....*....|....*....
gi 50053824 1020 NYEKCQADLKQLQSDL-----YGKESELL 1043
Cdd:PRK03918 688 RREEIKKTLEKLKEELeerekAKKELEKL 716
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
329-534 |
7.90e-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: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 329 SASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQH 408
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 409 GLQLQGEVSQLHCKLLETERQ-------LGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQH 481
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 50053824 482 QLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQK 534
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
347-968 |
8.11e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 347 QQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLET 426
Cdd:TIGR00618 166 KELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 427 ERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLRE 506
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 507 AQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKN 586
Cdd:TIGR00618 326 LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 587 QSESHKQAEENLHDQV-QEQKAHLRA---AQDRVLSLETSVSELSSQ--------LNESKEKVSQLDIQIKAKTELLLSA 654
Cdd:TIGR00618 406 QREQATIDTRTSAFRDlQGQLAHAKKqqeLQQRYAELCAAAITCTAQceklekihLQESAQSLKEREQQLQTKEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 655 EAAKAAQRADLQNH-----------LDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQE-----HCIQLESHLKDHKEKH 718
Cdd:TIGR00618 486 TRKKAVVLARLLELqeepcplcgscIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEedvyhQLTSERKQRASLKEQM 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 719 LSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVScTKLDLQNKSEILENI 798
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQD-VRLHLQQCSQELALK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 799 KQTLTKKEEEnvVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEK 878
Cdd:TIGR00618 645 LTALHALQLT--LTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 879 ENQKGKAAVLDLE---KACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVsqaQNTLKQKEKDEQ 955
Cdd:TIGR00618 723 IENASSSLGSDLAareDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEI---QFFNRLREEDTH 799
|
650
....*....|...
gi 50053824 956 QLQGTINQLKQSA 968
Cdd:TIGR00618 800 LLKTLEAEIGQEI 812
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
137-534 |
9.27e-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: 46.81 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 137 LQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIK---SKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTE 213
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKeelRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 214 LLQRpgiedvavlKKELVQVQTLMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKL 293
Cdd:pfam07888 127 HEAR---------IRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 294 KGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQAslhqrdldcqqLQARLTASEsslqraqgelsekaEA 373
Cdd:pfam07888 198 RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRS-----------LQERLNASE--------------RK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 374 AQKLREELREVESTRQHLKVEVKQLQQQreekeqhglqlqgeVSQLHCKLLETERQLGEAHGRLKEQR---QLSSEKLME 450
Cdd:pfam07888 253 VEGLGEELSSMAAQRDRTQAELHQARLQ--------------AAQLTLQLADASLALREGRARWAQERetlQQSAEADKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 451 K-EQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLE 529
Cdd:pfam07888 319 RiEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLE 398
|
....*
gi 50053824 530 ALLQK 534
Cdd:pfam07888 399 QRLET 403
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
499-727 |
9.40e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 499 SATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQ--KGKESVSLLEKEREDLYAKIQAGEGEtavLNQLQEKNHALQQQ 576
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQ---LAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 577 LTQLTEKLKNQSESHKQAEENlhDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEA 656
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50053824 657 AKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEhciQLESHLKDHKEKHLSLEQKVED 727
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE---LYESLLQRLEEARLAEALTVGN 387
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
939-1185 |
1.24e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 939 EVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAvsqktvlenklqqqssqaAQELAAEKGKLSALQ 1018
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL------------------QAEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1019 SNYEKCQADLKQLQSDLYgkesellaTRQDLKSVEEKLTLAQ--EDLISNRNQI----GNQNKSIQELQAAKASLEQDSA 1092
Cdd:COG3883 79 AEIEERREELGERARALY--------RSGGSVSYLDVLLGSEsfSDFLDRLSALskiaDADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1093 KKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQK 1172
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250
....*....|...
gi 50053824 1173 LELQGRVDSLKAA 1185
Cdd:COG3883 231 AAAAAAAAAAAAA 243
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
82-638 |
1.37e-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: 46.55 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 82 RDDITLLRQEVQDLQASLKEEKwysEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQMKDLF 161
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENK---KNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 162 EQKAAQLATEIADIKSKYDEEKSLRAAA---EQKVTHLTEDLNKQTTVIQDLKTELLQRPgiEDVAVLKKELVQVQTLMD 238
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNKSLESQIselKKQNNQLKDNIEKKQQEINEKTTEISNTQ--TQLNQLKDEQNKIKKQLS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 239 NMTLERERESEKLKDECKKLQSEHAHLEA--------TINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEK 310
Cdd:TIGR04523 271 EKQKELEQNNKKIKELEKQLNQLKSEISDlnnqkeqdWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 311 LQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQH 390
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 391 LKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLqLKLSRLEEQLK 470
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL-KKLNEEKKELE 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 471 EKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQkIQNLEALLQKGKESVSLLEKEREDLY 550
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE-IDEKNKEIEELKQTQKSLKKKQEEKQ 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 551 AKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQL 630
Cdd:TIGR04523 589 ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKI 668
|
....*...
gi 50053824 631 NESKEKVS 638
Cdd:TIGR04523 669 KESKTKID 676
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
770-985 |
1.50e-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: 45.91 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 770 LSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQ---DSKTQHKELGDRMQAAVTELTAVKA 846
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriaALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 847 QKDALLAELSTTKEKLSKVSDSL-KNSKSEFEKE--NQKGKAAVLDLEKACKELKHQLQVQAE---SALKEQEDLKKSLE 920
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALyRLGRQPPLALllSPEDFLDAVRRLQYLKYLAPARREQAEelrADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50053824 921 KEKETSQQLKIELNSVKGEVSQAQN----TLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNA 985
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAerqkLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
241-480 |
1.62e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 241 TLERERES-----EKLKDECKKLQSEHAHLEATINQ-LRSELAKGP-QEVAVYVQEIQKLKGSINELTQKNQNLTEKLQK 313
Cdd:PRK04863 790 QLRAEREElaeryATLSFDVQKLQRLHQAFSRFIGShLAVAFEADPeAELRQLNRRRVELERALADHESQEQQQRSQLEQ 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 314 ---------------KDLDYTHLEEKHNE--------ESASR------------KTLQASLHQRDLDCQQLQARLTASES 358
Cdd:PRK04863 870 akeglsalnrllprlNLLADETLADRVEEireqldeaEEAKRfvqqhgnalaqlEPIVSVLQSDPEQFEQLKQDYQQAQQ 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 359 SLQR----------------------AQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEV 416
Cdd:PRK04863 950 TQRDakqqafaltevvqrrahfsyedAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY 1029
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50053824 417 SQLHCKLLETERQLGE--------AHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQ 480
Cdd:PRK04863 1030 DAKRQMLQELKQELQDlgvpadsgAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLE 1101
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
902-1175 |
1.98e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 902 QVQAESALKEQEDLKKSLEKEKETSQQlkielnsvkgevSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGE 981
Cdd:PRK11281 28 RAASNGDLPTEADVQAQLDALNKQKLL------------EAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 982 VKNAVSQKTVLENKLQQQSSQAAQELAaekgkLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQE 1061
Cdd:PRK11281 96 LRQAQAELEALKDDNDEETRETLSTLS-----LRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1062 DLISNRNQIGNQNKS--------IQELQAAKASLEQDSAKKEALLK--EQSKALEDAQReksvkekELVAEKSKlaemee 1131
Cdd:PRK11281 171 RLQQIRNLLKGGKVGgkalrpsqRVLLQAEQALLNAQNDLQRKSLEgnTQLQDLLQKQR-------DYLTARIQ------ 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 50053824 1132 ikcRQEKEITKL----NEELKSHKQESIKEITNLKDAKQL----LIQQKLEL 1175
Cdd:PRK11281 238 ---RLEHQLQLLqeaiNSKRLTLSEKTVQEAQSQDEAARIqanpLVAQELEI 286
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
440-649 |
1.99e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 440 QRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIG 519
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 520 DKDQKIQNLEALLqkgkESVSLlekerEDLYAKIQAgegetavLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLH 599
Cdd:COG3883 97 RSGGSVSYLDVLL----GSESF-----SDFLDRLSA-------LSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 50053824 600 DQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTE 649
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
437-648 |
2.06e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 437 LKEQRQLSSEKLMEKEQQVADLQLK--LSRLEEQLKEKVTNSTELQHQLEKSKqqhqeqqalqqsatAKLREAQNDLEQV 514
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEAR--------------AELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 515 LRQIGDKDQKIQNLEA--LLQKGKESVSLLEKEREDLYAKIQAGEGE-TAVLNQLQEKNHALQQQLTQLTEKLKNQSESH 591
Cdd:COG3206 246 RAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDvIALRAQIAALRAQLQQEAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 592 KQAEENLHDQVQEQKAHLR---AAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKT 648
Cdd:COG3206 326 QAREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYESLLQRLEEARLAEALTV 385
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
814-1320 |
2.06e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 814 QEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDA--LLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLE 891
Cdd:PRK02224 165 EEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 892 K---------ACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGE----------VSQAQNTLkqkEK 952
Cdd:PRK02224 245 EheerreeleTLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREEL---ED 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 953 DEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENK---LQQQSSQAAQELAAEKGKLSALQSNYEKCQA--- 1026
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEaaeLESELEEAREAVEDRREEIEELEEEIEELRErfg 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1027 ----DLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNR---------------------NQIGNQNKSIQELQ 1081
Cdd:PRK02224 402 dapvDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpvegsphvETIEEDRERVEELE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1082 AAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKsKLAEMEEIKCRQEKEITKLNE---ELKSHKQESIKEI 1158
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEE-LIAERRETIEEKRERAEELREraaELEAEAEEKREAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1159 TNLKDAKQLLIQQKLELQGRVDSLKAALEQ-EKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEK-EAGMKKHEENE 1236
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKLAELKERIESlERIRTLLAAIADAEDEIERLREKREALAELNDERRERlAEKRERKRELE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1237 AKLT-MQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQ---DERRALLERCLKGE---GEIEKL 1309
Cdd:PRK02224 641 AEFDeARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEelrERREALENRVEALEalyDEAEEL 720
|
570
....*....|.
gi 50053824 1310 QTKALELQRKL 1320
Cdd:PRK02224 721 ESMYGDLRAEL 731
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
867-1322 |
2.32e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 867 DSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAEsALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQN- 945
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 946 --TLKQKEKDEQQLQGTINQLKQsAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEkgkLSALQSNYEK 1023
Cdd:COG4717 128 lpLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1024 CQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQ-EDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQS 1102
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAAlEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1103 KALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAkqllIQQKLELQGRVDSL 1182
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR----IEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1183 KAALEQEKESQQlmREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEE--NEAKLTMQVTTLNENLGTVKKEWQSS 1260
Cdd:COG4717 360 EEELQLEELEQE--IAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEEL 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50053824 1261 QRRVSELEKQTDDLRGEIAVLEATVQNnqderrallercLKGEGEIEKLQTKALELQRKLDN 1322
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQ------------LEEDGELAELLQELEELKAELRE 487
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
504-1038 |
2.37e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 504 LREAQNDLEQVLRQIgDKDQKIQNLEALLQKGKESVSLLEKEREdlYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEK 583
Cdd:COG4913 237 LERAHEALEDAREQI-ELLEPIRELAERYAAARERLAELEYLRA--ALRLWFAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 584 LKNQSESHKQAEENLHDQVQEQKAhlraaqDRVLSLETSVSELSSQLNESKEKVSQLDiqikaktELLLSAEAAKAAQRA 663
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERELEERERRRARLE-------ALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 664 DLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVED----LEGHIKKLEADA 739
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAlrdaLAEALGLDEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 740 ------LEVKASKEQ--------------------ALQSLQQQRQLSTDLELR-NAELSRELQEQEEVVSCTKLDLQNKS 792
Cdd:COG4913 461 pfvgelIEVRPEEERwrgaiervlggfaltllvppEHYAAALRWVNRLHLRGRlVYERVRTGLPDPERPRLDPDSLAGKL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 793 EILEN-----IKQTLTKKEE----ENVvlkQEFEK---------LSQDSKTQHkELGDRMQAA---VTELTAvKAQKDAL 851
Cdd:COG4913 541 DFKPHpfrawLEAELGRRFDyvcvDSP---EELRRhpraitragQVKGNGTRH-EKDDRRRIRsryVLGFDN-RAKLAAL 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 852 LAELSTTKEKLSKVSDSLKNSKSEfEKENQKGKAAVLDLEKACKElkhqlQVQAESALKEQEDLKKSLEKEKETSQQLKi 931
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAE-LDALQERREALQRLAEYSWD-----EIDVASAEREIAELEAELERLDASSDDLA- 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 932 elnSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEK 1011
Cdd:COG4913 689 ---ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVER 765
|
570 580
....*....|....*....|....*..
gi 50053824 1012 GKLSALQSNYEKCQADLKQLQSDLYGK 1038
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERA 792
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
332-640 |
2.58e-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: 45.71 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 332 RKTLQASLHQRDlDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELrevESTRQHLKVEVKQLQQQreEKEQHglq 411
Cdd:COG3096 281 RELSERALELRR-ELFGARRQLAEEQYRLVEMARELEELSARESDLEQDY---QAASDHLNLVQTALRQQ--EKIER--- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 412 LQGEVSQLHCKLLETERQLGEAHgrlkEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQ---HQLEKSKQ 488
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAA----EQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQqavQALEKARA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 489 QHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEK-----EREDLY------------A 551
Cdd:COG3096 428 LCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKiagevERSQAWqtarellrryrsQ 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 552 KIQAGEGET--AVLNQLqEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQ 629
Cdd:COG3096 508 QALAQRLQQlrAQLAEL-EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
330
....*....|.
gi 50053824 630 LNESKEKVSQL 640
Cdd:COG3096 587 LEQLRARIKEL 597
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
394-981 |
3.30e-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: 45.10 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 394 EVKQLQQQREEKEQHGLQLQGEVSQLHCKL----LETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQL 469
Cdd:pfam05483 170 KTKKYEYEREETRQVYMDLNNNIEKMILAFeelrVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 470 KEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQN-------LEALLQKGKESVSLL 542
Cdd:pfam05483 250 TEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRsmstqkaLEEDLQIATKTICQL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 543 EKEREDLYAKI-QAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLET 621
Cdd:pfam05483 330 TEEKEAQMEELnKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 622 SVSELSSQ--LNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQE 699
Cdd:pfam05483 410 LKKILAEDekLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 700 KQEHCIQLESHLKDhkekhlsLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEE 779
Cdd:pfam05483 490 LTAHCDKLLLENKE-------LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGD 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 780 VVSCT--KLDLQNKSEILENIKQTLTKKEEENVV--LKQEFEKLSQDSKTQHKE---LGDRMQAAVTELTAVKAQKDALL 852
Cdd:pfam05483 563 EVKCKldKSEENARSIEYEVLKKEKQMKILENKCnnLKKQIENKNKNIEELHQEnkaLKKKGSAENKQLNAYEIKVNKLE 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 853 AELSTTKEKLSKVSDslkNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIE 932
Cdd:pfam05483 643 LELASAKQKFEEIID---NYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKI 719
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 50053824 933 LNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGE 981
Cdd:pfam05483 720 IEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEE 768
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
372-616 |
3.47e-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: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 372 EAAQKLREELREVESTRQhlkvEVKQLQQQREekeqhglqlqgevsqlhckLLETERQLGEAHGRLKEQRQLSSEklMEK 451
Cdd:COG4913 225 EAADALVEHFDDLERAHE----ALEDAREQIE-------------------LLEPIRELAERYAAARERLAELEY--LRA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 452 EQQVADLQLKLSRLEEQLkekvtnsTELQHQLEKSKQQHQEQQALQQSATAKLREaqndLEQVLRQIGdkDQKIQNLEAL 531
Cdd:COG4913 280 ALRLWFAQRRLELLEAEL-------EELRAELARLEAELERLEARLDALREELDE----LEAQIRGNG--GDRLEQLERE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 532 LQKGKESVSLLEKEREDLYAKIQA----GEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENL---HDQVQE 604
Cdd:COG4913 347 IERLERELEERERRRARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLrreLRELEA 426
|
250
....*....|..
gi 50053824 605 QKAHLRAAQDRV 616
Cdd:COG4913 427 EIASLERRKSNI 438
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
281-815 |
3.60e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 281 QEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDldythleeKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSL 360
Cdd:pfam10174 185 RRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRN--------QLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 361 Q--RAQGELSekaeaAQKLREELREVESTRQH---LKVEVKQLQQQREEKEQHGLQLQGEvsqlhcklLETerqLGEAHG 435
Cdd:pfam10174 257 QmlKTNGLLH-----TEDREEEIKQMEVYKSHskfMKNKIDQLKQELSKKESELLALQTK--------LET---LTNQNS 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 436 RLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKskqqhqeQQALQQSATAKLREAQNDLEQVL 515
Cdd:pfam10174 321 DCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQD-------LTEEKSTLAGEIRDLKDMLDVKE 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 516 RQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQ-LQEKN---HALQQQLTQLTEKLKNQSESH 591
Cdd:pfam10174 394 RKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEaLSEKEriiERLKEQREREDRERLEELESL 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 592 KQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTE---------LLLSAEAAKAAQR 662
Cdd:pfam10174 474 KKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEecsklenqlKKAHNAEEAVRTN 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 663 ADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQE-------KQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKL 735
Cdd:pfam10174 554 PEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREvenekndKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKK 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 736 EADALEvKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQE 815
Cdd:pfam10174 634 GAQLLE-EARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQE 712
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
86-595 |
4.40e-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: 44.96 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 86 TLLRQEVQDLQASlKEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQMKDLFEQKA 165
Cdd:TIGR00618 349 TLHSQEIHIRDAH-EVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 166 AQLATEIADIKSKY------DEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRPGIEDVAVLKKELVQV------ 233
Cdd:TIGR00618 428 HAKKQQELQQRYAElcaaaiTCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEepcplc 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 234 -QTLMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQ 312
Cdd:TIGR00618 508 gSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 313 K----KDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTR 388
Cdd:TIGR00618 588 NlqniTVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSI 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 389 QHLKVEVKQLQQQREEKEQHGLQ----LQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSR 464
Cdd:TIGR00618 668 RVLPKELLASRQLALQKMQSEKEqltyWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKE 747
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 465 LEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKI-QNLEALLQKGKESVSLLE 543
Cdd:TIGR00618 748 LMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIgQEIPSDEDILNLQCETLV 827
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 50053824 544 KEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAE 595
Cdd:TIGR00618 828 QEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
76-314 |
4.41e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 76 AGLALTRDDITLLRQEVQDLQASLKEEKwysEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQtenfniK 155
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELE---KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE------A 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 156 QMKDLfEQKAAQLATEIADIKSKYdeEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRPGIEDVAVLKKELVQVQT 235
Cdd:COG4942 84 ELAEL-EKEIAELRAELEAQKEEL--AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50053824 236 LMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKK 314
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
510-1131 |
4.42e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.83 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 510 DLEQVLRQIGDKDQKIQNLEallQKGKESVSLLEKEReDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNqse 589
Cdd:pfam12128 197 DVKSMIVAILEDDGVVPPKS---RLNRQQVEHWIRDI-QAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKS--- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 590 sHKQAEENLHDQVQEQKAHLRaaqDRVLSLETSVSELSSQLNESKekvSQLDIQIKAKTELLLSAEAAKAAQRADLQNHL 669
Cdd:pfam12128 270 -DETLIASRQEERQETSAELN---QLLRTLDDQWKEKRDELNGEL---SAADAAVAKDRSELEALEDQHGAFLDADIETA 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 670 DTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLS-LEQKVEDLEGHIKKLEA------DALEv 742
Cdd:pfam12128 343 AADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAgIKDKLAKIREARDRQLAvaeddlQALE- 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 743 KASKEQALQSLQQQRQLSTDLELRNAELsRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQD 822
Cdd:pfam12128 422 SELREQLEAGKLEFNEEEYRLKSRLGEL-KLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKR 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 823 SKTQHKELGD---RMQAAVTELTAVKAQKDA----LLAELSTT----KEKLSKVSDSLKNSKS----EFEKENQKGKAAV 887
Cdd:pfam12128 501 RDQASEALRQasrRLEERQSALDELELQLFPqagtLLHFLRKEapdwEQSIGKVISPELLHRTdldpEVWDGSVGGELNL 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 888 LDLEKACKELKHQLQVQAESALKEQED-LKKSLEKEKETSQQLKIELNSVKGEVSQAQ-------NTLKQKEKDEQQLQG 959
Cdd:pfam12128 581 YGVKLDLKRIDVPEWAASEEELRERLDkAEEALQSAREKQAAAEEQLVQANGELEKASreetfarTALKNARLDLRRLFD 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 960 TINQLK-QSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQEL-------------------AAEKGKLSALQS 1019
Cdd:pfam12128 661 EKQSEKdKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKreartekqaywqvvegaldAQLALLKAAIAA 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1020 NYEKCQADLKQLQS----DLYGK---ESELLATRQDLKSVEEKLTLAQED---------------LISNRN---QIGNQN 1074
Cdd:pfam12128 741 RRSGAKAELKALETwykrDLASLgvdPDVIAKLKREIRTLERKIERIAVRrqevlryfdwyqetwLQRRPRlatQLSNIE 820
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 50053824 1075 KSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEE 1131
Cdd:pfam12128 821 RAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKE 877
|
|
| FYVE_CARP2 |
cd15770 |
FYVE-like domain found in caspase regulator CARP2 and similar proteins; CARP2, also termed E3 ... |
1356-1394 |
4.43e-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: 39.44 E-value: 4.43e-04
10 20 30
....*....|....*....|....*....|....*....
gi 50053824 1356 QNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPS 1394
Cdd:cd15770 2 ISCKACGIRFASCARKHPCMDCKKNYCTACSSQAENGPS 40
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
245-486 |
4.59e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 245 ERESEKLKDECKKLQSEHAHLEATINQLR--SELAKGPQEVAVYVQEIQKLKGSINELTQKN---QNLTEKLQKKDLDYT 319
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASSddlAALEEQLEELEAELE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 320 HLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVestRQHLKVEVKQLQ 399
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL---RENLEERIDALR 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 400 QQREEKEQHGLQLQGE-VSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQqvadlqlklsRLEEQLKEKVTNS-T 477
Cdd:COG4913 780 ARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYEE----------RFKELLNENSIEFvA 849
|
....*....
gi 50053824 478 ELQHQLEKS 486
Cdd:COG4913 850 DLLSKLRRA 858
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
544-1333 |
4.68e-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: 45.04 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 544 KEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEK-LKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETS 622
Cdd:TIGR00606 255 KEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 623 VSELSSQLNESKEKVSQLdiQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQE 702
Cdd:TIGR00606 335 RRLLNQEKTELLVEQGRL--QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 703 HCIQLESHLKDHKEKHLSLEQKVEDLeGHIKKLEADALEVKAS------KEQALQSLQQQRQLSTDLELRNAELSRELQE 776
Cdd:TIGR00606 413 LCADLQSKERLKQEQADEIRDEKKGL-GRTIELKKEILEKKQEelkfviKELQQLEGSSDRILELDQELRKAERELSKAE 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 777 QEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEklsqdSKTQHKELGDRMQAAVTELTAVKAQKDALLAELS 856
Cdd:TIGR00606 492 KNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTT-----TRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 857 ---TTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKkslekEKETSQQLKIEL 933
Cdd:TIGR00606 567 gyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLF-----DVCGSQDEESDL 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 934 NSVKGEvsqaqntLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLE---NKLQQQSSQAAQELAAE 1010
Cdd:TIGR00606 642 ERLKEE-------IEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQefiSDLQSKLRLAPDKLKST 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1011 KGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKsiqELQAAKASLEQD 1090
Cdd:TIGR00606 715 ESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMP---EEESAKVCLTDV 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1091 SAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQ 1170
Cdd:TIGR00606 792 TIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKS 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1171 QKLELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEaKLTMQVTTLNENL 1250
Cdd:TIGR00606 872 EKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK-KAQDKVNDIKEKV 950
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1251 GTVKKEWQSSQRRVSE-LEKQTDDLRGEIAVLEATVQNNQDERRALLE--RCLKGEGEIEKLQTKALELQRKLDNTTAAV 1327
Cdd:TIGR00606 951 KNIHGYMKDIENKIQDgKDDYLKQKETELNTVNAQLEECEKHQEKINEdmRLMRQDIDTQKIQERWLQDNLTLRKRENEL 1030
|
....*.
gi 50053824 1328 QELGRE 1333
Cdd:TIGR00606 1031 KEVEEE 1036
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
874-1342 |
5.21e-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: 44.71 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 874 SEFEKENQKGKAAVLDLEKACKELK---HQLQVQAESA-LKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQ 949
Cdd:pfam05483 172 KKYEYEREETRQVYMDLNNNIEKMIlafEELRVQAENArLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 950 KEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKgklsALQSNYEKCQADLK 1029
Cdd:pfam05483 252 KENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQK----ALEEDLQIATKTIC 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1030 QLQSDLYGKESELLATRQDLKSVEEKL---TLAQEDLISNRNQIGNQNKSIQELQAAKasleqdsakkealLKEQSKALE 1106
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSFVVTEFeatTCSLEELLRTEQQRLEKNEDQLKIITME-------------LQKKSSELE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1107 DAQREKSVKEKELVAEKSKLAEMEEIkCRQEKEITKLNEELKSHKQESI-------KEITNLKDAKQLLIQQKLELQGRV 1179
Cdd:pfam05483 395 EMTKFKNNKEVELEELKKILAEDEKL-LDEKKQFEKIAEELKGKEQELIfllqareKEIHDLEIQLTAIKTSEEHYLKEV 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1180 DSLKAALEQEKeSQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQS 1259
Cdd:pfam05483 474 EDLKTELEKEK-LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELES 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1260 SQRrvsELEKQTDDLRGEIavleatvQNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQI 1339
Cdd:pfam05483 553 VRE---EFIQKGDEVKCKL-------DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
...
gi 50053824 1340 KHT 1342
Cdd:pfam05483 623 KGS 625
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
287-607 |
5.33e-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: 44.29 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 287 VQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQrdldcqqLQARLTASESSLQRAQGE 366
Cdd:pfam19220 40 LRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAK-------LEAALREAEAAKEELRIE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 367 LSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSE 446
Cdd:pfam19220 113 LRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 447 ---KLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQS----ATAKLREAQNDLEQVLRQIG 519
Cdd:pfam19220 193 ltrRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMkleaLTARAAATEQLLAEARNQLR 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 520 DKDQKIQNLEALLQKG-------KESVSLLEKEREDLYAKIQ------------------AGEGETAVLNQLQEKNHALQ 574
Cdd:pfam19220 273 DRDEAIRAAERRLKEAsierdtlERRLAGLEADLERRTQQFQemqraraeleeraemltkALAAKDAALERAEERIASLS 352
|
330 340 350
....*....|....*....|....*....|...
gi 50053824 575 QQLTQLTEKLKNQSESHKQAEENLHDQVQEQKA 607
Cdd:pfam19220 353 DRIAELTKRFEVERAALEQANRRLKEELQRERA 385
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
677-983 |
5.43e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.51 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 677 QDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDhkeKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQ 756
Cdd:PLN02939 45 QQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLR---TVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 757 RQLSTDLEL-------RNAELS---------RELQEQEEVVScTKLDLQNKSEILE------NIKQTLTKKEEENV-VLK 813
Cdd:PLN02939 122 GEQLSDFQLedlvgmiQNAEKNilllnqarlQALEDLEKILT-EKEALQGKINILEmrlsetDARIKLAAQEKIHVeILE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 814 QEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSlKNSKSEFEKENQKGKAAVLDLEka 893
Cdd:PLN02939 201 EQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAET-EERVFKLEKERSLLDASLRELE-- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 894 CKELKHQLQVQAESALKEQedlkkSLEKEKETSQQLkieLNSVKGEVSQAQNTLKQkekdEQQLQGTINQLKQSAEQKK- 972
Cdd:PLN02939 278 SKFIVAQEDVSKLSPLQYD-----CWWEKVENLQDL---LDRATNQVEKAALVLDQ----NQDLRDKVDKLEASLKEANv 345
|
330
....*....|....*.
gi 50053824 973 -----KQIEALQGEVK 983
Cdd:PLN02939 346 skfssYKVELLQQKLK 361
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
928-1152 |
6.00e-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: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 928 QLKIELNSVKGEVSQ---AQNTLKQKEKDEQQLQgtinQLKQSAEQKKKQIEALQGEVKNavSQKTVLENK-------LQ 997
Cdd:NF012221 1539 ESSQQADAVSKHAKQddaAQNALADKERAEADRQ----RLEQEKQQQLAAISGSQSQLES--TDQNALETNgqaqrdaIL 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 998 QQSSQAAQELAAEKGKLSAL--QSNYEKCQAD----------LKQLQSDLygkesellatrQDLKS-VEEKLTLAQEDLI 1064
Cdd:NF012221 1613 EESRAVTKELTTLAQGLDALdsQATYAGESGDqwrnpfagglLDRVQEQL-----------DDAKKiSGKQLADAKQRHV 1681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1065 SNRNQI-------------GNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEK-SKLAEME 1130
Cdd:NF012221 1682 DNQQKVkdavakseagvaqGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQdASAAENK 1761
|
250 260
....*....|....*....|..
gi 50053824 1131 EIKCRQEKEITKLNEELKSHKQ 1152
Cdd:NF012221 1762 ANQAQADAKGAKQDESDKPNRQ 1783
|
|
| FYVE_CARP1 |
cd15769 |
FYVE-like domain found in caspase regulator CARP1 and similar proteins; CARP1, also termed E3 ... |
1358-1405 |
6.29e-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: 38.82 E-value: 6.29e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 50053824 1358 CMSCGKCFSVTVRRHHCRQCGNIFCAECSTknaltpsSKKPVRVCDAC 1405
Cdd:cd15769 4 CKACGLAFSVFRKKHVCCDCKKDFCSVCSV-------LQENLRRCSTC 44
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
672-924 |
6.51e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 672 AQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADalevkaskeqalq 751
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 752 slqqqrqlSTDLELRNAELSRELQEQEEVVsctkldlqnkSEILENIkQTLTKKEEENVVLKQEFEKLSQDSKTQHKELG 831
Cdd:COG4942 85 --------LAELEKEIAELRAELEAQKEEL----------AELLRAL-YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 832 DRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESAlKE 911
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA-EE 224
|
250
....*....|...
gi 50053824 912 QEDLKKSLEKEKE 924
Cdd:COG4942 225 LEALIARLEAEAA 237
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1079-1356 |
6.65e-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: 44.29 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1079 ELQAAKASLE---QDSAKKEALLKEQSKALEDAQREKSVKEK--ELVAEKSKlaemeeikcRQEKEITKLNEELKSHKQE 1153
Cdd:TIGR02169 171 KKEKALEELEeveENIERLDLIIDEKRQQLERLRREREKAERyqALLKEKRE---------YEGYELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1154 SIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHE 1233
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1234 ENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKA 1313
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 50053824 1314 LELQRKLDNttaaVQELGRENQSLQIKHTQALNRKWAEDNEVQ 1356
Cdd:TIGR02169 402 NELKRELDR----LQEELQRLSEELADLNAAIAGIEAKINELE 440
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
291-720 |
7.27e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 291 QKLKGSINELTQKNQNLTEKLQKKDlDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASE--SSLQRAQGELS 368
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 369 EKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKL 448
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 449 MEKEQQVADLQLKLSR--LEEQLKEK-----------------VTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQN 509
Cdd:COG4717 223 EELEEELEQLENELEAaaLEERLKEArlllliaaallallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 510 DLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQE--KNHALQQQLTQLTEKLKNQ 587
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 588 SESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNES--KEKVSQLDIQIKAKTELLLSAEAAKAAQRADL 665
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 50053824 666 QNHLDtaQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLS 720
Cdd:COG4717 463 EQLEE--DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
960-1189 |
7.43e-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: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 960 TINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQsdlygke 1039
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLE------- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1040 sellatrQDLKSVEEKLTLAQEDLISNRNQI-GNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKE 1118
Cdd:COG4913 309 -------AELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50053824 1119 LVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQE 1189
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
903-1109 |
7.50e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 903 VQAESALKEQEDLKKSLEKEKETSQQlkiELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEV 982
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQA---ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 983 KNAVS-------------------------QKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYG 1037
Cdd:COG3883 89 GERARalyrsggsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50053824 1038 KESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQ 1109
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
793-1197 |
9.55e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 793 EILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNS 872
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 873 ksEFEKENQKGKAAVLDLEKACKELKHQLQVQAEsALKEQEDLKKSLEKEKETSQQLKIELN-SVKGEVSQAQNTLKQKE 951
Cdd:COG4717 129 --PLYQELEALEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 952 KDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNY---------- 1021
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIagvlflvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1022 ------------EKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQ 1089
Cdd:COG4717 286 lallflllarekASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1090 DSAKKE--ALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEikcRQEKEITKLNEELKSHKQESIK-EITNLKDAKQ 1166
Cdd:COG4717 366 EELEQEiaALLAEAGVEDEEELRAALEQAEEYQELKEELEELEE---QLEELLGELEELLEALDEEELEeELEELEEELE 442
|
410 420 430
....*....|....*....|....*....|.
gi 50053824 1167 LLIQQKLELQGRVDSLKAALEQEKESQQLMR 1197
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
890-1063 |
1.04e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 890 LEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLK----IELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLK 965
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEALLAALG 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 966 QSAEQKKKQIEALQGEVKNAVSQktvlenkLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQS--DLYgkESELL 1043
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEA-------LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrkSNI--PARLL 443
|
170 180
....*....|....*....|
gi 50053824 1044 ATRQDLksvEEKLTLAQEDL 1063
Cdd:COG4913 444 ALRDAL---AEALGLDEAEL 460
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
135-568 |
1.11e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 135 AELQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAE-----QKVTHLTEDLNKQTTVIQD 209
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 210 LKTELLQ-RPGIEDVAVLKKELVQVQTLMDNmtlERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQ 288
Cdd:COG4717 151 LEERLEElRELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 289 EIQKLKGSINELTQKNQNLTEKLQKKD---------------------------------LDYTHLEEKHNEESASRKTL 335
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLLLIaaallallglggsllsliltiagvlflvlgllaLLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 336 QASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQhlkvevkQLQQQREEKEQHGLQLQGE 415
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE-------ELQLEELEQEIAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 416 VsqlhckllETERQLGEAHGRLKEQRQLsseklmEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEkskqqhqeqqa 495
Cdd:COG4717 381 V--------EDEEELRAALEQAEEYQEL------KEELEELEEQLEELLGELEELLEALDEEELEEELE----------- 435
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50053824 496 lqqSATAKLREAQNDLEQVLRQIGDKDQKIQNLEallqkGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQE 568
Cdd:COG4717 436 ---ELEEELEELEEELEELREELAELEAELEQLE-----EDGELAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1083-1240 |
1.12e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1083 AKASLEQDSAKKEALL---KEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEIT 1159
Cdd:PRK12704 45 EEAKKEAEAIKKEALLeakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1160 NL----KDAKQLLIQQKLELQgRVdslkAALEQEKESQQLMReqvkkeeekrkeefsekeaKLHSEIKEKEAGMKKHEEN 1235
Cdd:PRK12704 125 ELekkeEELEELIEEQLQELE-RI----SGLTAEEAKEILLE-------------------KVEEEARHEAAVLIKEIEE 180
|
....*
gi 50053824 1236 EAKLT 1240
Cdd:PRK12704 181 EAKEE 185
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
366-609 |
1.16e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 366 ELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQlQGEVSQLhckllETERQLGEAHGRLKEQRQLSS 445
Cdd:COG0497 159 EYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQ-PGEEEEL-----EEERRRLSNAEKLREALQEAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 446 EKLMEKEQQVADLqlkLSRLEEQLKEKVTNSTELQHQLEkskqqhqeqqaLQQSATAKLREAQNDLEQVLRQI------- 518
Cdd:COG0497 233 EALSGGEGGALDL---LGQALRALERLAEYDPSLAELAE-----------RLESALIELEEAASELRRYLDSLefdperl 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 519 GDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLknqSESHKQAEENL 598
Cdd:COG0497 299 EEVEERLALLRRLARKYGVTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKL---SAARKKAAKKL 375
|
250
....*....|.
gi 50053824 599 HDQVQEQKAHL 609
Cdd:COG0497 376 EKAVTAELADL 386
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
422-1156 |
1.48e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 422 KLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLkekvtnstELQHQLEKSKQQHQEQQALQQSAT 501
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQL--------ESSREIVKSYENELDPLKNRLKEI 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 502 AKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSL-LEKEREDLY----AKIQAGEGETAVLNQLQEKNHALQQQ 576
Cdd:TIGR00606 258 EHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQgTDEQLNDLYhnhqRTVREKERELVDCQRELEKLNKERRL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 577 LTQLTEKLKNQseshkqaEENLHDQVQEQKAHLRAAQDRVLSLETSvSELSSqLNESKEKVSQLDIQIKAKTELLLSAEA 656
Cdd:TIGR00606 338 LNQEKTELLVE-------QGRLQLQADRHQEHIRARDSLIQSLATR-LELDG-FERGPFSERQIKNFHTLVIERQEDEAK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 657 AKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQE---HCIQLESHLKDHKEKHLSLEQKVEDLEGHIK 733
Cdd:TIGR00606 409 TAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEelkFVIKELQQLEGSSDRILELDQELRKAERELS 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 734 KLEADALEVKASKEQALQSLQQQRQLST--DLELRNAELSRELQEQEEVVSCTKldlqNKSEILENIKQTLTKKEEENVV 811
Cdd:TIGR00606 489 KAEKNSLTETLKKEVKSLQNEKADLDRKlrKLDQEMEQLNHHTTTRTQMEMLTK----DKMDKDEQIRKIKSRHSDELTS 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 812 LKQEFEKLSQDSKTQH------KELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKA 885
Cdd:TIGR00606 565 LLGYFPNKKQLEDWLHskskeiNQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERL 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 886 AVlDLEKACKELK-------------HQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEK 952
Cdd:TIGR00606 645 KE-EIEKSSKQRAmlagatavysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEK 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 953 DEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEK---------GKLSALQSNYEK 1023
Cdd:TIGR00606 724 RRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEEsakvcltdvTIMERFQMELKD 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1024 CQADLKQLQSDLYGKESELLAT--RQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLkEQ 1101
Cdd:TIGR00606 804 VERKIAQQAAKLQGSDLDRTVQqvNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNL-QR 882
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 50053824 1102 SKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIK 1156
Cdd:TIGR00606 883 RQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK 937
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
890-1187 |
1.48e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 890 LEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAE 969
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 970 QKKKQIEALQGEVKNAVSQKTVLE---NKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATR 1046
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1047 QD--LKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKS 1124
Cdd:COG4372 185 LDelLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50053824 1125 KLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALE 1187
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
366-991 |
1.49e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 366 ELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSS 445
Cdd:PRK01156 160 EINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 446 EKlmekeQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKI 525
Cdd:PRK01156 240 AL-----NELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQIL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 526 QNLEALLQKGKESV---SLLEKEREDLYAKIQAGEGETAVLNQLQEkNHALQQQLTQLTEKLKNQSESHKQAEENLHDQV 602
Cdd:PRK01156 315 SNIDAEINKYHAIIkklSVLQKDYNDYIKKKSRYDDLNNQILELEG-YEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 603 QEQKAHLRAAQDRVLSLetsVSELSSQLNESKEKVSQLDIQIKAktelLLSAEAAKAAQRADLQNH-----------LDT 671
Cdd:PRK01156 394 SEILKIQEIDPDAIKKE---LNEINVKLQDISSKVSSLNQRIRA----LRENLDELSRNMEMLNGQsvcpvcgttlgEEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 672 AQHALQDKQQELNKVSVQLDQL---TAKFQEKQEHCIQLESHLKDHK-EKHLSLEQKVEDLEGHIKKLEADALEVKaske 747
Cdd:PRK01156 467 SNHIINHYNEKKSRLEEKIREIeieVKDIDEKIVDLKKRKEYLESEEiNKSINEYNKIESARADLEDIKIKINELK---- 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 748 qalqslqqqrqlstdlelrNAELSRElQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVvlkqefEKLSQDSKTQH 827
Cdd:PRK01156 543 -------------------DKHDKYE-EIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETN------RSRSNEIKKQL 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 828 KELGDRMQAAVTELTAVKaqkdallaelSTTKEKLSKVSDSLKNSKSEFeKENQKGKAAVLDLEKACKELKHQLQvQAES 907
Cdd:PRK01156 597 NDLESRLQEIEIGFPDDK----------SYIDKSIREIENEANNLNNKY-NEIQENKILIEKLRGKIDNYKKQIA-EIDS 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 908 ALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQ--GEVKNA 985
Cdd:PRK01156 665 IIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGdlKRLREA 744
|
....*.
gi 50053824 986 VSQKTV 991
Cdd:PRK01156 745 FDKSGV 750
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
560-773 |
1.69e-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: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 560 TAVLNQLQEKNHALQQQLTQLTEKLKNQseshKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQ 639
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 640 LDIQIKAKTELLLSAEAAKAAQRA--------------DLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCI 705
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50053824 706 QLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRE 773
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
92-579 |
1.74e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 92 VQDLQASLK--EEKwysEELKKELEKyqgLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQMKDLfEQKAAQLA 169
Cdd:PRK11281 62 QQDLEQTLAllDKI---DRQKEETEQ---LKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLRQL-ESRLAQTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 170 TEIADIkskydeEKSLRAAAEQKVTHLTEDLNKQTTViqdlkTELLQRpgiedvavlkkeLVQVQTLMDNMTLERERESE 249
Cdd:PRK11281 135 DQLQNA------QNDLAEYNSQLVSLQTQPERAQAAL-----YANSQR------------LQQIRNLLKGGKVGGKALRP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 250 KLKDeckKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLdythleekhneeS 329
Cdd:PRK11281 192 SQRV---LLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRL------------T 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 330 ASRKTLQASLHQRDLdcQQLQA-RLTASESSLQRaqgELSEK-AEAAQKLReelrevESTRQHLKveVKQ-----LQQQR 402
Cdd:PRK11281 257 LSEKTVQEAQSQDEA--ARIQAnPLVAQELEINL---QLSQRlLKATEKLN------TLTQQNLR--VKNwldrlTQSER 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 403 EEKEQHGLqLQGevSQLHCKLLeterqlgeahgrLKEQRQLSSEKLMEK-EQQVADLQLKLSRLEEQlKEKVTNSTELQH 481
Cdd:PRK11281 324 NIKEQISV-LKG--SLLLSRIL------------YQQQQALPSADLIEGlADRIADLRLEQFEINQQ-RDALFQPDAYID 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 482 QLEKSkqqhqeqqaLQQSATAKLREAQNDLEQVLRQIgdKDQKIQNLEALLQkgkESVSLlekeredlyakiqagegeta 561
Cdd:PRK11281 388 KLEAG---------HKSEVTDEVRDALLQLLDERREL--LDQLNKQLNNQLN---LAINL-------------------- 433
|
490 500
....*....|....*....|
gi 50053824 562 VLN--QLQEKNHALQQQLTQ 579
Cdd:PRK11281 434 QLNqqQLLSVSDSLQSTLTQ 453
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
291-593 |
1.83e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 291 QKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEK 370
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 371 AEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLME 450
Cdd:COG4372 100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 451 KEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEA 530
Cdd:COG4372 180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50053824 531 LLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQ 593
Cdd:COG4372 260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1078-1171 |
1.87e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1078 QELQAAKASLEQDSAKKEALLKEQSKALEdaQREKSVKEK--ELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESI 1155
Cdd:PRK12704 64 EEIHKLRNEFEKELRERRNELQKLEKRLL--QKEENLDRKleLLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQL 141
|
90 100
....*....|....*....|.
gi 50053824 1156 KE---ITNL--KDAKQLLIQQ 1171
Cdd:PRK12704 142 QElerISGLtaEEAKEILLEK 162
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
715-1357 |
1.87e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 715 KEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEI 794
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 795 LENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELtavkaQKDALLAELSTTKEKLSKVSDSLKNSKS 874
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL-----KSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 875 EFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDE 954
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 955 QQLQGTINQLKQSAEQKKKQIEALQGEVKnavsQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSD 1034
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKEELEILEEE----EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1035 LYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSV 1114
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1115 KEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQ 1194
Cdd:pfam02463 563 RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1195 LMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQS---SQRRVSELEKQT 1271
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRekeELKKLKLEAEEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1272 DDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQIKHTQALNRKWAE 1351
Cdd:pfam02463 723 LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE 802
|
....*.
gi 50053824 1352 DNEVQN 1357
Cdd:pfam02463 803 LRALEE 808
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
907-1185 |
2.00e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 907 SALKEQEDLKKSLEKEKETSQQLKIELNSVK-------GEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEAlq 979
Cdd:COG5022 814 SYLACIIKLQKTIKREKKLRETEEVEFSLKAevliqkfGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDV-- 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 980 GEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKC--QADLKQLQSDLYGKESELlatrQDLKSVEEKLT 1057
Cdd:COG5022 892 KSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLlnNIDLEEGPSIEYVKLPEL----NKLHEVESKLK 967
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1058 LAQED----LISNRNQIGNQNKSIQELQAAKASLEQDSAKKEAlLKEQSKALEDAQREKSVKE------KELVAEKSKLA 1127
Cdd:COG5022 968 ETSEEyedlLKKSTILVREGNKANSELKNFKKELAELSKQYGA-LQESTKQLKELPVEVAELQsaskiiSSESTELSILK 1046
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 50053824 1128 EMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAA 1185
Cdd:COG5022 1047 PLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVT 1104
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
878-1227 |
2.20e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 878 KENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQL 957
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 958 QGTINQLKQSAEQKKKQIEALQGEVKNAvsqktvlenklqqqssqaAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYG 1037
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEEL------------------QEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1038 KESELLATRQDLKSVEEKLTLAQEDLiSNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEK 1117
Cdd:COG4372 148 REEELKELEEQLESLQEELAALEQEL-QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1118 ELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMR 1197
Cdd:COG4372 227 LEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAA 306
|
330 340 350
....*....|....*....|....*....|
gi 50053824 1198 EQVKKEEEKRKEEFSEKEAKLHSEIKEKEA 1227
Cdd:COG4372 307 LSLIGALEDALLAALLELAKKLELALAILL 336
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
560-1224 |
2.33e-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: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 560 TAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQ 639
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQ 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 640 LDIQIKAKTELLLSAEAAKAAQRADLQNH------LDTAQHALQDKQQELNKVSVQLDQlTAKFQEKQEHCIQLESHLKD 713
Cdd:TIGR00618 305 IEQQAQRIHTELQSKMRSRAKLLMKRAAHvkqqssIEEQRRLLQTLHSQEIHIRDAHEV-ATSIREISCQQHTLTQHIHT 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 714 HKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSE 793
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 794 ILENIKQTLTKKEEENVVLKQEFEKlsQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLskvsdslknsk 873
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQETRK--KAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRM----------- 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 874 sefekenQKGKAAVLDLEKACKELKHQLQvqaeSALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLK--QKE 951
Cdd:TIGR00618 531 -------QRGEQTYAQLETSEEDVYHQLT----SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVrlQDL 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 952 KDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQAdLKQL 1031
Cdd:TIGR00618 600 TEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEL-LASR 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1032 QSDLYGKESELLATRQDLKSVEEKLTLAQEDLISnrnqIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQRE 1111
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETH----IEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1112 K--------SVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLK 1183
Cdd:TIGR00618 755 VlkarteahFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFL 834
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 50053824 1184 AALEQEKESQQLMREQVKK--EEEKRKEEFSEKEAKLHSEIKE 1224
Cdd:TIGR00618 835 SRLEEKSATLGEITHQLLKyeECSKQLAQLTQEQAKIIQLSDK 877
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
75-381 |
2.47e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 75 EAGLALTRDDITLLRQEVQDLQAslkEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDS-SAELQALEQQLEEAQTENFN 153
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHES---QEQQQRSQLEQAKEGLSALNRLLPRLNLLADETlADRVEEIREQLDEAEEAKRF 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 154 IKQMKDLFEQKAAQLAT------EIADIKSKYDEEKSLRAAAEQKVTHLtedlnkqttviqdlkTELLQRpgiedVAVLK 227
Cdd:PRK04863 913 VQQHGNALAQLEPIVSVlqsdpeQFEQLKQDYQQAQQTQRDAKQQAFAL---------------TEVVQR-----RAHFS 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 228 KElvqvqtlmdnmtlERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNL 307
Cdd:PRK04863 973 YE-------------DAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50053824 308 TEKLQkkDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREEL 381
Cdd:PRK04863 1040 KQELQ--DLGVPADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
915-1337 |
2.70e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 915 LKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLEN 994
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 995 KLQQQSSQAAQELAAEKgKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQN 1074
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLES-QISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNN 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1075 KSIQELqaaKASLEQDSAKKEALLKE-QSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQE 1153
Cdd:TIGR04523 281 KKIKEL---EKQLNQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1154 SIKEITNLKDAKQLLIQQKLELQGRVDSLKaaleqekesqqlmreqvkkeeekrkeefsekeaKLHSEIKEKEAGMKKHE 1233
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKENQSYKQEIK---------------------------------NLESQINDLESKIQNQE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1234 ENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKA 1313
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL 484
|
410 420
....*....|....*....|....
gi 50053824 1314 LELQRKLDNTTAAVQELGRENQSL 1337
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEEKKEL 508
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
763-1157 |
2.75e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 763 LELRNAELSRELQEQEEVVSCTKLdLQNKSEILENIKQT-LTKKEEENVVLKQEFEKLsqdsKTQHKELgdrmQAAVTEL 841
Cdd:COG5022 824 KTIKREKKLRETEEVEFSLKAEVL-IQKFGRSLKAKKRFsLLKKETIYLQSAQRVELA----ERQLQEL----KIDVKSI 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 842 TAVK---AQKDALLAEL-STTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKE-QEDLK 916
Cdd:COG5022 895 SSLKlvnLELESEIIELkKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKEtSEEYE 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 917 KSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQlqgtinqlKQSAEQKKKQIEALQGEVKNAVSQKTVLENKL 996
Cdd:COG5022 975 DLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQES--------TKQLKELPVEVAELQSASKIISSESTELSILK 1046
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 997 QQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQsdlygkESELLATRQDLKSVEEK-LTLAQEDLISNRNQIGN--- 1072
Cdd:COG5022 1047 PLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQ------LYQLESTENLLKTINVKdLEVTNRNLVKPANVLQFiva 1120
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1073 QNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKeITKLNEELKSHKQ 1152
Cdd:COG5022 1121 QMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSA-LYDEKSKLSSSEV 1199
|
....*
gi 50053824 1153 ESIKE 1157
Cdd:COG5022 1200 NDLKN 1204
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
349-484 |
2.79e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 349 LQARLTASESSLQRAQGELsekAEAAQKLREElrevESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETER 428
Cdd:PRK09039 44 LSREISGKDSALDRLNSQI---AELADLLSLE----RQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 50053824 429 QLGEAHGRLKEQRQLSSEKLMEKE---QQVADLQLKLSRLEEQLKEKVTNSTELQHQLE 484
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVEllnQQIAALRRQLAALEAALDASEKRDRESQAKIA 175
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
895-1112 |
3.16e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 895 KELKHQLQVQ------AESALKEQEDLKKSLEK---EKETSQQLKI-----ELNSVKGEVSQAQNTLKQKEKDEQQLQGT 960
Cdd:PHA02562 177 RELNQQIQTLdmkidhIQQQIKTYNKNIEEQRKkngENIARKQNKYdelveEAKTIKAEIEELTDELLNLVMDIEDPSAA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 961 INQLKQSAEQKKKQIEALQGEVKnaVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKcqadLKQLQSDLYGKES 1040
Cdd:PHA02562 257 LNKLNTAAAKIKSKIEQFQKVIK--MYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEK----LDTAIDELEEIMD 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50053824 1041 ELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREK 1112
Cdd:PHA02562 331 EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
825-1047 |
3.18e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 825 TQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQ 904
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 905 AES--------ALKEQEDLKKSLEKEKETSQQLKIELNSVKgEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIE 976
Cdd:COG3883 96 YRSggsvsyldVLLGSESFSDFLDRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50053824 977 ALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQ 1047
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
132-323 |
3.26e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 132 DSSAELQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLK 211
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 212 TEL------LQRPGIEDVAVLK------KELVQVQTLMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKG 279
Cdd:COG4942 104 EELaellraLYRLGRQPPLALLlspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 50053824 280 PQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEE 323
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1073-1283 |
3.37e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1073 QNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAeksklaemeeikcrQEKEITKLNEELKSHKQ 1152
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA--------------LARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1153 ESIKEITNLKDAKQLLIQQKLEL---------QGRVDSLKAALEQEKESQQLM-----------REQVKKEEEKRKEEFS 1212
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELaellralyrLGRQPPLALLLSPEDFLDAVRrlqylkylapaRREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50053824 1213 EKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEA 1283
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
347-563 |
3.77e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 347 QQLQARLTASESSLQ--RAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQL--HCK 422
Cdd:COG3206 185 PELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqSPV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 423 LLETERQLGEAHGRLKEQRQlsseKLMEKEQQVADLQLKLSRLEEQLKEkvtnstelqhQLEKSKQQHQEQQALQQSATA 502
Cdd:COG3206 265 IQQLRAQLAELEAELAELSA----RYTPNHPDVIALRAQIAALRAQLQQ----------EAQRILASLEAELEALQAREA 330
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50053824 503 KLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVL 563
Cdd:COG3206 331 SLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVI 391
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
366-474 |
4.02e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 366 ELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEK-EQHGLQLQGEVSQLHcKLLETERQLGEAHGRLKEQRQLS 444
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAElRDELAELEEELEALK-ARWEAEKELIEEIQELKEELEQR 483
|
90 100 110
....*....|....*....|....*....|
gi 50053824 445 SEKLMEKEQQVADLQLKLSRLEEQLKEKVT 474
Cdd:COG0542 484 YGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
907-1140 |
4.93e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 907 SALKEQEDLKKSLEKE-KETSQQLKIELNSVKGEVSQAQNTLKQKEK----DEQQLQGTINQLKQSAEQKKKQIEALQGE 981
Cdd:PHA02562 163 SVLSEMDKLNKDKIRElNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKkngeNIARKQNKYDELVEEAKTIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 982 VKNAVSQKTVLENKLQQQSSQAAQeLAAEKGKLSALQSNYEK---CQADLKQLqSDLYGKESELLATRQDLKSVEEKLTL 1058
Cdd:PHA02562 243 LLNLVMDIEDPSAALNKLNTAAAK-IKSKIEQFQKVIKMYEKggvCPTCTQQI-SEGPDRITKIKDKLKELQHSLEKLDT 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1059 AQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEK 1138
Cdd:PHA02562 321 AIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVK 400
|
..
gi 50053824 1139 EI 1140
Cdd:PHA02562 401 EK 402
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
241-621 |
5.02e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 241 TLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTH 320
Cdd:COG4717 106 ELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQ 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 321 LEEKHNEE----SASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELsEKAEAAQKLREELR--EVESTRQHLKVE 394
Cdd:COG4717 186 LSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-EAAALEERLKEARLllLIAAALLALLGL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 395 VKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVT 474
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 475 NSTELQHQLEKSKQQHQ--EQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAK 552
Cdd:COG4717 345 RIEELQELLREAEELEEelQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50053824 553 IQAGEGETAvLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEE-----NLHDQVQEQKAHLRAAQDRVLSLET 621
Cdd:COG4717 425 LDEEELEEE-LEELEEELEELEEELEELREELAELEAELEQLEEdgelaELLQELEELKAELRELAEEWAALKL 497
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
614-797 |
5.14e-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: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 614 DRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRAD---LQNHLdtaQHALQDKQQElnKVSVQl 690
Cdd:pfam09726 395 DALVRLEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQEndlLQTKL---HNAVSAKQKD--KQTVQ- 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 691 dQLTAKFQEKQEHCIQLESHLKDHK----------------------EKHLSLEQKVEDLEGHIKKLEadaLEVKASKEQ 748
Cdd:pfam09726 469 -QLEKRLKAEQEARASAEKQLAEEKkrkkeeeataaravalaaasrgECTESLKQRKRELESEIKKLT---HDIKLKEEQ 544
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 50053824 749 ALqslqqqrqlstDLELRNAELS--RELQEQEEVVSCTKLDLQNKSEILEN 797
Cdd:pfam09726 545 IR-----------ELEIKVQELRkyKESEKDTEVLMSALSAMQDKNQHLEN 584
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
78-487 |
5.16e-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: 41.49 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 78 LALTRDDITLLRQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQM 157
Cdd:TIGR00618 440 AELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQD 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 158 KDL----------FEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRPGIEDvaVLK 227
Cdd:TIGR00618 520 IDNpgpltrrmqrGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV--RLQ 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 228 KELVQVQTLMDNMTLERERESEKLKDECKKLQ---------SEHAHLEATINQLRSELAKGPQ-EVAVYVQEIQKLKGSI 297
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQPEQDLQDvrlhlqqcsQELALKLTALHALQLTLTQERVrEHALSIRVLPKELLAS 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 298 NELT-QKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQK 376
Cdd:TIGR00618 678 RQLAlQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 377 LREELREVESTRQHLKVEV-KQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQV 455
Cdd:TIGR00618 758 ARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL 837
|
410 420 430
....*....|....*....|....*....|..
gi 50053824 456 ADLQLKLSRLEEQLKEKVTNSTELQHQLEKSK 487
Cdd:TIGR00618 838 EEKSATLGEITHQLLKYEECSKQLAQLTQEQA 869
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
247-549 |
5.18e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 247 ESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHN 326
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 327 EESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVEstRQHLKVEVKQLQQQREEKE 406
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS--EAEAEQALDELLKEANRNA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 407 QHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKS 486
Cdd:COG4372 197 EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEE 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50053824 487 KQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDL 549
Cdd:COG4372 277 ELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
951-1161 |
5.24e-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: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 951 EKDEQQLQGTINQLKQSAEQKkkqIEALQGEVKNAVSQKTVLENKLQqqssqaaqELAAEKGKLSALQSNYEKCQA---- 1026
Cdd:COG4913 591 EKDDRRRIRSRYVLGFDNRAK---LAALEAELAELEEELAEAEERLE--------ALEAELDALQERREALQRLAEyswd 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1027 --DLKQLQSDLYGKESE---LLATRQDLKSVEEKLTLAQEDLISNRNQIGnqnksiqELQAAKASLEQDSAKKEALLKEQ 1101
Cdd:COG4913 660 eiDVASAEREIAELEAElerLDASSDDLAALEEQLEELEAELEELEEELD-------ELKGEIGRLEKELEQAEEELDEL 732
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1102 SKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNL 1161
Cdd:COG4913 733 QDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1077-1293 |
5.56e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1077 IQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQEsiK 1156
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL--L 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1157 EITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMReqvkkeeekrkeEFSEKEAKLHSEIKEKEAGMKKHEENe 1236
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE------------ELEAELAELQEELEELLEQLSLATEE- 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 50053824 1237 akltmQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERR 1293
Cdd:COG4717 193 -----ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
387-645 |
5.88e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 387 TRQHLKVEVKQLQQQRE-EKEQHGLQLQGEVSQLHCKLLETERQLGEAhgrLKEQRQLSSEKLMEKEQQVADLQLKLSRL 465
Cdd:PRK11281 37 TEADVQAQLDALNKQKLlEAEDKLVQQDLEQTLALLDKIDRQKEETEQ---LKQQLAQAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 466 EEQLKEKVTNsTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKE 545
Cdd:PRK11281 114 TRETLSTLSL-RQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 546 REDLY--------AKIQAGEGETAVLNQLQ-----------EKNHALQQQLTQLTEKL--KNQSESHKQAEenlhdQVQE 604
Cdd:PRK11281 193 QRVLLqaeqallnAQNDLQRKSLEGNTQLQdllqkqrdyltARIQRLEHQLQLLQEAInsKRLTLSEKTVQ-----EAQS 267
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 50053824 605 QKAHLRAAQDRVLSLETSVS-ELSSQLNESKEKVSQL---DIQIK 645
Cdd:PRK11281 268 QDEAARIQANPLVAQELEINlQLSQRLLKATEKLNTLtqqNLRVK 312
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
478-901 |
5.93e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 478 ELQHQLEKSKQQHQEqqalqqSATAKLreAQNDLEQVLRQIGDKDQKIQNLEAllqkgkesvslLEKEREDLYAKIQAGE 557
Cdd:PRK11281 40 DVQAQLDALNKQKLL------EAEDKL--VQQDLEQTLALLDKIDRQKEETEQ-----------LKQQLAQAPAKLRQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 558 GEtavLNQLQEKNHALQQQ------LTQLTEKLknqseshkqaeENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLN 631
Cdd:PRK11281 101 AE---LEALKDDNDEETREtlstlsLRQLESRL-----------AQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 632 ESKEKVSQLDIQIKaktelllSAEAAKAAQRADLQNHLDTAQHALQDK----QQELNKVSVQLDQLTAKFQEKQEHCIQL 707
Cdd:PRK11281 167 ANSQRLQQIRNLLK-------GGKVGGKALRPSQRVLLQAEQALLNAQndlqRKSLEGNTQLQDLLQKQRDYLTARIQRL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 708 ESHLKDHKE----KHLSL-EQKVEdleghikklEADALEVKASKEQALQSLQqqrqlstdlEL-RNAELSRELQEQ-EEV 780
Cdd:PRK11281 240 EHQLQLLQEainsKRLTLsEKTVQ---------EAQSQDEAARIQANPLVAQ---------ELeINLQLSQRLLKAtEKL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 781 VSCTKLDLQNKSeILENIKQTLTKKEEENVVLK----------QEFEKLSQDSKTqhKELGDRMQAAVTELTAVKAQKDA 850
Cdd:PRK11281 302 NTLTQQNLRVKN-WLDRLTQSERNIKEQISVLKgslllsrilyQQQQALPSADLI--EGLADRIADLRLEQFEINQQRDA 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 50053824 851 lLAELSTTKEKLskvsdsLKNSKSEFEKENQKGKAAVLD-----LEKACKELKHQL 901
Cdd:PRK11281 379 -LFQPDAYIDKL------EAGHKSEVTDEVRDALLQLLDerrelLDQLNKQLNNQL 427
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
87-646 |
7.30e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 87 LLRQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQALEQQLEEAQTENFNIKQ-MKDL--FEQ 163
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSaLNELssLED 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 164 KAAQLATEIADIKSKydeeKSLRAAAEQKVTHLTEDLNKQTTviqdlKTELLQRPGIEDVAVLKKELVQVQTLMDNMTLE 243
Cdd:PRK01156 250 MKNRYESEIKTAESD----LSMELEKNNYYKELEERHMKIIN-----DPVYKNRNYINDYFKYKNDIENKKQILSNIDAE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 244 RERESEKLKdECKKLQSEHAHLEAT------INQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNL----TEKLQK 313
Cdd:PRK01156 321 INKYHAIIK-KLSVLQKDYNDYIKKksryddLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMsafiSEILKI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 314 KDLDYTHLEEKHNEesasrktLQASLHQRDLDCQQLQARLTASESSLQraqgELSEKAE----------AAQKLREElrE 383
Cdd:PRK01156 400 QEIDPDAIKKELNE-------INVKLQDISSKVSSLNQRIRALRENLD----ELSRNMEmlngqsvcpvCGTTLGEE--K 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 384 VESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLhcKLLETERQLGEAHGRLKEQRQLSS-----EKLMEKEQQVADL 458
Cdd:PRK01156 467 SNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDL--KKRKEYLESEEINKSINEYNKIESaradlEDIKIKINELKDK 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 459 QLKLSRLEEQLkekvtNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQ-NLEALLQKGKE 537
Cdd:PRK01156 545 HDKYEEIKNRY-----KSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEiGFPDDKSYIDK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 538 SVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEE------NLHDQVQEQKAHLRA 611
Cdd:PRK01156 620 SIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDiednlkKSRKALDDAKANRAR 699
|
570 580 590
....*....|....*....|....*....|....*
gi 50053824 612 AQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKA 646
Cdd:PRK01156 700 LESTIEILRTRINELSDRINDINETLESMKKIKKA 734
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-649 |
7.33e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 101 EEKWYSEELKKELEKYQGLQQQEAKSDGLVTDSSAELQAlEQQLEEAQTENFNIKQMKDLFEQKA--AQLATEIADIKSK 178
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKKADAAKKKAeeAKKAAEAAKAEAE 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 179 YDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRpgiedVAVLKKELVQVQTLMDNmtLERERESEKLKDECKKL 258
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-----ADEAKKKAEEDKKKADE--LKKAAAAKKKADEAKKK 1426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 259 QSEHAHLEATinQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQnlTEKLQKKDLDYTHLEE-KHNEESASRKTLQA 337
Cdd:PTZ00121 1427 AEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK--ADEAKKKAEEAKKADEaKKKAEEAKKKADEA 1502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 338 SLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKlREELREVESTRQHLKV----EVKQLQQQREEKEQHGLQLQ 413
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK-AEEKKKADELKKAEELkkaeEKKKAEEAKKAEEDKNMALR 1581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 414 GevsqlhcklleterqlGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQ 493
Cdd:PTZ00121 1582 K----------------AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 494 QALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHAL 573
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50053824 574 QQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTE 649
Cdd:PTZ00121 1726 EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1162-1352 |
7.41e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1162 KDAKQLLIQQKLELQGRVDSLKAALEQ-EKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENE---A 1237
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEAlEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSddlA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1238 KLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEI----AVLEATVQNNQDERRALLERCLKGEGEIEKLQTKA 1313
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdelqDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180 190
....*....|....*....|....*....|....*....
gi 50053824 1314 LELQRKLDnttAAVQELGRENQSLqIKHTQALNRKWAED 1352
Cdd:COG4913 769 ENLEERID---ALRARLNRAEEEL-ERAMRAFNREWPAE 803
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1220-1337 |
8.38e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1220 SEIKEKEAGmKKHEENEAKLTMQVTTLNENLGTVKKewqsSQRRVSELEKQTDDLRGEIAVLEATVQNNQDE---RRALL 1296
Cdd:COG2433 383 EELIEKELP-EEEPEAEREKEHEERELTEEEEEIRR----LEEQVERLEAEVEELEAELEEKDERIERLERElseARSEE 457
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 50053824 1297 ERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSL 1337
Cdd:COG2433 458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1006-1119 |
8.62e-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: 40.10 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50053824 1006 ELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLisnrNQIgnQNKSIQELQAAKA 1085
Cdd:TIGR04320 248 PIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKEL----ANA--QAQALQTAQNNLA 321
|
90 100 110
....*....|....*....|....*....|....
gi 50053824 1086 SLEQDSAKKEALLKEQSKALEDAQREKSVKEKEL 1119
Cdd:TIGR04320 322 TAQAALANAEARLAKAKEALANLNADLAKKQAAL 355
|
|
| |
