|
Name |
Accession |
Description |
Interval |
E-value |
| FYVE_EEA1 |
cd15730 |
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ... |
1232-1294 |
1.72e-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: 1.72e-41
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967304 1232 RKWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDACFNDL 1294
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: ... |
1233-1295 |
3.34e-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: 3.34e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568967304 1233 KWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTP---SSKKPVRVCDACFNDLQ 1295
Cdd:pfam01363 2 VWVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLpelGSNKPVRVCDACYDTLQ 67
|
|
| FYVE |
smart00064 |
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ... |
1231-1296 |
1.31e-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: 1.31e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568967304 1231 NRKWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSS--KKPVRVCDACFNDLQG 1296
Cdd:smart00064 1 RPHWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENLNG 68
|
|
| FYVE_RUFY1_like |
cd15721 |
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ... |
1234-1291 |
5.15e-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: 5.15e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568967304 1234 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDACF 1291
Cdd:cd15721 1 WADDKEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
|
|
| FYVE_PKHF |
cd15717 |
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ... |
1234-1291 |
3.91e-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: 3.91e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1234 WAEDNEVQNCMSCGKC-FSVTVRRHHCRQCGNIFCAECSTKNALTPS-SKKPVRVCDACF 1291
Cdd:cd15717 2 WVPDSEAPVCMHCKKTkFTAINRRHHCRKCGAVVCGACSSKKFLLPHqSSKPLRVCDTCY 61
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
385-1219 |
4.17e-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: 4.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 385 ATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLlEKEREDLYAKIQAGEgetavLNQLQEKNHALQQQLTQ 464
Cdd:TIGR02168 177 TERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKEL-KAELRELELALLVLR-----LEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 465 LTEKLKNQSESHKQAE---ENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLsaea 541
Cdd:TIGR02168 251 AEEELEELTAELQELEeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE---- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 542 akaaqraDLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLE 621
Cdd:TIGR02168 327 -------ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 622 ADALEVKASKEQALQSLQQQRQLSTDL-----ELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVV 696
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 697 LKQEFEKLSQ--DSKTQHKELGDRMQAAVTELTAVKAQK---DALLAELSTTKEKLSK-------------VSDSLKNSK 758
Cdd:TIGR02168 480 AERELAQLQArlDSLERLQENLEGFSEGVKALLKNQSGLsgiLGVLSELISVDEGYEAaieaalggrlqavVVENLNAAK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 759 SEFE--KENQKGKAAVLDLEKACKElkhQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNtlkqke 836
Cdd:TIGR02168 560 KAIAflKQNELGRVTFLPLDSIKGT---EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDD------ 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 837 kdeqqLQGTINQLKQSAEQKKkqIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQL 916
Cdd:TIGR02168 631 -----LDNALELAKKLRPGYR--IVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAEL 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 917 QSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQignqnksIQELQAAKASLEQDSAKKEALLKEQSKALEDAQRE 996
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-------VEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 997 KSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQesikEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKE 1076
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE----EAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1077 SQQLMreqvkkeeEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQT 1156
Cdd:TIGR02168 853 DIESL--------AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568967304 1157 DDLRGEIAVLEATVQNNQDERRALLERCLKG-EGEIEKLQTKALELQRKLDNTTAAVQELGREN 1219
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSLTLEEaEALENKIEDDEEEARRRLKRLENKIKELGPVN 988
|
|
| FYVE_like_SF |
cd00065 |
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ... |
1242-1291 |
9.13e-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: 9.13e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568967304 1242 NCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSK--KPVRVCDACF 1291
Cdd:cd00065 1 RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSFGsgKPVRVCDSCY 52
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
128-955 |
9.47e-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: 95.89 E-value: 9.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 128 ERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLE 207
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 208 EKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQR 287
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 288 EEKEQHGLQLQGEVSQLHCKLLETERQLGEAhgrlkeQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKekvtnstELQHQ 367
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEA------ELKELQAELEELEEELEELQEELERLEEALE-------ELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 368 LEkskqqhqeqqalqqsataKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKERED-------LYAKIQA 440
Cdd:TIGR02168 470 LE------------------EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvLSELISV 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 441 GEG-ETAVLNQLQEknhALQQQLTqlteklknqseshkqaeENLHDQVQEQKAHLRAAQDRVLSLETSV-------SELS 512
Cdd:TIGR02168 532 DEGyEAAIEAALGG---RLQAVVV-----------------ENLNAAKKAIAFLKQNELGRVTFLPLDSikgteiqGNDR 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 513 SQLNESKEKVSQLDIQIKAKTEL--LLSAEAAKAAQRADlqnhLDTAQHALQDKQQELNKVSVQLDQLTAKF-----QEK 585
Cdd:TIGR02168 592 EILKNIEGFLGVAKDLVKFDPKLrkALSYLLGGVLVVDD----LDNALELAKKLRPGYRIVTLDGDLVRPGGvitggSAK 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 586 QEHCIqleshlkdhkekhLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEV 665
Cdd:TIGR02168 668 TNSSI-------------LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 666 VSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSqdsktqhkelgDRMQAAVTELTAVKAQKDALLAELSTTKE 745
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE-----------EELAEAEAEIEELEAQIEQLKEELKALRE 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 746 KLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKhQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEV 825
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 826 SQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSN 905
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENK 962
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 568967304 906 YEKCQADLKQLQSDLYGKESEL----LATRQDLKSVEEK---LTLAQEDLISNRNQI 955
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKELgpvnLAAIEEYEELKERydfLTAQKEDLTEAKETL 1019
|
|
| FYVE_LST2 |
cd15731 |
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ... |
1234-1292 |
2.08e-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: 2.08e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967304 1234 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSK--KPVRVCDACFN 1292
Cdd:cd15731 5 WVPDEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRYGqmKPVRVCNHCFM 65
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
255-1073 |
5.77e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 93.58 E-value: 5.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 255 KAEAAQKL---REELREVESTRQHLKVEVKQLQQQREEKEQHgLQLQGEVSQLHCKLLETERQlgeahgRLKEQRQLSSE 331
Cdd:TIGR02168 174 RKETERKLertRENLDRLEDILNELERQLKSLERQAEKAERY-KELKAELRELELALLVLRLE------ELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 332 KLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQ 411
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 412 NLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQK 491
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 492 AHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTElllsaeaakaaqrADLQNHLDTAQHALQDKQQELNKV 571
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL-------------EELQEELERLEEALEELREELEEA 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 572 SVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLS---LEQKVEDLEGHIKKLeADALEVKASKEQALQSLQQQRQLstDL 648
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLEGFSEGvkaLLKNQSGLSGILGVL-SELISVDEGYEAAIEAALGGRLQ--AV 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 649 ELRNAELSR---ELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVlkQEFEKLSQDSKTQHKELGDRMQ--AAV 723
Cdd:TIGR02168 551 VVENLNAAKkaiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFL--GVAKDLVKFDPKLRKALSYLLGgvLVV 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 724 TELTAVKAQKDALLAELS--TTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELK---HQLQVQAESALKEQE 798
Cdd:TIGR02168 629 DDLDNALELAKKLRPGYRivTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEekiAELEKALAELRKELE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 799 DLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLE 878
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 879 ---NKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQI 955
Cdd:TIGR02168 789 aqiEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 956 GNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSH 1035
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
810 820 830
....*....|....*....|....*....|....*...
gi 568967304 1036 KQESIKEITNLKDAKQLLIQqklELQGRVDSLKAALEQ 1073
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEE---EARRRLKRLENKIKE 983
|
|
| FYVE_ANFY1 |
cd15728 |
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ... |
1234-1294 |
6.96e-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: 6.96e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568967304 1234 WAEDNevqNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKnaLTPSSK----KPVRVCDACFNDL 1294
Cdd:cd15728 4 WADGD---YCYECGVKFGITTRKHHCRHCGRLLCSKCSTK--EVPIIKfdlnKPVRVCDVCFDVL 63
|
|
| FYVE_endofin |
cd15729 |
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ... |
1234-1294 |
7.39e-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: 7.39e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967304 1234 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAE-CSTKNALTPSSKKPVRVCDACFNDL 1294
Cdd:cd15729 7 WVPDSEAPNCMQCEVKFTFTKRRHHCRACGKVLCSAcCSLKARLEYLDNKEARVCVPCYQTL 68
|
|
| FYVE_WDFY3 |
cd15719 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ... |
1234-1294 |
7.84e-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: 7.84e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967304 1234 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSK--KPVRVCDACFNDL 1294
Cdd:cd15719 3 WVKDEGGDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFESEIRRLRisRPVRVCQACYNIL 65
|
|
| FYVE_RUFY1 |
cd15758 |
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ... |
1234-1294 |
1.81e-18 |
|
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.
Pssm-ID: 277297 [Multi-domain] Cd Length: 71 Bit Score: 80.88 E-value: 1.81e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967304 1234 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDACFNDL 1294
Cdd:cd15758 6 WLKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLL 66
|
|
| FYVE_Hrs |
cd15720 |
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ... |
1234-1294 |
3.25e-18 |
|
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) and similar proteins; Hrs, also termed protein pp110, is a tyrosine phosphorylated protein that plays an important role in the signaling pathway of HGF. It is localized to early endosomes and an essential component of the endosomal sorting and trafficking machinery. Hrs interacts with hypertonia-associated protein Trak1, a novel regulator of endosome-to-lysosome trafficking. It can also forms an Hrs/actinin-4/BERP/myosin V protein complex that is required for efficient transferrin receptor (TfR) recycling but not for epidermal growth factor receptor (EGFR) degradation. Moreover, Hrs, together with STAM proteins, STAM1 and STAM2, and EPs15, forms a multivalent ubiquitin-binding complex that sorts ubiquitinated proteins into the multivesicular body pathway, and plays a regulatory role in endocytosis/exocytosis. Furthermore, Hrs functions as an interactor of the neurofibromatosis 2 tumor suppressor protein schwannomin/merlin. It is also involved in the inhibition of citron kinase-mediated HIV-1 budding. Hrs contains a single ubiquitin-interacting motif (UIM) that is crucial for its function in receptor sorting, and a FYVE domain that harbors double Zn2+ binding sites.
Pssm-ID: 277260 [Multi-domain] Cd Length: 61 Bit Score: 79.74 E-value: 3.25e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967304 1234 WAEDNEvqnCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSS--KKPVRVCDACFNDL 1294
Cdd:cd15720 2 WKDGDE---CHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSSTIPKFgiEKEVRVCDPCYEKL 61
|
|
| FYVE_scVPS27p_like |
cd15760 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
1233-1291 |
4.56e-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: 4.56e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967304 1233 KWAEDNEvqnCMSCGKCFSVTVRRHHCRQCGNIFCAECSTK----NALTPSSkKPVRVCDACF 1291
Cdd:cd15760 1 HWKPDSR---CDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRriplPHLGPLG-VPQRVCDRCF 59
|
|
| FYVE_MTMR4 |
cd15733 |
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ... |
1234-1291 |
5.19e-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: 5.19e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1234 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSK--KPVRVCDACF 1291
Cdd:cd15733 1 WVPDHAASHCFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPDEQlyDPVRVCNSCY 60
|
|
| FYVE_PKHF2 |
cd15755 |
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ... |
1234-1294 |
2.64e-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: 2.64e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967304 1234 WAEDNEVQNCMSCGKC-FSVTVRRHHCRQCGNIFCAECSTKNALTPS-SKKPVRVCDACFNDL 1294
Cdd:cd15755 2 WVPDSEATVCMRCQKAkFTPVNRRHHCRKCGFVVCGPCSEKKFLLPSqSSKPVRVCDFCYDLL 64
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
331-1043 |
4.85e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 87.05 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 331 EKLMEKEQQVADLQLKLSRLEEQLKekvTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKI 410
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 411 QNLEALLQKGKESVSLLEKEREDLYAKIQA-GEGETavlNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEEnlhdQVQE 489
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQ---LRVKEKIGELEAEIASLERSIAEKERELEDAEE----RLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 490 QKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLdiqiKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELN 569
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL----KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 570 KVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLE 649
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 650 LRNAELSRELQEQEEVVSctkldlQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQ---HKELGDRMQAAVTEL 726
Cdd:TIGR02169 483 KELSKLQRELAEAEAQAR------ASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYAtaiEVAAGNRLNNVVVED 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 727 TAVKAQKDALLAE----------LSTTKEKLSKVSDSLKNSKS-------EFEKENQKGKAAVL-------DLEKACKEL 782
Cdd:TIGR02169 557 DAVAKEAIELLKRrkagratflpLNKMRDERRDLSILSEDGVIgfavdlvEFDPKYEPAFKYVFgdtlvveDIEAARRLM 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 783 --------------------------------KHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQN 830
Cdd:TIGR02169 637 gkyrmvtlegelfeksgamtggsraprggilfSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 831 TLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQ-ELAAEKGKLSALQSNYEKC 909
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKlEEALNDLEARLSHSRIPEI 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 910 QADLKQLQSDLYGKESELLATRQDLKSVEEKLTLA-------QEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEAL 982
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLekeiqelQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967304 983 LKEQSKALEDAQREKSVKEKELVAEKSKLAEMeEIKCRQEKEITKLNEELKSHKQESIKEI 1043
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLRELERKIEEL-EAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| FYVE_ZF21 |
cd15727 |
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ... |
1234-1290 |
1.16e-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: 1.16e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 568967304 1234 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTP--SSKKPVRVCDAC 1290
Cdd:cd15727 4 WVPDKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVPLPrmCFVDPVRVCNEC 62
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
128-661 |
2.15e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.99 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 128 ERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLE 207
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 208 EKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQR 287
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 288 EEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRL------KEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNS 361
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLerleeeLEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 362 TELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAG 441
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 442 EGETAVLNQLQEKN---------HALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELS 512
Cdd:COG1196 542 AALAAALQNIVVEDdevaaaaieYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 513 SQLNESKEKVSQLDIQIKAKT-ELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQ 591
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLaGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 592 LESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQE 661
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| FYVE_FYCO1 |
cd15726 |
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ... |
1234-1291 |
3.04e-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: 3.04e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568967304 1234 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDACF 1291
Cdd:cd15726 1 WQDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKACF 58
|
|
| FYVE_FGD6 |
cd15743 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ... |
1234-1291 |
3.12e-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: 3.12e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 568967304 1234 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNA-LTPSSKKPVRVCDACF 1291
Cdd:cd15743 3 WIPDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNKApLEYLKNKSARVCDECF 61
|
|
| FYVE_FGD1_2_4 |
cd15741 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ... |
1233-1294 |
6.99e-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: 6.99e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568967304 1233 KWAEDNEVQNCMSCGKCF-SVTVRRHHCRQCGNIFCAECSTKNA-LTPSSKKPVRVCDACFNDL 1294
Cdd:cd15741 2 RWVRDNEVTMCMRCKEPFnALTRRRHHCRACGYVVCWKCSDYKAtLEYDGNKLNRVCKHCYVIL 65
|
|
| FYVE_RBNS5 |
cd15716 |
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ... |
1234-1294 |
7.79e-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: 7.79e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967304 1234 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALtpsskkPVRVCDACFNDL 1294
Cdd:cd15716 4 WVNDSDVPFCPDCGKKFNLARRRHHCRLCGSIMCNKCSQFLPL------HIRCCHHCKDLL 58
|
|
| FYVE_MTMR3 |
cd15732 |
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ... |
1233-1291 |
1.05e-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: 1.05e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967304 1233 KWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSK--KPVRVCDACF 1291
Cdd:cd15732 1 RWVPDHLAASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLPVPSQQlfEPSRVCKSCF 61
|
|
| FYVE_RABE_unchar |
cd15739 |
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ... |
1233-1291 |
1.20e-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: 1.20e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 568967304 1233 KWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDACF 1291
Cdd:cd15739 3 RWQHEDDVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCH 61
|
|
| FYVE_ZFY26 |
cd15724 |
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ... |
1234-1292 |
2.27e-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: 2.27e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967304 1234 WAEDNEVQNCMSC-GKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKK-PVRVCDACFN 1292
Cdd:cd15724 1 WVPDEAVSVCMVCqVERFSMFNRRHHCRRCGRVVCSSCSTKKMLVEGYREnPVRVCDQCYE 61
|
|
| FYVE_ZFYV1 |
cd15734 |
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ... |
1234-1291 |
2.34e-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: 2.34e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1234 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSS--KKPVRVCDACF 1291
Cdd:cd15734 2 WVPDSEIKECSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRgwDHPVRVCDPCA 61
|
|
| FYVE_PKHF1 |
cd15754 |
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ... |
1234-1294 |
3.13e-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: 3.13e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967304 1234 WAEDNEVQNCMSCGKC-FSVTVRRHHCRQCGNIFCAECSTKNALTPS-SKKPVRVCDACFNDL 1294
Cdd:cd15754 2 WIPDKATDICMRCTQTnFSLLTRRHHCRKCGFVVCHECSRQRFLIPRlSPKPVRVCSLCYRKL 64
|
|
| FYVE_spVPS27p_like |
cd15735 |
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ... |
1237-1291 |
4.84e-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: 4.84e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568967304 1237 DNEVqnCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTP--SSKKPVRVCDACF 1291
Cdd:cd15735 5 DSDV--CMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPhfGINQPVRVCDGCY 59
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
396-1183 |
1.15e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 79.34 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 396 LEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGE----TAVLNQLQEKNHALQQQLTQLTEKLKN 471
Cdd:TIGR02169 197 RQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQlaslEEELEKLTEEISELEKRLEEIEQLLEE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 472 QSESHKQAEENLHDQVQEQKAHLRAAQDRvlsLETSVSELSSQLNESKEKVSQLDIQIKAktelLLSAEAAKAAQRADLQ 551
Cdd:TIGR02169 277 LNKKIKDLGEEEQLRVKEKIGELEAEIAS---LERSIAEKERELEDAEERLAKLEAEIDK----LLAEIEELEREIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 552 NHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASK 631
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 632 EQALQSLqqqrqlsTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKL------- 704
Cdd:TIGR02169 430 AGIEAKI-------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAeaqaras 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 705 ---SQDSKTQHKELGDRMQ---AAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKS-EFEKENQKGKAAVLDLEK 777
Cdd:TIGR02169 503 eerVRGGRAVEEVLKASIQgvhGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAiELLKRRKAGRATFLPLNK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 778 ACKELKHQLQVQAESALKEQEDLKKSLEK------------------EKETSQQLKIELNSVKGEVSQAQNTLKQKEKDE 839
Cdd:TIGR02169 583 MRDERRDLSILSEDGVIGFAVDLVEFDPKyepafkyvfgdtlvvediEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAP 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 840 QQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLEN---KLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQL 916
Cdd:TIGR02169 663 RGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 917 QSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKS-----IQELQAAKASLEQDSAKKEALLKEQSKALE 991
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLN 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 992 DAQREKSVKEKELVAEKSKLAEMEEikcrQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAAL 1071
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKE----QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1072 EQEKESQQLMREQVKKEEEKRKEEFSEKEAkLHSEIKEKEAGMKKHEENEAKLTmqvttlneNLGTVKKEWQSSQRRVSE 1151
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLSELKAKLEA-LEEELSEIEDPKGEDEEIPEEEL--------SLEDVQAELQRVEEEIRA 969
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 568967304 1152 LE--------------KQTDDLRGEIAVLEAtvqnnqdERRALLER 1183
Cdd:TIGR02169 970 LEpvnmlaiqeyeevlKRLDELKEKRAKLEE-------ERKAILER 1008
|
|
| FYVE_RUFY2 |
cd15759 |
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ... |
1234-1290 |
2.67e-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: 68.90 E-value: 2.67e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568967304 1234 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKPVRVCDAC 1290
Cdd:cd15759 4 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSC 60
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
649-1186 |
4.48e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.87 E-value: 4.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 649 ELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTA 728
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 729 VKAQKDAllAELSTTKEKlsKVSDSLKNSKSEFEKENQKGKAAVLDLEKAcKELKHQLQVQ--AESALKEQEDLKKSLEK 806
Cdd:PTZ00121 1362 AEEKAEA--AEKKKEEAK--KKADAAKKKAEEKKKADEAKKKAEEDKKKA-DELKKAAAAKkkADEAKKKAEEKKKADEA 1436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 807 EKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQgtinQLKQSAEQKKKQiEALQGEVKNAVSQKTVLENKLQQQSS 886
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD----EAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 887 QAAQELAAEKGKLSALQSNYEKCQADlkQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQElQ 966
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKKAEEAKKAD--EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK-K 1588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 967 AAKASLEQDSAKKEALLKEQSKALEDAQREKsVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKeitnl 1046
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAK-IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK----- 1662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1047 kdAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTM 1126
Cdd:PTZ00121 1663 --AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967304 1127 QVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEI-AVLEATVQNNQDERRALLERCLK 1186
Cdd:PTZ00121 1741 EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
494-1182 |
6.42e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.90 E-value: 6.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 494 LRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSV 573
Cdd:COG1196 181 LEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 574 QLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNA 653
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 654 ELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQK 733
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 734 DALLAELSTTKEKLSKvsdslknsKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQ 813
Cdd:COG1196 421 EELEELEEALAELEEE--------EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 814 LKIELNSVKGEVSQAQNTLKQKEKDEQQLqgtINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENkLQQQSSQAAQELA 893
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAALLLAGLRG---LAGAVAVLIGVEAAYEAALEAALAAALQNIVVED-DEVAAAAIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 894 AEKGKLSALQSNYEKcQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRnqignqnksiqELQAAKASLE 973
Cdd:COG1196 569 AKAGRATFLPLDKIR-ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT-----------LVAARLEAAL 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 974 QDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLL 1053
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1054 IQQKLELQgRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMkkheeneakltmqvttlnE 1133
Cdd:COG1196 717 LEEELEEE-ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI------------------E 777
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 568967304 1134 NLGTV----KKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQN-NQDERRALLE 1182
Cdd:COG1196 778 ALGPVnllaIEEYEELEERYDFLSEQREDLEEARETLEEAIEEiDRETRERFLE 831
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
123-434 |
1.11e-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: 76.25 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 123 DNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQE--------------IQKLKGSINELTQK 188
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEleelsrqisalrkdLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 189 NQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELRE 268
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 269 VESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHckllETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLS 348
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE----ELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 349 RLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLrqigdkDQKIQNLEALLQKGKESVSLLE 428
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA------EALENKIEDDEEEARRRLKRLE 978
|
....*.
gi 568967304 429 KEREDL 434
Cdd:TIGR02168 979 NKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
20-562 |
1.29e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.74 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 20 AELQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTEL 99
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 100 LQRpgIEDVAVLKKELVQVQTLMDNMTLERERESEKLKDECKKLQSEHAHL---EATINQLRSELAKGPQEVAVYVQEIQ 176
Cdd:COG1196 319 EEL--EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALleaEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 177 KLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKA 256
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 257 EAAQKLREELREVESTRQHLKVEVKQLQQQREE-KEQHGLQLQGEVSQLHCKLL----ETERQLGEAHGRLKEQRQLSSE 331
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGLAGAVAVLIgveaAYEAALEAALAAALQNIVVEDD 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 332 KLmEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDkdqkiq 411
Cdd:COG1196 557 EV-AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA------ 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 412 nlEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLtQLTEKLKNQSESHKQAEENLHDQVQEQK 491
Cdd:COG1196 630 --ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE-AELEELAERLAEEELELEEALLAEEEEE 706
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967304 492 AHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQ 562
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| FYVE2_Vac1p_like |
cd15737 |
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ... |
1233-1290 |
4.90e-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: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1233 KWAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCA----ECSTK---NALTPSS-----------------KKPVRVCD 1288
Cdd:cd15737 1 PWEDDSSVTHCPICLRSFGLLLRKHHCRLCGKVVCDdrrtKCSTEvplDLLSSALpdlpfvfkepqsdipddTKSVRVCR 80
|
..
gi 568967304 1289 AC 1290
Cdd:cd15737 81 DC 82
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
833-1182 |
5.60e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.94 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 833 KQKEKDEQQL---QGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKC 909
Cdd:TIGR02168 172 ERRKETERKLertRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 910 QADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKA 989
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 990 LEDAQREKSVKEKELVAEKSKLAEMEEikcrQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKA 1069
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEA----ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1070 ALEQEKESQQlmreqvkkeeEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRV 1149
Cdd:TIGR02168 408 RLERLEDRRE----------RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
330 340 350
....*....|....*....|....*....|...
gi 568967304 1150 SELEKQTDDLRGEIAVLEATVQNNQDERRALLE 1182
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
|
| FYVE_scVPS27p_Vac1p_like |
cd15736 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
1243-1291 |
6.51e-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: 6.51e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 568967304 1243 CMSCGKCFSVTVRRHHCRQCGNIFCAECSTKN------ALTPSSKKPVRVCDACF 1291
Cdd:cd15736 2 CHTCSRTFNLNIRAHHCRKCGKLFCRRHLPNMiplnlsAYDPRNGKWYRCCHSCF 56
|
|
| FYVE_FGD5 |
cd15742 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ... |
1240-1295 |
7.92e-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: 7.92e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 568967304 1240 VQNCMSCGKCFSVTVRRHHCRQCGNIFCAECS-TKNALTPSSKKPVRVCDACFNDLQ 1295
Cdd:cd15742 9 VMMCMNCGSDFTLTLRRHHCHACGKIVCRNCSrNKYPLKYLKDRPAKVCDGCFAELR 65
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
9-702 |
8.03e-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: 73.56 E-value: 8.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 9 AKSDGLVTDSSAELQALEQQLEEAQtenfniKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQ 88
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELN------KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 89 TTVIQDLKtellqrpgiEDVAVLKKELVQVQTLMDNMTlereRESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEV 168
Cdd:TIGR02169 328 EAEIDKLL---------AEIEELEREIEEERKRRDKLT----EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 169 AVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRA 248
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 249 QGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQL------HCKLLET----------- 311
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLgsvgerYATAIEVaagnrlnnvvv 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 312 --------------ERQLGEAHG-RLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEK---------VTNSTELQHQ 367
Cdd:TIGR02169 555 eddavakeaiellkRRKAGRATFlPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAfkyvfgdtlVVEDIEAARR 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 368 L--------------EKS------KQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLL 427
Cdd:TIGR02169 635 LmgkyrmvtlegelfEKSgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDA 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 428 EKEREDLYAKIQAGEGETAVLNQLQEknhALQQQLTQLTEKLKNQSESHKQAEENLhDQVQEQKAHLRAAQDRVLS--LE 505
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLE---ELEEDLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEArlSH 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 506 TSVSELSSQLNESKEKVSQLDIQIKAkTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKvsvQLDQLTAKFQEK 585
Cdd:TIGR02169 791 SRIPEIQAELSKLEEEVSRIEARLRE-IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK---EIENLNGKKEEL 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 586 QEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEV 665
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
|
730 740 750
....*....|....*....|....*....|....*..
gi 568967304 666 VSCTkLDLQNKSEILENIKQTLTKKEEENVVLKQEFE 702
Cdd:TIGR02169 947 PEEE-LSLEDVQAELQRVEEEIRALEPVNMLAIQEYE 982
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
205-941 |
9.15e-13 |
|
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: 73.23 E-value: 9.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 205 HLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELS-EKAEAAQKLREELREVESTRQHLKVEVKQL 283
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQmERDAMADIRRRESQSQEDLRNQLQNTVHEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 284 QQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQ-QVADLQLKLSRLEEQLKEKVTNST 362
Cdd:pfam15921 155 EAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSmSTMHFRSLGSAISKILRELDTEIS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 363 ELQHQLEKSKQQHQEQQAlqqsataklrEAQNDLEQVLRQIGDKdqkiqnLEALLQKGKESVSLLEKEREDLYAKIQAGE 442
Cdd:pfam15921 235 YLKGRIFPVEDQLEALKS----------ESQNKIELLLQQHQDR------IEQLISEHEVEITGLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 443 GETAVLN-QLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEK 521
Cdd:pfam15921 299 SQLEIIQeQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQ 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 522 VSQLDIQI-KAKTELLLSAEAAKAAQRADLQNHL--DTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKD 598
Cdd:pfam15921 379 LQKLLADLhKREKELSLEKEQNKRLWDRDTGNSItiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNE 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 599 HKEKHLSLEQKVEDLEGHIKK----LEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSR-------ELQEQEEVVS 667
Cdd:pfam15921 459 SLEKVSSLTAQLESTKEMLRKvveeLTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsrvdlKLQELQHLKN 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 668 cTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQ--------------DSKTQHKELGDRmQAAVTELTAVKAQK 733
Cdd:pfam15921 539 -EGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagamqvEKAQLEKEINDR-RLELQEFKILKDKK 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 734 DALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQ 813
Cdd:pfam15921 617 DAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNK 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 814 LKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVK-------NAVSQKTVL---ENKLQQ 883
Cdd:pfam15921 697 LKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQfleeamtNANKEKHFLkeeKNKLSQ 776
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967304 884 QSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQ-----SDLYGKESELLATRQDLKSVEEKL 941
Cdd:pfam15921 777 ELSTVATEKNKMAGELEVLRSQERRLKEKVANMEvaldkASLQFAECQDIIQRQEQESVRLKL 839
|
|
| FYVE_PIKfyve_Fab1 |
cd15725 |
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ... |
1234-1291 |
1.88e-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: 1.88e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1234 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPSSKKP--VRVCDACF 1291
Cdd:cd15725 2 WMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPgdLRVCTYCC 61
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
567-1223 |
2.24e-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: 72.02 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 567 ELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKL-EADALEVKASKEQALQSLQQQRQLS 645
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 646 TDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKL---SQDSKTQHKELGDRMQAA 722
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLraeLEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 723 VTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQvQAESALKEQEDLKK 802
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW-KLEQLAADLSKYEQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 803 SLEKEKETSQQLKIELNSVKGEVSQAQNTLKQ--------------KEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVK 868
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARAseervrggraveevLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 869 NAVsqktVLENKLqqqSSQAAQELAAEK--GKLSALQSNyekcqaDLKQLQSDL-YGKESELLATRQDLKSVEEKL---- 941
Cdd:TIGR02169 550 NNV----VVEDDA---VAKEAIELLKRRkaGRATFLPLN------KMRDERRDLsILSEDGVIGFAVDLVEFDPKYepaf 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 942 ------TLAQEDLISNRNQIGnqnksiqelQAAKASLEQDsakkealLKEQSKALEDAQREKSVKEKELVAEKSKLAEME 1015
Cdd:TIGR02169 617 kyvfgdTLVVEDIEAARRLMG---------KYRMVTLEGE-------LFEKSGAMTGGSRAPRGGILFSRSEPAELQRLR 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1016 EIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIqqklELQGRVDSLKAALEQEKESQQLMReQVKKEEEKRKEE 1095
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG----EIEKEIEQLEQEEEKLKERLEELE-EDLSSLEQEIEN 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1096 FSEKEAKLHSEIKEKEAGMKKHEENEAKLTM-----QVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATV 1170
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEArlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 568967304 1171 QNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQ 1223
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
718-1038 |
2.44e-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: 72.02 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 718 RMQAAVTELTAVKAQK---DALLAELSTTKEKLSK-VSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKhQLQVQAESA 793
Cdd:TIGR02169 171 KKEKALEELEEVEENIerlDLIIDEKRQQLERLRReREKAERYQALLKEKREYEGYELLKEKEALERQKE-AIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 794 LKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQ-AQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVS 872
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 873 QKtvleNKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNR 952
Cdd:TIGR02169 330 EI----DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 953 NQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEEL 1032
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
....*.
gi 568967304 1033 KSHKQE 1038
Cdd:TIGR02169 486 SKLQRE 491
|
|
| FYVE_MTMR_unchar |
cd15738 |
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ... |
1233-1291 |
2.60e-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: 2.60e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967304 1233 KWAEDNEVQNCmSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPS--SKKPVRVCDACF 1291
Cdd:cd15738 2 DWKSFRNVTEC-SCSTPFDHFSKKHHCWRCGNVFCTRCIDKQRALPGhlSQRPVPVCRACY 61
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9-706 |
4.28e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 9 AKSDGLVTDSSAELQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQ 88
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 89 TTVIQDLKTEllqrpgIEDVAVLKKELVQVQTLMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEV 168
Cdd:TIGR02168 343 EEKLEELKEE------LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 169 AVYVQEIQKL-----KGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASES 243
Cdd:TIGR02168 417 ERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 244 SLQRAQGE--------------------LSEKAEAAQKLREELREV-ESTRQHlkVEVKQLQQQREEKEqhgLQLQGEVS 302
Cdd:TIGR02168 497 LQENLEGFsegvkallknqsglsgilgvLSELISVDEGYEAAIEAAlGGRLQA--VVVENLNAAKKAIA---FLKQNELG 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 303 QLHCKLLET--ERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLK--EKVTNSTELQHQLEKSKQ----- 373
Cdd:TIGR02168 572 RVTFLPLDSikGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvDDLDNALELAKKLRPGYRivtld 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 374 ------------QHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAG 441
Cdd:TIGR02168 652 gdlvrpggvitgGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 442 EGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEK 521
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 522 VSQLDIQIKAKT---ELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKD 598
Cdd:TIGR02168 812 LTLLNEEAANLRerlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 599 HKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQ-QRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKS 677
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR 971
|
730 740
....*....|....*....|....*....
gi 568967304 678 EILENIKQTLTKKEEENVVLKQEFEKLSQ 706
Cdd:TIGR02168 972 RRLKRLENKIKELGPVNLAAIEEYEELKE 1000
|
|
| FYVE_WDFY1_like |
cd15718 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ... |
1234-1291 |
5.86e-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: 5.86e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967304 1234 WAEDNevqNCMSCGKCF-----------SVTVRRHHCRQCGNIFCAECSTKNALTPSS--KKPVRVCDACF 1291
Cdd:cd15718 3 WAESD---NCQKCSRPFfwnfkqmwekkTLGVRQHHCRKCGKAVCDKCSSNRSTIPVMgfEFPVRVCNECY 70
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
21-1004 |
9.54e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 69.82 E-value: 9.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 21 ELQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELL 100
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 101 QRPG-IEDVAVLKKELVQVQTLMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLK 179
Cdd:pfam01576 86 EEEErSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 180 GSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQ--------------ARLTASESSL 245
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQeqiaelqaqiaelrAQLAKKEEEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 246 QRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLET-ERQLGEAHGRLKE 324
Cdd:pfam01576 246 QAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTlDTTAAQQELRSKR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 325 QRQLSS-EKLMEKEQQVADLQlklsrLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQI 403
Cdd:pfam01576 326 EQEVTElKKALEEETRSHEAQ-----LQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 404 GDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGE----TAVLNQLQEKNHALQQQLTQLTEKLKNQSEshkqa 479
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSElesvSSLLNEAEGKNIKLSKDVSSLESQLQDTQE----- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 480 eenlhdQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADlqnhLDTAQH 559
Cdd:pfam01576 476 ------LLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT----LEALEE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 560 ALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQ 639
Cdd:pfam01576 546 GKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERD 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 640 QQRQLSTDLELRNAELSREL---QEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELG 716
Cdd:pfam01576 626 RAEAEAREKETRALSLARALeeaLEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELE 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 717 DRMQAAV-------TELTAVKAQKDA-LLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKhQLQV 788
Cdd:pfam01576 706 DELQATEdaklrleVNMQALKAQFERdLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLK-ELEA 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 789 QAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQ---SAEQKKKQIEA--- 862
Cdd:pfam01576 785 QIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEdlaASERARRQAQQerd 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 863 -LQGEVKNAVSQKTVLEN---KLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESellaTRQDLKSVE 938
Cdd:pfam01576 865 eLADEIASGASGKSALQDekrRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERS----TSQKSESAR 940
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568967304 939 EKLTLAQEDLISNRNQIGNQNKSiqELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKEL 1004
Cdd:pfam01576 941 QQLERQNKELKAKLQEMEGTVKS--KFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKL 1004
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
549-1223 |
1.38e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 549 DLQNHLDTAQHAL-----QDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEAD 623
Cdd:TIGR02168 217 ELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 624 ALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSctklDLQNKSEILENIKQTLTKKEEEnvvlkqeFEK 703
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA----ELEEKLEELKEELESLEAELEE-------LEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 704 LSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELK 783
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 784 HQLQVQAESALKEQEDLKKSLEKEKETSQQlkiELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQsAEQKKKQIEAL 863
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQ---ALDAAERELAQLQARLDSLERLQENLEGFSEGVKA-LLKNQSGLSGI 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 864 QGEVKNAVSQKT----------------VLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESEL 927
Cdd:TIGR02168 522 LGVLSELISVDEgyeaaieaalggrlqaVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFL 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 928 LATrQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKelvae 1007
Cdd:TIGR02168 602 GVA-KDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILER----- 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1008 KSKLAEMEEIKCRQEKEITKLNEELKSHKqesiKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLmREQVKK 1087
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELR----KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ-LEERIA 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1088 EEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNEnlgtvkkEWQSSQRRVSELEKQTDDLRGEIAVLE 1167
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE-------ELKALREALDELRAELTLLNEEAANLR 823
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 568967304 1168 ATVQNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQ 1223
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
19-621 |
1.67e-11 |
|
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: 68.93 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 19 SAELQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTE 98
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 99 LLQRpgIEDVAVLKKELVQVQTLMDNMTLERERESEKLKDECKKLQS-EHAHLEATINQLRSELAKGPQEVAVYVQEIQK 177
Cdd:TIGR02168 388 VAQL--ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 178 LKGSINELTQKNQNLTEKLQKKDLDYTHLE---EKHNEESASRKTLQASLHQRDLDCQQLQARL-------TASESSLQ- 246
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLErlqENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdegyeAAIEAALGg 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 247 RAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQL----------- 315
Cdd:TIGR02168 546 RLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsyllggv 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 316 --------------------------GE---AHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQH 366
Cdd:TIGR02168 626 lvvddldnalelakklrpgyrivtldGDlvrPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRK 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 367 QLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGEta 446
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE-- 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 447 vLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQ----------EQKAHLRAAQDRVLSLETSVSELSSQLN 516
Cdd:TIGR02168 784 -IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRErleslerriaATERRLEDLEEQIEELSEDIESLAAEIE 862
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 517 ESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQN----------HLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQ 586
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSELEElseelrelesKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568967304 587 E-----------------------------HCIQLESHLK--------------DHKEKHLSLEQKVEDLEGHIKKLE 621
Cdd:TIGR02168 943 ErlseeysltleeaealenkieddeeearrRLKRLENKIKelgpvnlaaieeyeELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
106-809 |
3.06e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.17 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 106 EDVAVLKKELVQVQTLMDNMTLERER-ESEKLKDE-CKKLQSEHAHLEATINQLRSELAkgpqevavyVQEIQKLKGSIN 183
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERlRREREKAErYQALLKEKREYEGYELLKEKEAL---------ERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 184 ELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQaslhqrDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLR 263
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 264 EELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQ---QV 340
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkrEI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 341 ADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKG 420
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 421 KESVSLLEKEREDLYAKIQAGEGE-------TAVLNQLQEKNHALQQQLTQLTEKLKNQSESH----------------K 477
Cdd:TIGR02169 482 EKELSKLQRELAEAEAQARASEERvrggravEEVLKASIQGVHGTVAQLGSVGERYATAIEVAagnrlnnvvveddavaK 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 478 QAEENLHDQVQEQKAHLRAAQDRVLSLETSVSEL--------------------------SSQLNESKEKVSQLDIQIKA 531
Cdd:TIGR02169 562 EAIELLKRRKAGRATFLPLNKMRDERRDLSILSEdgvigfavdlvefdpkyepafkyvfgDTLVVEDIEAARRLMGKYRM 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 532 KT---ELL----------------LSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQL 592
Cdd:TIGR02169 642 VTlegELFeksgamtggsraprggILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEI 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 593 ESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLD 672
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELS 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 673 LQNK-----SEILENIKQTLTKKEEENVVLKQEFEKLSQ---DSKTQHKELGDR---MQAAVTELTAVKAQKDALLAELS 741
Cdd:TIGR02169 802 KLEEevsriEARLREIEQKLNRLTLEKEYLEKEIQELQEqriDLKEQIKSIEKEienLNGKKEELEEELEELEAALRDLE 881
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568967304 742 TTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESaLKEQEDLKKSLEKEKE 809
Cdd:TIGR02169 882 SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE-LSEIEDPKGEDEEIPE 948
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
654-1240 |
3.74e-11 |
|
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: 68.16 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 654 ELSRELQEQEEVVSCTKLD-LQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQ 732
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 733 KDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAvldlekacKELKHQLQVQAESALKEQEDLKKSLEKEKETSQ 812
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL--------AEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 813 QLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLE-NKLQQQSSQAAQE 891
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 892 LAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKAS 971
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 972 LEQDS---AKKEALLKEQSKALEDAQREKSVKEKELVAEKSK----LAEMEEIKCRQEKEITKLNEELKSHKQESIKEIT 1044
Cdd:TIGR02168 529 ISVDEgyeAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELgrvtFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1045 NLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMREQVKK--------EEEKRKEEFSEKEAKLHSEIKEKEAGMKK 1116
Cdd:TIGR02168 609 KFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1117 HEENEAKLTMQVTT-------LNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLK--- 1186
Cdd:TIGR02168 689 LEEKIAELEKALAElrkeleeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEElee 768
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568967304 1187 -----------GEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQIKHTQALNRKWAEDNEV 1240
Cdd:TIGR02168 769 rleeaeeelaeAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
180-996 |
4.09e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 180 GSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARltASESSLQRAQ----GELSEK 255
Cdd:PTZ00121 1058 GKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEAR--KAEEAKKKAEdarkAEEARK 1135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 256 AEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLME 335
Cdd:PTZ00121 1136 AEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAE 1215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 336 KEQQVADlqlklsrleEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEA 415
Cdd:PTZ00121 1216 EARKAED---------AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 416 LLQKGKESVSLLEKEREDLYAKIQAGEGETAvlNQLQEKNHALQQQltqlTEKLKNQSESHKQAEENLHDQVQEQKAHLR 495
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKA--DEAKKKAEEAKKK----ADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 496 AAQDRVLSLETSVSELSSQLNESKEKVSQLDI--QIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSV 573
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 574 QLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLE----------GHIKKLEADALEVKASKEQALQSLQQQRQ 643
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakkadeakkkAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 644 LSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEIL----ENIKQTLTKKEEENvvlKQEFEKLSQDSKTQHKELGDRM 719
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELkkaeEKKKAEEAKKAEED---KNMALRKAEEAKKAEEARIEEV 1597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 720 QAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAA--VLDLEKACKELKHQLQVQAESALKEQ 797
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeeLKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 798 EDLKKSLEKEKETSQQLKIE------LNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEV--KN 869
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEaeeakkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeeKK 1757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 870 AVSQKTVLENKLQQQSSQAAQELAAE--KGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTlaqED 947
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAVIEEelDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAI---KE 1834
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 568967304 948 LISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQRE 996
Cdd:PTZ00121 1835 VADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEE 1883
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
585-1242 |
1.05e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 585 KQEHCIQLESHLKDHKEKHLSLEQKVEDL-EGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLelRNAELSRELQEQE 663
Cdd:PTZ00121 1135 KAEDARKAEEARKAEDAKRVEIARKAEDArKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDA--RKAEAARKAEEER 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 664 EVVSCTKLDLQNKSEILENIKQTLTKKEEENvvlKQEFEKLSQDSKtqhKELGDRMQAAVTELTAVKAQKDALLAELSTT 743
Cdd:PTZ00121 1213 KAEEARKAEDAKKAEAVKKAEEAKKDAEEAK---KAEEERNNEEIR---KFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 744 KEKlsKVSDSLKNSKSEFEKENQKGKAavlDLEKACKELKHQlqvqAESALKEQEDLKKSLEKEKETSQQLKIELNSVKG 823
Cdd:PTZ00121 1287 EEK--KKADEAKKAEEKKKADEAKKKA---EEAKKADEAKKK----AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 824 EVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQ 903
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK 1437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 904 SNYE-KCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISN--RNQIGNQNKSIQEL-QAAKASLEQDSAKK 979
Cdd:PTZ00121 1438 KKAEeAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADeaKKKAEEAKKKADEAkKAAEAKKKADEAKK 1517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 980 --EALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQK 1057
Cdd:PTZ00121 1518 aeEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1058 LELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEaKLHSEIKEKEAGMKKHEENEAKLTMQvttlnenlgt 1137
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK-KEAEEKKKAEELKKAEEENKIKAAEE---------- 1666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1138 vKKEWQSSQRRVSELEKQTDDLRGEiavLEATVQNNQDERRAllERCLKGEGEIEKlqtKALELQRKLDNTTAAVQELGR 1217
Cdd:PTZ00121 1667 -AKKAEEDKKKAEEAKKAEEDEKKA---AEALKKEAEEAKKA--EELKKKEAEEKK---KAEELKKAEEENKIKAEEAKK 1737
|
650 660
....*....|....*....|....*
gi 568967304 1218 ENQSlQIKHTQALNRKWAEDNEVQN 1242
Cdd:PTZ00121 1738 EAEE-DKKKAEEAKKDEEEKKKIAH 1761
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
601-1183 |
2.18e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 601 EKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEevvsctkldlqnkseiL 680
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE----------------L 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 681 ENIKQTLTKKEEENVVLKQEFEKLSQD---SKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNS 757
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDiarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 758 KSEFEKENQKGKAAVLDLEKACKELKhQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEK 837
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELE-ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 838 DEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQ 917
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 918 SDLYGKESELLAtrqdlksVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREK 997
Cdd:COG1196 516 LAGLRGLAGAVA-------VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAAL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 998 SVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKES 1077
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1078 QQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTD 1157
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
570 580
....*....|....*....|....*.
gi 568967304 1158 DLRGEIAVLEATVQNNQDERRALLER 1183
Cdd:COG1196 749 EEEALEELPEPPDLEELERELERLER 774
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
194-367 |
2.42e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 194 EKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDcqQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTR 273
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE--LLEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 274 --------QHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQL 345
Cdd:COG4913 333 rgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
170 180
....*....|....*....|..
gi 568967304 346 KLSRLEEQLKEKVTNSTELQHQ 367
Cdd:COG4913 413 ALRDLRRELRELEAEIASLERR 434
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
106-843 |
5.26e-10 |
|
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: 64.37 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 106 EDVAVLKKELVQVQTLMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINEL 185
Cdd:pfam15921 110 QSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 186 TQKNQNLTEKLQKKDLDYTHLEEKHNEESASrkTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAqkLREE 265
Cdd:pfam15921 190 RSILVDFEEASGKKIYEHDSMSTMHFRSLGS--AISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELL--LQQH 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 266 LREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEV-----------SQLHCKLLETERQLGEAHGRLKEQRQLSSEKLM 334
Cdd:pfam15921 266 QDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLeiiqeqarnqnSMYMRQLSDLESTVSQLRSELREAKRMYEDKIE 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 335 EKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEK-----SKQQHQEQQALQQSATAKLREAQND--LEQVLRQIGDKD 407
Cdd:pfam15921 346 ELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKlladlHKREKELSLEKEQNKRLWDRDTGNSitIDHLRRELDDRN 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 408 QKIQNLEALLQKGK-ESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKlKNQSESHKQAEENLHDQ 486
Cdd:pfam15921 426 MEVQRLEALLKAMKsECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAK-KMTLESSERTVSDLTAS 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 487 VQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDiQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQ 566
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR-NVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGR 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 567 ELNKVSVQLDQLTAKFQEKQEHCIQLEShLKDHKEKHL-SLEQKVEDLE-GHIKKLEADALEVKASKEQALQSlqqqrql 644
Cdd:pfam15921 584 TAGAMQVEKAQLEKEINDRRLELQEFKI-LKDKKDAKIrELEARVSDLElEKVKLVNAGSERLRAVKDIKQER------- 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 645 stDLELRNAELSR-ELQEQEEVVSCTKLDLQNKSEILENikqTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAV 723
Cdd:pfam15921 656 --DQLLNEVKTSRnELNSLSEDYEVLKRNFRNKSEEMET---TTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAM 730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 724 ---TELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELkhqlqvqaesalkeqEDL 800
Cdd:pfam15921 731 gmqKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGEL---------------EVL 795
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 568967304 801 KKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQ 843
Cdd:pfam15921 796 RSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| FYVE_FGD3 |
cd15740 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ... |
1237-1291 |
5.75e-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: 56.16 E-value: 5.75e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568967304 1237 DNEVQNCMSCGKCF-SVTVRRHHCRQCGNIFCAECSTknaLTPSSKKPVRVCDACF 1291
Cdd:cd15740 2 EKEKQTCKGCNESFnSITKRRHHCKQCGAVICGKCSE---FKDLASRHNRVCRDCF 54
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
251-1141 |
1.47e-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: 62.68 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 251 ELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSS 330
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 331 EKLMEKEQQVADLQLKLSRLEEQLKEKVtnstelqhqleksKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKI 410
Cdd:pfam02463 257 KQEIEKEEEKLAQVLKENKEEEKEKKLQ-------------EEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 411 QNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLtqltEKLKNQSESHKQAEENLHDQVQEQ 490
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL----LAKKKLESERLSSAAKLKEEELEL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 491 KahlraaqdrvlsletsvSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNK 570
Cdd:pfam02463 400 K-----------------SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 571 VSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLEL 650
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 651 RNAELSRELQEQEEVVSCTKLD--LQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTA 728
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEERQklVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 729 VKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEK 808
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIK 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 809 ETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQA 888
Cdd:pfam02463 703 KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREK 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 889 AQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLaqedlisnrnqigNQNKSIQELQAA 968
Cdd:pfam02463 783 TEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEE-------------LALELKEEQKLE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 969 KASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITnlkd 1048
Cdd:pfam02463 850 KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE---- 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1049 aKQLLIQQKLELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQV 1128
Cdd:pfam02463 926 -EAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEK 1004
|
890
....*....|...
gi 568967304 1129 TTLNENLGTVKKE 1141
Cdd:pfam02463 1005 KKLIRAIIEETCQ 1017
|
|
| FYVE_protrudin |
cd15723 |
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ... |
1242-1290 |
1.64e-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: 1.64e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568967304 1242 NCMSCGKCFSV-TVRRHHCRQCGNIFCAEC-------STKNALTPSSKK-PVRVCDAC 1290
Cdd:cd15723 1 NCTGCGASFSVlLKKRRSCNNCGNAFCSRCcskkvprSVMGATAPAAQReTVFVCSGC 58
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
320-1123 |
3.49e-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: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 320 GRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVtnstelqhqlEKSKQQHQEQQALQQSATAKLREAQNDLEQV 399
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLK----------EQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 400 LRqigdkdQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQA 479
Cdd:pfam02463 235 NE------ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 480 EENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQH 559
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 560 ALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQ 639
Cdd:pfam02463 389 AAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 640 QQRQLSTdlELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRM 719
Cdd:pfam02463 469 KSEDLLK--ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 720 QAAVTELTAVKAQKDALLaelstTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQED 799
Cdd:pfam02463 547 TAVIVEVSATADEVEERQ-----KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 800 LKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLEN 879
Cdd:pfam02463 622 AKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 880 KLQQQSSQAAQE---LAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIG 956
Cdd:pfam02463 702 KKKEQREKEELKklkLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEERE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 957 NQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKsvKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHK 1036
Cdd:pfam02463 782 KTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQL--LIEQEEKIKEEELEELALELKEEQKLEKLAEEELERL 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1037 QESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKEsQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKK 1116
Cdd:pfam02463 860 EEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEK-KELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE 938
|
....*..
gi 568967304 1117 HEENEAK 1123
Cdd:pfam02463 939 ELLLEEA 945
|
|
| FYVE_RUFY4 |
cd15745 |
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ... |
1243-1291 |
4.92e-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: 53.27 E-value: 4.92e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568967304 1243 CMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNAL--TPSSKKPVRVCDACF 1291
Cdd:cd15745 2 CAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVlsVPDTCIYLRVCKTCY 52
|
|
| FYVE_ZFY19 |
cd15749 |
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ... |
1242-1291 |
6.23e-09 |
|
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ZFY19, also termed mixed lineage leukemia (MLL) partner containing FYVE domain, is encoded by a novel gene, MLL partner containing FYVE domain (MPFYVE). The FYVE domain of ZFY19 resembles FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. The biological function of ZFY19 remains unclear.
Pssm-ID: 277288 [Multi-domain] Cd Length: 51 Bit Score: 52.89 E-value: 6.23e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568967304 1242 NCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPS-SKKPVRVCDACF 1291
Cdd:cd15749 1 RCFGCAAKFSLFKKECGCKNCGRSFCKGCLTFSAVVPRkGNQKQKVCKQCH 51
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
914-1217 |
6.78e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 6.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 914 KQLQSDLYGKESELLATRqdLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDA 993
Cdd:COG1196 216 RELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 994 QREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQ 1073
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1074 --EKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSE 1151
Cdd:COG1196 374 laEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568967304 1152 LEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGR 1217
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
454-1056 |
1.59e-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: 59.26 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 454 KNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLD---IQIK 530
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNsdlSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 531 AKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKV 610
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 611 EDLEGHIKKLEADALEVKASKEQA---LQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTL 687
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQKNkslESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 688 TKKEEEnvvlkqefeklSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLaeLSTTKEKLSKVSDSLKNSKSEFEKENQK 767
Cdd:TIGR04523 270 SEKQKE-----------LEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNQISQNNKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 768 GKAAVLDLEKACKELKH------QLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQ 841
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNsesensEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 842 LQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQelaaEKGKLSALQSNYEKCQADLKQLQSDLY 921
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES----LETQLKVLSRSINKIKQNLEQKQKELK 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 922 GKESELLA----------TRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQ-ELQAAKASLEQDSAKKEAL-------- 982
Cdd:TIGR04523 493 SKEKELKKlneekkeleeKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEdELNKDDFELKKENLEKEIDeknkeiee 572
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568967304 983 LKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQ 1056
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
132-622 |
2.69e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 132 ESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDL---DYTHLEE 208
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSlesQISELKK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 209 KHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQRE 288
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 289 EKEQHglQLQGEVSQLHCKLLETERQLGEahgrlkeqrqlSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQL 368
Cdd:TIGR04523 306 QDWNK--ELKSELKNQEKKLEEIQNQISQ-----------NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 369 EKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVL 448
Cdd:TIGR04523 373 EKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 449 NQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQ 528
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 529 IKAKTELLLSAEAAKAAQRADLQNhlDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQ 608
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDFELKK--ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEK 610
|
490
....*....|....
gi 568967304 609 KVEDLEGHIKKLEA 622
Cdd:TIGR04523 611 KISSLEKELEKAKK 624
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
111-534 |
2.77e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 111 LKKELVQVQTLMDNMTLERERESEKlKDECKKLQSEHAH-------LEATINQLRSELAKGPQEVAVYVQEIQKLKGSIN 183
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARET-RDEADEVLEEHEErreeletLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 184 ELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQ-------LQARLTASESSLQRAQGELSEKA 256
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAhneeaesLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 257 EAAQKLREELREVESTRQHLKVEVKQLQQ-------QREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLS 329
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRErfgdapvDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 330 SE-----------------KLMEKEQQVADLQLKLSRLEEQLkEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREA 392
Cdd:PRK02224 450 EAgkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEV-EEVEERLERAEDLVEAEDRIERLEERREDLEELIAER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 393 QNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQ----------LQEKNHALQQQL 462
Cdd:PRK02224 529 RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKErieslerirtLLAAIADAEDEI 608
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967304 463 TQLTEKLKNQSESHKQAEENLHDQvQEQKAHLRAAQDrvlslETSVSELSSQLNESKEKVSQLDIQIKAKTE 534
Cdd:PRK02224 609 ERLREKREALAELNDERRERLAEK-RERKRELEAEFD-----EARIEEAREDKERAEEYLEQVEEKLDELRE 674
|
|
| FYVE_WDFY1 |
cd15756 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ... |
1233-1295 |
3.17e-08 |
|
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar proteins; WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. In addition to FYVE domain, WDFY1 harbors multiple WD-40 repeats.
Pssm-ID: 277295 [Multi-domain] Cd Length: 76 Bit Score: 51.99 E-value: 3.17e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568967304 1233 KWAEDNevqNCMSCGKCF-----------SVTVRRHHCRQCGNIFCAECSTKNALTP--SSKKPVRVCDACFNDLQ 1295
Cdd:cd15756 2 QWLESD---SCQKCEQPFfwnikqmwdtkTLGLRQHHCRKCGQAVCGKCSSKRSSYPimGFEFQVRVCDSCFETIK 74
|
|
| FYVE_RUFY3 |
cd15744 |
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ... |
1243-1291 |
3.45e-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: 3.45e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568967304 1243 CMSCGKCFSVTVR-RHHCRQCGNIFCAECSTKNALTPSS-KKPVRVCDACF 1291
Cdd:cd15744 2 CSLCQEDFASLALpKHNCYNCGGTFCDACSSNELPLPSSiYEPARVCDVCY 52
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
171-356 |
3.70e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 58.00 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 171 YVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASR------KTLQASLHQRDLDCQQLQARLTASESS 244
Cdd:PRK11281 71 LLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslRQLESRLAQTLDQLQNAQNDLAEYNSQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 245 L-------QRAQGELSEKAEAAQKLREELREVESTRQHLKVEvkqlQQQREEKEQHGLQLQGEVSQlhcKLLETERQLGE 317
Cdd:PRK11281 151 LvslqtqpERAQAALYANSQRLQQIRNLLKGGKVGGKALRPS----QRVLLQAEQALLNAQNDLQR---KSLEGNTQLQD 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568967304 318 AhgrLKEQRQLSSEKLMEKEQQVADLQ-------LKLSrlEEQLKE 356
Cdd:PRK11281 224 L---LQKQRDYLTARIQRLEHQLQLLQeainskrLTLS--EKTVQE 264
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
960-1230 |
5.01e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 960 KSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEikcrqekEITKLNEELkshkQES 1039
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-------ELEEAQAEE----YEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1040 IKEITNLKDAKQLLIQQKLELQGRvdslKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHS---EIKEKEAGMKK 1116
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEER----LEELEEELAELEEELEELEEELEELEEELEEAEEELEEaeaELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1117 HEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQT 1196
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270
....*....|....*....|....*....|....
gi 568967304 1197 KALELQRKLDNTTAAVQELGRENQSLQIKHTQAL 1230
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
15-525 |
5.60e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 15 VTDSSAELQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQD 94
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 95 LKTELLQrpgiedvavLKKELVQVQTLMDnmtlERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQE 174
Cdd:COG1196 363 AEEALLE---------AEAELAEAEEELE----ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 175 IQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSE 254
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 255 KAEAAQK-LREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHG-RLKEQRQLSSEK 332
Cdd:COG1196 510 VKAALLLaGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFlPLDKIRARAALA 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 333 LMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQN 412
Cdd:COG1196 590 AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 413 LEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSEshkQAEENLHDQVQEQKA 492
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE---AEREELLEELLEEEE 746
|
490 500 510
....*....|....*....|....*....|...
gi 568967304 493 HLRAAQDRVLSLETSVSELSSQLNESKEKVSQL 525
Cdd:COG1196 747 LLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
234-474 |
9.02e-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: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 234 LQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETER 313
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 314 QLGEAHGRLKEQRqlsseklmekeQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQ 393
Cdd:COG4942 91 EIAELRAELEAQK-----------EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 394 NDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAV-LNQLQEKNHALQQQLTQLTEKLKNQ 472
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAeLAELQQEAEELEALIARLEAEAAAA 239
|
..
gi 568967304 473 SE 474
Cdd:COG4942 240 AE 241
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
124-969 |
1.11e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.52 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 124 NMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDY 203
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 204 THLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQ-RAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQ 282
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELkLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 283 LQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNST 362
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 363 ELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGE 442
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 443 GETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEqKAHLRAAQDRVLSLETSVSELSSQLNESKEKV 522
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLG-DLGVAVENYKVAISTAVIVEVSATADEVEERQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 523 SQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEK 602
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 603 HLSLEQKVEDLEGHIKKLEADA---------LEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDL 673
Cdd:pfam02463 645 ESGLRKGVSLEEGLAEKSEVKAslseltkelLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLA 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 674 QNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQaaVTELTAVKAQKDALLAELSTTKEKLSKVSDS 753
Cdd:pfam02463 725 DRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL--KEKELAEEREKTEKLKVEEEKEEKLKAQEEE 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 754 LKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLK 833
Cdd:pfam02463 803 LRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 834 QKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADL 913
Cdd:pfam02463 883 KLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERN 962
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 568967304 914 KQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAK 969
Cdd:pfam02463 963 KRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQR 1018
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
125-529 |
1.24e-07 |
|
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: 56.50 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 125 MTLERERESEKLKDECKKLQSEHAHLEA-----TINQLRSELakgpQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKK 199
Cdd:COG3096 243 MTLEAIRVTQSDRDLFKHLITEATNYVAadymrHANERRELS----ERALELRRELFGARRQLAEEQYRLVEMARELEEL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 200 DLDYTHLEEKHNEESASRKTLQASLHQRDlDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVE 279
Cdd:COG3096 319 SARESDLEQDYQAASDHLNLVQTALRQQE-KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQ 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 280 VKQLQQQREEKEQHGLQLQGEVSQLH-----CKLLE-TERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEE- 352
Cdd:COG3096 398 LADYQQALDVQQTRAIQYQQAVQALEkaralCGLPDlTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKa 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 353 -QLKEKVTNSTELQHQLEKSKQQHQEQQALQQSA--TAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEK 429
Cdd:COG3096 478 yELVCKIAGEVERSQAWQTARELLRRYRSQQALAqrLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEE 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 430 EREDLYAKIqagEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESH------KQAEENLHDQVQEQKAHLRAAQD---R 500
Cdd:COG3096 558 LLAELEAQL---EELEEQAAEAVEQRSELRQQLEQLRARIKELAARApawlaaQDALERLREQSGEALADSQEVTAamqQ 634
|
410 420
....*....|....*....|....*....
gi 568967304 501 VLSLETSVSELSSQLNESKEkvsQLDIQI 529
Cdd:COG3096 635 LLEREREATVERDELAARKQ---ALESQI 660
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
185-1061 |
2.22e-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: 55.82 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 185 LTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDcQQLQARLTASESSLQRAQGELSEKAEAAQKLRE 264
Cdd:TIGR00606 191 LRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS-REIVKSYENELDPLKNRLKEIEHNLSKIMKLDN 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 265 ELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLL-ETERQLGEAH---GRLKEQRQLSSEKLMEKEQQV 340
Cdd:TIGR00606 270 EIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVrEKERELVDCQrelEKLNKERRLLNQEKTELLVEQ 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 341 ADLQLKLSRLEEQLKEKVTNSTELQHQLEKS----------------KQQHQEQQALQQSATAKLREAQNDLEQVLRQIG 404
Cdd:TIGR00606 350 GRLQLQADRHQEHIRARDSLIQSLATRLELDgfergpfserqiknfhTLVIERQEDEAKTAAQLCADLQSKERLKQEQAD 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 405 DKDQKIQNLEALLQKGKEsvsLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEEnlh 484
Cdd:TIGR00606 430 EIRDEKKGLGRTIELKKE---ILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEV--- 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 485 dqvqeqkAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHL------DTAQ 558
Cdd:TIGR00606 504 -------KSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLgyfpnkKQLE 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 559 HALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKV------EDLEGHIKKLEADALEVKASKE 632
Cdd:TIGR00606 577 DWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRA 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 633 QALQSLQQQRQLSTDLELRNA----------ELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFE 702
Cdd:TIGR00606 657 MLAGATAVYSQFITQLTDENQsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQ 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 703 KLSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKN-----------SKSEFEKENQKGKAA 771
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDvtimerfqmelKDVERKIAQQAAKLQ 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 772 VLDLEKACKELKHQLQVQAE---SALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQ 848
Cdd:TIGR00606 817 GSDLDRTVQQVNQEKQEKQHeldTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 849 LKQ---SAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSD-LYGKE 924
Cdd:TIGR00606 897 VQSlirEIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDyLKQKE 976
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 925 SELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNksiqelqaakasleqdsaKKEALLKEQSKALEDAQREKSVKEKel 1004
Cdd:TIGR00606 977 TELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK------------------IQERWLQDNLTLRKRENELKEVEEE-- 1036
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 568967304 1005 vaEKSKLAEMEEIKCRQEK-EITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQ 1061
Cdd:TIGR00606 1037 --LKQHLKEMGQMQVLQMKqEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELR 1092
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
125-529 |
2.48e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 125 MTLERERESEKLKDECKKLQSEH-AHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDY 203
Cdd:PRK04863 244 MTLEAIRVTQSDRDLFKHLITEStNYVAADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 204 THLEEKHNEESASRKTLQASLHQR------DLDCQQLQARLTASESSLQRAQG---ELSEKAEAAQKlreelrEVESTRQ 274
Cdd:PRK04863 324 SDLEQDYQAASDHLNLVQTALRQQekieryQADLEELEERLEEQNEVVEEADEqqeENEARAEAAEE------EVDELKS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 275 HLkVEVKQ---LQQQREEKEQHGLQLQGEVSQLhCKLLE-TERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRL 350
Cdd:PRK04863 398 QL-ADYQQaldVQQTRAIQYQQAVQALERAKQL-CGLPDlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQF 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 351 EE--QLKEKVTNSTELQ--HQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSL 426
Cdd:PRK04863 476 EQayQLVRKIAGEVSRSeaWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDE 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 427 LEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAE---ENLHDQVQEQKAHLRAAQDRVLS 503
Cdd:PRK04863 556 LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQdalARLREQSGEEFEDSQDVTEYMQQ 635
|
410 420
....*....|....*....|....*.
gi 568967304 504 LETSVSELSSQLNESKEKVSQLDIQI 529
Cdd:PRK04863 636 LLERERELTVERDELAARKQALDEEI 661
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
809-1032 |
2.65e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 809 ETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAvsqktvlenklqqqssqa 888
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 889 AQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKES----ELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQE 964
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967304 965 LQAAKASLEQDSAKKEALLKEQS---KALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEEL 1032
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEeerAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| FYVE_CARP |
cd15750 |
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ... |
1242-1290 |
3.24e-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: 48.13 E-value: 3.24e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568967304 1242 NCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKnaltpsSKKPVRVCDAC 1290
Cdd:cd15750 2 PCESCGAKFSVFKRKRTCADCKRYFCSNCLSK------EERGRRRCRRC 44
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
251-962 |
3.81e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 251 ELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLH-CKLLETERQLGEAHGRLKEQRQLS 329
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEdAKKAEAVKKAEEAKKDAEEAKKAE 1246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 330 SEKLME--KEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSA--TAKLREAQNDLEQVLRQIGD 405
Cdd:PTZ00121 1247 EERNNEeiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEE 1326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 406 KDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLH- 484
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKk 1406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 485 -DQVQEQKAHLRAAQD-RVLSLETSVSELSSQLNESKEKVSQLDIQIK-AKTELLLSAEAAKAAQRADLQNHLDTAQHA- 560
Cdd:PTZ00121 1407 aDELKKAAAAKKKADEaKKKAEEKKKADEAKKKAEEAKKADEAKKKAEeAKKAEEAKKKAEEAKKADEAKKKAEEAKKAd 1486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 561 -LQDKQQELNKVSVQLDQlTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADAL----EVKASKEQAL 635
Cdd:PTZ00121 1487 eAKKKAEEAKKKADEAKK-AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkkaeELKKAEEKKK 1565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 636 QSLQQQRQLSTDLELRNAELSRELQEQ--EEVVSCTKLDLQNKSEIL-----ENIKQTLTKKEEENVVLKQEFEKLSQDS 708
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEAriEEVMKLYEEEKKMKAEEAkkaeeAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 709 KTQHKEL--GDRMQAAVTELTAVKAQKDALLAE-LSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKAcKELKHQ 785
Cdd:PTZ00121 1646 KKKAEELkkAEEENKIKAAEEAKKAEEDKKKAEeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-EELKKA 1724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 786 LQVQA----ESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIE 861
Cdd:PTZ00121 1725 EEENKikaeEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF 1804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 862 ALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKL 941
Cdd:PTZ00121 1805 DNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEI 1884
|
730 740 750
....*....|....*....|....*....|.
gi 568967304 942 TLAQ----------EDLISNRNQIGNQNKSI 962
Cdd:PTZ00121 1885 EEADeiekidkddiEREIPNNNMAGKNNDII 1915
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
320-920 |
6.14e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 6.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 320 GRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKV-TNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQ 398
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEeKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 399 VLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQageGETAVLNQLQEKNhalqqqltqltEKLKNQSESHKQ 478
Cdd:PRK02224 242 VLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVR---DLRERLEELEEER-----------DDLLAEAGLDDA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 479 AEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTElllsaeaakaaQRADLQNHLDTAQ 558
Cdd:PRK02224 308 DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE-----------EAAELESELEEAR 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 559 HALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKL-----EADAL-------- 625
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTArerveEAEALleagkcpe 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 626 ---EVKASKEQALQSLQQQRQLSTDLELRNAELSRE-----------LQEQEEVVSCTKLDLQNKSEILENIKQTLTKKE 691
Cdd:PRK02224 457 cgqPVEGSPHVETIEEDRERVEELEAELEDLEEEVEeveerleraedLVEAEDRIERLEERREDLEELIAERRETIEEKR 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 692 EENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDAlLAELSTTKEKLSKVSDSLknsksefekenqkgkAA 771
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSK-LAELKERIESLERIRTLL---------------AA 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 772 VLDLEKACKELKHQLQvqaesALKEQEDLKKSLEKEK-ETSQQLKIELNSVKgeVSQAQNTLKQKEKDEQQLQGTINQLk 850
Cdd:PRK02224 601 IADAEDEIERLREKRE-----ALAELNDERRERLAEKrERKRELEAEFDEAR--IEEAREDKERAEEYLEQVEEKLDEL- 672
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 851 qsaEQKKKQIEALQGEVKNAVSQKTVLENKLqqqssqaaQELAAEKGKLSALQSNYEKCQADLKQLQSDL 920
Cdd:PRK02224 673 ---REERDDLQAEIGAVENELEELEELRERR--------EALENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
561-1109 |
9.15e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 561 LQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQ---- 636
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyikl 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 637 --SLQQQRQLSTDLELRNAELSRELQEQEEVVSctklDLQNKSEILENIKQTLTKKEEENVVLKqEFEKLSQDSKTQHKE 714
Cdd:PRK03918 299 seFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 715 LgDRMQAAVTELTAVKAQKdaLLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKA---CKELKHQLQVQAE 791
Cdd:PRK03918 374 L-ERLKKRLTGLTPEKLEK--ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkCPVCGRELTEEHR 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 792 SALKEQ-----EDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQqLQGTINQLK----QSAEQKKKQIEA 862
Cdd:PRK03918 451 KELLEEytaelKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLKkynlEELEKKAEEYEK 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 863 LQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKgklsALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLT 942
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK----KLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 943 laqeDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQE 1022
Cdd:PRK03918 606 ----ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAE 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1023 KEitklneELKSHKQESIKEITNLKDAKQLLIQQKLELQgrvdslkaALEQEKESQQLMREQVKKEEEKRKEEFSEKEAK 1102
Cdd:PRK03918 682 LE------ELEKRREEIKKTLEKLKEELEEREKAKKELE--------KLEKALERVEELREKVKKYKALLKERALSKVGE 747
|
....*..
gi 568967304 1103 LHSEIKE 1109
Cdd:PRK03918 748 IASEIFE 754
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
613-1159 |
9.84e-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: 53.49 E-value: 9.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 613 LEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEE 692
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 693 ENVVLKQEFEKlsqdsktqHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAV 772
Cdd:TIGR04523 202 LLSNLKKKIQK--------NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 773 LDLEKACKELKhQLQVQAESALKEQEDLKKslEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQS 852
Cdd:TIGR04523 274 KELEQNNKKIK-ELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 853 AEQKKKQIEALQGEVKnavsQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQ 932
Cdd:TIGR04523 351 LTNSESENSEKQRELE----EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 933 DLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLA 1012
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1013 EMEEIKCRQEKEITKLNE---ELKSHKQESIKEITNLKD---------AKQLLIQQKLELQGRVDSLKAALEQEKESQQL 1080
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEkieKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQEE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1081 MREQVKKEEEKRK------EEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEK 1154
Cdd:TIGR04523 587 KQELIDQKEKEKKdlikeiEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIK 666
|
....*
gi 568967304 1155 QTDDL 1159
Cdd:TIGR04523 667 KIKES 671
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
52-507 |
1.00e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.58 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 52 QLATEIADIKSKY----DEEKSLRAAAEQKVTHLTEDLnkqttviQDLKTELLQRPGIEdVAVLKKELVQVQTLMDNMTL 127
Cdd:pfam15921 228 ELDTEISYLKGRIfpveDQLEALKSESQNKIELLLQQH-------QDRIEQLISEHEVE-ITGLTEKASSARSQANSIQS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 128 ERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQK-----------LKGSINELTQKNQNLTEKL 196
Cdd:pfam15921 300 QLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKqlvlanselteARTERDQFSQESGNLDDQL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 197 QK------KDLDYTHLEEKHNEESASRKT--------LQASLHQRDLDCQQLQARLTASESslqRAQGELSEKAEAAQKL 262
Cdd:pfam15921 380 QKlladlhKREKELSLEKEQNKRLWDRDTgnsitidhLRRELDDRNMEVQRLEALLKAMKS---ECQGQMERQMAAIQGK 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 263 REELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGE---VSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLME---- 335
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSertVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQElqhl 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 336 --KEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQ---QHQEQQALQQSATAKLREAQNDLEQVLRQI----GDK 406
Cdd:pfam15921 537 knEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgQHGRTAGAMQVEKAQLEKEINDRRLELQEFkilkDKK 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 407 DQKIQNLEALLQKGK-ESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKN---HALQQQLTQLTEKLKNQSESHKQAEEN 482
Cdd:pfam15921 617 DAKIRELEARVSDLElEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRnelNSLSEDYEVLKRNFRNKSEEMETTTNK 696
|
490 500
....*....|....*....|....*
gi 568967304 483 LHDQVQEQKAHLRAAQDRVLSLETS 507
Cdd:pfam15921 697 LKMQLKSAQSELEQTRNTLKSMEGS 721
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
252-440 |
1.50e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 252 LSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVsqlhcKLLETERQLGEAHGRLKEQRQlSSE 331
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEAELERLDA-SSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 332 KLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQN-DLEQVLRQIGDKDQKI 410
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRaLLEERFAAALGDAVER 765
|
170 180 190
....*....|....*....|....*....|
gi 568967304 411 QNLEALLQKGKESVSLLEKEREDLYAKIQA 440
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
790-1013 |
1.91e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 790 AESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKN 869
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 870 AVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYE---KCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQE 946
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLdavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568967304 947 DLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAE 1013
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
20-522 |
1.98e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 20 AELQALEQQLEEAQTENFNIKQMKDLFEQKAAQlaTEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTEL 99
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 100 LQRPGiEDVAVLKKELVQVQTLMDnmtlERERESEKLKDECKKLQSEHAHLEATINQLRSELAkgpqevavyvQEIQKLK 179
Cdd:COG4913 333 RGNGG-DRLEQLEREIERLERELE----ERERRRARLEALLAALGLPLPASAEEFAALRAEAA----------ALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 180 GSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQ-RDLDCQQLQArltaSESSLQRAqGEL---SEK 255
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAlRDALAEALGL----DEAELPFV-GELievRPE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 256 AEA-------------------AQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQ------------------LQ 298
Cdd:COG4913 473 EERwrgaiervlggfaltllvpPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDpdslagkldfkphpfrawLE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 299 GEVSQ---LHCklLETERQL---------------GEAHGRLKEQRQLSS---------EKLMEKEQQVADLQLKLSRLE 351
Cdd:COG4913 553 AELGRrfdYVC--VDSPEELrrhpraitragqvkgNGTRHEKDDRRRIRSryvlgfdnrAKLAALEAELAELEEELAEAE 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 352 EQLKEkvtnSTELQHQLEKSKQQHQEQqalqqsatAKLREAQNDLEQVLRQIGDKDQKIQNLEAllqkGKESVSLLEKER 431
Cdd:COG4913 631 ERLEA----LEAELDALQERREALQRL--------AEYSWDEIDVASAEREIAELEAELERLDA----SSDDLAALEEQL 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 432 EDLYAKIQAGEGEtavLNQLQEKNHALQQQLTQLTEKLKnqsESHKQAEENLHDQVQEQKAHL-----RAAQDRVL---- 502
Cdd:COG4913 695 EELEAELEELEEE---LDELKGEIGRLEKELEQAEEELD---ELQDRLEAAEDLARLELRALLeerfaAALGDAVErelr 768
|
570 580
....*....|....*....|.
gi 568967304 503 -SLETSVSELSSQLNESKEKV 522
Cdd:COG4913 769 eNLEERIDALRARLNRAEEEL 789
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
48-292 |
3.00e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 48 QKAAQLATEIAD------IKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKtellQRPGIEDVAVLKKELVQVQTl 121
Cdd:COG3206 148 ELAAAVANALAEayleqnLELRREEARKALEFLEEQLPELRKELEEAEAALEEFR----QKNGLVDLSEEAKLLLQQLS- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 122 mdnmTLEREREseklkdeckKLQSEHAHLEATINQLRSELAKGPQEVAVYVQ--EIQKLKGSINELTQKNQNLTEKLQKK 199
Cdd:COG3206 223 ----ELESQLA---------EARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPN 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 200 DLDYTHLEEKHNE-ESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKV 278
Cdd:COG3206 290 HPDVIALRAQIAAlRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
250
....*....|....
gi 568967304 279 EVKQLQQQREEKEQ 292
Cdd:COG3206 370 LLQRLEEARLAEAL 383
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
597-1133 |
3.03e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 597 KDHKEKHLSLEQKVEDLEGhikkleadalEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEvvscTKLDLQNK 676
Cdd:PRK03918 178 IERLEKFIKRTENIEELIK----------EKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 677 SEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGD--RMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSL 754
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 755 KNSKSEFEKENQKgKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQ 834
Cdd:PRK03918 324 NGIEERIKELEEK-EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 835 KEKDEQQLQGTINQLKQSAEQKKKQIEALQG-EVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADL 913
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKaKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 914 KQLQSDLyGKESELLATRQ---DLKSVEEKLT-LAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEAL---LKEQ 986
Cdd:PRK03918 483 RELEKVL-KKESELIKLKElaeQLKELEEKLKkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELkkkLAEL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 987 SKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDS 1066
Cdd:PRK03918 562 EKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568967304 1067 LKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNE 1133
Cdd:PRK03918 642 LEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
|
|
| PTZ00303 |
PTZ00303 |
phosphatidylinositol kinase; Provisional |
1210-1295 |
5.61e-06 |
|
phosphatidylinositol kinase; Provisional
Pssm-ID: 140324 [Multi-domain] Cd Length: 1374 Bit Score: 51.24 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1210 AAVQELGRENQSLQIKHTQAL-NRKWAEDNEVQN-CMSCGKCF-----SVTVRRHHCRQCGNIFCAECSTKNA------- 1275
Cdd:PTZ00303 428 ATVGGVAEENELNTFGLTKLLhNPSWQKDDESSDsCPSCGRAFislsrPLGTRAHHCRSCGIRLCVFCITKRAhysfakl 507
|
90 100
....*....|....*....|...
gi 568967304 1276 LTPSSKKPVR---VCDACFNDLQ 1295
Cdd:PTZ00303 508 AKPGSSDEAEerlVCDTCYKEYE 530
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
14-932 |
7.11e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.82 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 14 LVTDSSAELQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRaAAEQKVTHLTEDLNKQTTVIQ 93
Cdd:TIGR00606 194 VRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLK-NRLKEIEHNLSKIMKLDNEIK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 94 DLKTELLQRPGIEDVAVLKKELVQVQTlmdnmtlerereSEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQ 173
Cdd:TIGR00606 273 ALKSRKKQMEKDNSELELKMEKVFQGT------------DEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQ 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 174 EIQKLKGSINELTQKNQNLTEKLQKKDLDY----THLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTAseSSLQRAQ 249
Cdd:TIGR00606 341 EKTELLVEQGRLQLQADRHQEHIRARDSLIqslaTRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAA--QLCADLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 250 GELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQG---EVSQLHCKLLETERQLGEAHGRLKEQR 326
Cdd:TIGR00606 419 SKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGssdRILELDQELRKAERELSKAEKNSLTET 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 327 QLSSEKLMEKEQqvADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREaqndleqVLRQIGDK 406
Cdd:TIGR00606 499 LKKEVKSLQNEK--ADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDE-------LTSLLGYF 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 407 DQKIQnLEALLQKGKESVSLLEKEREDLYAKIQAGEGETavlNQLQEKNHALQQQLTQLTEKLKN--QSESHKQAEENLH 484
Cdd:TIGR00606 570 PNKKQ-LEDWLHSKSKEINQTRDRLAKLNKELASLEQNK---NHINNELESKEEQLSSYEDKLFDvcGSQDEESDLERLK 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 485 DQVQEQKAHlRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSaeaakaaqraDLQNHLDTAQHALQDK 564
Cdd:TIGR00606 646 EEIEKSSKQ-RAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFIS----------DLQSKLRLAPDKLKST 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 565 QQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEAdALEVKASKEQALQSLQQQRQL 644
Cdd:TIGR00606 715 ESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET-LLGTIMPEEESAKVCLTDVTI 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 645 STDLELRNAELSRELQEQeevvsCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELgDRMQAAVT 724
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQ-----AAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI-QHLKSKTN 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 725 ELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSL 804
Cdd:TIGR00606 868 ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK 947
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 805 EKEKETSQQLKIELNSVKgevSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQ 884
Cdd:TIGR00606 948 EKVKNIHGYMKDIENKIQ---DGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLR 1024
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 568967304 885 SSQA-----AQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQ 932
Cdd:TIGR00606 1025 KRENelkevEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQ 1077
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
658-1167 |
7.71e-06 |
|
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: 50.40 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 658 ELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLsqdsKTQHKELGDRMQAAVTELTAVKAQKDALL 737
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKIL----EQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 738 AELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKhQLQVQAESALKEQEDLKKSLEKEKETSQQLKIE 817
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELE-KLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 818 LNSVKGEVSQAQNTL---KQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVknavSQKTVLENKLQQQSSQAAQELAA 894
Cdd:TIGR04523 189 IDKIKNKLLKLELLLsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI----NEKTTEISNTQTQLNQLKDEQNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 895 EKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQ------------DLKSVEEKLTLAQEDLISNRNQIGNQNKSI 962
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkeqdwnkelksELKNQEKKLEEIQNQISQNNKIISQLNEQI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 963 QELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKE 1042
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1043 ITNLKDAKQLLIQQKLELQgrvDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENea 1122
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIK---DLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK-- 499
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 568967304 1123 KLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLE 1167
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
747-1223 |
1.05e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 747 LSKVSDSLKNSKSEFEKENQKGKAAVL-DLEKACKELKHQL---QVQAESALKEQEDLKKSLEKEKETSQqlkiELNSVK 822
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLnGLESELAELDEEIeryEEQREQARETRDEADEVLEEHEERRE----ELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 823 GEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVK-NAVSQKTVLENK--LQQQSSQAAQELAAEKGKL 899
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlDDADAEAVEARReeLEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 900 SALQSNYEKCQADLKQLQSDLYGK-------ESELLATRQDLKSVEEKLTLAQEDLISNRN-------QIGNQNKSIQEL 965
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELreeaaelESELEEAREAVEDRREEIEELEEEIEELRErfgdapvDLGNAEDFLEEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 966 QAAKASLEQDSAKKEALLKEQSKALEDAQR---EKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKE 1042
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEEAEAlleAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEER 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1043 ITNLKDAKqlliqqklELQGRVDSLKaalEQEKESQQLM--REQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEEN 1120
Cdd:PRK02224 498 LERAEDLV--------EAEDRIERLE---ERREDLEELIaeRRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1121 EAKLTMQVTTLNENLGTVKKEWQsSQRRVSELEKQTDDLRGEIAVLE---ATVQNNQDERRALL----ERCLKGEGE--- 1190
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERIE-SLERIRTLLAAIADAEDEIERLRekrEALAELNDERRERLaekrERKRELEAEfde 645
|
490 500 510
....*....|....*....|....*....|....*
gi 568967304 1191 --IEKLQTKALELQRKLDNTTAAVQELGRENQSLQ 1223
Cdd:PRK02224 646 arIEEAREDKERAEEYLEQVEEKLDELREERDDLQ 680
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
854-1178 |
1.16e-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: 50.07 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 854 EQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQD 933
Cdd:TIGR02169 194 DEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 934 LKSVEEKLtlaqEDLISNRnqignqnksIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAE 1013
Cdd:TIGR02169 274 LEELNKKI----KDLGEEE---------QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1014 MEEIKCRQEKEITKLNEELKSHKQE---SIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEqEKESQQLMREQVKKEEE 1090
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEEledLRAELEEVDKEFAETRDELKDYREKLEKLKREIN-ELKRELDRLQEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1091 KRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATV 1170
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
....*...
gi 568967304 1171 QNNQDERR 1178
Cdd:TIGR02169 500 RASEERVR 507
|
|
| FYVE_WDFY2 |
cd15757 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); WDFY2, also ... |
1252-1290 |
1.22e-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: 1.22e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 568967304 1252 VTVRRHHCRQCGNIFCAECSTKNALTP--SSKKPVRVCDAC 1290
Cdd:cd15757 29 IGLRQHHCRKCGKAVCGKCSSKRSTIPlmGFEFEVRVCDSC 69
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
138-370 |
1.45e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 138 DECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKkdldythLEEKHNEESASR 217
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-------LEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 218 KTLQASLHQRDldcQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQhglqL 297
Cdd:COG4942 93 AELRAELEAQK---EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA----L 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967304 298 QGEVSQLHCKLLETERQLGEAHGRLKEQRQlsseklmEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEK 370
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKA-------ERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
389-948 |
1.50e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.51 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 389 LREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEK 468
Cdd:PRK01156 178 LRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 469 LKnQSESHKQAEENLHDQVQE-QKAHLRAAQDRVLSLETSVSE---LSSQLNESKEKVSQLDIQIKAKTELLlsaeaaka 544
Cdd:PRK01156 258 IK-TAESDLSMELEKNNYYKElEERHMKIINDPVYKNRNYINDyfkYKNDIENKKQILSNIDAEINKYHAII-------- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 545 AQRADLQNHLDTaqhaLQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADA 624
Cdd:PRK01156 329 KKLSVLQKDYND----YIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 625 LEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEE-----------VVSCTKLDLQNKSEILENIKQTLTKKEEE 693
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRnmemlngqsvcPVCGTTLGEEKSNHIINHYNEKKSRLEEK 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 694 NVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDslKNSKSEfEKENQKGKAAVL 773
Cdd:PRK01156 485 IREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKD--KHDKYE-EIKNRYKSLKLE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 774 DLEKACKELKHQLQVQA----ESALKEQEDLKKSLEKEKETSQQLKIELNSVKgevSQAQNTLKQKEKDEQQLQGTINQL 849
Cdd:PRK01156 562 DLDSKRTSWLNALAVISlidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLNNKYNEI 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 850 kqsaEQKKKQIEALQGEVKNAVSQktvlenklQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLA 929
Cdd:PRK01156 639 ----QENKILIEKLRGKIDNYKKQ--------IAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEI 706
|
570
....*....|....*....
gi 568967304 930 TRQDLKSVEEKLTLAQEDL 948
Cdd:PRK01156 707 LRTRINELSDRINDINETL 725
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
251-497 |
1.79e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 251 ELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHgLQLQGEVSQLhcklleteRQLGEAHGRLKEQR--QL 328
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERY-AAARERLAEL--------EYLRAALRLWFAQRrlEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 329 SSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKqqhqeqqalqqsaTAKLREAQNDLEQVLRQIGDKDQ 408
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG-------------GDRLEQLEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 409 KIQNLEALLQKGKESVSLLEKEREDLYAKIQA-GEGETAVLNQLQEKNHALQQQLTQLTEK---LKNQSESHKQAEENLH 484
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRAEAAAlLEALEEELEALEEALAEAEAALRDLRRElreLEAEIASLERRKSNIP 439
|
250
....*....|...
gi 568967304 485 DQVQEQKAHLRAA 497
Cdd:COG4913 440 ARLLALRDALAEA 452
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
745-1228 |
1.91e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 745 EKLSKVSDSLKNSKSEFEKENQKGKaavlDLEKACKELKHQLQvQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGE 824
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEKEKELE-EVLREINEISSELPELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 825 VSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAaqELAAEKGKLSALQS 904
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE--EYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 905 NYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLisnrnqignqnKSIQELQAAKASLEQDSAKKEALLK 984
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH-----------ELYEEAKAKKEELERLKKRLTGLTP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 985 EQSKA-LEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKL---------------NEELKSHKQESIKEITNLKD 1048
Cdd:PRK03918 387 EKLEKeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcgreltEEHRKELLEEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1049 AKQLLIQQKLELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRK-----EEFSEKEAKLHSEIKEKEAGMKKHEENEAK 1123
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKlkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1124 LTMQVTTLNENLGTVKKEWQSSQRRVSELEKQ--------TDDLRGEIAVLEA------TVQNNQDERRALLERclkgeg 1189
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLDELEEELAELLKEleelgfesVEELEERLKELEPfyneylELKDAEKELEREEKE------ 620
|
490 500 510
....*....|....*....|....*....|....*....
gi 568967304 1190 eIEKLQTKALELQRKLDNTTAAVQELGRENQSLQIKHTQ 1228
Cdd:PRK03918 621 -LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
574-1073 |
2.13e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 574 QLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNA 653
Cdd:PRK02224 238 EADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 654 ELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMqaavTELTAVKAQK 733
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRR----EEIEELEEEI 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 734 DALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAE----------------SALKEQ 797
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvETIEED 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 798 EDLKKSLEKEKEtsqQLKIELNSVKGEVSQAQnTLKQKEKDEQQLqgtinqlkqsaEQKKKQIEALQGEVKNAVSQKTVL 877
Cdd:PRK02224 474 RERVEELEAELE---DLEEEVEEVEERLERAE-DLVEAEDRIERL-----------EERREDLEELIAERRETIEEKRER 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 878 ENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLygkeSELLATRQDLKSVEEKLTLAQEdlisNRNQIGN 957
Cdd:PRK02224 539 AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL----AELKERIESLERIRTLLAAIAD----AEDEIER 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 958 QNKSIQELQA----AKASLEQDSAKKEALLKE-QSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEEL 1032
Cdd:PRK02224 611 LREKREALAElndeRRERLAEKRERKRELEAEfDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL 690
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 568967304 1033 KSHK--QESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQ 1073
Cdd:PRK02224 691 EELEelRERREALENRVEALEALYDEAEELESMYGDLRAELRQ 733
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
127-529 |
3.20e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 127 LERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSIN--ELTQKNQNLTEKLQKKDLDYT 204
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 205 HLEEKHNEesasRKTLQASLHQRDLDCQQLQARL-TASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQL 283
Cdd:COG4717 150 ELEERLEE----LRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 284 QQQREEKEQHGLQLQgevsqlHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTE 363
Cdd:COG4717 226 EEELEQLENELEAAA------LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 364 LQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKE-----SVSLLEKEREDLYAKI 438
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEleeelQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 439 QAGEGETAV--------LNQLQEKNHALQQQLTQLTEKLKNQSESHKqaEENLHDQVQEQKAHLRAAQDRVLSLETSVSE 510
Cdd:COG4717 380 GVEDEEELRaaleqaeeYQELKEELEELEEQLEELLGELEELLEALD--EEELEEELEELEEELEELEEELEELREELAE 457
|
410 420
....*....|....*....|.
gi 568967304 511 LSSQLN--ESKEKVSQLDIQI 529
Cdd:COG4717 458 LEAELEqlEEDGELAELLQEL 478
|
|
| FYVE1_Vac1p_like |
cd15761 |
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ... |
1234-1291 |
3.24e-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: 3.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568967304 1234 WAEDNEVQNCMSCGKCFSVTVRRHHCRQCGNIFCAECST------KNA-LTPSSKKPVRVCDACF 1291
Cdd:cd15761 4 WKKPSGKSRCSECGKTLNKKNGIVNCRKCGELFCNEHCRnriklnNSAeYDPKNGKWCRCCEKCF 68
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
213-358 |
4.43e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 47.77 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 213 ESASRKTLQASLHQRDLDcqQLQARLTASE---SSLQRAQGELSEkaEAAQKLREELREVESTRQHLKvevkqlQQQREE 289
Cdd:COG0542 397 EAAARVRMEIDSKPEELD--ELERRLEQLEiekEALKKEQDEASF--ERLAELRDELAELEEELEALK------ARWEAE 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 290 KE--QHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSE--------------------KLMEKEQQvadlqlKL 347
Cdd:COG0542 467 KEliEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREevteediaevvsrwtgipvgKLLEGERE------KL 540
|
170
....*....|.
gi 568967304 348 SRLEEQLKEKV 358
Cdd:COG0542 541 LNLEEELHERV 551
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
112-614 |
4.69e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 112 KKELVQVQTLMDNMTLERERESEKLkDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKnqn 191
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE--- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 192 lTEKLQKKDLDYTHLEEKHNEESASRKtLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVES 271
Cdd:PRK03918 275 -IEELEEKVKELKELKEKAEEYIKLSE-FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 272 TRQHLKVEVKQLQQQREEKEqhglQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEK----EQQVADLQLKL 347
Cdd:PRK03918 353 RLEELEERHELYEEAKAKKE----ELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARigelKKEIKELKKAI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 348 SRLEEQLKEKVTNSTELQHQ-----LEKSKQQHQEQQALQQSATAKLREAQNDLEQV---------LRQIGDKDQKIQNL 413
Cdd:PRK03918 429 EELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELekvlkkeseLIKLKELAEQLKEL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 414 EALLQK-GKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLH-------D 485
Cdd:PRK03918 509 EEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfesvE 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 486 QVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDiQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHalQDKQ 565
Cdd:PRK03918 589 ELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELD-KAFEELAETEKRLEELRKELEELEKKYSEEEY--EELR 665
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 568967304 566 QELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLE 614
Cdd:PRK03918 666 EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
892-1145 |
6.08e-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: 47.07 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 892 LAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKAS 971
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 972 LEQDSAKKEALLKEQSKAledAQREKSVKEKELVAEKSKLAEMEeikcrqekeitKLNEELKSHKQESIKEITNLKDAKQ 1051
Cdd:COG4942 95 LRAELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAV-----------RRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1052 LLIQQKLELQGRVDSLKAALEQEKESQQLMReqvkkeeeKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTL 1131
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALE--------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|....
gi 568967304 1132 NENLGTVKKEWQSS 1145
Cdd:COG4942 233 EAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
825-1073 |
6.52e-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: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 825 VSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSqaaqELAAEKGKLSALQS 904
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ----ELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 905 NYEKCQADLKQLQSDLygkeSELLATRQDLKSVEE-KLTLAQEDLisnrnqignqnksiqelqaakasleQDSAKKEALL 983
Cdd:COG4942 91 EIAELRAELEAQKEEL----AELLRALYRLGRQPPlALLLSPEDF-------------------------LDAVRRLQYL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 984 KEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGR 1063
Cdd:COG4942 142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
250
....*....|
gi 568967304 1064 VDSLKAALEQ 1073
Cdd:COG4942 222 AEELEALIAR 231
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
60-284 |
6.81e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 60 IKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTELLQRPG-----IEDVAVLKKELVQVQTLMDNMTLERERESE 134
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIArkqnkYDELVEEAKTIKAEIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 135 KLKDECKKLQSEHAHLEATINQLRSELA--KGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNE 212
Cdd:PHA02562 252 DPSAALNKLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDE 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568967304 213 ESASRKT---LQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQ 284
Cdd:PHA02562 332 FNEQSKKlleLKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRG 406
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
821-1239 |
7.40e-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: 47.53 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 821 VKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLS 900
Cdd:pfam12128 239 IRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 901 ALQSNYEKCQADLKQLQSD----LYGKESELLATRQDLKSVEEKLTLaqedlisnrnQIGNQNKSIQELQAAKASLEQDS 976
Cdd:pfam12128 319 KDRSELEALEDQHGAFLDAdietAAADQEQLPSWQSELENLEERLKA----------LTGKHQDVTAKYNRRRSKIKEQN 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 977 AKK-EALLKEQSKALEDAQREKSVKEKELVAEKSKL------------AEMEEIKCRQEKEITKLN-----EELKSHKQE 1038
Cdd:pfam12128 389 NRDiAGIKDKLAKIREARDRQLAVAEDDLQALESELreqleagklefnEEEYRLKSRLGELKLRLNqatatPELLLQLEN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1039 SIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHE 1118
Cdd:pfam12128 469 FDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWE 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1119 ENEAKLTMQVTTLNENLGTVKKEWQSSQRR-------------VSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCL 1185
Cdd:pfam12128 549 QSIGKVISPELLHRTDLDPEVWDGSVGGELnlygvkldlkridVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLV 628
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 568967304 1186 KGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQIKHTQALNRKWAEDNE 1239
Cdd:pfam12128 629 QANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANE 682
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
529-1125 |
7.95e-05 |
|
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: 47.02 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 529 IKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQ 608
Cdd:pfam05483 196 ILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 609 KV----EDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEE--------------VVSCTK 670
Cdd:pfam05483 276 KTklqdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAqmeelnkakaahsfVVTEFE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 671 LDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKeLGDRMQAAVTELTAVKAQKDALLAElsttKEKLSKV 750
Cdd:pfam05483 356 ATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTK-FKNNKEVELEELKKILAEDEKLLDE----KKQFEKI 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 751 SDSLKNSKSEFEKENQKGKAAVLDLEKACKELKhqlqVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQN 830
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKEIHDLEIQLTAIK----TSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQ 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 831 TLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQgevknavSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQ 910
Cdd:pfam05483 507 EASDMTLELKKHQEDIINCKKQEERMLKQIENLE-------EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIE 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 911 ADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKAL 990
Cdd:pfam05483 580 YEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNY 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 991 EDAQREKSVKEKELVAEKSKLAEMEEikcrqekEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAA 1070
Cdd:pfam05483 660 QKEIEDKKISEEKLLEEVEKAKAIAD-------EAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKN 732
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 568967304 1071 LEQEKESqqlMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLT 1125
Cdd:pfam05483 733 KEQEQSS---AKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
924-1223 |
8.07e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 924 ESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQdsaKKEALLKEQSKALEDAQREKSVKEKE 1003
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKE---KREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1004 LVAEKSKLAEMEEIKCRQEKEITKLNEELKshkqESIKEITNLKDAKQLLIQQKL-ELQGRVDSLKAALEqEKESQQLMR 1082
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLE----ELNKKIKDLGEEEQLRVKEKIgELEAEIASLERSIA-EKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1083 EQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGE 1162
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967304 1163 IAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQ 1223
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
239-626 |
8.26e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 8.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 239 TASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQqREEKEQHGLQLQGEVSQLHCKLLETERQLGEA 318
Cdd:PRK04863 289 LELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASD-HLNLVQTALRQQEKIERYQADLEELEERLEEQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 319 HGRLK---EQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQH---QLEKSKQQHQEQQALQQSATAKLREA 392
Cdd:PRK04863 368 NEVVEeadEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQavqALERAKQLCGLPDLTADNAEDWLEEF 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 393 QNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEK-----EREDLY----AKIQAGEGETAVLNQLQ---------EK 454
Cdd:PRK04863 448 QAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagevSRSEAWdvarELLRRLREQRHLAEQLQqlrmrlselEQ 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 455 NHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAhlraaqdRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTE 534
Cdd:PRK04863 528 RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEA-------RLESLSESVSEARERRMALRQQLEQLQARIQRLAA 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 535 LllsaeaakaaqradlqnhlDTAQHALQDKqqelnkvsvqLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLE 614
Cdd:PRK04863 601 R-------------------APAWLAAQDA----------LARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELA 651
|
410
....*....|..
gi 568967304 615 GHIKKLEADALE 626
Cdd:PRK04863 652 ARKQALDEEIER 663
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
329-531 |
8.76e-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: 46.30 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 329 SSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQ 408
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 409 KIQNLEALLQK--------GKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLtEKLKNQSESHKQAE 480
Cdd:COG4942 98 ELEAQKEELAEllralyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL-AALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568967304 481 ENLHDQVQEQKAHLRAAQDR----VLSLETSVSELSSQLNESKEKVSQLDIQIKA 531
Cdd:COG4942 177 EALLAELEEERAALEALKAErqklLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
964-1229 |
1.10e-04 |
|
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: 46.97 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 964 ELQAAKASLEQDSAKKEALlKEQSKALEDAQREKSVKEKElvAEKSKLAEMEEIKCRQEKEITKLNEELkshkQESIKEI 1043
Cdd:TIGR02168 197 ELERQLKSLERQAEKAERY-KELKAELRELELALLVLRLE--ELREELEELQEELKEAEEELEELTAEL----QELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1044 TNLKDAKQLLIQQKLELQGRVDSLKAalEQEKESQQLMReqvkkeeekrkeeFSEKEAKLHSEIKEKEAGMKKHEENEAK 1123
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALAN--EISRLEQQKQI-------------LRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1124 LTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKALELQR 1203
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260
....*....|....*....|....*.
gi 568967304 1204 KLDNTTAAVQELGRENQSLQIKHTQA 1229
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQA 440
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
214-419 |
1.41e-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: 45.91 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 214 SASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQH 293
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 294 GLQLQGEVSQLHCKLLETERQ-------LGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQH 366
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568967304 367 QLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQK 419
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
384-612 |
1.47e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 384 SATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQ--KGKESVSLLEKEREDLYAKIQAGEGEtavLNQLQEKNHALQQQ 461
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQ---LAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 462 LTQLTEKLKNQSESHKQAEENlhDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEA 541
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967304 542 AKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEhciQLESHLKDHKEKHLSLEQKVED 612
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE---LYESLLQRLEEARLAEALTVGN 387
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
176-1182 |
2.00e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 176 QKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEK 255
Cdd:pfam01576 22 QKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 256 AEAAQKLREELREVESTRQHLKVE-------VKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQL 328
Cdd:pfam01576 102 QQHIQDLEEQLDEEEAARQKLQLEkvtteakIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 329 SS----------EKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQ 398
Cdd:pfam01576 182 KNkheamisdleERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 399 VLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETA----VLNQLQEKNHALQQQLTQLTEKLKNQSE 474
Cdd:pfam01576 262 ALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdtldTTAAQQELRSKREQEVTELKKALEEETR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 475 SHK-----------QAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLneskEKVSQLDIQIKAKTELLLSAEAAK 543
Cdd:pfam01576 342 SHEaqlqemrqkhtQALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL----RTLQQAKQDSEHKRKKLEGQLQEL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 544 AAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEAD 623
Cdd:pfam01576 418 QARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDE 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 624 ALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEK 703
Cdd:pfam01576 498 RNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 704 LSQDSKTQHKELgDRMQAAVTELTAVKAQKDALLAELSTtkeklskVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELK 783
Cdd:pfam01576 578 LQQELDDLLVDL-DHQRQLVSNLEKKQKKFDQMLAEEKA-------ISARYAEERDRAEAEAREKETRALSLARALEEAL 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 784 hqlqvqaeSALKEQEDLKKSLEKEKEtsqqlkiELNSVKGEVSqaqntlkqkeKDEQQLQGTINQLKQSAEQKKKQIEAL 863
Cdd:pfam01576 650 --------EAKEELERTNKQLRAEME-------DLVSSKDDVG----------KNVHELERSKRALEQQVEEMKTQLEEL 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 864 QGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTL 943
Cdd:pfam01576 705 EDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEA 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 944 AQEDLISNRNQIGNQNKSIQ-ELQAAKASLEQDSAKKEALLKEQskaledaqREKSVKEKELVAEKSKLAEMEEIKCRQE 1022
Cdd:pfam01576 785 QIDAANKGREEAVKQLKKLQaQMKDLQRELEEARASRDEILAQS--------KESEKKLKNLEAELLQLQEDLAASERAR 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1023 KEITKLNEELKshkqesiKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMreqvkkeeekrkeefsekeak 1102
Cdd:pfam01576 857 RQAQQERDELA-------DEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELL--------------------- 908
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1103 lhseikekeagmkkhEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLE 1182
Cdd:pfam01576 909 ---------------NDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALE 973
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
350-1073 |
2.09e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 350 LEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGD-KDQKIQNLEALLQKGKESVSLLE 428
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADiRRRESQSQEDLRNQLQNTVHELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 429 KEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENL------------HDQVQEQKAHLRA 496
Cdd:pfam15921 156 AAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMstmhfrslgsaiSKILRELDTEISY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 497 AQDRVLSLETSVSELSSqlnESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQD-----KQQELNKV 571
Cdd:pfam15921 236 LKGRIFPVEDQLEALKS---ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSqleiiQEQARNQN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 572 SVQLDQLTakfqEKQEHCIQLESHLKDHKEKHlslEQKVEDLEGHIKKLEADALEVKASKEQALQSL----QQQRQLSTD 647
Cdd:pfam15921 313 SMYMRQLS----DLESTVSQLRSELREAKRMY---EDKIEELEKQLVLANSELTEARTERDQFSQESgnldDQLQKLLAD 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 648 LELRNAELSRELQEQEEVvscTKLDLQNkSEILENIKQTLTKKEEEnvvlKQEFEKLSQDSKTQHKELGDRMQAAVTELT 727
Cdd:pfam15921 386 LHKREKELSLEKEQNKRL---WDRDTGN-SITIDHLRRELDDRNME----VQRLEALLKAMKSECQGQMERQMAAIQGKN 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 728 AVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQkgkaAVLDLEKACKELKHQLQVQAE--SALKEQEDLK---- 801
Cdd:pfam15921 458 ESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSER----TVSDLTASLQEKERAIEATNAeiTKLRSRVDLKlqel 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 802 KSLEKEKETSQQLKIELNSVKGEVSQAQNT---LKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLE 878
Cdd:pfam15921 534 QHLKNEGDHLRNVQTECEALKLQMAEKDKVieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILK 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 879 NKLQQ---QSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYgkeSELLATRQDLKSVEEKLTLAQEDLISNRNQI 955
Cdd:pfam15921 614 DKKDAkirELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLL---NEVKTSRNELNSLSEDYEVLKRNFRNKSEEM 690
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 956 -GNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDA---QREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEE 1031
Cdd:pfam15921 691 eTTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAmgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEE 770
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 568967304 1032 LKSHKQE---SIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQ 1073
Cdd:pfam15921 771 KNKLSQElstVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
19-625 |
2.13e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.98 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 19 SAELQALEQQLEEAQTENFNIKQMKDLFEQKAA-QLATEIADIKSKYD---EEKSLRAAAEQKV-----THLTEDLNKQT 89
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYNRRRSKIKeQNNRDIAGIKDKLAkirEARDRQLAVAEDDlqaleSELREQLEAGK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 90 TVIQDLKTELlqrpgIEDVAVLKKELVQVQtlmdnMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVA 169
Cdd:pfam12128 433 LEFNEEEYRL-----KSRLGELKLRLNQAT-----ATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRD 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 170 VYVQEIQKLKGSINELTQKNQNLTEKLQKKD---LDYTHLEEKHNEESASRKTLQASLHQRDLD----CQQLQARLTASE 242
Cdd:pfam12128 503 QASEALRQASRRLEERQSALDELELQLFPQAgtlLHFLRKEAPDWEQSIGKVISPELLHRTDLDpevwDGSVGGELNLYG 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 243 SSLQRAQGELSEKAEAAQKLREELREVESTrqhlkvevkqLQQQREEKEQhglqLQGEVSQLHCKLLETERQLGEAHGRL 322
Cdd:pfam12128 583 VKLDLKRIDVPEWAASEEELRERLDKAEEA----------LQSAREKQAA----AEEQLVQANGELEKASREETFARTAL 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 323 KEQRQLSSEKLMEKEQqvadLQLKLSR-LEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLr 401
Cdd:pfam12128 649 KNARLDLRRLFDEKQS----EKDKKNKaLAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVV- 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 402 qIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETavlnqlQEKNHALQQQLTQLTEKLKNqSESHKQAEE 481
Cdd:pfam12128 724 -EGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVD------PDVIAKLKREIRTLERKIER-IAVRRQEVL 795
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 482 NLHDQVQEQ-KAHLRAAQDRVLSLETSVSELSSQLNeskekvsqldiQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHA 560
Cdd:pfam12128 796 RYFDWYQETwLQRRPRLATQLSNIERAISELQQQLA-----------RLIADTKLRRAKLEMERKASEKQQVRLSENLRG 864
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568967304 561 LQDKQQELNKVsvQLDQLTAKFQEKQEHCI-QLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADAL 625
Cdd:pfam12128 865 LRCEMSKLATL--KEDANSEQAQGSIGERLaQLEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGL 928
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
485-1034 |
2.14e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 485 DQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLlsaeAAKAAQRADLQNHLDTAQHALQDK 564
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELC----AEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 565 QQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQqrql 644
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKL---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 645 stdLELRNAELSRELQEQEEVV-SCTKLDLQNKSEILEnIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDrMQAAV 723
Cdd:pfam01576 157 ---LEERISEFTSNLAEEEEKAkSLSKLKNKHEAMISD-LEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAE-LQAQI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 724 TELTAVKAQKD-------ALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQV-------- 788
Cdd:pfam01576 232 AELRAQLAKKEeelqaalARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEAlkteledt 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 789 -------QAESALKEQE--DLKKSLEKEKETSQQlkiELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQ 859
Cdd:pfam01576 312 ldttaaqQELRSKREQEvtELKKALEEETRSHEA---QLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 860 IEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEE 939
Cdd:pfam01576 389 LQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLES 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 940 KLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKC 1019
Cdd:pfam01576 469 QLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKK 548
|
570
....*....|....*
gi 568967304 1020 RQEKEITKLNEELKS 1034
Cdd:pfam01576 549 RLQRELEALTQQLEE 563
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
123-418 |
2.31e-04 |
|
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: 45.50 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 123 DNMTLERERESEKLKDECKKLQSEhahleatinQLRSElakgpqEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDld 202
Cdd:pfam17380 340 ERMAMERERELERIRQEERKRELE---------RIRQE------EIAMEISRMRELERLQMERQQKNERVRQELEAAR-- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 203 ythlEEKHNEESASRKTLQASLHQRDLDCQQLQARltasesslqraQGELSEKAEAAQKLREELREVESTRQHlkvEVKQ 282
Cdd:pfam17380 403 ----KVKILEEERQRKIQQQKVEMEQIRAEQEEAR-----------QREVRRLEEERAREMERVRLEEQERQQ---QVER 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 283 LQQQREEKEQHGLQLQGEvsqlhckllETERQLGEahgrlKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNST 362
Cdd:pfam17380 465 LRQQEEERKRKKLELEKE---------KRDRKRAE-----EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIY 530
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568967304 363 ELQH----QLEKSKQQHQEQQALQQSATAKLREAQNDLE------QVLRQIGDKDQKIQNLEALLQ 418
Cdd:pfam17380 531 EEERrreaEEERRKQQEMEERRRIQEQMRKATEERSRLEamererEMMRQIVESEKARAEYEATTP 596
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
219-365 |
2.41e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 219 TLQASLHQRDLDCQQLQARLTASESSLQR--------AQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEK 290
Cdd:PRK04863 939 QLKQDYQQAQQTQRDAKQQAFALTEVVQRrahfsyedAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQY 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 291 EQHGLQLQGEVSQLHCKLLETERQLGE--------AHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNST 362
Cdd:PRK04863 1019 NQVLASLKSSYDAKRQMLQELKQELQDlgvpadsgAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLR 1098
|
...
gi 568967304 363 ELQ 365
Cdd:PRK04863 1099 KLE 1101
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
787-1060 |
2.59e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 787 QVQAESALKEQEDLKKSLEKEKETSQQlkielnsvkgevSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGE 866
Cdd:PRK11281 28 RAASNGDLPTEADVQAQLDALNKQKLL------------EAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 867 VKNAVSQKTVLENKLQQQSSQAAQELAaekgkLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQE 946
Cdd:PRK11281 96 LRQAQAELEALKDDNDEETRETLSTLS-----LRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 947 DLISNRNQIGNQNKS--------IQELQAAKASLEQDSAKKEALLK--EQSKALEDAQReksvkekELVAEKSKlaemee 1016
Cdd:PRK11281 171 RLQQIRNLLKGGKVGgkalrpsqRVLLQAEQALLNAQNDLQRKSLEgnTQLQDLLQKQR-------DYLTARIQ------ 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568967304 1017 ikcRQEKEITKL----NEELKSHKQESIKEITNLKDAKQL----LIQQKLEL 1060
Cdd:PRK11281 238 ---RLEHQLQLLqeaiNSKRLTLSEKTVQEAQSQDEAARIqanpLVAQELEI 286
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
824-1070 |
2.72e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 824 EVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAvsqktvlenklqqqssqaAQELAAEKGKLSALQ 903
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL------------------QAEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 904 SNYEKCQADLKQLQSDLYgkesellaTRQDLKSVEEKLTLAQ--EDLISNRNQI----GNQNKSIQELQAAKASLEQDSA 977
Cdd:COG3883 79 AEIEERREELGERARALY--------RSGGSVSYLDVLLGSEsfSDFLDRLSALskiaDADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 978 KKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQK 1057
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250
....*....|...
gi 568967304 1058 LELQGRVDSLKAA 1070
Cdd:COG3883 231 AAAAAAAAAAAAA 243
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
325-534 |
3.35e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 325 QRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIG 404
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 405 DKDQKIQNLEALLqkgkESVSLlekerEDLYAKIQAgegetavLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLH 484
Cdd:COG3883 97 RSGGSVSYLDVLL----GSESF-----SDFLDRLSA-------LSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568967304 485 DQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTE 534
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
672-870 |
3.48e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 672 DLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVS 751
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 752 DSL-KNSKSEFEKE--NQKGKAAVLDLEKACKELKHQLQVQAE---SALKEQEDLKKSLEKEKETSQQLKIELNSVKGEV 825
Cdd:COG4942 111 RALyRLGRQPPLALllSPEDFLDAVRRLQYLKYLAPARREQAEelrADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568967304 826 SQAQN----TLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNA 870
Cdd:COG4942 191 EALKAerqkLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
322-533 |
3.84e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 322 LKEQRQLSSEKLMEKEQQVADLQLK--LSRLEEQLKEKVTNSTELQHQLEKSKqqhqeqqalqqsatAKLREAQNDLEQV 399
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEAR--------------AELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 400 LRQIGDKDQKIQNLEA--LLQKGKESVSLLEKEREDLYAKIQAGEGE-TAVLNQLQEKNHALQQQLTQLTEKLKNQSESH 476
Cdd:COG3206 246 RAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDvIALRAQIAALRAQLQQEAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 477 KQAEENLHDQVQEQKAHLR---AAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKT 533
Cdd:COG3206 326 QAREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYESLLQRLEEARLAEALTV 385
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
22-419 |
4.48e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.50 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 22 LQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIK---SKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLKTE 98
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKeelRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 99 LLQRpgiedvavlKKELVQVQTLMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKL 178
Cdd:pfam07888 127 HEAR---------IRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 179 KGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQAslhqrdldcqqLQARLTASEsslqraqgelsekaEA 258
Cdd:pfam07888 198 RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRS-----------LQERLNASE--------------RK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 259 AQKLREELREVESTRQHLKVEVKQLQQQreekeqhglqlqgeVSQLHCKLLETERQLGEAHGRLKEQR---QLSSEKLME 335
Cdd:pfam07888 253 VEGLGEELSSMAAQRDRTQAELHQARLQ--------------AAQLTLQLADASLALREGRARWAQERetlQQSAEADKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 336 K-EQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLE 414
Cdd:pfam07888 319 RiEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLE 398
|
....*
gi 568967304 415 ALLQK 419
Cdd:pfam07888 399 QRLET 403
|
|
| FYVE_CARP2 |
cd15770 |
FYVE-like domain found in caspase regulator CARP2 and similar proteins; CARP2, also termed E3 ... |
1241-1279 |
4.90e-04 |
|
FYVE-like domain found in caspase regulator CARP2 and similar proteins; CARP2, also termed E3 ubiquitin-protein ligase rififylin, or caspases-8 and -10-associated RING finger protein 2, or FYVE-RING finger protein Sakura (Fring), or RING finger and FYVE-like domain-containing protein 1, or RING finger protein 189, or RING finger protein 34-like, is a novel caspase regulator containing a FYVE-type zinc finger domain. It regulates the p53 signaling pathway through degrading 14-3-3 sigma and stabilizing MDM2. CARP2 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, CARP2 has an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus it belongs to a family of unique FYVE-type domains called FYVE-like domains. In addition to the N-terminal FYVE-like domain, CARP2 harbors a C-terminal RING domain.
Pssm-ID: 277309 Cd Length: 49 Bit Score: 39.06 E-value: 4.90e-04
10 20 30
....*....|....*....|....*....|....*....
gi 568967304 1241 QNCMSCGKCFSVTVRRHHCRQCGNIFCAECSTKNALTPS 1279
Cdd:cd15770 2 ISCKACGIRFASCARKHPCMDCKKNYCTACSSQAENGPS 40
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
389-923 |
5.14e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 389 LREAQNDLEQVLRQIgDKDQKIQNLEALLQKGKESVSLLEKEREdlYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEK 468
Cdd:COG4913 237 LERAHEALEDAREQI-ELLEPIRELAERYAAARERLAELEYLRA--ALRLWFAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 469 LKNQSESHKQAEENLHDQVQEQKAhlraaqDRVLSLETSVSELSSQLNESKEKVSQLDiqikaktELLLSAEAAKAAQRA 548
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERELEERERRRARLE-------ALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 549 DLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVED----LEGHIKKLEADA 624
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAlrdaLAEALGLDEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 625 ------LEVKASKEQ--------------------ALQSLQQQRQLSTDLELR-NAELSRELQEQEEVVSCTKLDLQNKS 677
Cdd:COG4913 461 pfvgelIEVRPEEERwrgaiervlggfaltllvppEHYAAALRWVNRLHLRGRlVYERVRTGLPDPERPRLDPDSLAGKL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 678 EILEN-----IKQTLTKKEE----ENVvlkQEFEK---------LSQDSKTQHkELGDRMQAA---VTELTAvKAQKDAL 736
Cdd:COG4913 541 DFKPHpfrawLEAELGRRFDyvcvDSP---EELRRhpraitragQVKGNGTRH-EKDDRRRIRsryVLGFDN-RAKLAAL 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 737 LAELSTTKEKLSKVSDSLKNSKSEfEKENQKGKAAVLDLEKACKElkhqlQVQAESALKEQEDLKKSLEKEKETSQQLKi 816
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAE-LDALQERREALQRLAEYSWD-----EIDVASAEREIAELEAELERLDASSDDLA- 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 817 elnSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEK 896
Cdd:COG4913 689 ---ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVER 765
|
570 580
....*....|....*....|....*..
gi 568967304 897 GKLSALQSNYEKCQADLKQLQSDLYGK 923
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERA 792
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
813-1037 |
5.18e-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: 44.83 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 813 QLKIELNSVKGEVSQ---AQNTLKQKEKDEQQLQgtinQLKQSAEQKKKQIEALQGEVKNavSQKTVLENK-------LQ 882
Cdd:NF012221 1539 ESSQQADAVSKHAKQddaAQNALADKERAEADRQ----RLEQEKQQQLAAISGSQSQLES--TDQNALETNgqaqrdaIL 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 883 QQSSQAAQELAAEKGKLSAL--QSNYEKCQAD----------LKQLQSDLygkesellatrQDLKS-VEEKLTLAQEDLI 949
Cdd:NF012221 1613 EESRAVTKELTTLAQGLDALdsQATYAGESGDqwrnpfagglLDRVQEQL-----------DDAKKiSGKQLADAKQRHV 1681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 950 SNRNQI-------------GNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEK-SKLAEME 1015
Cdd:NF012221 1682 DNQQKVkdavakseagvaqGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQdASAAENK 1761
|
250 260
....*....|....*....|..
gi 568967304 1016 EIKCRQEKEITKLNEELKSHKQ 1037
Cdd:NF012221 1762 ANQAQADAKGAKQDESDKPNRQ 1783
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
257-501 |
5.32e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 257 EAAQKLREELREVESTRQhlkvEVKQLQQQREekeqhglqlqgevsqlhckLLETERQLGEAHGRLKEQRQLSSEklMEK 336
Cdd:COG4913 225 EAADALVEHFDDLERAHE----ALEDAREQIE-------------------LLEPIRELAERYAAARERLAELEY--LRA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 337 EQQVADLQLKLSRLEEQLkekvtnsTELQHQLEKSKQQHQEQQALQQSATAKLREaqndLEQVLRQIGdkDQKIQNLEAL 416
Cdd:COG4913 280 ALRLWFAQRRLELLEAEL-------EELRAELARLEAELERLEARLDALREELDE----LEAQIRGNG--GDRLEQLERE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 417 LQKGKESVSLLEKEREDLYAKIQA----GEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENL---HDQVQE 489
Cdd:COG4913 347 IERLERELEERERRRARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLrreLRELEA 426
|
250
....*....|..
gi 568967304 490 QKAHLRAAQDRV 501
Cdd:COG4913 427 EIASLERRKSNI 438
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
699-1205 |
5.72e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 699 QEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDA--LLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLE 776
Cdd:PRK02224 165 EEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 777 K---------ACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGE----------VSQAQNTLkqkEK 837
Cdd:PRK02224 245 EheerreeleTLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeaVEARREEL---ED 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 838 DEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENK---LQQQSSQAAQELAAEKGKLSALQSNYEKCQA--- 911
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEaaeLESELEEAREAVEDRREEIEELEEEIEELRErfg 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 912 ----DLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNR---------------------NQIGNQNKSIQELQ 966
Cdd:PRK02224 402 dapvDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpvegsphvETIEEDRERVEELE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 967 AAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKsKLAEMEEIKCRQEKEITKLNE---ELKSHKQESIKEI 1043
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEE-LIAERRETIEEKRERAEELREraaELEAEAEEKREAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1044 TNLKDAKQLLIQQKLELQGRVDSLKAALEQ-EKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEK-EAGMKKHEENE 1121
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKLAELKERIESlERIRTLLAAIADAEDEIERLREKREALAELNDERRERlAEKRERKRELE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1122 AKLT-MQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQ---DERRALLERCLKGE---GEIEKL 1194
Cdd:PRK02224 641 AEFDeARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEelrERREALENRVEALEalyDEAEEL 720
|
570
....*....|.
gi 568967304 1195 QTKALELQRKL 1205
Cdd:PRK02224 721 ESMYGDLRAEL 731
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
130-371 |
6.86e-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: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 130 ERESEKLKDECKKLQSEHAHLEATINQLR--SELAKGPQEVAVYVQEIQKLKGSINELTQKN---QNLTEKLQKKDLDYT 204
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASSddlAALEEQLEELEAELE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 205 HLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVestRQHLKVEVKQLQ 284
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL---RENLEERIDALR 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 285 QQREEKEQHGLQLQGE-VSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQqvadlqlklsRLEEQLKEKVTNS-T 362
Cdd:COG4913 780 ARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYEE----------RFKELLNENSIEFvA 849
|
....*....
gi 568967304 363 ELQHQLEKS 371
Cdd:COG4913 850 DLLSKLRRA 858
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
433-1170 |
7.35e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 433 DLYAKIQAGEGETAVLNQLQEKNHA---LQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVS 509
Cdd:pfam15921 62 DSPRKIIAYPGKEHIERVLEEYSHQvkdLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 510 ELSSQLNESkekVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHldtaqhalQDKQQELNKVSVQLDQLTAK--FQEKQE 587
Cdd:pfam15921 142 DLRNQLQNT---VHELEAAKCLKEDMLEDSNTQIEQLRKMMLSH--------EGVLQEIRSILVDFEEASGKkiYEHDSM 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 588 HCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELS-RELQEQEEVV 666
Cdd:pfam15921 211 STMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEiTGLTEKASSA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 667 SCTKLDLQNKSEILENIKQT--------LTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLA 738
Cdd:pfam15921 291 RSQANSIQSQLEIIQEQARNqnsmymrqLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 739 ELSTTKEKLSKVSDSLKNSKSEFEKENQKGK------------------------AAVLDLEKACKELKHQLQVQAESAL 794
Cdd:pfam15921 371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKrlwdrdtgnsitidhlrrelddrnMEVQRLEALLKAMKSECQGQMERQM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 795 KEQEDLKKSLEKEKETSQQL---KIELNSVKGEVSQAQNTLKQKEKdeqqlqgTINQLKQSAEQKKKQIEALQGEVknav 871
Cdd:pfam15921 451 AAIQGKNESLEKVSSLTAQLestKEMLRKVVEELTAKKMTLESSER-------TVSDLTASLQEKERAIEATNAEI---- 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 872 sqktvleNKLQQQSSQAAQELAAEKGKLSALQSNYEKCQAdlkqLQSDLYGKESELLATRQDLKSVEEkltlaqedlisn 951
Cdd:pfam15921 520 -------TKLRSRVDLKLQELQHLKNEGDHLRNVQTECEA----LKLQMAEKDKVIEILRQQIENMTQ------------ 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 952 rnQIGNQNKSIQELQAAKASLEQDSAKKEALLKEqSKALEDAQ----REKSVKEKELVAEKSKLAEMEEIKCRQEKEITK 1027
Cdd:pfam15921 577 --LVGQHGRTAGAMQVEKAQLEKEINDRRLELQE-FKILKDKKdakiRELEARVSDLELEKVKLVNAGSERLRAVKDIKQ 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1028 LNEELKSHKQESIKEITNLKDAKQLL---IQQKLE--------LQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEF 1096
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNSLSEDYEVLkrnFRNKSEemetttnkLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1097 SEKEAK------LHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATV 1170
Cdd:pfam15921 734 KQITAKrgqidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
360-920 |
7.50e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 360 NSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIG-------DKDQKIQNLEALLQKGKESVSLLEKERE 432
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINeisselpELREELEKLEKEVKELEELKEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 433 DLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLhdqvqEQKAHLRAAQDRVLSLETSVSELS 512
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI-----KLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 513 SQLNESKEKVSQLDIQIKAKTELLLSAEAakaaqradlqnhldtaqhaLQDKQQELNKVSVQLDQLTAKFQEKQEHCIQL 592
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKE-------------------LEKRLEELEERHELYEEAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 593 ESHLKDHKEKHL-SLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRElqEQEEVVSCTKL 671
Cdd:PRK03918 382 TGLTPEKLEKELeELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE--HRKELLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 672 DLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQDSKtqHKELGDRMQAAVTELTAVKAQK-DALLAELSTTKEKLSKV 750
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK--LKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 751 SDSLKNSKSEFEKENQ-KGKAAVL-----DLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSqqlkIELNSVKGE 824
Cdd:PRK03918 538 KGEIKSLKKELEKLEElKKKLAELekkldELEEELAELLKELEELGFESVEELEERLKELEPFYNEY----LELKDAEKE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 825 VSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEvknaVSQKTvlENKLQQQSSQAAQELAAEKGKLSALQS 904
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK----YSEEE--YEELREEYLELSRELAGLRAELEELEK 687
|
570
....*....|....*.
gi 568967304 905 NYEKCQADLKQLQSDL 920
Cdd:PRK03918 688 RREEIKKTLEKLKEEL 703
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
232-853 |
7.73e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 232 QQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLET 311
Cdd:TIGR00618 166 KELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 312 ERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLRE 391
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 392 AQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKN 471
Cdd:TIGR00618 326 LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 472 QSESHKQAEEN----------LHDQVQEQKAHLRAAQDRVLSLETSVSELSSQ--LNESKEKVSQLDIQIKAKTELLLSA 539
Cdd:TIGR00618 406 QREQATIDTRTsafrdlqgqlAHAKKQQELQQRYAELCAAAITCTAQCEKLEKihLQESAQSLKEREQQLQTKEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 540 EAAKAAQRADLQNH-----------LDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQE-----HCIQLESHLKDHKEKH 603
Cdd:TIGR00618 486 TRKKAVVLARLLELqeepcplcgscIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEedvyhQLTSERKQRASLKEQM 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 604 LSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVScTKLDLQNKSEILENI 683
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQD-VRLHLQQCSQELALK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 684 KQTLTKKEEEnvVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEK 763
Cdd:TIGR00618 645 LTALHALQLT--LTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 764 ENQKGKAAVLDLE---KACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVsqaQNTLKQKEKDEQ 840
Cdd:TIGR00618 723 IENASSSLGSDLAareDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEI---QFFNRLREEDTH 799
|
650
....*....|...
gi 568967304 841 QLQGTINQLKQSA 853
Cdd:TIGR00618 800 LLKTLEAEIGQEI 812
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
562-868 |
8.06e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.74 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 562 QDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDhkeKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQ 641
Cdd:PLN02939 45 QQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLR---TVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 642 RQLSTDLEL-------RNAELS---------RELQEQEEVVScTKLDLQNKSEILE------NIKQTLTKKEEENV-VLK 698
Cdd:PLN02939 122 GEQLSDFQLedlvgmiQNAEKNilllnqarlQALEDLEKILT-EKEALQGKINILEmrlsetDARIKLAAQEKIHVeILE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 699 QEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSlKNSKSEFEKENQKGKAAVLDLEka 778
Cdd:PLN02939 201 EQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAET-EERVFKLEKERSLLDASLRELE-- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 779 CKELKHQLQVQAESALKEQedlkkSLEKEKETSQQLkieLNSVKGEVSQAQNTLKQkekdEQQLQGTINQLKQSAEQKK- 857
Cdd:PLN02939 278 SKFIVAQEDVSKLSPLQYD-----CWWEKVENLQDL---LDRATNQVEKAALVLDQ----NQDLRDKVDKLEASLKEANv 345
|
330
....*....|....*.
gi 568967304 858 -----KQIEALQGEVK 868
Cdd:PLN02939 346 skfssYKVELLQQKLK 361
|
|
| FYVE_CARP1 |
cd15769 |
FYVE-like domain found in caspase regulator CARP1 and similar proteins; CARP1, also termed E3 ... |
1243-1290 |
8.15e-04 |
|
FYVE-like domain found in caspase regulator CARP1 and similar proteins; CARP1, also termed E3 ubiquitin-protein ligase RNF34, or caspases-8 and -10-associated RING finger protein 1, or FYVE-RING finger protein Momo, or RING finger homologous to inhibitor of apoptosis protein (RFI), or RING finger protein 34, or RING finger protein RIFF, is a nuclear protein that functions as a specific E3 ubiquitin ligase for the transcriptional coactivator PGC-1alpha, a master regulator of energy metabolism and adaptive thermogenesis in the brown fat cell, and negatively regulates brown fat cell metabolism. It is preferentially expressed in esophageal, gastric and colorectal cancers, suggesting a possible association with the development of the digestive tract cancers. It regulates the p53 signaling pathway through degrading 14-3-3 sigma and stabilizing MDM2. CARP1 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, CARP1 has an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus it belongs to a family of unique FYVE-type domains called FYVE-like domains. In addition to the N-terminal FYVE-like domain, CARP1 harbors a C-terminal RING domain.
Pssm-ID: 277308 Cd Length: 47 Bit Score: 38.43 E-value: 8.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 568967304 1243 CMSCGKCFSVTVRRHHCRQCGNIFCAECSTknaltpsSKKPVRVCDAC 1290
Cdd:cd15769 4 CKACGLAFSVFRKKHVCCDCKKDFCSVCSV-------LQENLRRCSTC 44
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
845-1074 |
9.38e-04 |
|
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: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 845 TINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQsdlygke 924
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLE------- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 925 sellatrQDLKSVEEKLTLAQEDLISNRNQI-GNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKE 1003
Cdd:COG4913 309 -------AELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967304 1004 LVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQE 1074
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
752-1207 |
1.27e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 752 DSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAEsALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQN- 830
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 831 --TLKQKEKDEQQLQGTINQLKQsAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEkgkLSALQSNYEK 908
Cdd:COG4717 128 lpLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 909 CQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQ-EDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQS 987
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAAlEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 988 KALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAkqllIQQKLELQGRVDSL 1067
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR----IEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1068 KAALEQEKESQQlmREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEE--NEAKLTMQVTTLNENLGTVKKEWQSS 1145
Cdd:COG4717 360 EEELQLEELEQE--IAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEqlEELLGELEELLEALDEEELEEELEEL 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967304 1146 QRRVSELEKQTDDLRGEIAVLEATVQNnqderrallercLKGEGEIEKLQTKALELQRKLDN 1207
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQ------------LEEDGELAELLQELEELKAELRE 487
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
788-994 |
1.32e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 788 VQAESALKEQEDLKKSLEKEKETSQQlkiELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEV 867
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQA---ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 868 KNAVS-------------------------QKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYG 922
Cdd:COG3883 89 GERARalyrsggsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967304 923 KESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQ 994
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
775-1072 |
1.34e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 775 LEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAE 854
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 855 QKKKQIEALQGEVKNAVSQKTVLE---NKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATR 931
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 932 QD--LKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKS 1009
Cdd:COG4372 185 LDelLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967304 1010 KLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALE 1072
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
973-1241 |
1.39e-03 |
|
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: 43.13 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 973 EQDSAKKEALLKEQSKALEDAQREKSVKEK--ELVAEKSKlaemeeikcRQEKEITKLNEELKSHKQESIKEITNLKDAK 1050
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERyqALLKEKRE---------YEGYELLKEKEALERQKEAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1051 QLLIQQKLELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTT 1130
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1131 LNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNtta 1210
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR--- 410
|
250 260 270
....*....|....*....|....*....|.
gi 568967304 1211 aVQELGRENQSLQIKHTQALNRKWAEDNEVQ 1241
Cdd:TIGR02169 411 -LQEELQRLSEELADLNAAIAGIEAKINELE 440
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
775-948 |
1.42e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 775 LEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLK----IELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLK 850
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEALLAALG 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 851 QSAEQKKKQIEALQGEVKNAVSQktvlenkLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQS--DLYgkESELL 928
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEA-------LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrkSNI--PARLL 443
|
170 180
....*....|....*....|
gi 568967304 929 ATRQDLksvEEKLTLAQEDL 948
Cdd:COG4913 444 ALRDAL---AEALGLDEAEL 460
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
251-494 |
1.50e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 251 ELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQlQGEVSQLhckllETERQLGEAHGRLKEQRQLSS 330
Cdd:COG0497 159 EYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQ-PGEEEEL-----EEERRRLSNAEKLREALQEAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 331 EKLMEKEQQVADLqlkLSRLEEQLKEKVTNSTELQHQLEkskqqhqeqqaLQQSATAKLREAQNDLEQVLRQI------- 403
Cdd:COG0497 233 EALSGGEGGALDL---LGQALRALERLAEYDPSLAELAE-----------RLESALIELEEAASELRRYLDSLefdperl 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 404 GDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLknqSESHKQAEENL 483
Cdd:COG0497 299 EEVEERLALLRRLARKYGVTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKL---SAARKKAAKKL 375
|
250
....*....|.
gi 568967304 484 HDQVQEQKAHL 494
Cdd:COG0497 376 EKAVTAELADL 386
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
557-809 |
1.52e-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: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 557 AQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADalevkaskeqalq 636
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 637 slqqqrqlSTDLELRNAELSRELQEQEEVVsctkldlqnkSEILENIkQTLTKKEEENVVLKQEFEKLSQDSKTQHKELG 716
Cdd:COG4942 85 --------LAELEKEIAELRAELEAQKEEL----------AELLRAL-YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 717 DRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESAlKE 796
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA-EE 224
|
250
....*....|...
gi 568967304 797 QEDLKKSLEKEKE 809
Cdd:COG4942 225 LEALIARLEAEAA 237
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
176-478 |
1.65e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 176 QKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEK 255
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 256 AEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLME 335
Cdd:COG4372 100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 336 KEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEA 415
Cdd:COG4372 180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967304 416 LLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQ 478
Cdd:COG4372 260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
172-492 |
1.77e-03 |
|
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: 42.36 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 172 VQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQrdldcqqLQARLTASESSLQRAQGE 251
Cdd:pfam19220 40 LRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAK-------LEAALREAEAAKEELRIE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 252 LSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSE 331
Cdd:pfam19220 113 LRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 332 ---KLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQS----ATAKLREAQNDLEQVLRQIG 404
Cdd:pfam19220 193 ltrRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMkleaLTARAAATEQLLAEARNQLR 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 405 DKDQKIQNLEALLQKG-------KESVSLLEKEREDLYAKIQ------------------AGEGETAVLNQLQEKNHALQ 459
Cdd:pfam19220 273 DRDEAIRAAERRLKEAsierdtlERRLAGLEADLERRTQQFQemqraraeleeraemltkALAAKDAALERAEERIASLS 352
|
330 340 350
....*....|....*....|....*....|...
gi 568967304 460 QQLTQLTEKLKNQSESHKQAEENLHDQVQEQKA 492
Cdd:pfam19220 353 DRIAELTKRFEVERAALEQANRRLKEELQRERA 385
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
12-428 |
1.80e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 42.37 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 12 DGLVTDSSAELQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQ------KVTHLTEDL 85
Cdd:pfam05622 51 DDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQAlkdemdILRESSDKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 86 NKQTTVIQDLKTELlqrpgiEDVAVLKKelvQVQTLMDNMTLERERESEkLKDECKKLQSEHAHLEAtinqlrselakgp 165
Cdd:pfam05622 131 KKLEATVETYKKKL------EDLGDLRR---QVKLLEERNAEYMQRTLQ-LEEELKKANALRGQLET------------- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 166 qevavYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQrdLDCQQLQARltasesSL 245
Cdd:pfam05622 188 -----YKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRETNEE--LRCAQLQQA------EL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 246 QRAQGELSEKAEAAQKLREELR--EVESTRQHLKVEVKQLQQQREEKEQHglqlqgevsqlhcKLLETERQLGEAHGR-- 321
Cdd:pfam05622 255 SQADALLSPSSDPGDNLAAEIMpaEIREKLIRLQHENKMLRLGQEGSYRE-------------RLTELQQLLEDANRRkn 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 322 -LKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQalqqsataKLREAQNDLEQVL 400
Cdd:pfam05622 322 eLETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQ--------KKKEQIEELEPKQ 393
|
410 420
....*....|....*....|....*...
gi 568967304 401 RQigDKDQKIQNLEALLQKGKESVSLLE 428
Cdd:pfam05622 394 DS--NLAQKIDELQEALRKKDEDMKAME 419
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
968-1125 |
1.85e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 968 AKASLEQDSAKKEALL---KEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEIT 1044
Cdd:PRK12704 45 EEAKKEAEAIKKEALLeakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1045 NLKDAKQLLIQQKLELQGRVDSLkAALEQEKESQQLMReqvkkeeekrkeefsekeaKLHSEIKEKEAGMKKHEENEAKL 1124
Cdd:PRK12704 125 ELEKKEEELEELIEEQLQELERI-SGLTAEEAKEILLE-------------------KVEEEARHEAAVLIKEIEEEAKE 184
|
.
gi 568967304 1125 T 1125
Cdd:PRK12704 185 E 185
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
763-1112 |
1.96e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 763 KENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQL 842
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 843 QGTINQLKQSAEQKKKQIEALQGEVKNAvsqktvlenklqqqssqaAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYG 922
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEEL------------------QEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 923 KESELLATRQDLKSVEEKLTLAQEDLiSNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEK 1002
Cdd:COG4372 148 REEELKELEEQLESLQEELAALEQEL-QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1003 ELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAALEQEKESQQLMR 1082
Cdd:COG4372 227 LEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAA 306
|
330 340 350
....*....|....*....|....*....|
gi 568967304 1083 EQVKKEEEKRKEEFSEKEAKLHSEIKEKEA 1112
Cdd:COG4372 307 LSLIGALEDALLAALLELAKKLELALAILL 336
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
395-1016 |
2.23e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 395 DLEQVLRQIGDKDQKIQNLEallQKGKESVSLLEKEReDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNqse 474
Cdd:pfam12128 197 DVKSMIVAILEDDGVVPPKS---RLNRQQVEHWIRDI-QAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKS--- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 475 sHKQAEENLHDQVQEQKAHLRaaqDRVLSLETSVSELSSQLNESKekvSQLDIQIKAKTELLLSAEAAKAAQRADLQNHL 554
Cdd:pfam12128 270 -DETLIASRQEERQETSAELN---QLLRTLDDQWKEKRDELNGEL---SAADAAVAKDRSELEALEDQHGAFLDADIETA 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 555 DTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLS-LEQKVEDLEGHIKKLEA------DALEv 627
Cdd:pfam12128 343 AADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAgIKDKLAKIREARDRQLAvaeddlQALE- 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 628 KASKEQALQSLQQQRQLSTDLELRNAELsRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEKLSQD 707
Cdd:pfam12128 422 SELREQLEAGKLEFNEEEYRLKSRLGEL-KLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKR 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 708 SKTQHKELGD---RMQAAVTELTAVKAQKDA----LLAELSTT----KEKLSKVSDSLKNSKS----EFEKENQKGKAAV 772
Cdd:pfam12128 501 RDQASEALRQasrRLEERQSALDELELQLFPqagtLLHFLRKEapdwEQSIGKVISPELLHRTdldpEVWDGSVGGELNL 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 773 LDLEKACKELKHQLQVQAESALKEQED-LKKSLEKEKETSQQLKIELNSVKGEVSQAQ-------NTLKQKEKDEQQLQG 844
Cdd:pfam12128 581 YGVKLDLKRIDVPEWAASEEELRERLDkAEEALQSAREKQAAAEEQLVQANGELEKASreetfarTALKNARLDLRRLFD 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 845 TINQLK-QSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQEL-------------------AAEKGKLSALQS 904
Cdd:pfam12128 661 EKQSEKdKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKreartekqaywqvvegaldAQLALLKAAIAA 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 905 NYEKCQADLKQLQS----DLYGK---ESELLATRQDLKSVEEKLTLAQED---------------LISNRN---QIGNQN 959
Cdd:pfam12128 741 RRSGAKAELKALETwykrDLASLgvdPDVIAKLKREIRTLERKIERIAVRrqevlryfdwyqetwLQRRPRlatQLSNIE 820
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 568967304 960 KSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEE 1016
Cdd:pfam12128 821 RAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKE 877
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
166-700 |
2.47e-03 |
|
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: 42.12 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 166 QEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDldythleeKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSL 245
Cdd:pfam10174 185 RRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRN--------QLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 246 Q--RAQGELSekaeaAQKLREELREVESTRQH---LKVEVKQLQQQREEKEQHGLQLQGEvsqlhcklLETerqLGEAHG 320
Cdd:pfam10174 257 QmlKTNGLLH-----TEDREEEIKQMEVYKSHskfMKNKIDQLKQELSKKESELLALQTK--------LET---LTNQNS 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 321 RLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKskqqhqeQQALQQSATAKLREAQNDLEQVL 400
Cdd:pfam10174 321 DCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQD-------LTEEKSTLAGEIRDLKDMLDVKE 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 401 RQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQ-LQEKN---HALQQQLTQLTEKLKNQSESH 476
Cdd:pfam10174 394 RKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEaLSEKEriiERLKEQREREDRERLEELESL 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 477 KQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTE---------LLLSAEAAKAAQR 547
Cdd:pfam10174 474 KKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEecsklenqlKKAHNAEEAVRTN 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 548 ADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQE-------KQEHCIQLESHLKDHKEKHLSLEQKVEDLEGHIKKL 620
Cdd:pfam10174 554 PEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREvenekndKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKK 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 621 EADALEvKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQE 700
Cdd:pfam10174 634 GAQLLE-EARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQE 712
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
963-1056 |
2.91e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 963 QELQAAKASLEQDSAKKEALLKEQSKALEdaQREKSVKEK--ELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESI 1040
Cdd:PRK12704 64 EEIHKLRNEFEKELRERRNELQKLEKRLL--QKEENLDRKleLLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQL 141
|
90 100
....*....|....*....|.
gi 568967304 1041 KE---ITNL--KDAKQLLIQQ 1056
Cdd:PRK12704 142 QElerISGLtaEEAKEILLEK 162
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
445-658 |
3.09e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 445 TAVLNQLQEKNHALQQQLTQLTEKLKNQseshKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQ 524
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 525 LDIQIKAKTELLLSAEAAKAAQRA--------------DLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCI 590
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568967304 591 QLESHLKDHKEKHLSLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRE 658
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
16-603 |
3.15e-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: 41.88 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 16 TDSSAELQALEQQLEEAQ----------TENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDL 85
Cdd:TIGR00618 218 HERKQVLEKELKHLREALqqtqqshaylTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 86 NKQTTVIQDLKTELLQRPGIEDVAVLKKELVQVQTLmdnmtLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGP 165
Cdd:TIGR00618 298 HIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH-----VKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISC 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 166 QEVAVyVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASESSL 245
Cdd:TIGR00618 373 QQHTL-TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 246 QRAQGELSEKAEAAQKLREELREVEstrqhlkvEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLgEAHGRLKEQ 325
Cdd:TIGR00618 452 QCEKLEKIHLQESAQSLKEREQQLQ--------TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHP-NPARQDIDN 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 326 RQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVL----R 401
Cdd:TIGR00618 523 PGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQdlteK 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 402 QIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAV----LNQLQEKNHALQQQLTQLTEKLKNQSESHK 477
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALhalqLTLTQERVREHALSIRVLPKELLASRQLAL 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 478 QAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTA 557
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEA 762
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 568967304 558 QHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKH 603
Cdd:TIGR00618 763 HFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEI 808
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
234-369 |
3.18e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 234 LQARLTASESSLQRAQGELsekAEAAQKLREElrevESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETER 313
Cdd:PRK09039 44 LSREISGKDSALDRLNSQI---AELADLLSLE----RQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568967304 314 QLGEAHGRLKEQRQLSSEKLMEKE---QQVADLQLKLSRLEEQLKEKVTNSTELQHQLE 369
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVEllnQQIAALRRQLAALEAALDASEKRDRESQAKIA 175
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
792-1070 |
3.24e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.99 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 792 SALKEQEDLKKSLEKEKETSQQLKIELNSVK-------GEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEAlq 864
Cdd:COG5022 814 SYLACIIKLQKTIKREKKLRETEEVEFSLKAevliqkfGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDV-- 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 865 GEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKC--QADLKQLQSDLYGKESELLATRQDLKSVEEKLT 942
Cdd:COG5022 892 KSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLlnNIDLEEGPSIEYVKLPELNKLHEVESKLKETSE 971
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 943 LAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEAlLKEQSKALEDAQREKSVKE------KELVAEKSKLAEMEE 1016
Cdd:COG5022 972 EYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGA-LQESTKQLKELPVEVAELQsaskiiSSESTELSILKPLQK 1050
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568967304 1017 IKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQQKLELQGRVDSLKAA 1070
Cdd:COG5022 1051 LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVT 1104
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
176-605 |
3.30e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 176 QKLKGSINELTQKNQNLTEKLQKKDlDYTHLEEKHNEESASRKTLQASLHQRDLDCQQLQARLTASE--SSLQRAQGELS 253
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 254 EKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKL 333
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 334 MEKEQQVADLQLKLSR--LEEQLKEK-----------------VTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQN 394
Cdd:COG4717 223 EELEEELEQLENELEAaaLEERLKEArlllliaaallallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 395 DLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQE--KNHALQQQLTQLTEKLKNQ 472
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 473 SESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVSELSSQLNES--KEKVSQLDIQIKAKTELLLSAEAAKAAQRADL 550
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 568967304 551 QNHLDtaQHALQDKQQELNKVSVQLDQLTAKFQEKQEHCIQLESHLKDHKEKHLS 605
Cdd:COG4717 463 EQLEE--DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
429-1218 |
3.39e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 429 KEREDLYAKIQAGEGETAVLNQLQEKNHALQQQLTQLTEK-LKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETS 507
Cdd:TIGR00606 255 KEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 508 VSELSSQLNESKEKVSQLdiQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQEKQE 587
Cdd:TIGR00606 335 RRLLNQEKTELLVEQGRL--QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 588 HCIQLESHLKDHKEKHLSLEQKVEDLeGHIKKLEADALEVKAS------KEQALQSLQQQRQLSTDLELRNAELSRELQE 661
Cdd:TIGR00606 413 LCADLQSKERLKQEQADEIRDEKKGL-GRTIELKKEILEKKQEelkfviKELQQLEGSSDRILELDQELRKAERELSKAE 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 662 QEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVVLKQEFEklsqdSKTQHKELGDRMQAAVTELTAVKAQKDALLAELS 741
Cdd:TIGR00606 492 KNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTT-----TRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 742 ---TTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKkslekEKETSQQLKIEL 818
Cdd:TIGR00606 567 gyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLF-----DVCGSQDEESDL 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 819 NSVKGEvsqaqntLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLE---NKLQQQSSQAAQELAAE 895
Cdd:TIGR00606 642 ERLKEE-------IEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQefiSDLQSKLRLAPDKLKST 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 896 KGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKsiqELQAAKASLEQD 975
Cdd:TIGR00606 715 ESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMP---EEESAKVCLTDV 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 976 SAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNLKDAKQLLIQ 1055
Cdd:TIGR00606 792 TIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKS 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1056 QKLELQGRVDSLKAALEQEKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEaKLTMQVTTLNENL 1135
Cdd:TIGR00606 872 EKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK-KAQDKVNDIKEKV 950
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1136 GTVKKEWQSSQRRVSE-LEKQTDDLRGEIAVLEATVQNNQDERRALLE--RCLKGEGEIEKLQTKALELQRKLDNTTAAV 1212
Cdd:TIGR00606 951 KNIHGYMKDIENKIQDgKDDYLKQKETELNTVNAQLEECEKHQEKINEdmRLMRQDIDTQKIQERWLQDNLTLRKRENEL 1030
|
....*.
gi 568967304 1213 QELGRE 1218
Cdd:TIGR00606 1031 KEVEEE 1036
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
17-174 |
3.42e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 17 DSSAELQALEQQLEEAQTEnfnikqmkdlfeqkAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTV--IQD 94
Cdd:COG4913 607 DNRAKLAALEAELAELEEE--------------LAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEreIAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 95 LKTELLQ-RPGIEDVAVLKKELVQVQTLMDnmTLEREResEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQ 173
Cdd:COG4913 673 LEAELERlDASSDDLAALEEQLEELEAELE--ELEEEL--DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
.
gi 568967304 174 E 174
Cdd:COG4913 749 A 749
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
130-752 |
4.21e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.75 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 130 ERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKL----KGSINELTQKNQNLTEKLQKKDLDYTH 205
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLddqwKEKRDELNGELSAADAAVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 206 LEEKHneesasRKTLQASLHQRDLDcqqlQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQ 285
Cdd:pfam12128 327 LEDQH------GAFLDADIETAAAD----QEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 286 QREEKEQHGLQLQGEVSQLHCKLLETE--RQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQlklsrLEEQLKEKVTNSTE 363
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDDLQALESElrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQAT-----ATPELLLQLENFDE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 364 LqhqLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKE-----SVSLLEKER------E 432
Cdd:pfam12128 472 R---IERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELqlfpqAGTLLHFLRkeapdwE 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 433 DLYAKIQAGE--GETAVLNQLQEKNHALQQQLTQLTEKLKN-QSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLETSVS 509
Cdd:pfam12128 549 QSIGKVISPEllHRTDLDPEVWDGSVGGELNLYGVKLDLKRiDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 510 ELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQhalQDKQQELNKVSVQLDQLTAKFQE-KQEH 588
Cdd:pfam12128 629 QANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERK---DSANERLNSLEAQLKQLDKKHQAwLEEQ 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 589 CIQLESHLKDHKEKHLSLEQKVEDLEGHIK----------KLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRE 658
Cdd:pfam12128 706 KEQKREARTEKQAYWQVVEGALDAQLALLKaaiaarrsgaKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIE 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 659 LQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVV--LKQEFEKLSQDSKTQHKELgdrmqaaVTELTAVKAQKDAL 736
Cdd:pfam12128 786 RIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAIseLQQQLARLIADTKLRRAKL-------EMERKASEKQQVRL 858
|
650
....*....|....*.
gi 568967304 737 LAELSTTKEKLSKVSD 752
Cdd:pfam12128 859 SENLRGLRCEMSKLAT 874
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
251-359 |
4.48e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 251 ELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEK-EQHGLQLQGEVSQLHcKLLETERQLGEAHGRLKEQRQLS 329
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAElRDELAELEEELEALK-ARWEAEKELIEEIQELKEELEQR 483
|
90 100 110
....*....|....*....|....*....|
gi 568967304 330 SEKLMEKEQQVADLQLKLSRLEEQLKEKVT 359
Cdd:COG0542 484 YGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
279-866 |
4.53e-03 |
|
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: 41.25 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 279 EVKQLQQQREEKEQHGLQLQGEVSQLHCKL----LETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQL 354
Cdd:pfam05483 170 KTKKYEYEREETRQVYMDLNNNIEKMILAFeelrVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 355 KEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQN-------LEALLQKGKESVSLL 427
Cdd:pfam05483 250 TEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRsmstqkaLEEDLQIATKTICQL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 428 EKEREDLYAKI-QAGEGETAVLNQLQEKNHALQQQLTQLTEKLKNQSESHKQAEENLHDQVQEQKAHLRAAQDRVLSLET 506
Cdd:pfam05483 330 TEEKEAQMEELnKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 507 SVSELSSQ--LNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRADLQNHLDTAQHALQDKQQELNKVSVQLDQLTAKFQE 584
Cdd:pfam05483 410 LKKILAEDekLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 585 KQEHCIQLESHLKDhkekhlsLEQKVEDLEGHIKKLEADALEVKASKEQALQSLQQQRQLSTDLELRNAELSRELQEQEE 664
Cdd:pfam05483 490 LTAHCDKLLLENKE-------LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGD 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 665 VVSCT--KLDLQNKSEILENIKQTLTKKEEENVV--LKQEFEKLSQDSKTQHKE---LGDRMQAAVTELTAVKAQKDALL 737
Cdd:pfam05483 563 EVKCKldKSEENARSIEYEVLKKEKQMKILENKCnnLKKQIENKNKNIEELHQEnkaLKKKGSAENKQLNAYEIKVNKLE 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 738 AELSTTKEKLSKVSDslkNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKEQEDLKKSLEKEKETSQQLKIE 817
Cdd:pfam05483 643 LELASAKQKFEEIID---NYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKI 719
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 568967304 818 LNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQGE 866
Cdd:pfam05483 720 IEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEE 768
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
678-1082 |
4.60e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 678 EILENIKQTLTKKEEENVVLKQEFEKLSQDSKTQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNS 757
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 758 ksEFEKENQKGKAAVLDLEKACKELKHQLQVQAEsALKEQEDLKKSLEKEKETSQQLKIELN-SVKGEVSQAQNTLKQKE 836
Cdd:COG4717 129 --PLYQELEALEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 837 KDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNY---------- 906
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIagvlflvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 907 ------------EKCQADLKQLQSDLYGKESELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQ 974
Cdd:COG4717 286 lallflllarekASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 975 DSAKKE--ALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEikcRQEKEITKLNEELKSHKQESIK-EITNLKDAKQ 1051
Cdd:COG4717 366 EELEQEiaALLAEAGVEDEEELRAALEQAEEYQELKEELEELEE---QLEELLGELEELLEALDEEELEeELEELEEELE 442
|
410 420 430
....*....|....*....|....*....|.
gi 568967304 1052 LLIQQKLELQGRVDSLKAALEQEKESQQLMR 1082
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
132-434 |
4.71e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 132 ESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHN 211
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 212 EESASRKTLQASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVEstRQHLKVEVKQLQQQREEKE 291
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS--EAEAEQALDELLKEANRNA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 292 QHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKS 371
Cdd:COG4372 197 EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEE 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967304 372 KQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDL 434
Cdd:COG4372 277 ELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
780-997 |
4.80e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 780 KELKHQLQVQ------AESALKEQEDLKKSLEK---EKETSQQLKI-----ELNSVKGEVSQAQNTLKQKEKDEQQLQGT 845
Cdd:PHA02562 177 RELNQQIQTLdmkidhIQQQIKTYNKNIEEQRKkngENIARKQNKYdelveEAKTIKAEIEELTDELLNLVMDIEDPSAA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 846 INQLKQSAEQKKKQIEALQGEVKnaVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKcqadLKQLQSDLYGKES 925
Cdd:PHA02562 257 LNKLNTAAAKIKSKIEQFQKVIK--MYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEK----LDTAIDELEEIMD 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568967304 926 ELLATRQDLKSVEEKLTLAQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREK 997
Cdd:PHA02562 331 EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
648-1042 |
5.81e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.22 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 648 LELRNAELSRELQEQEEVVSCTKLdLQNKSEILENIKQT-LTKKEEENVVLKQEFEKLSQDSKTQHKELGDrmqaaVTEL 726
Cdd:COG5022 824 KTIKREKKLRETEEVEFSLKAEVL-IQKFGRSLKAKKRFsLLKKETIYLQSAQRVELAERQLQELKIDVKS-----ISSL 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 727 TAVKAQKDALLAEL-STTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQAESALKE-QEDLKKSL 804
Cdd:COG5022 898 KLVNLELESEIIELkKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKEtSEEYEDLL 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 805 EKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQlqgtinqlKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQ 884
Cdd:COG5022 978 KKSTILVREGNKANSELKNFKKELAELSKQYGALQES--------TKQLKELPVEVAELQSASKIISSESTELSILKPLQ 1049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 885 SSQAAQELAAEKGKLSALQSNYEKCQADLKQLQsdlygkESELLATRQDLKSVEEK-LTLAQEDLISNRNQIGN---QNK 960
Cdd:COG5022 1050 KLKGLLLLENNQLQARYKALKLRRENSLLDDKQ------LYQLESTENLLKTINVKdLEVTNRNLVKPANVLQFivaQMI 1123
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 961 SIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKeITKLNEELKSHKQESI 1040
Cdd:COG5022 1124 KLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSA-LYDEKSKLSSSEVNDL 1202
|
..
gi 568967304 1041 KE 1042
Cdd:COG5022 1203 KN 1204
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
20-130 |
5.97e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 20 AELQALEQQLEEAQTENFNIKQMKDLFEQ-KAAQLATEIADIKSKYDEeksLRAAAEQKVTHLTEdlnkqttvIQDLKTE 98
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFeRLAELRDELAELEEELEA---LKARWEAEKELIEE--------IQELKEE 479
|
90 100 110
....*....|....*....|....*....|...
gi 568967304 99 LLQRPGieDVAVLKKELVQVQT-LMDNMTLERE 130
Cdd:COG0542 480 LEQRYG--KIPELEKELAELEEeLAELAPLLRE 510
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
710-932 |
6.04e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 710 TQHKELGDRMQAAVTELTAVKAQKDALLAELSTTKEKLSKVSDSLKNSKSEFEKENQKGKAAVLDLEKACKELKHQLQVQ 789
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 790 AES--------ALKEQEDLKKSLEKEKETSQQLKIELNSVKgEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIE 861
Cdd:COG3883 96 YRSggsvsyldVLLGSESFSDFLDRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967304 862 ALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKGKLSALQSNYEKCQADLKQLQSDLYGKESELLATRQ 932
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
232-448 |
6.10e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 232 QQLQARLTASESSLQ--RAQGELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQL--HCK 307
Cdd:COG3206 185 PELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqSPV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 308 LLETERQLGEAHGRLKEQRQlsseKLMEKEQQVADLQLKLSRLEEQLKEkvtnstelqhQLEKSKQQHQEQQALQQSATA 387
Cdd:COG3206 265 IQQLRAQLAELEAELAELSA----RYTPNHPDVIALRAQIAALRAQLQQ----------EAQRILASLEAELEALQAREA 330
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967304 388 KLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGETAVL 448
Cdd:COG3206 331 SLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVI 391
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
17-208 |
6.74e-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: 40.52 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 17 DSSAELQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAEQKVTHLTEDLNKQTTVIQDLK 96
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 97 TEL------LQRPGIEDVAVLK------KELVQVQTLMDNMTLERERESEKLKDECKKLQSEHAHLEATINQLRSELAKG 164
Cdd:COG4942 104 EELaellraLYRLGRQPPLALLlspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568967304 165 PQEVAVYVQEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEE 208
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
251-876 |
6.75e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 251 ELSEKAEAAQKLREELREVESTRQHLKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLGEAHGRLKEQRQLSS 330
Cdd:PRK01156 160 EINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 331 EKlmekeQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKI 410
Cdd:PRK01156 240 AL-----NELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQIL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 411 QNLEALLQKGKESV---SLLEKEREDLYAKIQAGEGETAVLNQLQEkNHALQQQLTQLTEKLKNQSESHKQAEENLHDQV 487
Cdd:PRK01156 315 SNIDAEINKYHAIIkklSVLQKDYNDYIKKKSRYDDLNNQILELEG-YEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 488 QEQKAHLRAAQDRVLSLetsVSELSSQLNESKEKVSQLDIQIKAktelLLSAEAAKAAQRADLQNH-----------LDT 556
Cdd:PRK01156 394 SEILKIQEIDPDAIKKE---LNEINVKLQDISSKVSSLNQRIRA----LRENLDELSRNMEMLNGQsvcpvcgttlgEEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 557 AQHALQDKQQELNKVSVQLDQL---TAKFQEKQEHCIQLESHLKDHK-EKHLSLEQKVEDLEGHIKKLEADALEVKaske 632
Cdd:PRK01156 467 SNHIINHYNEKKSRLEEKIREIeieVKDIDEKIVDLKKRKEYLESEEiNKSINEYNKIESARADLEDIKIKINELK---- 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 633 qalqslqqqrqlstdlelrNAELSRElQEQEEVVSCTKLDLQNKSEILENIKQTLTKKEEENVvlkqefEKLSQDSKTQH 712
Cdd:PRK01156 543 -------------------DKHDKYE-EIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETN------RSRSNEIKKQL 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 713 KELGDRMQAAVTELTAVKaqkdallaelSTTKEKLSKVSDSLKNSKSEFeKENQKGKAAVLDLEKACKELKHQLQvQAES 792
Cdd:PRK01156 597 NDLESRLQEIEIGFPDDK----------SYIDKSIREIENEANNLNNKY-NEIQENKILIEKLRGKIDNYKKQIA-EIDS 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 793 ALKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQKEKDEQQLQGTINQLKQSAEQKKKQIEALQ--GEVKNA 870
Cdd:PRK01156 665 IIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGdlKRLREA 744
|
....*.
gi 568967304 871 VSQKTV 876
Cdd:PRK01156 745 FDKSGV 750
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
272-530 |
7.37e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 272 TRQHLKVEVKQLQQQRE-EKEQHGLQLQGEVSQLHCKLLETERQLGEAhgrLKEQRQLSSEKLMEKEQQVADLQLKLSRL 350
Cdd:PRK11281 37 TEADVQAQLDALNKQKLlEAEDKLVQQDLEQTLALLDKIDRQKEETEQ---LKQQLAQAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 351 EEQLKEKVTNsTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKE 430
Cdd:PRK11281 114 TRETLSTLSL-RQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 431 REDLY--------AKIQAGEGETAVLNQLQ-----------EKNHALQQQLTQLTEKL--KNQSESHKQAEenlhdQVQE 489
Cdd:PRK11281 193 QRVLLqaeqallnAQNDLQRKSLEGNTQLQdllqkqrdyltARIQRLEHQLQLLQEAInsKRLTLSEKTVQ-----EAQS 267
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568967304 490 QKAHLRAAQDRVLSLETSVS-ELSSQLNESKEKVSQL---DIQIK 530
Cdd:PRK11281 268 QDEAARIQANPLVAQELEINlQLSQRLLKATEKLNTLtqqNLRVK 312
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
958-1168 |
7.42e-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: 40.13 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 958 QNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAeksklaemeeikcrQEKEITKLNEELKSHKQ 1037
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA--------------LARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1038 ESIKEITNLKDAKQLLIQQKLEL---------QGRVDSLKAALEQEKESQQLM-----------REQVKKEEEKRKEEFS 1097
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELaellralyrLGRQPPLALLLSPEDFLDAVRrlqylkylapaRREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568967304 1098 EKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEA 1168
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
792-1025 |
8.07e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 792 SALKEQEDLKKSLEKE-KETSQQLKIELNSVKGEVSQAQNTLKQKEK----DEQQLQGTINQLKQSAEQKKKQIEALQGE 866
Cdd:PHA02562 163 SVLSEMDKLNKDKIRElNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKkngeNIARKQNKYDELVEEAKTIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 867 VKNAVSQKTVLENKLQQQSSQAAQeLAAEKGKLSALQSNYEK---CQADLKQLqSDLYGKESELLATRQDLKSVEEKLTL 943
Cdd:PHA02562 243 LLNLVMDIEDPSAALNKLNTAAAK-IKSKIEQFQKVIKMYEKggvCPTCTQQI-SEGPDRITKIKDKLKELQHSLEKLDT 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 944 AQEDLISNRNQIGNQNKSIQELQAAKASLEQDSAKKEALLKEQSKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEK 1023
Cdd:PHA02562 321 AIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVK 400
|
..
gi 568967304 1024 EI 1025
Cdd:PHA02562 401 EK 402
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
836-1046 |
8.11e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 836 EKDEQQLQGTINQLKQSAEQKkkqIEALQGEVKNAVSQKTVLENKLQqqssqaaqELAAEKGKLSALQSNYEKCQA---- 911
Cdd:COG4913 591 EKDDRRRIRSRYVLGFDNRAK---LAALEAELAELEEELAEAEERLE--------ALEAELDALQERREALQRLAEyswd 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 912 --DLKQLQSDLYGKESE---LLATRQDLKSVEEKLTLAQEDLISNRNQIGnqnksiqELQAAKASLEQDSAKKEALLKEQ 986
Cdd:COG4913 660 eiDVASAEREIAELEAElerLDASSDDLAALEEQLEELEAELEELEEELD-------ELKGEIGRLEKELEQAEEELDEL 732
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 987 SKALEDAQREKSVKEKELVAEKSKLAEMEEIKCRQEKEITKLNEELKSHKQESIKEITNL 1046
Cdd:COG4913 733 QDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
21-511 |
8.12e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 21 ELQALEQQLEEAQTENFNIKQMKDLFEQKAAQL-------ATEIADIKSKYDEEKSLRAAAEQKVThLTEDLNKQTTVIQ 93
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELeerieelKKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 94 DLKTELlqrpgiedvAVLKKELVQVQTLMDNMTlERERESEKLKDECKKLQSEHAHLEA------TINQLRSELAKGPQE 167
Cdd:PRK03918 311 EIEKRL---------SRLEEEINGIEERIKELE-EKEERLEELKKKLKELEKRLEELEErhelyeEAKAKKEELERLKKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 168 VAVYvqEIQKLKGSINELTQKNQNLTEKLQKKDLDYTHLEEKHNEESASRKTLQAS-----LHQRDLDCQQLQARLTASE 242
Cdd:PRK03918 381 LTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYT 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 243 SSLQRAQGELSEKAEAAQKLREELREVESTRQH------LKVEVKQLQQQREEKEQHGLQLQGEVSQLHCKLLETERQLG 316
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKeselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLK 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 317 EAHGRLKEqrqlSSEKLMEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEKSKQQHQEQQALQQSATAKLREAQNDL 396
Cdd:PRK03918 539 GEIKSLKK----ELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKEL 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 397 EQVLRQIGDKDQKIQNLEALLQKGKESVSLLEKEREDLYAKIQAGEGEtavlnQLQEKNHALQQQLTQLTEKLKNQSESH 476
Cdd:PRK03918 615 EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE-----ELREEYLELSRELAGLRAELEELEKRR 689
|
490 500 510
....*....|....*....|....*....|....*
gi 568967304 477 KQAEENLhDQVQEQKAHLRAAQDRVLSLETSVSEL 511
Cdd:PRK03918 690 EEIKKTL-EKLKEELEEREKAKKELEKLEKALERV 723
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
20-453 |
8.57e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 20 AELQALEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEEKSLRAAAE-----QKVTHLTEDLNKQTTVIQD 94
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 95 LKTELLQ-RPGIEDVAVLKKELVQVQTLMDNmtlERERESEKLKDECKKLQSEHAHLEATINQLRSELAKGPQEVAVYVQ 173
Cdd:COG4717 151 LEERLEElRELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 174 EIQKLKGSINELTQKNQNLTEKLQKKD---------------------------------LDYTHLEEKHNEESASRKTL 220
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLLLIaaallallglggsllsliltiagvlflvlgllaLLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 221 QASLHQRDLDCQQLQARLTASESSLQRAQGELSEKAEAAQKLREELREVESTRQhlkvevkQLQQQREEKEQHGLQLQGE 300
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE-------ELQLEELEQEIAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 301 VsqlhckllETERQLGEAHGRLKEQRQLsseklmEKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLEkskqqhqeqqa 380
Cdd:COG4717 381 V--------EDEEELRAALEQAEEYQEL------KEELEELEEQLEELLGELEELLEALDEEELEEELE----------- 435
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568967304 381 lqqSATAKLREAQNDLEQVLRQIGDKDQKIQNLEallqkGKESVSLLEKEREDLYAKIQAGEGETAVLNQLQE 453
Cdd:COG4717 436 ---ELEEELEELEEELEELREELAELEAELEQLE-----EDGELAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
759-1227 |
8.77e-03 |
|
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: 40.48 E-value: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 759 SEFEKENQKGKAAVLDLEKACKELK---HQLQVQAESA-LKEQEDLKKSLEKEKETSQQLKIELNSVKGEVSQAQNTLKQ 834
Cdd:pfam05483 172 KKYEYEREETRQVYMDLNNNIEKMIlafEELRVQAENArLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 835 KEKDEQQLQGTINQLKQSAEQKKKQIEALQGEVKNAVSQKTVLENKLQQQSSQAAQELAAEKgklsALQSNYEKCQADLK 914
Cdd:pfam05483 252 KENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQK----ALEEDLQIATKTIC 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 915 QLQSDLYGKESELLATRQDLKSVEEKL---TLAQEDLISNRNQIGNQNKSIQELQAAKasleqdsakkealLKEQSKALE 991
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSFVVTEFeatTCSLEELLRTEQQRLEKNEDQLKIITME-------------LQKKSSELE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 992 DAQREKSVKEKELVAEKSKLAEMEEIkCRQEKEITKLNEELKSHKQESI-------KEITNLKDAKQLLIQQKLELQGRV 1064
Cdd:pfam05483 395 EMTKFKNNKEVELEELKKILAEDEKL-LDEKKQFEKIAEELKGKEQELIfllqareKEIHDLEIQLTAIKTSEEHYLKEV 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1065 DSLKAALEQEKeSQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENEAKLTMQVTTLNENLGTVKKEWQS 1144
Cdd:pfam05483 474 EDLKTELEKEK-LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELES 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1145 SQRrvsELEKQTDDLRGEIavleatvQNNQDERRALLERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSLQI 1224
Cdd:pfam05483 553 VRE---EFIQKGDEVKCKL-------DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
...
gi 568967304 1225 KHT 1227
Cdd:pfam05483 623 KGS 625
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
499-682 |
8.84e-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: 40.22 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 499 DRVLSLETSVSELSSQLNESKEKVSQLDIQIKAKTELLLSAEAAKAAQRAD---LQNHLdtaQHALQDKQQElnKVSVQl 575
Cdd:pfam09726 395 DALVRLEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQEndlLQTKL---HNAVSAKQKD--KQTVQ- 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 576 dQLTAKFQEKQEHCIQLESHLKDHK----------------------EKHLSLEQKVEDLEGHIKKLEadaLEVKASKEQ 633
Cdd:pfam09726 469 -QLEKRLKAEQEARASAEKQLAEEKkrkkeeeataaravalaaasrgECTESLKQRKRELESEIKKLT---HDIKLKEEQ 544
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568967304 634 ALqslqqqrqlstDLELRNAELS--RELQEQEEVVSCTKLDLQNKSEILEN 682
Cdd:pfam09726 545 IR-----------ELEIKVQELRkyKESEKDTEVLMSALSAMQDKNQHLEN 584
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1047-1237 |
9.77e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1047 KDAKQLLIQQKLELQGRVDSLKAALEQ-EKESQQLMREQVKKEEEKRKEEFSEKEAKLHSEIKEKEAGMKKHEENE---A 1122
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEAlEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSddlA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1123 KLTMQVTTLNENLGTVKKEWQSSQRRVSELEKQTDDLRGEI----AVLEATVQNNQDERRALLERCLKGEGEIEKLQTKA 1198
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdelqDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180 190
....*....|....*....|....*....|....*....
gi 568967304 1199 LELQRKLDnttAAVQELGRENQSLqIKHTQALNRKWAED 1237
Cdd:COG4913 769 ENLEERID---ALRARLNRAEEEL-ERAMRAFNREWPAE 803
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1105-1222 |
9.92e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967304 1105 SEIKEKEAGmKKHEENEAKLTMQVTTLNENLGTVKKewqsSQRRVSELEKQTDDLRGEIAVLEATVQNNQDE---RRALL 1181
Cdd:COG2433 383 EELIEKELP-EEEPEAEREKEHEERELTEEEEEIRR----LEEQVERLEAEVEELEAELEEKDERIERLERElseARSEE 457
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 568967304 1182 ERCLKGEGEIEKLQTKALELQRKLDNTTAAVQELGRENQSL 1222
Cdd:COG2433 458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| |
