|
Name |
Accession |
Description |
Interval |
E-value |
| FYVE_EEA1 |
cd15730 |
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ... |
1347-1409 |
4.24e-43 |
|
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: 150.63 E-value: 4.24e-43
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1653960520 1347 RKWAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSSKKPVRVCDACFNDL 1409
Cdd:cd15730 1 RKWADDEEVQNCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDACFDDL 63
|
|
| FYVE |
pfam01363 |
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ... |
1348-1410 |
3.30e-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: 108.62 E-value: 3.30e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1653960520 1348 KWAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTP---SSKKPVRVCDACFNDLQ 1410
Cdd:pfam01363 2 VWVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLpelGSNKPVRVCDACYDTLQ 67
|
|
| FYVE |
smart00064 |
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ... |
1346-1411 |
5.28e-28 |
|
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: 107.90 E-value: 5.28e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1653960520 1346 NRKWAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSS--KKPVRVCDACFNDLQG 1411
Cdd:smart00064 1 RPHWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLgiERPVRVCDDCYENLNG 68
|
|
| FYVE_RUFY1_like |
cd15721 |
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ... |
1349-1406 |
1.87e-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: 100.15 E-value: 1.87e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1653960520 1349 WAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSSKKPVRVCDACF 1406
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), ... |
1349-1406 |
1.02e-21 |
|
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: 89.73 E-value: 1.02e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1349 WAEDNEVQNCMACGKG-FSVTVRRHHCRQCGNIFCAECSAKNALTPS-SKKPVRVCDACF 1406
Cdd:cd15717 2 WVPDSEAPVCMHCKKTkFTAINRRHHCRKCGAVVCGACSSKKFLLPHqSSKPLRVCDTCY 61
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
609-1340 |
3.76e-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: 100.90 E-value: 3.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 609 LRAAQDRVLSLETSVNELNSQLNeSKEKVSQLDIQIKAKTELLLSAEAAKTAQRAD-LQNHLDTAQNALQDKQQELNKIT 687
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLK-SLERQAEKAERYKELKAELRELELALLVLRLEeLREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 688 TQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLELRA 767
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 768 TELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQetkiQHEELNNRIQTTVTELQKVKME 847
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL----QIASLNNEIERLEARLERLEDR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 848 KEALMTELSTVKDKLSkvsdslKNSKSEFEKENQKGKAAILDLEKTCKELKHQLQVQMENTLKEQKELKKSLEKEKEASH 927
Cdd:TIGR02168 416 RERLQQEIEELLKKLE------EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 928 QLKLeLNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQS---SEQKKKQIEALQGELKIAVLQKTE---------LENK 995
Cdd:TIGR02168 490 RLDS-LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELisvDEGYEAAIEAALGGRLQAVVVENLnaakkaiafLKQN 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 996 LQQQLTQAAQELAAEKEkISVLQNNYEKSQETFKQLQSDFYGRESELLATRQDLKS---VEEKLSLAQEDLISNR----- 1067
Cdd:TIGR02168 569 ELGRVTFLPLDSIKGTE-IQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGgvlVVDDLDNALELAKKLRpgyri 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1068 ----------------------NQIGNQNKLIQELKTAKATLEQDSAKKEQQLQERCKALQDIQKEKSLKEKELVNEKSK 1125
Cdd:TIGR02168 648 vtldgdlvrpggvitggsaktnSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1126 LAEIEEIKCRQEKEITKLNEELKSHKlesiKEITNLKDAKQLLIQQKLELQGKADSLKAAVEQEKRNQQILKDQVKKEEE 1205
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLS----KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1206 ELKKEFIEKEAkLHSEIKEKEVGMKKHEENEAKLTMQITALNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATV 1285
Cdd:TIGR02168 804 ALDELRAELTL-LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1653960520 1286 QNNQDERRALLERCLKGEGEIEKLQTKVLELQRKLDNTTAAVQELGRENQSLQIK 1340
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
375-1153 |
5.41e-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: 100.13 E-value: 5.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 375 QKLKEELSEVETKYQHLKAEFKQ---LQQQREEKEQHGLQLQS-EINQLHSKLLETERQLGEAHGRLKEqrqlSSEKLMD 450
Cdd:TIGR02168 189 DRLEDILNELERQLKSLERQAEKaerYKELKAELRELELALLVlRLEELREELEELQEELKEAEEELEE----LTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 451 KEQQVADLQLKLSRLEEQLkekvtnsTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEA 530
Cdd:TIGR02168 265 LEEKLEELRLEVSELEEEI-------EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 531 LLQKSKENISLLEKEREDLYAKIQAGEgetAVLNQLQEKNHTLQEQVTQLTEKLKnqseSHKQAQENLHDQVQEQKAHLR 610
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELE---AELEELESRLEELEEQLETLRSKVA----QLELQIASLNNEIERLEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 611 AAQDRVLSLETSVNELNSQLNESKEKVSQLDIqikaktelllsaeAAKTAQRADLQNHLDTAQNALQDKQQELNKITTQL 690
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELKELQAEL-------------EELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 691 DQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEG--QIKKLEADSLEVKASKEQALQDLQQQRQLN---TDLEL 765
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsGILGVLSELISVDEGYEAAIEAALGGRLQAvvvENLNA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 766 RATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETKIQHEELNN-RIQTTVTELQKV 844
Cdd:TIGR02168 558 AKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGvLVVDDLDNALEL 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 845 KMEKEALMTeLSTVKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKTCKELK---HQLQVQMENTLKEQKELKKSLEK 921
Cdd:TIGR02168 638 AKKLRPGYR-IVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEekiAELEKALAELRKELEELEEELEQ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 922 EKEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKIAVLQKTELEnklqQQLT 1001
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE----AQIE 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1002 QAAQELAAEKEKISVLQNNYEKSQETFKQLQSDFYGRESELLATRQDLKSVEEKLSLAQEDLISNRNQIGNQNKLIQELK 1081
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1653960520 1082 TAKATLEQDSAKKEQQLQERCKALQDIQKEkslkekelvnekskLAEIEEIKCRQEKEITKLNEELKSHKLE 1153
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEE--------------LRELESKRSELRRELEELREKLAQLELR 930
|
|
| FYVE_LST2 |
cd15731 |
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ... |
1349-1407 |
1.23e-20 |
|
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: 86.63 E-value: 1.23e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1653960520 1349 WAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSSK--KPVRVCDACFN 1407
Cdd:cd15731 5 WVPDEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRYGqmKPVRVCNHCFM 65
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
500-1334 |
1.32e-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: 98.98 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 500 TTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLlEKEREDLYAKIQAGEgetavLNQLQEKNHTLQEQVTQ 579
Cdd:TIGR02168 177 TERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKEL-KAELRELELALLVLR-----LEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 580 LTEKLKNQSESHKQAQ---ENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTElllsaea 656
Cdd:TIGR02168 251 AEEELEELTAELQELEeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA------- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 657 aktaQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLE 736
Cdd:TIGR02168 324 ----QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 737 ADSLEVKASKEQALQDLQQQRQLNTDL-----ELRATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKI 811
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 812 LKQDFETLSQETKIQhEELNNRIQTTVTELQKVKMEKEALMTELSTVKDKLskvsdslknsksEFEKENQKGKAAILDle 891
Cdd:TIGR02168 480 AERELAQLQARLDSL-ERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI------------SVDEGYEAAIEAALG-- 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 892 ktckelKHQLQVQMENtlKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNEKEeqQLQGNINELKQSSEQK 971
Cdd:TIGR02168 545 ------GRLQAVVVEN--LNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIE--GFLGVAKDLVKFDPKL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 972 KKQIEALQGELKIAvlqkTELENKLQQQLTQAAQEL-----------------AAEKEKISVLQNNYEksqetFKQLQSD 1034
Cdd:TIGR02168 615 RKALSYLLGGVLVV----DDLDNALELAKKLRPGYRivtldgdlvrpggvitgGSAKTNSSILERRRE-----IEELEEK 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1035 FYGRESELLATRQDLKSVEEKLSLAQEDLISNRNQIGNQNKLIQELKTAKATLEQDSAKKEQQLQERCKALQDIQKEKSL 1114
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1115 KEKELVNEKSKLAEIEEIKCRQEKEITKLNEELKShkleSIKEITNLKDAKQLLIQQKLELQGKADSLKAAVEQEKRNQQ 1194
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA----LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1195 ILKDQVKKEEEELKK------EFIEKEAKLHSEIKEKEVGMKKHEENEAKLTMQITALNENLGTVKKEWQSSQRRVSELE 1268
Cdd:TIGR02168 842 DLEEQIEELSEDIESlaaeieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1653960520 1269 KQTDDLRGEIAVLEATVQNNQDERRALLERCLKG-EGEIEKLQTKVLELQRKLDNTTAAVQELGREN 1334
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEaEALENKIEDDEEEARRRLKRLENKIKELGPVN 988
|
|
| FYVE_like_SF |
cd00065 |
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ... |
1357-1406 |
1.53e-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: 86.05 E-value: 1.53e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1653960520 1357 NCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSSK--KPVRVCDACF 1406
Cdd:cd00065 1 RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSFGsgKPVRVCDSCY 52
|
|
| FYVE_WDFY3 |
cd15719 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ... |
1349-1409 |
1.73e-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: 83.59 E-value: 1.73e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1653960520 1349 WAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSSK--KPVRVCDACFNDL 1409
Cdd:cd15719 3 WVKDEGGDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFESEIRRLRisRPVRVCQACYNIL 65
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
243-964 |
3.95e-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: 94.35 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 243 ERERESEKLKDECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQKNQTLtenllkkeqdytkle 322
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL--------------- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 323 ekhneeSVSKKNIQATLHQKDLDCQQLQSRLSASETSLHRIHVELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQR 402
Cdd:TIGR02168 308 ------RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 403 EEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQLSSEKLMDK-EQQVADLQLKLSRLEEQLKEKVTNSTELQH 481
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELEELQEELERLEE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 482 QLDKTKQQHqeqqalqqsttAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEKERED-------LYAKIQ 554
Cdd:TIGR02168 462 ALEELREEL-----------EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvLSELIS 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 555 AGEG-ETAVLNQLQEKNHTL----QEQVTQLTEKLKNQ-----------SESHKQAQENLHDQVQEQKAHLRAAQDRV-- 616
Cdd:TIGR02168 531 VDEGyEAAIEAALGGRLQAVvvenLNAAKKAIAFLKQNelgrvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVkf 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 617 -----------LSLETSVNELNSQLNESKEKVSQLDIQIKAKTelLLSAEAAKTAQRADlqnhldtAQNALQDKQQELNK 685
Cdd:TIGR02168 611 dpklrkalsylLGGVLVVDDLDNALELAKKLRPGYRIVTLDGD--LVRPGGVITGGSAK-------TNSSILERRREIEE 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 686 ITTQLDQVTAKLQdkqehcsQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLEL 765
Cdd:TIGR02168 682 LEEKIEELEEKIA-------ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 766 RATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQEtkiqHEELNNRIQTTVTELQKVK 845
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE----LTLLNEEAANLRERLESLE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 846 MEKEALMTELSTVKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKTcKELKHQLQVQMENTLKEQKELKKSLEKEKEA 925
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL-LNERASLEEALALLRSELEELSEELRELESK 909
|
730 740 750
....*....|....*....|....*....|....*....
gi 1653960520 926 SHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINEL 964
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| FYVE_RUFY1 |
cd15758 |
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ... |
1349-1409 |
5.39e-19 |
|
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: 82.42 E-value: 5.39e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1653960520 1349 WAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSSKKPVRVCDACFNDL 1409
Cdd:cd15758 6 WLKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLL 66
|
|
| FYVE_Hrs |
cd15720 |
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ... |
1349-1409 |
6.12e-19 |
|
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: 81.66 E-value: 6.12e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1653960520 1349 WAEDNEvqnCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSS--KKPVRVCDACFNDL 1409
Cdd:cd15720 2 WKDGDE---CHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSSTIPKFgiEKEVRVCDPCYEKL 61
|
|
| FYVE_ANFY1 |
cd15728 |
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ... |
1349-1409 |
6.88e-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: 6.88e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1653960520 1349 WAEDNevqNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKnaLTPSSK----KPVRVCDACFNDL 1409
Cdd:cd15728 4 WADGD---YCYECGVKFGITTRKHHCRHCGRLLCSKCSTK--EVPIIKfdlnKPVRVCDVCFDVL 63
|
|
| FYVE_scVPS27p_like |
cd15760 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
1348-1406 |
1.10e-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: 81.19 E-value: 1.10e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1653960520 1348 KWAEDNEvqnCMACGKGFSVTVRRHHCRQCGNIFCAECSAK----NALTPSSkKPVRVCDACF 1406
Cdd:cd15760 1 HWKPDSR---CDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRriplPHLGPLG-VPQRVCDRCF 59
|
|
| FYVE_endofin |
cd15729 |
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ... |
1349-1409 |
1.59e-18 |
|
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: 80.86 E-value: 1.59e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1653960520 1349 WAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAE-CSAKNALTPSSKKPVRVCDACFNDL 1409
Cdd:cd15729 7 WVPDSEAPNCMQCEVKFTFTKRRHHCRACGKVLCSAcCSLKARLEYLDNKEARVCVPCYQTL 68
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-864 |
7.12e-18 |
|
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: 90.12 E-value: 7.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 137 LQSLEQQLEEAQTEnfnIKQMKDLFEQKAAQLATEIADIKSKYDEERSLREAAEQKVTRLTEELNKEATVIQDLKTELLQ 216
Cdd:TIGR02168 202 LKSLERQAEKAERY---KELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 217 RPgiEDVAVLKKELVQVQTLMDNMTLERERESEKLKDeckkLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLKSS 296
Cdd:TIGR02168 279 LE--EEIEELQKELYALANEISRLEQQKQILRERLAN----LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 297 VNELTQKNQTLTENLLKKEQDYTKLEEKHNEES--VSKKNIQATLHQKDLdcQQLQSRLSASETSLHRIHVELSEKGEAT 374
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRskVAQLELQIASLNNEI--ERLEARLERLEDRRERLQQEIEELLKKL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 375 QKLkeELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLK--EQRQLSSEKLMDKE 452
Cdd:TIGR02168 431 EEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDslERLQENLEGFSEGV 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 453 QQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAK-----LREAQNDLEQVLRQIGDKDQKIQN 527
Cdd:TIGR02168 509 KALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAAKkaiafLKQNELGRVTFLPLDSIKGTEIQG 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 528 LEALLQKSKEN----ISLLEKEREDLYAKIQAGEGETAVLNQLQE-----KNHTLQEQVTQLTEKLKNQSESHKQAQENL 598
Cdd:TIGR02168 589 NDREILKNIEGflgvAKDLVKFDPKLRKALSYLLGGVLVVDDLDNalelaKKLRPGYRIVTLDGDLVRPGGVITGGSAKT 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 599 HDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTAQRADLQNHLDTAQNALQD 678
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 679 KQQELNKITTQLDQVTAKLQDKQEhcsqLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQ 758
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEE----AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 759 LNTDLELRATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQ---ETKIQHEELNNRIQ 835
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEalaLLRSELEELSEELR 904
|
730 740
....*....|....*....|....*....
gi 1653960520 836 TTVTELQKVKMEKEALMTELSTVKDKLSK 864
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEG 933
|
|
| FYVE_MTMR4 |
cd15733 |
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ... |
1349-1406 |
1.62e-17 |
|
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: 77.86 E-value: 1.62e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1349 WAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSSK--KPVRVCDACF 1406
Cdd:cd15733 1 WVPDHAASHCFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPDEQlyDPVRVCNSCY 60
|
|
| FYVE_PKHF2 |
cd15755 |
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ... |
1349-1409 |
4.55e-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: 76.61 E-value: 4.55e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1653960520 1349 WAEDNEVQNCMACGKG-FSVTVRRHHCRQCGNIFCAECSAKNALTPS-SKKPVRVCDACFNDL 1409
Cdd:cd15755 2 WVPDSEATVCMRCQKAkFTPVNRRHHCRKCGFVVCGPCSEKKFLLPSqSSKPVRVCDFCYDLL 64
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
243-808 |
1.50e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.76 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 243 ERERESEKLKDECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQKNQTLTENLLKKEQDYTKLE 322
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 323 EKHNEESVSKKNIQATLHQKDLDCQQLQSRLSASETSLHRIHVELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQR 402
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 403 EEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQLSSEklmdKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQ 482
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE----LEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 483 LDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGEGETAV 562
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 563 LNQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSqlneskekVSQLDI 642
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL--------VASDLR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 643 QIKAKTELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLE 722
Cdd:COG1196 610 EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 723 QKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLELRATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKL 802
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL 769
|
....*.
gi 1653960520 803 TKQEEE 808
Cdd:COG1196 770 ERLERE 775
|
|
| FYVE_MTMR3 |
cd15732 |
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ... |
1348-1406 |
1.53e-16 |
|
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: 74.94 E-value: 1.53e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1653960520 1348 KWAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSSK--KPVRVCDACF 1406
Cdd:cd15732 1 RWVPDHLAASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLPVPSQQlfEPSRVCKSCF 61
|
|
| FYVE_ZF21 |
cd15727 |
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ... |
1349-1405 |
3.77e-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: 73.95 E-value: 3.77e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1653960520 1349 WAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTP--SSKKPVRVCDAC 1405
Cdd:cd15727 4 WVPDKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVPLPrmCFVDPVRVCNEC 62
|
|
| FYVE_FGD6 |
cd15743 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ... |
1349-1406 |
4.52e-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: 73.63 E-value: 4.52e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1653960520 1349 WAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNA-LTPSSKKPVRVCDACF 1406
Cdd:cd15743 3 WIPDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNKApLEYLKNKSARVCDECF 61
|
|
| FYVE_RABE_unchar |
cd15739 |
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ... |
1348-1406 |
6.27e-16 |
|
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: 73.53 E-value: 6.27e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1653960520 1348 KWAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSSKKPVRVCDACF 1406
Cdd:cd15739 3 RWQHEDDVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCH 61
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
114-911 |
6.97e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 83.57 E-value: 6.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 114 EKYQGLQQQEAKPDGLVtdSSAELQSLEQQLEEAQTEnfnIKQMKDLFEQKAAQLATeiadIKSKYDEERSLREAAEQKV 193
Cdd:TIGR02168 213 ERYKELKAELRELELAL--LVLRLEELREELEELQEE---LKEAEEELEELTAELQE----LEEKLEELRLEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 194 TRLTEELNKEATVIQDLKTELlqrpgiedvAVLKKELVQVQTLMDnmtlERERESEKLKDECKKLQSQYASSEATISQLR 273
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQK---------QILRERLANLERQLE----ELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 274 SELAKGPQEVAVYVQELQKLKSSVNELTQKNQTLTENLLKKEQDYTKLEEKHNEESVSKKNIQAtlHQKDLDCQQLQSRL 353
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED--RRERLQQEIEELLK 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 354 SASETSLHRIHVELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHS------------ 421
Cdd:TIGR02168 429 KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERlqenlegfsegv 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 422 -KLLETERQLGEAHGRLKEQRQLSSEK---------------LMDKEQQVADLQlklSRLEEQLKEKVTN---STELQHQ 482
Cdd:TIGR02168 509 kALLKNQSGLSGILGVLSELISVDEGYeaaieaalggrlqavVVENLNAAKKAI---AFLKQNELGRVTFlplDSIKGTE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 483 LDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLR---------------------------------------------- 516
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitggs 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 517 -----QIGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGEgetavlNQLQEKNHTLQEQVTQLTEkLKNQSESH 591
Cdd:TIGR02168 666 aktnsSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELE------EELEQLRKELEELSRQISA-LRKDLARL 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 592 KQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTAQRADLQNHldt 671
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL--- 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 672 aQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQ 751
Cdd:TIGR02168 816 -NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 752 DLQQQRQLNTDLELRATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTkqeEEKKILKQDFETLSQETKIQHEELN 831
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEAR 971
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 832 NRI---QTTVTELQKVKMEKEALMTELSTVKDKLSKVSDSLKNSKSEFEKenqkgkaAILDLEKTCKELKHQLQVQMENT 908
Cdd:TIGR02168 972 RRLkrlENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE-------AIEEIDREARERFKDTFDQVNEN 1044
|
...
gi 1653960520 909 LKE 911
Cdd:TIGR02168 1045 FQR 1047
|
|
| FYVE_FYCO1 |
cd15726 |
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ... |
1349-1406 |
7.88e-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: 72.98 E-value: 7.88e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1653960520 1349 WAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSSKKPVRVCDACF 1406
Cdd:cd15726 1 WQDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKACF 58
|
|
| FYVE_FGD1_2_4 |
cd15741 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ... |
1348-1409 |
1.33e-15 |
|
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: 72.52 E-value: 1.33e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1653960520 1348 KWAEDNEVQNCMACGKGF-SVTVRRHHCRQCGNIFCAECSAKNA-LTPSSKKPVRVCDACFNDL 1409
Cdd:cd15741 2 RWVRDNEVTMCMRCKEPFnALTRRRHHCRACGYVVCWKCSDYKAtLEYDGNKLNRVCKHCYVIL 65
|
|
| FYVE_RBNS5 |
cd15716 |
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ... |
1349-1409 |
2.08e-15 |
|
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: 71.99 E-value: 2.08e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1653960520 1349 WAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALtpsskkPVRVCDACFNDL 1409
Cdd:cd15716 4 WVNDSDVPFCPDCGKKFNLARRRHHCRLCGSIMCNKCSQFLPL------HIRCCHHCKDLL 58
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
267-1011 |
3.35e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 81.27 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 267 ATISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQKNQTLTENLLKKEQ-----------DYTKLEEKHNEESVSKKNI 335
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqallkekreyEGYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 336 QATLHQKDLDCQQLQSRLSASETSLHRIHVELSEKGEATQKL-KEELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQS 414
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 415 EINQLHS---KLLETERQLGEAHGRLKEQRQLSSEKLMDKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQqhq 491
Cdd:TIGR02169 323 RLAKLEAeidKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR--- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 492 eqqalqqsttaKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGEGEtavLNQLQEKNH 571
Cdd:TIGR02169 400 -----------EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK---LEQLAADLS 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 572 TLQEQVTQLTEKLKNQSESHKQAQENLhdqvQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLdIQIKAKTELL 651
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQREL----AEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL-GSVGERYATA 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 652 LSAEAAKTAQRADLQNHLDTAQ------------------NALQDKQQELNKITTQ------LDQV-------------- 693
Cdd:TIGR02169 541 IEVAAGNRLNNVVVEDDAVAKEaiellkrrkagratflplNKMRDERRDLSILSEDgvigfaVDLVefdpkyepafkyvf 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 694 ----------TAKLQDKQEHCSQLESHL---------------------KEYKEKYLSLEQKTEELEGQIKKLEADSLEV 742
Cdd:TIGR02169 621 gdtlvvedieAARRLMGKYRMVTLEGELfeksgamtggsraprggilfsRSEPAELQRLRERLEGLKRELSSLQSELRRI 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 743 KASKEQALQDLQQQRQLNTDLELRATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETL-SQ 821
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLeEA 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 822 ETKIQHEELNNRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSdslkNSKSEFEKENQKGKAAILDLEKTCKELKhql 901
Cdd:TIGR02169 781 LNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT----LEKEYLEKEIQELQEQRIDLKEQIKSIE--- 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 902 qvqmentlKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGE 981
Cdd:TIGR02169 854 --------KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
810 820 830
....*....|....*....|....*....|
gi 1653960520 982 LKIAVLQKTELENKLQQQLTQAAQELAAEK 1011
Cdd:TIGR02169 926 LEALEEELSEIEDPKGEDEEIPEEELSLED 955
|
|
| FYVE_ZFY26 |
cd15724 |
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ... |
1349-1407 |
4.85e-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: 70.62 E-value: 4.85e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1653960520 1349 WAEDNEVQNCMAC-GKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSSKK-PVRVCDACFN 1407
Cdd:cd15724 1 WVPDEAVSVCMVCqVERFSMFNRRHHCRRCGRVVCSSCSTKKMLVEGYREnPVRVCDQCYE 61
|
|
| FYVE_PKHF1 |
cd15754 |
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ... |
1349-1409 |
5.19e-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: 70.76 E-value: 5.19e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1653960520 1349 WAEDNEVQNCMACGK-GFSVTVRRHHCRQCGNIFCAECSAKNALTPS-SKKPVRVCDACFNDL 1409
Cdd:cd15754 2 WIPDKATDICMRCTQtNFSLLTRRHHCRKCGFVVCHECSRQRFLIPRlSPKPVRVCSLCYRKL 64
|
|
| FYVE_spVPS27p_like |
cd15735 |
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ... |
1352-1406 |
5.33e-15 |
|
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 (spVps27p) and similar proteins; spVps27p, also termed suppressor of ste12 deletion protein 4 (Sst4p), is a conserved homolog of budding Saccharomyces cerevisiae Vps27 and of mammalian Hrs. It functions as a downstream factor for phosphatidylinositol 3-kinase (PtdIns 3-kinase) in forespore membrane formation with normal morphology. It colocalizes and interacts with Hse1p, a homolog of Saccharomyces cerevisiae Hse1p and of mammalian STAM, to form a complex whose ubiquitin-interacting motifs (UIMs) are important for sporulation. spVps27p contains a VHS (Vps27p/Hrs/Stam) domain, a FYVE domain, and two UIMs.
Pssm-ID: 277274 [Multi-domain] Cd Length: 59 Bit Score: 70.64 E-value: 5.33e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1653960520 1352 DNEVqnCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTP--SSKKPVRVCDACF 1406
Cdd:cd15735 5 DSDV--CMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPhfGINQPVRVCDGCY 59
|
|
| FYVE_ZFYV1 |
cd15734 |
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ... |
1349-1406 |
5.62e-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: 70.44 E-value: 5.62e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1349 WAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSS--KKPVRVCDACF 1406
Cdd:cd15734 2 WVPDSEIKECSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRgwDHPVRVCDPCA 61
|
|
| FYVE_RUFY2 |
cd15759 |
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ... |
1349-1405 |
6.49e-15 |
|
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: 70.82 E-value: 6.49e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1653960520 1349 WAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSSKKPVRVCDAC 1405
Cdd:cd15759 4 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSC 60
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
502-1298 |
8.88e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 80.11 E-value: 8.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 502 AKLREAQNDLEQVLRQIGDKD----QKIQNLEAL------------LQKSKENI--SLLEKEREDLYAKIQAGEGE---- 559
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDliidEKRQQLERLrrerekaeryqaLLKEKREYegYELLKEKEALERQKEAIERQlasl 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 560 TAVLNQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDRvlsLETSVNELNSQLNESKEKVSQ 639
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAS---LERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 640 LDIQIKAKTELLLSAEAAKTAQRADLqnhlDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYL 719
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRR----DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 720 SLEQKTEELEGQIKKLEADSLEVKASKEQALQDLqqqrqlnTDLELRATELSKQLEMEKEIVSSTRLDLQKKSEALESIK 799
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKI-------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 800 QKLTKQEEEKKILKQDFETL----------SQETKIQHEELNNRIQ---TTVTELQKVKmEKEALMTElSTVKDKLSKV- 865
Cdd:TIGR02169 476 EEYDRVEKELSKLQRELAEAeaqaraseerVRGGRAVEEVLKASIQgvhGTVAQLGSVG-ERYATAIE-VAAGNRLNNVv 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 866 --SDSLKNSKSEFEKENQKGKAAILDLEKTCKELKHQLQVQMENTLKEQKELKKSLEK------------------EKEA 925
Cdd:TIGR02169 554 veDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafkyvfgdtlvvediEAAR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 926 SHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKIAVLQKTELEN---KLQQQLTQ 1002
Cdd:TIGR02169 634 RLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENrldELSQELSD 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1003 AAQELAAEKEKISVLQNNYEKSQETFKQLQSDFYGRESELLATRQDLKSVEEKLSLAQEDLISNRNQIGN-----QNKLI 1077
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRI 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1078 QELKTAKATLEQDSAKKEQQLQERCKALQDIQKEKSLKEKELVNEKSKLAEIEEikcrQEKEITKLNEELKSHKLESIKE 1157
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE----QIKSIEKEIENLNGKKEELEEE 869
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1158 ITNLKDAKQLLIQQKLELQGKADSLKAAVEQEKRNQQILKDQVKKEEEELKKEFIEKEAkLHSEIKEKEVGMKKHEEnea 1237
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA-LEEELSEIEDPKGEDEE--- 945
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1653960520 1238 kltmqITALNENLGTVKKEWQSSQRRVSELE--------------KQTDDLRGEIAVLEAtvqnnqdERRALLER 1298
Cdd:TIGR02169 946 -----IPEEELSLEDVQAELQRVEEEIRALEpvnmlaiqeyeevlKRLDELKEKRAKLEE-------ERKAILER 1008
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
888-1191 |
6.06e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.28 E-value: 6.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 888 LDLEKTCKELKHQLQV-QMENTLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQ 966
Cdd:COG1196 216 RELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 967 SSEQKKKQIEALQGELKIAVLQKTELEnklqQQLTQAAQELAAEKEKISVLQNNYEKSQETFKQLQSDFYGRESELLATR 1046
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELE----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1047 QDLKSVEEKLSLAQEDLISNRNQIGNQNKLIQELKTAKATLEQDSAKKEQQLQERCKALQDIQKEKSLKEKELVNEKSKL 1126
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1653960520 1127 AEIEEIKCRQEKEITKLNEELKSHKLESIKEITNLKDAKQ---LLIQQKLELQGKADSLKAAVEQEKR 1191
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAArllLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
114-677 |
8.09e-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: 8.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 114 EKYQGLQQQEAKPDGLVT-----DSSAELQSLEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEERSLREA 188
Cdd:COG1196 213 ERYRELKEELKELEAELLllklrELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 189 AEQKVTRLTEELNKEATVIQDLKTELLQRpgIEDVAVLKKELVQVQTLMDNMTLERERESEKLKDECKKL---QSQYASS 265
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEEL--EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELaeaEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 266 EATISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQKNQTLTENLLKKEQDYTKLEEKHNEESVSKKNIQATLHQKDLD 345
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 346 CQQLQSRLSASETSLHRIHVELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREE-KEQHGLQLQSEINQLHSKLL 424
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGLAGAVAVLI 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 425 ----ETERQLGEAHGRLKEQRQLSSEKLMdKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQST 500
Cdd:COG1196 531 gveaAYEAALEAALAAALQNIVVEDDEVA-AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 501 TAKLREAQNDLEQVLRQIgdkdqkiqnLEALLQKSKENISLLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQL 580
Cdd:COG1196 610 EADARYYVLGDTLLGRTL---------VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 581 TEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTA 660
Cdd:COG1196 681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
570
....*....|....*..
gi 1653960520 661 QRADLQNHLDTAQNALQ 677
Cdd:COG1196 761 DLEELERELERLEREIE 777
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
74-939 |
3.53e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.72 E-value: 3.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 74 GESNLALKRDDvtlLRQEVQDLQASLKEEKWYS--EELKKELEKYQGLQQQEAKPDGLVTDSSAELQSLEQQLEEAQten 151
Cdd:TIGR02169 205 REREKAERYQA---LLKEKREYEGYELLKEKEAleRQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELN--- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 152 fniKQMKDLFEQKAAQLATEIADIKSKYDEERSLREAAEQKVTRLTEELNKEATVIQDLKtellqrpgiEDVAVLKKELV 231
Cdd:TIGR02169 279 ---KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL---------AEIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 232 QVQTLMDNMTlereRESEKLKDECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQKNQTLTENL 311
Cdd:TIGR02169 347 EERKRRDKLT----EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 312 LKKEQDYTKLEEKHNEESVSKKNIQATLHQKDLDCQQLQSRLSASETSLHRIHVELSEKGEATQKLKEELSEVETKyqhl 391
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ---- 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 392 kaefkqlQQQREEKEQHGLQLQSEINQLHSKLLETERQLgeahGRLKEQRQLSSEKLMDKEQQ--VADLQLKLSRLEEQL 469
Cdd:TIGR02169 499 -------ARASEERVRGGRAVEEVLKASIQGVHGTVAQL----GSVGERYATAIEVAAGNRLNnvVVEDDAVAKEAIELL 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 470 KEKVTNSTELqhqLDKTKQQHQEQQALQQSTTAKLREAQNdleqvlrqIGDKDQKIQNLEALLQKSKENISLLEKEREDL 549
Cdd:TIGR02169 568 KRRKAGRATF---LPLNKMRDERRDLSILSEDGVIGFAVD--------LVEFDPKYEPAFKYVFGDTLVVEDIEAARRLM 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 550 -YAKIQAGEGEtavlnqLQEKNHTLQEQVTQLTEKLKNQSESHKQAQEnLHDQVQEQKAHLRAAQDRVLSLETSVNELNS 628
Cdd:TIGR02169 637 gKYRMVTLEGE------LFEKSGAMTGGSRAPRGGILFSRSEPAELQR-LRERLEGLKRELSSLQSELRRIENRLDELSQ 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 629 QLNESKEKVSQLDIQIkaktELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLE 708
Cdd:TIGR02169 710 ELSDASRKIGEIEKEI----EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 709 SHLKEykEKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLELRATELSKQLEMEKEIVSSTRLDL 788
Cdd:TIGR02169 786 ARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 789 QKKSEALESIKQKLTKQEEEKKILKQDFEtlsqETKIQHEELNNRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDS 868
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERD----ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 869 LKNSKSEFEKEnqkgkAAILDLEKTCKELKHQLQV----------QMENTLKEQKELKKSLEKEKEASHQLKLELNSMQE 938
Cdd:TIGR02169 940 KGEDEEIPEEE-----LSLEDVQAELQRVEEEIRAlepvnmlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
.
gi 1653960520 939 Q 939
Cdd:TIGR02169 1015 K 1015
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-747 |
4.35e-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: 74.32 E-value: 4.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 88 LRQEVQDLQASLKEEKWYSEELKKELEKYQG----LQQQEAKPDGLVTDSSAELQSLEQQLEEAQTENFNIKQMKDLFEQ 163
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKelyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 164 KAAQLATEIADIKSKYDEERSLREAAEQKVTRLTEELNKEATVIQDLKTELLQRpgIEDVAVLKKELVQVQTLMDNMTLE 243
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL--ELQIASLNNEIERLEARLERLEDR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 244 RERESEKLKDECKKLQS-QYASSEATISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQKNQTLTENLLKKEQDYTKLE 322
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 323 ---EKHNEESVSKKNIQATLHQKDLDCQQLQSRLS-------ASETSL-HRIHVELSEKGEATQKLKEELSEVET----- 386
Cdd:TIGR02168 496 rlqENLEGFSEGVKALLKNQSGLSGILGVLSELISvdegyeaAIEAALgGRLQAVVVENLNAAKKAIAFLKQNELgrvtf 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 387 ------KYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKL----------------LETERQLGE------AHGRLK 438
Cdd:TIGR02168 576 lpldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvvddldnaLELAKKLRPgyrivtLDGDLV 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 439 EQRQLSSEKLMDKEQQVADLQLKLSRLEEQLK-------EKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDL 511
Cdd:TIGR02168 656 RPGGVITGGSAKTNSSILERRREIEELEEKIEeleekiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 512 EQVLRQIGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGEGEtavLNQLQEKNHTLQEQVTQLTEKLKNQSESH 591
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE---IEELEAQIEQLKEELKALREALDELRAEL 812
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 592 KQAQENLHDQVQEQKAHLRaaqdRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLlsaeAAKTAQRADLQNHLDT 671
Cdd:TIGR02168 813 TLLNEEAANLRERLESLER----RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI----EELESELEALLNERAS 884
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1653960520 672 AQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASKE 747
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE 960
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
375-1158 |
6.28e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.95 E-value: 6.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 375 QKLKEELSEVETKYQHLKAEFKQLQQQREekeqhglQLQSEINQ-LHSKLLETERQLGEAHGRLKEQRQLSSEKlMDKEQ 453
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLE-------RLRREREKaERYQALLKEKREYEGYELLKEKEALERQK-EAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 454 QVADLQLKLSRLEEQLKEKVTNSTELQHQLDK-TKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALL 532
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 533 QKSKENISLLEKEREDLYAKIQagegetavlnqlqeknhTLQEQVTQLTEKLKNQseshKQAQENLHDQVQEQKAHLRAA 612
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIE-----------------EERKRRDKLTEEYAEL----KEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 613 QDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTAQRADLqNHLDTaqnALQDKQQELNKITTQLDQ 692
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI-NELEE---EKEDKALEIKKQEWKLEQ 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 693 VTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLELRATELSK 772
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYAT 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 773 QLEME-----KEIVSSTRLDLQKKSEALESIKQ------KLTKQEEEKKILKQDFETLSQETKIQHEELNNRIQTTVT-- 839
Cdd:TIGR02169 540 AIEVAagnrlNNVVVEDDAVAKEAIELLKRRKAgratflPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKyv 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 840 ----------ELQKVKMEKEALMTELSTVKDKL-SKVSDSLKNSKSEFEKENQKGKAAildlektckelkhQLQVQMENT 908
Cdd:TIGR02169 620 fgdtlvvediEAARRLMGKYRMVTLEGELFEKSgAMTGGSRAPRGGILFSRSEPAELQ-------------RLRERLEGL 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 909 LKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELK--IAV 986
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKelEAR 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 987 LQKTELEnKLQQQLTQAAQELAAEKEKISVLQNNYEKSQETFKQLQSDFYGRESELLATRQDLKSVEEKLSLAQEDLISN 1066
Cdd:TIGR02169 767 IEELEED-LHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1067 RNQIGNQNKLIQELKTAKATLEQDSAKKEQQLQERCKALQDIQKEKSLKEKELVNEKSKLAEIeEIKCRQEKEITKLNEE 1146
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL-EAQIEKKRKRLSELKA 924
|
810
....*....|..
gi 1653960520 1147 LKSHKLESIKEI 1158
Cdd:TIGR02169 925 KLEALEEELSEI 936
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
446-1320 |
8.45e-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: 8.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 446 EKLMDKEQQVADLQLKLSRLEEQLKekvTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKI 525
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 526 QNLEALLQKSKENISLLEKEREDLYAKIQA-GEGETavlNQLQEKNHTLQEQVtqltEKLKNQSESHKQAQENLHDQVQE 604
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQ---LRVKEKIGELEAEI----ASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 605 QKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLdiqiKAKTELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELN 684
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL----KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 685 KITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEAdslevkaskeqalqdlqqqrqlntdle 764
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW--------------------------- 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 765 lRATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILkqdfETLSQETKIQHEELNNRIQT---TVTEL 841
Cdd:TIGR02169 456 -KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS----EERVRGGRAVEEVLKASIQGvhgTVAQL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 842 QKVKmEKEALMTElSTVKDKLSKV---SDSLKNSKSEFEKENQKGKAAILDLEKTCKELKHQLQVQMENTLKEQKELKKS 918
Cdd:TIGR02169 531 GSVG-ERYATAIE-VAAGNRLNNVvveDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEF 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 919 LEK------------------EKEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQG 980
Cdd:TIGR02169 609 DPKyepafkyvfgdtlvvediEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 981 ELKIAVLQKTELENklqqQLTQAAQELAAEKEKISVLQNNYEKSQEtfkqlqsdfygresELLATRQDLKSVEEKLSLAQ 1060
Cdd:TIGR02169 689 ELSSLQSELRRIEN----RLDELSQELSDASRKIGEIEKEIEQLEQ--------------EEEKLKERLEELEEDLSSLE 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1061 EDlisnrnqignqnklIQELKTAKATLEQDSAKKEQQLQERCKALQDIqkEKSLKEKELVNEKSKLAEIEEIKCRQEKEI 1140
Cdd:TIGR02169 751 QE--------------IENVKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARL 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1141 TKLNEELKSHKLEsiKEItnLKDAKQLLIQQKLELQGKADSLKAAVEQEKrnqqilkdqvkkeeeelkkefiEKEAKLHS 1220
Cdd:TIGR02169 815 REIEQKLNRLTLE--KEY--LEKEIQELQEQRIDLKEQIKSIEKEIENLN----------------------GKKEELEE 868
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1221 EIKEKEVGMKKHEENEAKLTMQITALNENLGTVkkewqssQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCL 1300
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLREL-------ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
890 900
....*....|....*....|....*.
gi 1653960520 1301 KGEGE------IEKLQTKVLELQRKL 1320
Cdd:TIGR02169 942 EDEEIpeeelsLEDVQAELQRVEEEI 967
|
|
| FYVE_PIKfyve_Fab1 |
cd15725 |
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ... |
1349-1406 |
8.76e-13 |
|
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: 64.27 E-value: 8.76e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1349 WAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPSSKKP--VRVCDACF 1406
Cdd:cd15725 2 WMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPgdLRVCTYCC 61
|
|
| FYVE_MTMR_unchar |
cd15738 |
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ... |
1348-1406 |
1.16e-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: 63.89 E-value: 1.16e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1653960520 1348 KWAEDNEVQNCmACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPS--SKKPVRVCDACF 1406
Cdd:cd15738 2 DWKSFRNVTEC-SCSTPFDHFSKKHHCWRCGNVFCTRCIDKQRALPGhlSQRPVPVCRACY 61
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
716-1298 |
1.29e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 716 EKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLELRATElsKQLEMEKEIVSSTRLDLQKKSEAL 795
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE--AELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 796 ESIKQKLTKQEEEKKILK---QDFETLSQETKIQHEELNNRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDSLKNS 872
Cdd:COG1196 291 YELLAELARLEQDIARLEerrRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 873 KSEFEKENqkgkaaildlektckELKHQLQVQMENTLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNEK 952
Cdd:COG1196 371 EAELAEAE---------------EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 953 EEQQLQGNINELKQSSEQKKKQIEALQGELKIAVLQKTELENKLQQQLTQAAQELAAEKEKISVLQNNYEKSQETFKQLQ 1032
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1033 SDFYGRESELLATRQDLKSVEEKL---SLAQEDLISNRNQIGNQNKLIQELKTAK---ATLEQDSAKKEQQLQERCKALQ 1106
Cdd:COG1196 516 LAGLRGLAGAVAVLIGVEAAYEAAleaALAAALQNIVVEDDEVAAAAIEYLKAAKagrATFLPLDKIRARAALAAALARG 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1107 DIQKEKSLKEKELVNEKSKLAEIEEIKcrQEKEITKLNEELKSHKLESIKEITNLKDAKQLLIQQKLELQGKADSLKAAV 1186
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTL--LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1187 EQEKRNQQILKDQVKKEEEELKKEFIEKEAKLHSEIKEKEVGMKKHEENEAKLTMQITALNENlgtvkkewqssQRRVSE 1266
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE-----------LLEELL 742
|
570 580 590
....*....|....*....|....*....|..
gi 1653960520 1267 LEKQTDDLRGEIAVLEATVQNNQDERRALLER 1298
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELERELERLER 774
|
|
| FYVE_FGD5 |
cd15742 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ... |
1355-1410 |
1.37e-12 |
|
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: 64.19 E-value: 1.37e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1653960520 1355 VQNCMACGKGFSVTVRRHHCRQCGNIFCAECSA-KNALTPSSKKPVRVCDACFNDLQ 1410
Cdd:cd15742 9 VMMCMNCGSDFTLTLRRHHCHACGKIVCRNCSRnKYPLKYLKDRPAKVCDGCFAELR 65
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
696-1355 |
1.48e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.78 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 696 KLQDKQEHCSQLESHLKEYKEKYLSLEQKTE------ELEGQIKKLEADSLevKASKEQALQDLQQQRQLNTDLELRATE 769
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKSLERQAEkaerykELKAELRELELALL--VLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 770 LSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLtkqeEEKKILKQDFETLSQETKIQHEELNNRIQTTVTELQKVKMEKE 849
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKEL----YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 850 ALMTELSTVKDKLskvsDSLKNSKSEFEKENQKGKAAILDLEKTCKELKHQLQvQMENTLKEQKELKKSLEKEKEASHQL 929
Cdd:TIGR02168 334 ELAEELAELEEKL----EELKEELESLEAELEELEAELEELESRLEELEEQLE-TLRSKVAQLELQIASLNNEIERLEAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 930 KLELNSMQEQLIQAQNTL--KQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKIAVLQKTELENKLQQQLTQAAqEL 1007
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELlkKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA-QL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1008 AAEKEKISVLQNNYEKSQETFKQL---QSDFYGreseLLATRQDLKSVEEKLSLAQE-DLISNRNQIGNQNKliQELKTA 1083
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEGVKALlknQSGLSG----ILGVLSELISVDEGYEAAIEaALGGRLQAVVVENL--NAAKKA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1084 KATLEQDSAKKEQQLQERCKALQDIQKEKSLKEKELVNEKSKLAEIEEIKCRQEKEITKLneelkshkLESIKEITNLKD 1163
Cdd:TIGR02168 562 IAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYL--------LGGVLVVDDLDN 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1164 AKQLLIQQKLE-----LQGKADSLKAAV--EQEKRNQQIL-KDQVKKEEEELKKEFIEKEAKLHSEIKEKEVGMKKHEEN 1235
Cdd:TIGR02168 634 ALELAKKLRPGyrivtLDGDLVRPGGVItgGSAKTNSSILeRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEE 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1236 EAKLTMQITALNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKVLE 1315
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1653960520 1316 LQRKLDNTTAAVQELGRENQSLQIKHTQALNRKWAEDNEV 1355
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
|
| FYVE_scVPS27p_Vac1p_like |
cd15736 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
1358-1406 |
1.79e-12 |
|
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: 63.36 E-value: 1.79e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1653960520 1358 CMACGKGFSVTVRRHHCRQCGNIFCAECSAKN------ALTPSSKKPVRVCDACF 1406
Cdd:cd15736 2 CHTCSRTFNLNIRAHHCRKCGKLFCRRHLPNMiplnlsAYDPRNGKWYRCCHSCF 56
|
|
| FYVE2_Vac1p_like |
cd15737 |
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ... |
1348-1405 |
2.06e-12 |
|
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: 64.06 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1348 KWAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCA----ECS--------------------AKNALTPSSKKPVRVCD 1403
Cdd:cd15737 1 PWEDDSSVTHCPICLRSFGLLLRKHHCRLCGKVVCDdrrtKCStevpldllssalpdlpfvfkEPQSDIPDDTKSVRVCR 80
|
..
gi 1653960520 1404 AC 1405
Cdd:cd15737 81 DC 82
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
629-1340 |
5.58e-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: 70.87 E-value: 5.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 629 QLNESKEKVSQLDIQIKAKTELL--LSAEAAKTAQRADLQNHLDTAQNALqdKQQELNKITTQLDQVTAKLQDKQEHCSQ 706
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLerLRREREKAERYQALLKEKREYEGYE--LLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 707 LESHLKEYKEKYLSLEQKTEELEGQIKKL-EADSLEVKASKEQALQDLQQQRQLNTDLELRATELSKQLEMEKEIVSSTR 785
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 786 LDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETkiqhEELNNRIQTTVTELQKVKMEKEALMTELSTVKDKLSKV 865
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL----EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 866 SDSLKNSKSEFEKENQKGKAAILDLEKTCKELKhQLQVQMENTLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQN 945
Cdd:TIGR02169 412 QEELQRLSEELADLNAAIAGIEAKINELEEEKE-DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 946 TLKQNEKEEQQLQ---------------------GNINELKQSSEQKKKQIEALQGELKIAVLQKTELENKL-------- 996
Cdd:TIGR02169 491 ELAEAEAQARASEervrggraveevlkasiqgvhGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKEaiellkrr 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 997 -----------QQQLTQAAQELAAEKEKISVLQNNYE---KSQETFKQLQSDFYGRESELLATRQDLK--------SVEE 1054
Cdd:TIGR02169 571 kagratflplnKMRDERRDLSILSEDGVIGFAVDLVEfdpKYEPAFKYVFGDTLVVEDIEAARRLMGKyrmvtlegELFE 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1055 KLSLAQEDLISNRNQIGNQNKL----------IQELKTAKATLEQDSAKKEQQLQERCKALQDIQKEKSLKEKelvneks 1124
Cdd:TIGR02169 651 KSGAMTGGSRAPRGGILFSRSEpaelqrlrerLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK------- 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1125 klaEIEEIKCRQEKEITKLnEELKSHKLESIKEITNLKDAKQLLIQQKLELQGKADSLKAAVEQEKRNQqilkdqvkkee 1204
Cdd:TIGR02169 724 ---EIEQLEQEEEKLKERL-EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL----------- 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1205 eelkkefiekeakLHSEIKEKEVGMKKHEENEAKLTMQITALNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEAT 1284
Cdd:TIGR02169 789 -------------SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1653960520 1285 VQNNQDERRALLERCLKGEGEIEKLQTKVLELQRKLDNTTAAVQELGRENQSLQIK 1340
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
221-1023 |
5.97e-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: 70.87 E-value: 5.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 221 EDVAVLKKELVQVQTLMDNM-----TLERERE---------SEKLKDECKKLQSQYASSEATISQLRSELAKGPQEVAVY 286
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKrqqleRLRREREkaeryqallKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 287 VQELQKLKSSVNELTQKNQTLTENLLKK-EQDYTKLEEKHNEESVSKKNIQATLHQKDLDCQQLQSRLSASETSLHRIHV 365
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 366 ELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQLGEahgrlkeqrqlss 445
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE------------- 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 446 eklmdkeqqvadLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKI 525
Cdd:TIGR02169 404 ------------LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 526 QNLEALLQKSKENISLLEKEREDLYAKIQAGE----GETAVLNQLQEKNHTLQEQVTQLTE---------------KLKN 586
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQARASEervrGGRAVEEVLKASIQGVHGTVAQLGSvgeryataievaagnRLNN 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 587 ----QSESHKQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLN--------------------------ESKEK 636
Cdd:TIGR02169 552 vvveDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGfavdlvefdpkyepafkyvfgdtlvvEDIEA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 637 VSQLDIQIKAKT---ELLLSAEAAKTAQRADLQNHLDTAQnaLQDKQQELNKITTQLDQVTAKLQDKQEHcsqLESHLKE 713
Cdd:TIGR02169 632 ARRLMGKYRMVTlegELFEKSGAMTGGSRAPRGGILFSRS--EPAELQRLRERLEGLKRELSSLQSELRR---IENRLDE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 714 YKEKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLELRATELSKQLEmekeivsSTRLDLQKKSE 793
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE-------ELEEDLHKLEE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 794 ALESIKQKLTK---QEEEKKILKQDFETLSQETKIQH-EELNNRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDSL 869
Cdd:TIGR02169 780 ALNDLEARLSHsriPEIQAELSKLEEEVSRIEARLREiEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 870 KNSKSEFEKENQKGKAAILDLEKTCKELKHQ---LQVQMENTLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNT 946
Cdd:TIGR02169 860 NGKKEELEEELEELEAALRDLESRLGDLKKErdeLEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP 939
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1653960520 947 LKQnEKEEQQLQGNINELKQSSEQKKKQIEALqGELKIAVLQKTELENKLQQQLTQAAQELAAEKEKISVLQNNYEK 1023
Cdd:TIGR02169 940 KGE-DEEIPEEELSLEDVQAELQRVEEEIRAL-EPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| FYVE_WDFY1_like |
cd15718 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ... |
1349-1406 |
7.70e-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: 61.95 E-value: 7.70e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1653960520 1349 WAEDNevqNCMACGKGF-----------SVTVRRHHCRQCGNIFCAECSAKNALTPSS--KKPVRVCDACF 1406
Cdd:cd15718 3 WAESD---NCQKCSRPFfwnfkqmwekkTLGVRQHHCRKCGKAVCDKCSSNRSTIPVMgfEFPVRVCNECY 70
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
366-1248 |
1.14e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 70.00 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 366 ELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQLSS 445
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 446 EKLMDKEQQVADLQLKLSRLEEQLKEkvtNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKI 525
Cdd:pfam02463 257 KQEIEKEEEKLAQVLKENKEEEKEKK---LQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 526 QNLEALLQKSKEnisLLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQENLHDQVQEQ 605
Cdd:pfam02463 334 KEEIEELEKELK---ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 606 KAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNK 685
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLL 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 686 ITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIkkleADSLEVKASKEQALQDLQQQRQLNTDLEL 765
Cdd:pfam02463 491 SRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVA----VENYKVAISTAVIVEVSATADEVEERQKL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 766 RATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETKIQHEELnnriqttvTELQKVK 845
Cdd:pfam02463 567 VRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKD--------TELTKLK 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 846 MEKEALMTELSTVKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKTCKELKHQLQVQMENTLKEQKELKKSLEKEKEA 925
Cdd:pfam02463 639 ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 926 SHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKIAVLQKTELENKLQQQLTQAAQ 1005
Cdd:pfam02463 719 AEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKA 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1006 ELAAEKEKISVLQNNYEKSQETFKQLQSDFYGRESELLATRQDLKSVEEKLSLAQEDLISNRNQIGNQNKLIQELKTAKA 1085
Cdd:pfam02463 799 QEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEE 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1086 TLEQDSAKKEQQLQERCKALQDIQKEKSLKEKELVNEKSKLAE-IEEIKCRQEKEITKLNEELKSHKLESIKEITNLKDA 1164
Cdd:pfam02463 879 LEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEErIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEE 958
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1165 KQLLIQQKLELQGKADSLKAAVEQEKRNQQILKDQVKKEEEELKKEFIEKEAKLHSEIKEKEVGMKKHEENEAKLTMQIT 1244
Cdd:pfam02463 959 EERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFF 1038
|
....
gi 1653960520 1245 ALNE 1248
Cdd:pfam02463 1039 YLEL 1042
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
77-737 |
2.84e-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: 68.54 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 77 NLALKRDDVTLLRQEVQDLQASLKEEKWYSEELKKELEKYQ-----------GLQQQEAKPDGLVTDSSAELQSLEQQLE 145
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqletlrskvaQLELQIASLNNEIERLEARLERLEDRRE 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 146 EAQTEnfNIKQMKDLFEQKAAQLATEIADIKSKYDEERSLREAAEQKVTRLTEELNKEATVIQDLKTELlqrpgiedvav 225
Cdd:TIGR02168 418 RLQQE--IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL----------- 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 226 lkKELVQVQTLMDNMTLERERESEKLKdECKKLQSQYASSEATISQLRS---------ELAKGPQEVAVYVQELQKLKSS 296
Cdd:TIGR02168 485 --AQLQARLDSLERLQENLEGFSEGVK-ALLKNQSGLSGILGVLSELISvdegyeaaiEAALGGRLQAVVVENLNAAKKA 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 297 VNELTQKNQTLTENLLKKEQDYTKLEEKHNEESVSKKNIQATLhqkdLDCQQLQSRLSAS-ETSLHRIHV--ELSEKGEA 373
Cdd:TIGR02168 562 IAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVA----KDLVKFDPKLRKAlSYLLGGVLVvdDLDNALEL 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 374 TQKLKEELSEVETKYQHLKAEFKQLqQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQLSSE---KLMD 450
Cdd:TIGR02168 638 AKKLRPGYRIVTLDGDLVRPGGVIT-GGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEEleeELEQ 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 451 KEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEA 530
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 531 LLQKSKENISLLEKEredlyakiqagegetavLNQLQEKNHTLQEQVtqltEKLKNQSESHKQAQENLHDQVQEQKAHLR 610
Cdd:TIGR02168 797 ELKALREALDELRAE-----------------LTLLNEEAANLRERL----ESLERRIAATERRLEDLEEQIEELSEDIE 855
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 611 AAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIkaktELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNKITTQL 690
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEALLNERASLEEAL----ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1653960520 691 DQVTAKLQDKQEHCSQLES-HLKEYKEKYLSLEQKTEELEGQIKKLEA 737
Cdd:TIGR02168 932 EGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
625-1297 |
3.79e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 625 ELNSQLNESKEKVSQLDIQ-IKAKTELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEH 703
Cdd:COG1196 217 ELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 704 CSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASKEqalqdlqqqrqlntdlelratELSKQLEMEKEIVSS 783
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE---------------------ELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 784 TRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETkiqhEELNNRIQTTVTELQKVKMEKEALMTELStvkdkls 863
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA----AELAAQLEELEEAEEALLERLERLEEELE------- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 864 kvsdslknsksefekenqkgkaaildlektckelkhQLQVQMENTLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQA 943
Cdd:COG1196 425 ------------------------------------ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 944 QNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKIAVLQKTELENKLQQQL------TQAAQELAAEKEKISVL 1017
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvavligVEAAYEAALEAALAAAL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1018 QNNYEKSQETFKQ----LQSDFYGRESELLATRQdlkSVEEKLSLAQEDLISNRNQIGNQNKLIQELktAKATLEQDSAK 1093
Cdd:COG1196 549 QNIVVEDDEVAAAaieyLKAAKAGRATFLPLDKI---RARAALAAALARGAIGAAVDLVASDLREAD--ARYYVLGDTLL 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1094 KEQQLQERCKALQDIQKEKSLKEKELVNEKSKLAEIEEIKCRQEKEITKLNEELKSHKLESIKEITNLKDAKQLLIQQKL 1173
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1174 ELQGKADSLKAAVEQEKRNQQILKDQVKKEEEELKKEFIEKEAKLHSEIKEKEVGMKKHEENEAKLTmQITALNENLGTV 1253
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE-RLEREIEALGPV 782
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1653960520 1254 ----KKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQN-NQDERRALLE 1297
Cdd:COG1196 783 nllaIEEYEELEERYDFLSEQREDLEEARETLEEAIEEiDRETRERFLE 831
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
380-995 |
4.05e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 67.74 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 380 ELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQ----------LSSEKLM 449
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDkinklnsdlsKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 450 DKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLE 529
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 530 ALLQKSKENISLLEKeredlyaKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQENLHDQVQEQKAHL 609
Cdd:TIGR04523 194 NKLLKLELLLSNLKK-------KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 610 RAAQDRVLSLETS---VNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAK----------------------TAQRAD 664
Cdd:TIGR04523 267 KQLSEKQKELEQNnkkIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNqekkleeiqnqisqnnkiisqlNEQISQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 665 LQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKA 744
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 745 SKEQALQDLQQQRQLNTDLELRATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETK 824
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 825 iqheELNNRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDSLKNSKSEFEKENQKGKaaILDLEKTCKELKHQlqvq 904
Cdd:TIGR04523 507 ----ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE--IDEKNKEIEELKQT---- 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 905 MENTLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKI 984
Cdd:TIGR04523 577 QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
650
....*....|.
gi 1653960520 985 AVLQKTELENK 995
Cdd:TIGR04523 657 IRNKWPEIIKK 667
|
|
| FYVE_RUFY4 |
cd15745 |
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ... |
1358-1406 |
1.81e-10 |
|
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: 57.51 E-value: 1.81e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1653960520 1358 CMACGKGFSVTVRRHHCRQCGNIFCAECSAKNAL--TPSSKKPVRVCDACF 1406
Cdd:cd15745 2 CAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVlsVPDTCIYLRVCKTCY 52
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
713-1270 |
2.26e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 713 EYKEKYLSLEQKTEElegqiKKLEADSLEVKASKEQALQDLQQQRQLNTDLELRATELSKQLEMEKEIVSSTRLD-LQKK 791
Cdd:PTZ00121 1312 EEAKKADEAKKKAEE-----AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaAKKK 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 792 SEALESIKQKLTKQEEEKKilKQDFETLSQETKIQHEELNNRIQttvtelQKVKMEKEALMTELSTVKDKLSKVSDSLKN 871
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKK--KADELKKAAAAKKKADEAKKKAE------EKKKADEAKKKAEEAKKADEAKKKAEEAKK 1458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 872 SKSEFEKENQKGKAAILDLEKTCKELKHQLQVQMENTLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNE 951
Cdd:PTZ00121 1459 AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 952 KEEQQLQGNINELKQSSEQKKKQiealqgELKIAVLQKTELENKLQQQLTQAAQELAAEKEKISVLQNNYEKSQETFKQL 1031
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAE------EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1032 QsdfygRESELLATRQDLKSVEEKLSLAQEDLISNRNQIGNQNKLIQELKTAKATLEQDsAKKEQQLQERCKALQDIQKE 1111
Cdd:PTZ00121 1613 K-----KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE-AKKAEEDKKKAEEAKKAEED 1686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1112 KSLKEKELVNEKSKLAEIEEIKCRQEKEITKLNEELKSHKLESIKEITNLKDA---KQLLIQQKLELQGKADSLKAAVEQ 1188
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAeedKKKAEEAKKDEEEKKKIAHLKKEE 1766
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1189 EKRNQQILKDQVKKEEEELKKEFIEKEAKLHSEIKEKEVGMKKHEENEAKLTMQITALNENLGTVKKEWQSSQRRVSELE 1268
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEA 1846
|
..
gi 1653960520 1269 KQ 1270
Cdd:PTZ00121 1847 DA 1848
|
|
| FYVE_FGD3 |
cd15740 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ... |
1352-1406 |
3.62e-10 |
|
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar proteins; FGD3, also termed zinc finger FYVE domain-containing protein 5, is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) that undergoes the ubiquitin ligase SCFFWD1/beta-TrCP-mediated proteasomal degradation. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Due to this difference, FGD3 may play different roles from that of FGD1 to regulate cell morphology or motility. The FYVE domain of FGD3 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.
Pssm-ID: 277279 [Multi-domain] Cd Length: 54 Bit Score: 56.93 E-value: 3.62e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1653960520 1352 DNEVQNCMACGKGF-SVTVRRHHCRQCGNIFCAECSaknALTPSSKKPVRVCDACF 1406
Cdd:cd15740 2 EKEKQTCKGCNESFnSITKRRHHCKQCGAVICGKCS---EFKDLASRHNRVCRDCF 54
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
182-994 |
5.15e-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: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 182 ERSLREAAEQkVTRLTEELNKEATVIQDLKTELLQrpgieDVAVLKKELVQVQTLMDNMTLERERESEKLKDECKKLQSQ 261
Cdd:pfam15921 77 ERVLEEYSHQ-VKDLQRRLNESNELHEKQKFYLRQ-----SVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 262 YASSEATISqLRSELAKgpqEVAVYVQELQKLKSSVNELTQKNQTLTENLlkKEQDYTKLEEKHNEESVSKKN----IQA 337
Cdd:pfam15921 151 VHELEAAKC-LKEDMLE---DSNTQIEQLRKMMLSHEGVLQEIRSILVDF--EEASGKKIYEHDSMSTMHFRSlgsaISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 338 TLHQKDLDCQQLQSRLSASETSLH-------------------RIHVELSEKGEATQKLKEELSEVETKYQHLKAEFKQL 398
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQLEalksesqnkielllqqhqdRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 399 QQQREEKE----QHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQLSSEKLMDKEQQVADLQLKLSRLEEQLKEKVT 474
Cdd:pfam15921 305 QEQARNQNsmymRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 475 NSTELQHQLDKTKQQHQEQQALQQSTTAKlreaqndLEQVLRQIGDKDQKIQNLEALLQKSKeniSLLEKEREDLYAKIQ 554
Cdd:pfam15921 385 DLHKREKELSLEKEQNKRLWDRDTGNSIT-------IDHLRRELDDRNMEVQRLEALLKAMK---SECQGQMERQMAAIQ 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 555 AgegetavlnqlqeKNHTLqEQVTQLTEKLknqsESHKQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESK 634
Cdd:pfam15921 455 G-------------KNESL-EKVSSLTAQL----ESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATN 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 635 EKVSQLDIQIKAKTELLlsaeaaktaqradlqNHLDTAQNALQDKQQELNKITTQL---DQVTAKLQDKQEHCSQLeshL 711
Cdd:pfam15921 517 AEITKLRSRVDLKLQEL---------------QHLKNEGDHLRNVQTECEALKLQMaekDKVIEILRQQIENMTQL---V 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 712 KEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLELRATELSKqlemekeiVSSTRLdlqkk 791
Cdd:pfam15921 579 GQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVN--------AGSERL----- 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 792 sEALESIKQKLTKQEEEKKILKQDFETLSQETKIQHEELNNRIQTTVTELQKVKMEKEALMTELstvkdklskvsDSLKN 871
Cdd:pfam15921 646 -RAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSEL-----------EQTRN 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 872 SKSEFEKENQKGKAAILDLEKTCKELKHQLQVqMENTLKEQKELKKSLEKEKeasHQLKLELNSMQEQLIQAQNtlkqne 951
Cdd:pfam15921 714 TLKSMEGSDGHAMKVAMGMQKQITAKRGQIDA-LQSKIQFLEEAMTNANKEK---HFLKEEKNKLSQELSTVAT------ 783
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 1653960520 952 kEEQQLQGNINELKQSSEQKKKQIEALQGELKIAVLQKTELEN 994
Cdd:pfam15921 784 -EKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQD 825
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
226-709 |
1.07e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.14 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 226 LKKELVQVQTLMDNMTLERERESEKLKD------ECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLKSSVNE 299
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEadevleEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 300 LTQKNQTLTENLLKKEQDYTKLEEKHNEESVSKKNIQATLHQKDLDCQ--------------QLQSRLSASETSLHRIHV 365
Cdd:PRK02224 291 LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQahneeaeslredadDLEERAEELREEAAELES 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 366 ELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQLSS 445
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 446 E-----------------KLMDKEQQVADLQLKLSRLEEQLkEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQ 508
Cdd:PRK02224 451 AgkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEV-EEVEERLERAEDLVEAEDRIERLEERREDLEELIAERR 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 509 NDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEkLKNQS 588
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEI 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 589 ESHKQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNElnSQLNESKEKVSQLDIQIKAKTELLlsaeAAKTAQRADLQNH 668
Cdd:PRK02224 609 ERLREKREALAELNDERRERLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKL----DELREERDDLQAE 682
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1653960520 669 LDTAQNALqDKQQELNKITTQLDQVTAKLQDKQEHCSQLES 709
Cdd:PRK02224 683 IGAVENEL-EELEELRERREALENRVEALEALYDEAEELES 722
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
955-1257 |
1.61e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 955 QQLQGNINELKQSSEQKKK------QIEALQGELKIAVLQKTELEnklqqqLTQAAQELAAEKEKISVLQNNYEKSQETF 1028
Cdd:COG1196 196 GELERQLEPLERQAEKAERyrelkeELKELEAELLLLKLRELEAE------LEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1029 KQLQSDFYGRESELLATRQDLKSVEEKLSLAQEDLISNRNQIGNQNKLIQELKTAKATLEQDSAKKEQQLQERCKALQDI 1108
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1109 QKEKSLKEKELVNEKSKLAEIEeikcRQEKEITKLNEELKSHKLESIKEITNLKDAKQLLIQQKLELQGKADSLKAAVEQ 1188
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAE----AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1653960520 1189 EKRNQQILKDQVKKEEEELKKEFIEKEAKLHSEIKEKEVGMKKHEENEAKLTMQITALNENLGTVKKEW 1257
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| FYVE_protrudin |
cd15723 |
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ... |
1357-1405 |
2.01e-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: 54.81 E-value: 2.01e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1653960520 1357 NCMACGKGFSV-TVRRHHCRQCGNIFCAEC-------SAKNALTPSSKK-PVRVCDAC 1405
Cdd:cd15723 1 NCTGCGASFSVlLKKRRSCNNCGNAFCSRCcskkvprSVMGATAPAAQReTVFVCSGC 58
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
372-589 |
3.47e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 372 EATQKLKEELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKE---QRQLSSEKL 448
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 449 MDKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNL 528
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1653960520 529 EALLQKSKENISLLEKEREDLYAKIQAGEGETAV-LNQLQEKNHTLQEQVTQLTEKLKNQSE 589
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAeLAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
435-1043 |
3.50e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 435 GRLKEQRQLSSEKLMDKEQQVADLQLKLSRLEEQLKEKVtnSTELQHQLDKTKQQHQEQQALQQSTTAK---LREAQNDL 511
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKE--EKDLHERLNGLESELAELDEEIERYEEQreqARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 512 EQVLRQIGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQagEGETAVLNQLQEKNHTLQEqvtqlteklknqSESH 591
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVR--DLRERLEELEEERDDLLAE------------AGLD 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 592 KQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTAQRADlqnhLDT 671
Cdd:PRK02224 306 DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREA----VED 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 672 AQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQ 751
Cdd:PRK02224 382 RREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPV 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 752 DLQQQRQLNTDLELRATELSKQLEMEKEivssTRLDLQKKSEALESikqkLTKQEEEKKILKQDFETLSQETKIQHEELN 831
Cdd:PRK02224 462 EGSPHVETIEEDRERVEELEAELEDLEE----EVEEVEERLERAED----LVEAEDRIERLEERREDLEELIAERRETIE 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 832 NRiQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEK---------TCKELKHQLQ 902
Cdd:PRK02224 534 EK-RERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaaiaDAEDEIERLR 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 903 VQMENTLKEQKELKKSLEKEKEASHQLKLELNsmQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGEL 982
Cdd:PRK02224 613 EKREALAELNDERRERLAEKRERKRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL 690
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1653960520 983 KiavlqktELENklqqqLTQAAQELAAEKEKISVLQNNYEKSQETFKQLQSDFYGRESELL 1043
Cdd:PRK02224 691 E-------ELEE-----LRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETL 739
|
|
| FYVE_ZFY19 |
cd15749 |
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ... |
1357-1406 |
4.45e-09 |
|
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ZFY19, also termed mixed lineage leukemia (MLL) partner containing FYVE domain, is encoded by a novel gene, MLL partner containing FYVE domain (MPFYVE). The FYVE domain of ZFY19 resembles FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. The biological function of ZFY19 remains unclear.
Pssm-ID: 277288 [Multi-domain] Cd Length: 51 Bit Score: 53.66 E-value: 4.45e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1653960520 1357 NCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPS-SKKPVRVCDACF 1406
Cdd:cd15749 1 RCFGCAAKFSLFKKECGCKNCGRSFCKGCLTFSAVVPRkGNQKQKVCKQCH 51
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
465-1151 |
4.89e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.89 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 465 LEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEK 544
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 545 EREDL-YAKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDRVLSLETSV 623
Cdd:pfam05483 177 EREETrQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKM 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 624 NELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAK---TAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDK 700
Cdd:pfam05483 257 KDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKdhlTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQ 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 701 QEHCSQLESH----LKEYKEKYLSLEQ--KTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLELratELSKQL 774
Cdd:pfam05483 337 MEELNKAKAAhsfvVTEFEATTCSLEEllRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL---EELKKI 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 775 EMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETKIQHEELNNRIQTTVTELQKVKMEKealmTE 854
Cdd:pfam05483 414 LAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKN----IE 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 855 LSTVKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKTCKELKHQLQVQMENTLKEQKELKKSLEKEKEASHQLKLELN 934
Cdd:pfam05483 490 LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLD 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 935 SMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKiAVLQKTELENKL----QQQLTQAAQELAAE 1010
Cdd:pfam05483 570 KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENK-ALKKKGSAENKQlnayEIKVNKLELELASA 648
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1011 KEKISVLQNNYEKSQETFKQLQSDFYGRESELLATRQDLKSVEEKLSLAQEDLISNRNQIGNQNKLIQELKTAKATLEQD 1090
Cdd:pfam05483 649 KQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELG 728
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1653960520 1091 SAKKEQQLQERCKAlqDIQKEKSLKEKELVNEKSKLAEIEEIKCRQEKEITKLNEELKSHK 1151
Cdd:pfam05483 729 LYKNKEQEQSSAKA--ALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
75-580 |
6.03e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 75 ESNLALKRDDVTLLRQEVQDLQASLKEEKWYSEELKKELEKYQG----LQQQEAKPDGLVTDSSAELQSLEQQLEEAQTE 150
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAeeyeLLAELARLEQDIARLEERRRELEERLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 151 NFNIKQMKDLFEQKAAQLATEIADIKSKYDEERSLREAAEQKVTRLTEELNKEATVIQDLKTELLQRpgIEDVAVLKKEL 230
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA--LRAAAELAAQL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 231 VQVQTLMDNMTLERER-----------------ESEKLKDECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKL 293
Cdd:COG1196 403 EELEEAEEALLERLERleeeleeleealaeleeEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 294 KSSVNELTQKNQTLTENLLKKEQDYTKLEEKHNEESVSKKNIQATLHQKDLDCQQLQSRLSASETSLHRIHVELSEKGEA 373
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAA 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 374 TQKLKEELSEVETKYQHLKAEFKQLQQQREEKEQHG---------LQLQSEINQLHSKLLETERQLGEAHGRLKEQRQLS 444
Cdd:COG1196 563 IEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGaavdlvasdLREADARYYVLGDTLLGRTLVAARLEAALRRAVTL 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 445 SEKLMDKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDL-EQVLRQIGDKDQ 523
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELaEAEEERLEEELE 722
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1653960520 524 KIQNLEALLQKSKENISLLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQL 580
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
696-1274 |
6.45e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 696 KLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKaskeqalqdlQQQRQLNTDLELRATELSKqLE 775
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVL----------REINEISSELPELREELEK-LE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 776 MEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFEtlsqETKIQHEELNNRIQTtVTELQKVKMEKEALMTEL 855
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE----ELKKEIEELEEKVKE-LKELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 856 STVKDKLSKVSDSLKNSKSEFE------KENQKGKAAILDLEKTCKELKHQLQVQMENTLKEQKELKKSLEKEKEASHQL 929
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINgieeriKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 930 KLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKIAVLQKTEL-ENKLQQQLTQAAQELA 1008
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELtEEHRKELLEEYTAELK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1009 AEKEKISVLQNNYEKSQETFKQLQSdFYGRESELLATRQ---DLKSVEEKLSlaqedlISNRNQIGNQNKLIQELKTAKA 1085
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKElaeQLKELEEKLK------KYNLEELEKKAEEYEKLKEKLI 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1086 TLEqdsaKKEQQLQERCKALQDIQKEKSLKEKELVNEKSKLAEIE-EIKCRQEKEITKLNEELKShkLESI-KEITNLKD 1163
Cdd:PRK03918 536 KLK----GEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLkELEELGFESVEELEERLKE--LEPFyNEYLELKD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1164 AKQLLIQQKLELQGKADSLKAA---VEQEKRNQQILKDQVKKEEEELKKEFIEKEAKLHSEIKEKEVGMKKHEENEAKLT 1240
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAfeeLAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRR 689
|
570 580 590
....*....|....*....|....*....|....
gi 1653960520 1241 MQITALNENLGTVKKEWQSSQRRVSELEKQTDDL 1274
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKKELEKLEKALERV 723
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
764-1357 |
6.57e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.93 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 764 ELRATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETKIQHEELNNRIQTTVTELQK 843
Cdd:PTZ00121 1198 DARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA 1277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 844 VKMEkealmtELSTVKDKlsKVSDSLKNSKSEFEKENQKGKAailDLEKTCKELKHQlqvqMENTLKEQKELKKSLEKEK 923
Cdd:PTZ00121 1278 RKAD------ELKKAEEK--KKADEAKKAEEKKKADEAKKKA---EEAKKADEAKKK----AEEAKKKADAAKKKAEEAK 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 924 EASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQgelKIAVLQKTELENKLQQQLTQA 1003
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK---KAEEDKKKADELKKAAAAKKK 1419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1004 AQELAAEKEKISVLQNNYEKSQETFKQLQSDFYGRES----ELLATRQDLKSVEEKLSLAQEDLISN--RNQIGNQNKLI 1077
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkaeEAKKKAEEAKKADEAKKKAEEAKKADeaKKKAEEAKKKA 1499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1078 QEL-KTAKATLEQDSAKK--EQQLQERCKALQDIQKEKSLKEKELVNEKSKLAEIEEIKCRQEKEITKLNEELKSHKLES 1154
Cdd:PTZ00121 1500 DEAkKAAEAKKKADEAKKaeEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1155 IKEITNLKDAKQLLIQQKLELQGKADSLKAAVEQEKRNQQILKDQVKKEEEELKKEFIEKEaKLHSEIKEKEVGMKKHEE 1234
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK-KEAEEKKKAEELKKAEEE 1658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1235 NEAKLTMQitalnenlgtvKKEWQSSQRRVSELEKQTDDLRGEiavlEATVQNNQDERRALLERCLKGEGEIEKLQtkvl 1314
Cdd:PTZ00121 1659 NKIKAAEE-----------AKKAEEDKKKAEEAKKAEEDEKKA----AEALKKEAEEAKKAEELKKKEAEEKKKAE---- 1719
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1653960520 1315 ELQRKLDNTTAAVQELGRENQSlQIKHTQALNRKWAEDNEVQN 1357
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEE-DKKKAEEAKKDEEEKKKIAH 1761
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
896-1128 |
7.20e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 7.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 896 ELKHQLQVQMENTLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQI 975
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 976 EALQGELK--IAVLQKTELENKLQQQLTQAAQELAAekekisvlqnnyeKSQETFKQLQSDFYGRESELLATRQDLKSVE 1053
Cdd:COG4942 100 EAQKEELAelLRALYRLGRQPPLALLLSPEDFLDAV-------------RRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1653960520 1054 EKLSLAQEDLISNRNQIGNQNKLIQELKTAKATLEQDSAKKEQQLQERCKALQDIQKEKSLKEKELVNEKSKLAE 1128
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
108-465 |
1.43e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 108 ELKKELEKYQGLQQQEAKPDGLVTDSSAELQSLEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEERSLRE 187
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 188 AAEQKVTRLTEELNKEATVIQdlktellqrpgiedvavlkkelvqvqtlmdnmtlERERESEKLKDECKKLQSQYASSEA 267
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELA----------------------------------EAEAEIEELEAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 268 TISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQKNQTLTENLLKKEQDYTKLEEKHNEESVSKKNIQATLhqkdldcQ 347
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-------E 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 348 QLQSRLSASETSLHRIHVELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEkeqhglqLQSEINQLHSKLLETE 427
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG-------LEVRIDNLQERLSEEY 949
|
330 340 350
....*....|....*....|....*....|....*...
gi 1653960520 428 RQLGEAHGRLKEQRQLSSEKLmdkEQQVADLQLKLSRL 465
Cdd:TIGR02168 950 SLTLEEAEALENKIEDDEEEA---RRRLKRLENKIKEL 984
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
928-1156 |
1.48e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 928 QLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKIAVLQKTELENKLQQQLTQAAQEL 1007
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1008 AAEKEKISVLQNNYEKSQETFKQLQSDFYGRESELLATRQDLKSVEEKLSLAQEDLISNRNQIGNQNKLIQELKTAKATL 1087
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1653960520 1088 EQDSAKKEQQLQERCKALQDIQKEKSLKEKELVNEKSKLAEIEEIKCRQEKEITKLNEELKSHKLESIK 1156
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
771-1333 |
1.74e-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: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 771 SKQLEMEKEIvSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETKiqheELNNRIQTTVTELQKVKMEKEA 850
Cdd:TIGR04523 33 TEEKQLEKKL-KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIK----DLNDKLKKNKDKINKLNSDLSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 851 LMTELSTVKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKTCKELKhQLQVQMENTLKEQKELKKSLEKEKEASHQLK 930
Cdd:TIGR04523 108 INSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELE-KLNNKYNDLKKQKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 931 LELNSMQEQLIQAQNTL---KQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKiavlQKTELENKLQQQLTQAAQEL 1007
Cdd:TIGR04523 187 KNIDKIKNKLLKLELLLsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEIN----EKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1008 AAEKEKISVLQNNYEKSQETFKQLQSDFYGRESELLATRQ------------DLKSVEEKLSLAQEDLISNRNQIGNQNK 1075
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkeqdwnkelksELKNQEKKLEEIQNQISQNNKIISQLNE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1076 LIQELKTAKATLEQDSAKKEQQLQERCKALQDIQKEKSLKEKELVNEKSKLAEIEEIKCRQEKEITKLNEELK---SHKL 1152
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKklqQEKE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1153 ESIKEITNLKDAKQLLIQQKLELQGKADSLKAAVEQEKRNQQILKDQVKKEEEELKKEFIEKEaKLHSEIKEKEVGMKKH 1232
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLE-QKQKELKSKEKELKKL 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1233 EENEAKLTMQITALNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQ--DERRALLERCLKGEGEIEKLQ 1310
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQKSLK 581
|
570 580
....*....|....*....|...
gi 1653960520 1311 TKVLELQRKLDNTTAAVQELGRE 1333
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKE 604
|
|
| FYVE_RUFY3 |
cd15744 |
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ... |
1358-1406 |
3.18e-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: 51.26 E-value: 3.18e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1653960520 1358 CMACGK-GFSVTVRRHHCRQCGNIFCAECSAKNALTPSS-KKPVRVCDACF 1406
Cdd:cd15744 2 CSLCQEdFASLALPKHNCYNCGGTFCDACSSNELPLPSSiYEPARVCDVCY 52
|
|
| FYVE_WDFY1 |
cd15756 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ... |
1348-1410 |
4.21e-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: 51.61 E-value: 4.21e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1653960520 1348 KWAEDNevqNCMACGKGF-----------SVTVRRHHCRQCGNIFCAECSAKNALTP--SSKKPVRVCDACFNDLQ 1410
Cdd:cd15756 2 QWLESD---SCQKCEQPFfwnikqmwdtkTLGLRQHHCRKCGQAVCGKCSSKRSSYPimGFEFQVRVCDSCFETIK 74
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1053-1347 |
4.42e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1053 EEKLSLAQEDLisNRNQIgnqnkLIQELKTAKATLEQDSAK-----------KEQQLQERCKALQDIQKEKSLKEKELVN 1121
Cdd:COG1196 178 ERKLEATEENL--ERLED-----ILGELERQLEPLERQAEKaeryrelkeelKELEAELLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1122 EKSKLAEIEEikcrQEKEITKLNEELKSHKLESIKEITNLKDAKQLLIQQKLELQGKADSLKAAVEQEKRNQQILKDQvk 1201
Cdd:COG1196 251 LEAELEELEA----ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE-- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1202 keeeelKKEFIEKEAKLHSEIKEKEVGMKKHEENEAKLTMQITALNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVL 1281
Cdd:COG1196 325 ------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1653960520 1282 EATVQNNQDERRALLERCLKGEGEIEKLQTKVLELQRKLDNTTAAVQELGRENQSLQIKHTQALNR 1347
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
251-1128 |
4.47e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.13 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 251 LKDECKKLQSQYASSEATISQLRSELakgpQEVAVYVQELQKLKSSVNELTQKNQTLTENLLKKEQDYTKLEEKHneesv 330
Cdd:TIGR00606 222 IRDQITSKEAQLESSREIVKSYENEL----DPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKM----- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 331 sKKNIQATLHQKDLDCQQLQSRLSASETSLHRIHVELSEKGEATQKLKEELSE--VETKYQHLKAEFKQLQQQREEKEQH 408
Cdd:TIGR00606 293 -EKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTEllVEQGRLQLQADRHQEHIRARDSLIQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 409 GLQLQSEINQLHSKLlETERQLGEAHgRLKEQRQLSSEKLMDkeQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQ 488
Cdd:TIGR00606 372 SLATRLELDGFERGP-FSERQIKNFH-TLVIERQEDEAKTAA--QLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 489 QHQEQQALQQSTTAKLREAQNDLEQVLRqigdKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGE---GETAVLNQ 565
Cdd:TIGR00606 448 ILEKKQEELKFVIKELQQLEGSSDRILE----LDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADldrKLRKLDQE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 566 LQEKNH--TLQEQVTQLTEKLKNQSESHKQAQENLHDQVQEQKAH----------LRAAQDRVLSLETSVNELNSQLNES 633
Cdd:TIGR00606 524 MEQLNHhtTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfpnkkqledwLHSKSKEINQTRDRLAKLNKELASL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 634 KEKVSQLDIQIKAKTELLLSAE------AAKTAQRADLQNHLDTAQNALQDKQQeLNKITTQLDQVTAKLQDKQEHC--- 704
Cdd:TIGR00606 604 EQNKNHINNELESKEEQLSSYEdklfdvCGSQDEESDLERLKEEIEKSSKQRAM-LAGATAVYSQFITQLTDENQSCcpv 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 705 --------SQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLELRATELSKQLEM 776
Cdd:TIGR00606 683 cqrvfqteAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQR 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 777 EKEivsstrlDLQKKSEALESIKQKltkqEEEKKILKQDFeTLSQETKIQHEELNNRIQTTVTELQKVKMEKEalMTELS 856
Cdd:TIGR00606 763 LKN-------DIEEQETLLGTIMPE----EESAKVCLTDV-TIMERFQMELKDVERKIAQQAAKLQGSDLDRT--VQQVN 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 857 TVKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKTCKELKHQlQVQMENTLKEQKELKKSLEKEKEASHQLKLELNSM 936
Cdd:TIGR00606 829 QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE-KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 937 QEQLIQAQNTLKQNEKEEQQLqgnINELKQSSEQKKKQIEALQGELKIAVLQKTELENKLQQQLTQAAQELAAEKEKISV 1016
Cdd:TIGR00606 908 KEQDSPLETFLEKDQQEKEEL---ISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNA 984
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1017 LQNNYEKSQETFKQ-------------LQSDFYGRESELLATRQDLKSVEEklSLAQEDLISNRNQIGNQNKLIQELKTA 1083
Cdd:TIGR00606 985 QLEECEKHQEKINEdmrlmrqdidtqkIQERWLQDNLTLRKRENELKEVEE--ELKQHLKEMGQMQVLQMKQEHQKLEEN 1062
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 1653960520 1084 KATLEQDSAKKEQQLQERCKalQDIQKEKSLKEKELVNEKSKLAE 1128
Cdd:TIGR00606 1063 IDLIKRNHVLALGRQKGYEK--EIKHFKKELREPQFRDAEEKYRE 1105
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
499-738 |
4.64e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 499 STTAKLREAQNDLEQVlrqigdkDQKIQNLEALLQKSKENISLLEKEREDLYAKIqagegetavlNQLQEKNHTLQEQVT 578
Cdd:COG4942 17 AQADAAAEAEAELEQL-------QQEIAELEKELAALKKEEKALLKQLAALERRI----------AALARRIRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 579 QLTEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQdrVLSLETSVNELNSQlnESKEKVSQLDIQIKAKTELLLSAEAAK 658
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAELLRALY--RLGRQPPLALLLSP--EDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 659 TAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEAD 738
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
247-737 |
5.69e-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: 57.34 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 247 ESEKLKDECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLKssvNELTQKNQTLTeNLLKKEQDYTKLEEKHN 326
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK---NKLLKLELLLS-NLKKKIQKNKSLESQIS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 327 EESVSKKNIQATLHQKDLDCQQLQSRLSASETSLHRIhveLSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEKE 406
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL---KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 407 QHGLQLQSEIN-QLHSKLLETERQLGEAHGRLKEQRQLSSEKlmdkEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDK 485
Cdd:TIGR04523 299 DLNNQKEQDWNkELKSELKNQEKKLEEIQNQISQNNKIISQL----NEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 486 TKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGEGETAVLNQ 565
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 566 LQEKNHTLQEQVTQLTEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIK 645
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 646 AKTELLLSAEAAKTAQRADLQNhlDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKT 725
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKK--ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI 612
|
490
....*....|..
gi 1653960520 726 EELEGQIKKLEA 737
Cdd:TIGR04523 613 SSLEKELEKAKK 624
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
265-692 |
6.82e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 57.23 E-value: 6.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 265 SEATISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQknqtltenllkkeQDYTKLEEKHNEESVSKKNIQATLHQKDL 344
Cdd:PRK11281 78 QKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETR-------------ETLSTLSLRQLESRLAQTLDQLQNAQNDL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 345 DcqQLQSRLSASETSLHRIHVELSEKGEATQKLKEELSEVETKYQHLKAEfkqlQQQREEKEQHGLQLQSEINQlhsKLL 424
Cdd:PRK11281 145 A--EYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPS----QRVLLQAEQALLNAQNDLQR---KSL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 425 ETERQLGEAhgrLKEQRQLSSEKLMDKEQQVADLQlklsrleEQLKEKvtnstelqhqldktkqqhqeqqalqqsttaKL 504
Cdd:PRK11281 216 EGNTQLQDL---LQKQRDYLTARIQRLEHQLQLLQ-------EAINSK------------------------------RL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 505 REAQNDLEQVLRQigDKDQKIQNLEALLQKSKENISLlekeREDLyakIQAgegeTAVLNQLQEKNhtlqeqvtqltEKL 584
Cdd:PRK11281 256 TLSEKTVQEAQSQ--DEAARIQANPLVAQELEINLQL----SQRL---LKA----TEKLNTLTQQN-----------LRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 585 KNQSESHKQAQENLHDQV-------------QEQKAHLRAAQ------DRVLSLETSVNELNSQlnesKEKVSQLDIQIK 645
Cdd:PRK11281 312 KNWLDRLTQSERNIKEQIsvlkgslllsrilYQQQQALPSADlieglaDRIADLRLEQFEINQQ----RDALFQPDAYID 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1653960520 646 AkteLLLSAEAAKTAQ-RADLQNHLDTAQNALQDKQQELN-----KITTQLDQ 692
Cdd:PRK11281 388 K---LEAGHKSEVTDEvRDALLQLLDERRELLDQLNKQLNnqlnlAINLQLNQ 437
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
943-1149 |
1.08e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 943 AQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELK---IAVLQKTELENKLQQQLTQAAQELAAEKEKISVLQN 1019
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAaleRRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1020 NYEKSQETFKQLQSDFY--GRES--ELLATRQDLKSVEEKLSLAQEDLISNRNQIGNQNKLIQELKTAKATLEQDSAKKE 1095
Cdd:COG4942 98 ELEAQKEELAELLRALYrlGRQPplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1653960520 1096 QQLQERCKALQDIQKEKSLKEKELVNEKSKLAEIEEIKCRQEKEITKLNEELKS 1149
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| FYVE_CARP |
cd15750 |
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ... |
1357-1405 |
1.16e-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: 49.28 E-value: 1.16e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1653960520 1357 NCMACGKGFSVTVRRHHCRQCGNIFCAECSAKnaltpsSKKPVRVCDAC 1405
Cdd:cd15750 2 PCESCGAKFSVFKRKRTCADCKRYFCSNCLSK------EERGRRRCRRC 44
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
348-851 |
1.44e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 348 QLQSRLSASETSLHRIHVELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEKEqhglQLQSEINQLHSKLLETE 427
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELE----SLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 428 RQLGEAHGRLKEQRqlSSEKLMDKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREA 507
Cdd:PRK03918 266 ERIEELKKEIEELE--EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 508 QNDLEQVLRQIGDKDQKIQNLEALLQKsKENISLLEKEREDLyakiqAGEGETAVLNQLQEKNHTLQEQVTQLTEK---L 584
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYEEAKAK-KEELERLKKRLTGL-----TPEKLEKELEELEKAKEEIEEEISKITARigeL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 585 KNQSESHKQAQENLHD------------QVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLL 652
Cdd:PRK03918 418 KKEIKELKKAIEELKKakgkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 653 SAEAAKtaQRADLQNHLDTAQ-NALQDKQQELNKITTQLDQVTAK---LQDKQEHCSQLESHLKEYKEKYLSLEQKTEEL 728
Cdd:PRK03918 498 LKELAE--QLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEiksLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 729 EGQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLELRATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTK---- 804
Cdd:PRK03918 576 LKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElekk 655
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1653960520 805 -QEEEKKILKQDFETLSQE---TKIQHEELNNRIQTTVTELQKVKMEKEAL 851
Cdd:PRK03918 656 ySEEEYEELREEYLELSRElagLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
564-1149 |
1.54e-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: 56.18 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 564 NQLQEKNHTLQEQVTQLTEKLKNQseshKQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQ 643
Cdd:TIGR04523 71 NNSNNKIKILEQQIKDLNDKLKKN----KDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 644 IKAKTELLLSAEAAK---TAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLqdkqehcsqleSHLKEYKEKYLS 720
Cdd:TIGR04523 147 IKKKEKELEKLNNKYndlKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLL-----------SNLKKKIQKNKS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 721 LEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLELRATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQ 800
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 801 KLTKQEEEKK-ILKQDFETLSQETKIQHEELNNRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDSLKNSKSEFE-- 877
Cdd:TIGR04523 296 EISDLNNQKEqDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEkl 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 878 -KENQKGKAAILDLEKTCKELKHQLQVQMENTLKEQKELKKsLEKEKEashQLKLELNSMQEQLIQAQNTLKQNEKEEQQ 956
Cdd:TIGR04523 376 kKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK-LQQEKE---LLEKEIERLKETIIKNNSEIKDLTNQDSV 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 957 LQGNINELKQSSEQKKKQIEALQGELKIAvlqKTELENKLQQQLTQAAqELAAEKEKISVLQNNYEKSQETFKQLQSDFY 1036
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSRSINKI---KQNLEQKQKELKSKEK-ELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1037 GRESELLATRQDLKSVEEKLSLAQEDLISN--RNQIGNQNKLIQELKTAKATLEQDSAKKEQQLQERCKALQDIQKEKSL 1114
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE 607
|
570 580 590
....*....|....*....|....*....|....*
gi 1653960520 1115 KEKELVNEKSKLAEIEEIKCRQEKEITKLNEELKS 1149
Cdd:TIGR04523 608 KEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNK 642
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
135-743 |
1.62e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 135 AELQSLEQQLEEAQTENFNIKQMKDLFEQKAAQlaTEIADIKSKYDEERSLREAAEQKVTRLTEELNKEATVIQDLKTEL 214
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 215 LQRPGiEDVAVLKKELVQVQTLMDnmtlERERESEKLKDECKKLQSQYASSEATISQLRSELAkgpqevavyvQELQKLK 294
Cdd:COG4913 333 RGNGG-DRLEQLEREIERLERELE----ERERRRARLEALLAALGLPLPASAEEFAALRAEAA----------ALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 295 SSVNELTQKNQTLTENLLKKEQDYTKLEEKHNEESVSKKNIQATLHQ-KDldcqQLQSRLSASETSLHRI--HVELSEKG 371
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAlRD----ALAEALGLDEAELPFVgeLIEVRPEE 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 372 EA----------TQKL-----KEELSEVETKYQHLKAEfKQLQQQREEKEQHGLQLQS-EINQLHSKLL----------- 424
Cdd:COG4913 474 ERwrgaiervlgGFALtllvpPEHYAAALRWVNRLHLR-GRLVYERVRTGLPDPERPRlDPDSLAGKLDfkphpfrawle 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 425 ------------ETERQL---------------GEAHGRLKEQRQLSS---------EKLMDKEQQVADLQLKLSRLEEQ 468
Cdd:COG4913 553 aelgrrfdyvcvDSPEELrrhpraitragqvkgNGTRHEKDDRRRIRSryvlgfdnrAKLAALEAELAELEEELAEAEER 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 469 LKEkvtnSTELQHQLDKtkqqhqeqQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEAllqkSKENISLLEKERED 548
Cdd:COG4913 633 LEA----LEAELDALQE--------RREALQRLAEYSWDEIDVASAEREIAELEAELERLDA----SSDDLAALEEQLEE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 549 LYAKIQAGEGEtavLNQLQEKNHTLQEQVTQLTEKLknqseshKQAQENLHDQVQEQKAHLRAAQDRVLSLEtsvnelns 628
Cdd:COG4913 697 LEAELEELEEE---LDELKGEIGRLEKELEQAEEEL-------DELQDRLEAAEDLARLELRALLEERFAAA-------- 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 629 qlneskekvsqldiqikAKTELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNK----ITTQLDQVTAKLQDKQEHC 704
Cdd:COG4913 759 -----------------LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRewpaETADLDADLESLPEYLALL 821
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1653960520 705 SQLE-SHLKEYKEKYLSL--EQKTEELEGQIKKLEADSLEVK 743
Cdd:COG4913 822 DRLEeDGLPEYEERFKELlnENSIEFVADLLSKLRRAIREIK 863
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
478-702 |
1.86e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 478 ELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGE 557
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 558 GETAVLNQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDRvlsletsVNELNSQLNESKEKV 637
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1653960520 638 SQLDIQIKAKTELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQE 702
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
511-1285 |
1.96e-07 |
|
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: 55.89 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 511 LEQVLRQIGDKDQKIQNLEALLQKSKeniSLLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEKLKNQSES 590
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQK---FYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 591 HKQAQENLHDQVQEQKAHLRAAqdrVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTAQradLQNHLD 670
Cdd:pfam15921 157 AKCLKEDMLEDSNTQIEQLRKM---MLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISK---ILRELD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 671 TAQNALQDKqqeLNKITTQLDQVTAKLQDK-----QEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEAdslEVKAS 745
Cdd:pfam15921 231 TEISYLKGR---IFPVEDQLEALKSESQNKielllQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQS---QLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 746 KEQALQDLQQQRQLNTDLELRATELSKQLEMEKEIVSstrldlqkksEALESIKQKLTKQEEEKKILKQDFETLSQETKi 825
Cdd:pfam15921 305 QEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE----------DKIEELEKQLVLANSELTEARTERDQFSQESG- 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 826 qheELNNRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDSLKNSKSEFEKENQKgkaaILDLEKTCKELKHQLQVQM 905
Cdd:pfam15921 374 ---NLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNME----VQRLEALLKAMKSECQGQM 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 906 ENTLKEQKELKKSLEKEKEASHQL---KLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQG-- 980
Cdd:pfam15921 447 ERQMAAIQGKNESLEKVSSLTAQLestKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSrv 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 981 ELKIAVLQKTELENKLQQQLTQAAQELA---AEKEK-ISVLQNNYEKSQETFKQlqsdfYGRESEllATRQDLKSVEEKL 1056
Cdd:pfam15921 527 DLKLQELQHLKNEGDHLRNVQTECEALKlqmAEKDKvIEILRQQIENMTQLVGQ-----HGRTAG--AMQVEKAQLEKEI 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1057 SLAQEDLISNRNQIGNQNKLIQELKTAKATLEQDSAKKEQQLQERCKALQDIQKEKSLKEKELVNEKSKLAEIEEikcrq 1136
Cdd:pfam15921 600 NDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE----- 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1137 EKEITKLNEELKSHKLEsikeiTNLKDAKQLLIQQKLELQGKADSLKAaveQEKRNQQILKdqVKKEEEELKKEFIEKEA 1216
Cdd:pfam15921 675 DYEVLKRNFRNKSEEME-----TTTNKLKMQLKSAQSELEQTRNTLKS---MEGSDGHAMK--VAMGMQKQITAKRGQID 744
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1653960520 1217 KLHSEIKEKEVGMKKHEENEAKLTMQITALNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATV 1285
Cdd:pfam15921 745 ALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
650-886 |
2.44e-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: 54.77 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 650 LLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELE 729
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 730 GQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLELRATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEK 809
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1653960520 810 KILKQDFETLSQETKIQHEELNNRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDSLKNSKSEFEKENQKGKAA 886
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
107-944 |
4.20e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.98 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 107 EELKKELEKYQGLQQQEAKPDGLVTDSsaELQSLEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEErsLR 186
Cdd:pfam02463 204 EQAKKALEYYQLKEKLELEEEYLLYLD--YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEE--EK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 187 EAAEQKVTRLTEELNKEATVIQDLKTELLQRPGIEDVAVLKKELVQVQTLMDNMTLERErESEKLKDECKKLQSQYASSE 266
Cdd:pfam02463 280 EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIE-ELEKELKELEIKREAEEEEE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 267 ATISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQKNQTLTENLLKKEQDYTKLEEKHNEESVSKKNIQATLHQKDLDC 346
Cdd:pfam02463 359 EELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEES 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 347 QQLQSRLSasetslhrihvelsekgeatQKLKEELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLET 426
Cdd:pfam02463 439 IELKQGKL--------------------TEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 427 ERQLGEAHGRLKEQRQLSSEKLMDKEQQVADLQLKLSRLEEqlKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLRE 506
Cdd:pfam02463 499 SQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE--NYKVAISTAVIVEVSATADEVEERQKLVRALTELPLG 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 507 AqndleQVLRQIGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEKLKN 586
Cdd:pfam02463 577 A-----RKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKG 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 587 QSESHKQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTAQRADLQ 666
Cdd:pfam02463 652 VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 667 NHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASK 746
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 747 EQALQDLQQQRQLNTDLELRATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETKIQ 826
Cdd:pfam02463 812 EEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESK 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 827 HEELNNRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDSLkNSKSEFEKENQKGKAAILDLEKTCKELKHQLQVQME 906
Cdd:pfam02463 892 EEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE-EEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKE 970
|
810 820 830
....*....|....*....|....*....|....*...
gi 1653960520 907 NTLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQ 944
Cdd:pfam02463 971 ELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
630-1157 |
4.41e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 630 LNESKEKVSQLDIQIKAKTElllsaeaaktaqrADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQD---------- 699
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEE-------------KDLHERLNGLESELAELDEEIERYEEQREQARETRDEadevleehee 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 700 KQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLELRATELSKQLEMEKE 779
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 780 IVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETL------------SQETKI-----QHEELNNRIQTTVTELQ 842
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELeseleeareaveDRREEIeeleeEIEELRERFGDAPVDLG 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 843 KVKMEKEALMTELSTVKDKLSKVSDSLKNSksefekENQKGKAAILDLEKTCKELKHQLQ-VQMENTLKEQKELKKSLEK 921
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEATLRTA------RERVEEAEALLEAGKCPECGQPVEgSPHVETIEEDRERVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 922 EKEashQLKLELNSMQEQLIQAQnTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKIAVLQKTELEnklqqqlt 1001
Cdd:PRK02224 483 ELE---DLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELE-------- 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1002 qaaQELAAEKEKISVLQNNYEKSQETFKQLQSdfygRESELLATRQDLKSVEEKLSLAQEdlisNRNQIGNQNkliqELK 1081
Cdd:PRK02224 551 ---AEAEEKREAAAEAEEEAEEAREEVAELNS----KLAELKERIESLERIRTLLAAIAD----AEDEIERLR----EKR 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1082 TAKATLEQDSAKKEQQLQERCKAL---------QDIQKEKSLKEKELVNEKSKLAEIEEIKCRQEKEITKLNEELKShkL 1152
Cdd:PRK02224 616 EALAELNDERRERLAEKRERKRELeaefdeariEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE--L 693
|
....*
gi 1653960520 1153 ESIKE 1157
Cdd:PRK02224 694 EELRE 698
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
81-625 |
4.52e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 81 KRDDVTLLRQEVQDLQASLKEEKWYSEELKKEL-EKYQGLQQQEAKPDGLVTDS---SAELQSLEQQLEEAQTENfnikq 156
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVrDLRERLEELEEERDDLLAEAgldDADAEAVEARREELEDRD----- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 157 mkdlfEQKAAQLATEIADIKSKYDEERSLREAAEQKVTRLTEELNKEATVIQDL-KTELLQRPGIEDVAVLKKELVQVQT 235
Cdd:PRK02224 324 -----EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELeEAREAVEDRREEIEELEEEIEELRE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 236 LMDNMTLERER---ESEKLKDECKKLQSQYASSEATISQLRSELAKGPQ--EVAVYVQELQKLKSS-----VNELTQKNQ 305
Cdd:PRK02224 399 RFGDAPVDLGNaedFLEELREERDELREREAELEATLRTARERVEEAEAllEAGKCPECGQPVEGSphvetIEEDRERVE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 306 TLTENLLKKEQDYTKLEEKHNE-ESVSKKNIQAtlhqkdldcQQLQSRLSASETSLHRIHVELSEKGEATQKLKEELSEV 384
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERaEDLVEAEDRI---------ERLEERREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 385 ETKyqhlkaefkqlqqqREEKEQHGLQLQSEINQLHSKLLETERQLGEahgrLKEQRQlSSEKLMDKEQQVADLQLKLSR 464
Cdd:PRK02224 550 EAE--------------AEEKREAAAEAEEEAEEAREEVAELNSKLAE----LKERIE-SLERIRTLLAAIADAEDEIER 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 465 LEEQLKEKVTNSTELQHQLdktkqqhqeqqalqqsttAKLREAQNDLEQVL--RQIGDKDQKIQNLEALLQKSKENISLL 542
Cdd:PRK02224 611 LREKREALAELNDERRERL------------------AEKRERKRELEAEFdeARIEEAREDKERAEEYLEQVEEKLDEL 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 543 EKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLteklknqsESHKQAQENLHDQVQEQKAHLRaaQDRVLSLETS 622
Cdd:PRK02224 673 REERDDLQAEIGAVENELEELEELRERREALENRVEAL--------EALYDEAEELESMYGDLRAELR--QRNVETLERM 742
|
...
gi 1653960520 623 VNE 625
Cdd:PRK02224 743 LNE 745
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
381-978 |
5.95e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.14 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 381 LSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQLSSEKlmdkeqqvadlql 460
Cdd:PRK01156 185 IDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMK------------- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 461 klSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENI- 539
Cdd:PRK01156 252 --NRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIk 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 540 --SLLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLtEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDRVL 617
Cdd:PRK01156 330 klSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSI-ESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 618 SLetsVNELNSQLNESKEKVSQLDIQIKAKTELLLsaEAAKTAQRADLQN-------HL--DTAQNALQDKQQELNKITT 688
Cdd:PRK01156 409 KE---LNEINVKLQDISSKVSSLNQRIRALRENLD--ELSRNMEMLNGQSvcpvcgtTLgeEKSNHIINHYNEKKSRLEE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 689 QLDQV---TAKLQDKQEHCSQLESHL-KEYKEKYLSLEQKTEELEGQIKKLEADSLEVKaskeqalqdlqqqrqlntDLE 764
Cdd:PRK01156 484 KIREIeieVKDIDEKIVDLKKRKEYLeSEEINKSINEYNKIESARADLEDIKIKINELK------------------DKH 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 765 LRATELSKQLE-MEKEIVSSTRLDLQKKSEALESIK-QKLTKQEEEKKILKQDFETLSQETKIQHEELNNRIQTTVTelq 842
Cdd:PRK01156 546 DKYEEIKNRYKsLKLEDLDSKRTSWLNALAVISLIDiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIR--- 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 843 kvKMEKEAlmtelstvkdklskvsDSLKNSKsefeKENQKGKAAILDLEKTCKELKHQLQvQMENTLKEQKELKKSLEKE 922
Cdd:PRK01156 623 --EIENEA----------------NNLNNKY----NEIQENKILIEKLRGKIDNYKKQIA-EIDSIIPDLKEITSRINDI 679
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1653960520 923 KEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEAL 978
Cdd:PRK01156 680 EDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
600-1147 |
6.84e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.03 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 600 DQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEaaktAQRADLQNHLDTAQNALQDK 679
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAE----EMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 680 QQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQqrql 759
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKL---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 760 ntdLELRATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQE---EEKKILKQDFETLSQETKIQHEELNNRIQT 836
Cdd:pfam01576 157 ---LEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEkgrQELEKAKRKLEGESTDLQEQIAELQAQIAE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 837 TVTELQKVKMEKEALMTEL---STVKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKTCKELKHQLQV---QMENTL- 909
Cdd:pfam01576 234 LRAQLAKKEEELQAALARLeeeTAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEAlktELEDTLd 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 910 -------------KEQKELKKSLEKEKEASHQLKLE--------LNSMQEQLIQAQNTLKQNEKEEQQLQGNINEL---- 964
Cdd:pfam01576 314 ttaaqqelrskreQEVTELKKALEEETRSHEAQLQEmrqkhtqaLEELTEQLEQAKRNKANLEKAKQALESENAELqael 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 965 ------KQSSEQKKKQIEALQGELKIAVLQKTELENKLQQQLTQAAQELAAEKEKISVLQNNYEKSQETFKQLQSDFYGR 1038
Cdd:pfam01576 394 rtlqqaKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1039 ESELLATRQDLKSVEEKLSLAQEDLISNRNQIGNQNKLIQELKTAKATLEQDSAKKEQQLQERCKALQDIQKEKSLKEKE 1118
Cdd:pfam01576 474 QELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE 553
|
570 580
....*....|....*....|....*....
gi 1653960520 1119 LVNEKSKLAEIEEIKCRQEKEITKLNEEL 1147
Cdd:pfam01576 554 LEALTQQLEEKAAAYDKLEKTKNRLQQEL 582
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
503-1240 |
7.36e-07 |
|
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: 53.96 E-value: 7.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 503 KLREAQNDLEQVLRQigdKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGEGETAVL----NQLQEKNHTLQEQVT 578
Cdd:pfam05483 89 KIKKWKVSIEAELKQ---KENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLikenNATRHLCNLLKETCA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 579 QLTEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTElllsaeaak 658
Cdd:pfam05483 166 RSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEIN--------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 659 taqraDLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLeqkTEELEGQIKKLEAD 738
Cdd:pfam05483 237 -----DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHL---TKELEDIKMSLQRS 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 739 SLEVKASKEQALQDLQQQRQLNTDLELRATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFET 818
Cdd:pfam05483 309 MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 819 LSQETKiQHEELNNRIQTTVTELQKVKMEKEALMTElstvKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKTCKELK 898
Cdd:pfam05483 389 KSSELE-EMTKFKNNKEVELEELKKILAEDEKLLDE----KKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIK 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 899 hqlqVQMENTLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEAL 978
Cdd:pfam05483 464 ----TSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENL 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 979 QGelkiavlQKTELENKLQQQLTQAAQELAAEKEKISVLQNNYEKSQETFKQLQSDFYGRESELLATRQDLKSVEEKLSL 1058
Cdd:pfam05483 540 EE-------KEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1059 AQEDLISNRNQIGNQNKLIQELKTAKATLEQDSAKKEQQLQERCKALQDIQKEKSLKEKELVNEKSKLAEIEEikcrqek 1138
Cdd:pfam05483 613 LHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIAD------- 685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1139 EITKLNEELKSHKLESIKEITNLKDAKQLLIQQKLELQGKADSLKAAVEQEkrnQQILKDQVKKEEEELKKEFIEKEAKL 1218
Cdd:pfam05483 686 EAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE---QSSAKAALEIELSNIKAELLSLKKQL 762
|
730 740
....*....|....*....|..
gi 1653960520 1219 HSEIKEKEVGMKKHEENEAKLT 1240
Cdd:pfam05483 763 EIEKEEKEKLKMEAKENTAILK 784
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1075-1345 |
7.42e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1075 KLIQELKTAKATLEQDSAKKEQQLQERCKALQDIQKEKSLKEKELVNEKSKLAEIEEikcrqekEITKLNEELkshkLES 1154
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-------ELEEAQAEE----YEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1155 IKEITNLKDAKQLLIQQKLELQGKADSLKAAVEQEKRNQQILKDQvkkeEEELKKEFIEKEAKLHS---EIKEKEVGMKK 1231
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEELEEaeaELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1232 HEENEAKLTMQITALNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQT 1311
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270
....*....|....*....|....*....|....
gi 1653960520 1312 KVLELQRKLDNTTAAVQELGRENQSLQIKHTQAL 1345
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
785-1094 |
1.13e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 53.37 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 785 RLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQetKIQHEE-----LNNRIQTTVTELQKVKMEKEALMTELSTVK 859
Cdd:PLN02939 99 RASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVG--MIQNAEknillLNQARLQALEDLEKILTEKEALQGKINILE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 860 DKLSKVSDSLKNSKsefekenqKGKAAILDLEKTCKELKHQLQVQMENTLKEQKELKKSLEKEKEASHQLKLELNSMQEQ 939
Cdd:PLN02939 177 MRLSETDARIKLAA--------QEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 940 LIQAQNT---LKQNEKEEQQLQGNINELKQsseqkkKQIEALQGELKIAVLQKTELENKLQQQLTQAAQELAAEKEKISV 1016
Cdd:PLN02939 249 LIEVAETeerVFKLEKERSLLDASLRELES------KFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1017 LQNNY------EKSQETFKQLQ-SDFYGRESELLatRQDLKSVEEKLSLAQEDLISnrnQIGNQNKLIQELKTAKATLEQ 1089
Cdd:PLN02939 323 LDQNQdlrdkvDKLEASLKEANvSKFSSYKVELL--QQKLKLLEERLQASDHEIHS---YIQLYQESIKEFQDTLSKLKE 397
|
....*
gi 1653960520 1090 DSAKK 1094
Cdd:PLN02939 398 ESKKR 402
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
347-561 |
1.17e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 347 QQLQSRLSASETSLHRIHVELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLET 426
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 427 ERQLGEAHGRLKEQRQLSSEKLMDKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLRE 506
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1653960520 507 AQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGEGETA 561
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
156-686 |
1.18e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 156 QMKDLFEQKAAQLATEIADIKSKYDEERSLREAAEqKVTRLTEELNKEATVIQDLKTELLQRPGieDVAVLKKELVQVQT 235
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELE-KLEKEVKELEELKEEIEELEKELESLEG--SKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 236 LMDNMTLERERESEKLKD--ECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQKNQTLTENLLK 313
Cdd:PRK03918 267 RIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 314 KEQ---DYTKLEEKHneesvskkniqatlhqkdldcqQLQSRLSASETSLHRIHVELseKGEATQKLKEELSEVETKYQH 390
Cdd:PRK03918 347 LKElekRLEELEERH----------------------ELYEEAKAKKEELERLKKRL--TGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 391 LKAEFKQLQQQREEKEQHGLQLQSEINQLHS---KLLETERQLGEAH-GRLKEQRQLSSEKLMDKEQQVADLQLKLSRLE 466
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKakgKCPVCGRELTEEHrKELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 467 EQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKEnislLEKER 546
Cdd:PRK03918 483 RELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE----LKKKL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 547 EDLYAKIQAGEGETA-VLNQLQEKNHTLQEQVTQLTEKLK------NQSESHKQAQENLHDQVQEQKAHLRAAQDRVLSL 619
Cdd:PRK03918 559 AELEKKLDELEEELAeLLKELEELGFESVEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAET 638
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1653960520 620 ETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAE-AAKTAQRADLQNHLDTAQNALQDKQQELNKI 686
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSEEEYEELREEYLELSRElAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
137-534 |
1.40e-06 |
|
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: 52.59 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 137 LQSLEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIK---SKYDEERSLREAAEQKVTRLTEELNKEATVIQDLKTE 213
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKeelRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 214 LLQRpgiedvavlKKELVQVQTLMDNMTLERERESEKLKDECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKL 293
Cdd:pfam07888 127 HEAR---------IRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 294 KSSVNELTQKNQTLTENLLKKEQDYTKLEEKHNEESVSKKNIQAtlhqkdldcqqLQSRLSASEtslhrihvelsekgEA 373
Cdd:pfam07888 198 RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRS-----------LQERLNASE--------------RK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 374 TQKLKEELSEVETkyqhlkaefkqlQQQREEKEQHGLQLQSEinQLHSKLLETERQLGEAHGRLKEQR---QLSSEKLMD 450
Cdd:pfam07888 253 VEGLGEELSSMAA------------QRDRTQAELHQARLQAA--QLTLQLADASLALREGRARWAQERetlQQSAEADKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 451 K-EQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLE 529
Cdd:pfam07888 319 RiEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLE 398
|
....*
gi 1653960520 530 ALLQK 534
Cdd:pfam07888 399 QRLET 403
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1054-1270 |
1.42e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1054 EKLSLAQEDLISNRNQIGNQNKLIQELKTAKATLEQDSAKKEQQLQERCKALQDIQKEKSLKEKELVNEKSKLAEIEEIK 1133
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1134 CRQEKEITKLNEEL-KSHKLESIKEITNLKDAKQLLIQQKLeLQGKADSLKAAVEQEKRNQQILKdQVKKEEEELKKEFI 1212
Cdd:COG4942 100 EAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELA-ALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1653960520 1213 EKEAKLHSEIKEKEVGMKKHEENEAKLTMQITALNENLGTVKKEWQSSQRRVSELEKQ 1270
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1053-1338 |
1.53e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1053 EEKLSLAQEDLISNRNQIGNQNKLIQELKTAKATLEQDSAKKE--QQLQERCK--ALQDIQKEKSLKEKELVNEKSKLAE 1128
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQALLKEKReyEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1129 IEEIKCRQEKEITKLNEELKS--HKLESI-KEITNLKDAKQLLIQQKL-ELQGKADSLKAAVEQEKRNQQILKDQVKKEE 1204
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEieQLLEELnKKIKDLGEEEQLRVKEKIgELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1205 EELKKEFIEKeAKLHSEIKEKEVGMKKHEENEAKLTMQITALNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEAT 1284
Cdd:TIGR02169 329 AEIDKLLAEI-EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE 407
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1653960520 1285 VQNNQDERRALLERCLKGEGEIEKLQTKVLELQRKLDNTTAAVQELGRENQSLQ 1338
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
129-982 |
1.66e-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: 52.74 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 129 LVTDSSAELQSLEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEERSLREaAEQKVTRLTEELNKEATVIQ 208
Cdd:TIGR00606 194 VRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKN-RLKEIEHNLSKIMKLDNEIK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 209 DLKTELLQRPGIEDVAVLKKELVQVQTLMDNMTLERE-----RESEKLKDECKKLQSQYASSEATISQLRSELAKGPQEV 283
Cdd:TIGR00606 273 ALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNhqrtvREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 284 AVYVQELQKLKSSVNELTQKNQTLTEnLLKKEQDYTKLEEKHNEESVSKKNIQATLHQKDLDCQQLQSRLSASETSLHRI 363
Cdd:TIGR00606 353 QLQADRHQEHIRARDSLIQSLATRLE-LDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEI 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 364 HVELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREekeqhglqlqsEINQLHSKLLETERQLGEAHGRLKEQRQL 443
Cdd:TIGR00606 432 RDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD-----------RILELDQELRKAERELSKAEKNSLTETLK 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 444 SSEKLMDKEQqvADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREaqndleqVLRQIGDKDQ 523
Cdd:TIGR00606 501 KEVKSLQNEK--ADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDE-------LTSLLGYFPN 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 524 KIQnLEALLQKSKENISLLEKEREDLYAKIQAGEGETavlNQLQEKNHTLQEQVTQLTEKLKN--QSESHKQAQENLHDQ 601
Cdd:TIGR00606 572 KKQ-LEDWLHSKSKEINQTRDRLAKLNKELASLEQNK---NHINNELESKEEQLSSYEDKLFDvcGSQDEESDLERLKEE 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 602 VQEQKAHLRAAQDRVLSLETSVNELNSQlNESKEKVSQLDIQIKAKTELLLSaeaaktaqraDLQNHLDTAQNALQDKQQ 681
Cdd:TIGR00606 648 IEKSSKQRAMLAGATAVYSQFITQLTDE-NQSCCPVCQRVFQTEAELQEFIS----------DLQSKLRLAPDKLKSTES 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 682 ELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEAdSLEVKASKEQALQDLQQQRQLNT 761
Cdd:TIGR00606 717 ELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET-LLGTIMPEEESAKVCLTDVTIME 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 762 DLELRATELSKQLEMEKEIVSSTRLD-----LQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETKIQHEELNNRIQT 836
Cdd:TIGR00606 796 RFQMELKDVERKIAQQAAKLQGSDLDrtvqqVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQ 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 837 TVTELQKVKMEKEALMTELSTVKDKLSKVSDSLKNSK--SEFEKENQKGKAAILDLEKTCKELKHQLQVQMENTLKEQKE 914
Cdd:TIGR00606 876 IGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSplETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHG 955
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1653960520 915 LKKSLEKEKEASHQLKLELNSMQEQLIQAQntLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGEL 982
Cdd:TIGR00606 956 YMKDIENKIQDGKDDYLKQKETELNTVNAQ--LEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNL 1021
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
779-985 |
2.38e-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: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 779 EIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQ---ETKIQHEELNNRIQTTVTELQKVKMEKEALMTEL 855
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriaALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 856 STVKDKLSKVSDSL-KNSKSEFEK-----ENQKGKAAILDLEKTCKELKHQLQVQMENTLKEQKELKKSLEKEKEASHQL 929
Cdd:COG4942 100 EAQKEELAELLRALyRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 930 KLELNSMQEQLIQAQN----TLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKIA 985
Cdd:COG4942 180 LAELEEERAALEALKAerqkLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
504-709 |
3.18e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 504 LREAQNDLEQVLRQIgDKDQKIQNLEALLQKSKENISLLEKEREdlYAKIQAGEGETAVLNQLQEKnhtLQEQVTQLTEK 583
Cdd:COG4913 237 LERAHEALEDAREQI-ELLEPIRELAERYAAARERLAELEYLRA--ALRLWFAQRRLELLEAELEE---LRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 584 LKNQSESHKQAQENLhDQVQEQkaHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTAQRA 663
Cdd:COG4913 311 LERLEARLDALREEL-DELEAQ--IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1653960520 664 DLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLES 709
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
242-718 |
3.89e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 242 LERERESEKLKDECKKLQSQYASSEATISQLRSELAKGP-----QEVAVYVQELQKLKSSVNELTQKNQTLTENLLKKEQ 316
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 317 DYTKLEEKHNEESVSKKN-IQATLHQKDLDCQQLQSRLSASETSLHRIHVEL--SEKG---------EATQKLKEELSEV 384
Cdd:COG4913 324 ELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLPLpaSAEEfaalraeaaALLEALEEELEAL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 385 ETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQLSSEkLMDKEQQVADLQ----- 459
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGE-LIEVRPEEERWRgaier 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 460 ----LKLSRL--EEQLKE--KVTNSTELQHQLD-----KTKQQHQEQQALQQSTTAKLR----EAQNDLEQVLRQIGD-- 520
Cdd:COG4913 483 vlggFALTLLvpPEHYAAalRWVNRLHLRGRLVyervrTGLPDPERPRLDPDSLAGKLDfkphPFRAWLEAELGRRFDyv 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 521 -----------------------------KDQKIQNLEALL--QKSKENISLLEKEREDLYAKIQAGEGETAVLNQLQEK 569
Cdd:COG4913 563 cvdspeelrrhpraitragqvkgngtrheKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDA 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 570 NHTLQEQVTQLTEKLKNQSEsHKQAQENLhDQVQEQKAHLRAAQDRVLSLE-------TSVNELNSQLNESKEKVSQLDI 642
Cdd:COG4913 643 LQERREALQRLAEYSWDEID-VASAEREI-AELEAELERLDASSDDLAALEeqleeleAELEELEEELDELKGEIGRLEK 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 643 QIKAKTELLLSAEA--------AKTAQRADLQNHLdtAQNALQDKQQEL-NKITTQLDQVTAKLQDKQEhcsQLESHLKE 713
Cdd:COG4913 721 ELEQAEEELDELQDrleaaedlARLELRALLEERF--AAALGDAVERELrENLEERIDALRARLNRAEE---ELERAMRA 795
|
....*
gi 1653960520 714 YKEKY 718
Cdd:COG4913 796 FNREW 800
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
499-729 |
5.96e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 499 STTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQ--KSKENISLLEKEREDLYAKIQAGEGEtavLNQLQEKNHTLQEQ 576
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQ---LAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 577 VTQLTEKLKNQSESHKQAQENlhDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLsaea 656
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL---- 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1653960520 657 aktaqrADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEhcsqLESHLKEYKEKYLSLEQKTEELE 729
Cdd:COG3206 316 ------ASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR----LEREVEVARELYESLLQRLEEAR 378
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
452-700 |
6.02e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 452 EQQVADLQLKLSRLEEQLKEKVTNSTELQHQLD--KTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLE 529
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 530 ALLQKSKENISLLekeredlyakiqageGETAVLNQLQEKnhtLQEQVTQLTEKLKNQSESHKQAQEnLHDQVQEQKAHL 609
Cdd:COG3206 247 AQLGSGPDALPEL---------------LQSPVIQQLRAQ---LAELEAELAELSARYTPNHPDVIA-LRAQIAALRAQL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 610 RAAQDRVL-SLETSVNELNSQLNESKEKVSQLDIQIKAktelllsaEAAKTAQRADLQNHLDTAQ---NALQDKQQELnK 685
Cdd:COG3206 308 QQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAE--------LPELEAELRRLEREVEVARelyESLLQRLEEA-R 378
|
250
....*....|....*
gi 1653960520 686 ITTQLDQVTAKLQDK 700
Cdd:COG3206 379 LAEALTVGNVRVIDP 393
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
366-645 |
6.04e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.07 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 366 ELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQlgeAHGRLkEQRQLSS 445
Cdd:PRK11281 53 LLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRE---TLSTL-SLRQLES 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 446 eKLMDKEQQVADLQLKLSRLEEQL-----------KEKVTNSTELQhQLDKTKQQHQEQQALQQSTTAKLREAqndlEQV 514
Cdd:PRK11281 129 -RLAQTLDQLQNAQNDLAEYNSQLvslqtqperaqAALYANSQRLQ-QIRNLLKGGKVGGKALRPSQRVLLQA----EQA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 515 LRqigdkDQKIQNLEALLQKSKENISLLEKEREDLYAKIQagegetavlnQLQEKNHTLQEQVTQlteklKNQSESHKQA 594
Cdd:PRK11281 203 LL-----NAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQ----------RLEHQLQLLQEAINS-----KRLTLSEKTV 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1653960520 595 QenlhdQVQEQKAHLRAAQDRVLSLETSVN-ELNSQLNESKEKVSQL---DIQIK 645
Cdd:PRK11281 263 Q-----EAQSQDEAARIQANPLVAQELEINlQLSQRLLKATEKLNTLtqqNLRVK 312
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
240-644 |
8.73e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 240 MTLERERESEKLKDECKKLQSQYAS-SEATISQLRSELAKGPQEVAVYVQELQKLKSSV-------NELTQKNQTLTENL 311
Cdd:PRK04863 244 MTLEAIRVTQSDRDLFKHLITESTNyVAADYMRHANERRVHLEEALELRRELYTSRRQLaaeqyrlVEMARELAELNEAE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 312 LKKEQDYTKLEEKHNeesvskKNIQATLHQKDLdcQQLQSRLSASETSLHRIHVELSEKGEATQKLKEELSEVETKYQHL 391
Cdd:PRK04863 324 SDLEQDYQAASDHLN------LVQTALRQQEKI--ERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDEL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 392 K---AEFKQ---LQQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQLSSEKLMDKEQQVADLQLKLSRL 465
Cdd:PRK04863 396 KsqlADYQQaldVQQTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQF 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 466 EE--QLKEKVTNSTELQ--HQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISL 541
Cdd:PRK04863 476 EQayQLVRKIAGEVSRSeaWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDE 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 542 LEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQ---ENLHDQVQEQKAHLRAAQDRVLS 618
Cdd:PRK04863 556 LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQdalARLREQSGEEFEDSQDVTEYMQQ 635
|
410 420
....*....|....*....|....*.
gi 1653960520 619 LETSVNELNSQLNESKEKVSQLDIQI 644
Cdd:PRK04863 636 LLERERELTVERDELAARKQALDEEI 661
|
|
| FYVE_WDFY2 |
cd15757 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); WDFY2, also ... |
1367-1405 |
9.08e-06 |
|
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: 44.67 E-value: 9.08e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1653960520 1367 VTVRRHHCRQCGNIFCAECSAKNALTP--SSKKPVRVCDAC 1405
Cdd:cd15757 29 IGLRQHHCRKCGKAVCGKCSSKRSTIPlmGFEFEVRVCDSC 69
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1007-1260 |
1.01e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1007 LAAEKEKISVLQNNYEKSQETFKQLQSDFYGRESELLATRQDLKSVEEKLSLAQEDLISNRNQIGNQNKLIQELKTAKAT 1086
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1087 LEQDSAKKEQQLQERCKALQDIQKEKSLkeKELVNEKSKLAEIeeikcRQEKEITKLNEELKshklesiKEITNLKDAKQ 1166
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPL--ALLLSPEDFLDAV-----RRLQYLKYLAPARR-------EQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1167 LLIQQKLELQGKADSLKAAVEQEKRNQQILKDQvkkeeeelKKEFIEKEAKLHSEIKEKEVGMKKHEENEAKLTMQITAL 1246
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEAL--------KAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|....
gi 1653960520 1247 NENLGTVKKEWQSS 1260
Cdd:COG4942 233 EAEAAAAAERTPAA 246
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
422-1270 |
1.01e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.43 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 422 KLLETERQLGEAHGRLKEQRQLSSEKLMDKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDktkqqhqeqqalqqstt 501
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELD----------------- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 502 aKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQagegetavlNQLQEKNHTLQEQVTQLT 581
Cdd:TIGR00606 249 -PLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTD---------EQLNDLYHNHQRTVREKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 582 EKL--------KNQSESHKQAQENLHDQVQEQKAHLRA----AQDRVLSLETSVNELNSQLnESKEKVSQLDIQIKAKTE 649
Cdd:TIGR00606 319 RELvdcqreleKLNKERRLLNQEKTELLVEQGRLQLQAdrhqEHIRARDSLIQSLATRLEL-DGFERGPFSERQIKNFHT 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 650 LLLSAEA--AKTAQR--ADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYK---EKYLSLE 722
Cdd:TIGR00606 398 LVIERQEdeAKTAAQlcADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEgssDRILELD 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 723 QKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLELraTELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKL 802
Cdd:TIGR00606 478 QELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKL--DQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIK 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 803 TKQEEE----------KKILKQDFETLSQETKIQHEEL---NNRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDS- 868
Cdd:TIGR00606 556 SRHSDEltsllgyfpnKKQLEDWLHSKSKEINQTRDRLaklNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSq 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 869 -----LKNSKSEFEKENQK-----GKAAILD----------------------LEKTCKELKHQLQVQMENTLKEQKELK 916
Cdd:TIGR00606 636 deesdLERLKEEIEKSSKQramlaGATAVYSqfitqltdenqsccpvcqrvfqTEAELQEFISDLQSKLRLAPDKLKSTE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 917 KSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKIAVLQKTELENKL 996
Cdd:TIGR00606 716 SELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIME 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 997 QQQLTQAAQELAAEKEKISVLQNNYEKSQETFKQLQSDFYGRESELLATRQDLKSVEEKLSLAQEDLISNRNQIGNQNKL 1076
Cdd:TIGR00606 796 RFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQ 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1077 IQELKTAKATLEQDSAKKEQQLQERCKALQDIQKEKS----LKEKELVNEKSKLAEIEEIKCRQEKEITKLNEELKSHKL 1152
Cdd:TIGR00606 876 IGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSpletFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHG 955
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1153 ESIKEITNLKDAKQ-LLIQQKLELQGKADSLKAAVEQEKRNQQILKDQVKKEEEELKKEF----IEKEAKLHSEIKEKEV 1227
Cdd:TIGR00606 956 YMKDIENKIQDGKDdYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERwlqdNLTLRKRENELKEVEE 1035
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 1653960520 1228 GMKKH--EENEAKLTMQITA---LNENLGTVKKEWQSSQRRVSELEKQ 1270
Cdd:TIGR00606 1036 ELKQHlkEMGQMQVLQMKQEhqkLEENIDLIKRNHVLALGRQKGYEKE 1083
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
578-810 |
1.02e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 578 TQLTEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAA 657
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 658 KTAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEA 737
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1653960520 738 DSLEVKASKEQALQDLQQQRQLNTDLELRATELSKQLEmekeivsstrlDLQKKSEALESIKQKLTKQEEEKK 810
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELA-----------ELQQEAEELEALIARLEAEAAAAA 240
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
447-663 |
1.13e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 447 KLMDKEQQVADLQLKLSRLEEQLKEkvtnsteLQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQ 526
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDA-------LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 527 NLEALLQKSKENISLLE-----KEREDLYAKIQAgegetavLNQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQENLHDQ 601
Cdd:COG3883 90 ERARALYRSGGSVSYLDvllgsESFSDFLDRLSA-------LSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1653960520 602 VQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTAQRA 663
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
187-736 |
1.44e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.90 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 187 EAAEQKVTRLTEELNKEATVIQDLKTELlqRPGIEDVAVLKKELVQVQTLMDNMTLERERES------EKLKDECKKLQS 260
Cdd:PRK01156 165 ERNYDKLKDVIDMLRAEISNIDYLEEKL--KSSNLELENIKKQIADDEKSHSITLKEIERLSieynnaMDDYNNLKSALN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 261 QYASSEATISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQKNQTLTENLLKKEQDYTKLEEKHNEESVSKKNIQATLH 340
Cdd:PRK01156 243 ELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEIN 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 341 QKDLDCQQLqsrlsASETSLHRIHVELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLH 420
Cdd:PRK01156 323 KYHAIIKKL-----SVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEIL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 421 SKLLETERQlgeahgrLKEQRQLSSEKLMDKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQ----LDKTKQQHQEQQAL 496
Cdd:PRK01156 398 KIQEIDPDA-------IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpVCGTTLGEEKSNHI 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 497 QQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQK-SKENISLLEKER---EDLYAKIQAGEGETAVLNQLQEKNHT 572
Cdd:PRK01156 471 INHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYlESEEINKSINEYnkiESARADLEDIKIKINELKDKHDKYEE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 573 LQEQVTQL-TEKLKNQSESHKQAQ--------ENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQ 643
Cdd:PRK01156 551 IKNRYKSLkLEDLDSKRTSWLNALavislidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANN 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 644 IKAKTELLLSAEAAKTAQRADLQNH------LDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEK 717
Cdd:PRK01156 631 LNNKYNEIQENKILIEKLRGKIDNYkkqiaeIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTR 710
|
570
....*....|....*....
gi 1653960520 718 YLSLEQKTEELEGQIKKLE 736
Cdd:PRK01156 711 INELSDRINDINETLESMK 729
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
145-972 |
1.48e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 145 EEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEERSLREAAEQKVTRLTEELNKEATVIQDLKTELLQRPGIEDVA 224
Cdd:PTZ00121 1090 DEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEA 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 225 VLKKELVQVQTLMDNMTLERERESEKLKDECKKLQSQYASSEATISQLR-------SELAKGPQEVAVYVQELQKL-KSS 296
Cdd:PTZ00121 1170 RKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARkaedakkAEAVKKAEEAKKDAEEAKKAeEER 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 297 VNELTQKNQTLTENLLKKEQDYTKLEEKHNEESVSKkniqatlhqkdldCQQLQSRLSASETSLHRIHVELSEKGEATQK 376
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-------------AEEKKKADEAKKAEEKKKADEAKKKAEEAKK 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 377 LKEelseVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQlGEAHGRLKEQRQLSSEKLMDKEQQVA 456
Cdd:PTZ00121 1317 ADE----AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 457 DLQlKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSK 536
Cdd:PTZ00121 1392 KAD-EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 537 ENISLLEKEREDLYAKIQAGEGETAVLNQLQEKNhtlQEQVTQLTEKLKnQSESHKQAQENLHDQVQEQKAHLRAAQDRV 616
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK---AAEAKKKADEAK-KAEEAKKADEAKKAEEAKKADEAKKAEEKK 1546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 617 LSLETSVNElNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAK 696
Cdd:PTZ00121 1547 KADELKKAE-ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 697 LQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKK--LEADSLEVKASKEQALQDLQQQRQLNTDLELRATELSKQL 774
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAaeEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 775 EMEKEIVSSTRLDLQ-KKSEALESIK--QKLTKQEEEKKILKQDFETLSQETKIQHEELNNRIQTTVTELQKVKMEKEAL 851
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEElKKAEEENKIKaeEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 852 MTELSTVKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKTckelkhqlqvqMENTLKEQKELKKSLEKEKEASHQLKL 931
Cdd:PTZ00121 1786 DEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEM-----------EDSAIKEVADSKNMQLEEADAFEKHKF 1854
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 1653960520 932 ELNSMQEqliQAQNTLKQNEKEEQQLQGNINELKQSSEQKK 972
Cdd:PTZ00121 1855 NKNNENG---EDGNKEADFNKEKDLKEDDEEEIEEADEIEK 1892
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
860-1343 |
1.70e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 860 DKLSKVSDSLKNSKSEFEKEnQKGKAAILDLEKTCKELKHQLQVQMENTLKEQKELKK---SLEKEKEASHQLKLELNSM 936
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRR-IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSelpELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 937 QEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALqgELKIAVLQKTELENKLQQQLTQAAQELAAEKEKISV 1016
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL--EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEK 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1017 LQNNYEKSQETFKQLQSDFYGRESELLATRQDLKSVEEKLSLAQEDLisnrnqignqnKLIQELKTAKATLEQDSAKKEQ 1096
Cdd:PRK03918 315 RLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH-----------ELYEEAKAKKEELERLKKRLTG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1097 QLQERCKA-LQDIQKEKSLKEKELVNEKSKLAEIEEIKCRQEKEITKL---------------NEELKSHKLESIKEITN 1160
Cdd:PRK03918 384 LTPEKLEKeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcgreltEEHRKELLEEYTAELKR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1161 LKDAKQLLIQQKLELQGKADSLKAAVEQEKR---NQQILKD--QVKKEEEELKKEFIEKEAKLHSEIKEKEVGMKKHEEN 1235
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKESElikLKELAEQlkELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1236 EAKLTMQITALNENLGTVKKEWQSSQRRVSELEKQ--------TDDLRGEIAVLEA------TVQNNQDERRALLERclk 1301
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELLKEleelgfesVEELEERLKELEPfyneylELKDAEKELEREEKE--- 620
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1653960520 1302 gegeIEKLQTKVLELQRKLDNTTAAVQELGRENQSLQIKHTQ 1343
Cdd:PRK03918 621 ----LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
366-738 |
1.71e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 366 ELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEKEQH--GLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQL 443
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEERLEELREL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 444 SsEKLMDKEQQVADLQLKLSRLEEQLkekvtnSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQ 523
Cdd:COG4717 162 E-EELEELEAELAELQEELEELLEQL------SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 524 KIQNLEALLQKSKENISL---------------LEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEKLKNQS 588
Cdd:COG4717 235 ELEAAALEERLKEARLLLliaaallallglggsLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 589 ESHKQAQENLHDQVQ----EQKAHLRAAQDRVLSLETSVNELNS-----QLNESKEKVSQLDIQIKAKTELLLSAEAAKT 659
Cdd:COG4717 315 ELEEEELEELLAALGlppdLSPEELLELLDRIEELQELLREAEEleeelQLEELEQEIAALLAEAGVEDEEELRAALEQA 394
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1653960520 660 AQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDkqehcSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEAD 738
Cdd:COG4717 395 EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEEL-----EELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
305-1340 |
1.81e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.40 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 305 QTLTENLLKKEQDYTKLEEKHNEESVSKKNIQATLHQKDLDC---QQLQSRLSASETSLHRIHVELSEKGEATQKLKEEL 381
Cdd:pfam01576 15 QKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCaeaEEMRARLAARKQELEEILHELESRLEEEEERSQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 382 SEVETKYQhlkAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQ---LGEAHGRLKEQRQLSSEKLMDKEQQVADL 458
Cdd:pfam01576 95 QNEKKKMQ---QHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDillLEDQNSKLSKERKLLEERISEFTSNLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 459 QLKLSRLEEQLKEKVTNSTELQHQL---DKTKQQHQEQQALQQSTTAKLREA----QNDLEQVLRQIGDKDQKIQNLEAL 531
Cdd:pfam01576 172 EEKAKSLSKLKNKHEAMISDLEERLkkeEKGRQELEKAKRKLEGESTDLQEQiaelQAQIAELRAQLAKKEEELQAALAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 532 LQKSKENISLLEKEREDLYAKI----QAGEGETAVLNQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQENLHDQVQEQKA 607
Cdd:pfam01576 252 LEEETAQKNNALKKIRELEAQIselqEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 608 HLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNKIT 687
Cdd:pfam01576 332 LKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 688 TQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKL--EADSLEVKASKEQALQDLQQQRQLNTDLEL 765
Cdd:pfam01576 412 GQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLskDVSSLESQLQDTQELLQEETRQKLNLSTRL 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 766 RATE-----LSKQLEMEKEI-------VSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQ------ETKIQH 827
Cdd:pfam01576 492 RQLEdernsLQEQLEEEEEAkrnverqLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQqleekaAAYDKL 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 828 EELNNRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKTCKELKHQLQvqmen 907
Cdd:pfam01576 572 EKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALE----- 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 908 tlkEQKELKKSLEKekeASHQLKLELnsmqEQLIQAQNTLKQNEKEeqqLQGNINELKQSSEQKKKQIEALQGELKIAVL 987
Cdd:pfam01576 647 ---EALEAKEELER---TNKQLRAEM----EDLVSSKDDVGKNVHE---LERSKRALEQQVEEMKTQLEELEDELQATED 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 988 QKTELENKLQQQLTQAAQELAAEKEKisvlqnNYEKSQETFKQLQSDFYGRESElLATRQDLKSVEEKLSLAQEDLISNR 1067
Cdd:pfam01576 714 AKLRLEVNMQALKAQFERDLQARDEQ------GEEKRRQLVKQVRELEAELEDE-RKQRAQAVAAKKKLELDLKELEAQI 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1068 NQIG-NQNKLIQELKTAKATLEQDSAKKEQQLQERCKAL-QDIQKEKSLK--EKELVNEKSKLAEIEEIKCRQEKEITKL 1143
Cdd:pfam01576 787 DAANkGREEAVKQLKKLQAQMKDLQRELEEARASRDEILaQSKESEKKLKnlEAELLQLQEDLAASERARRQAQQERDEL 866
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1144 NEELKSHKLesikeitnlkdAKQLLIQQKLELQGKADSLKAAVEQEKRNQQILKDQVKKEEEELKK-----------EFI 1212
Cdd:pfam01576 867 ADEIASGAS-----------GKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQlttelaaerstSQK 935
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1213 EKEAKLHSEIKEKEVGMK----------KHEENEAKLTMQITALNENLGTVKKEWQSSQRRVSELEK-------QTDDLR 1275
Cdd:pfam01576 936 SESARQQLERQNKELKAKlqemegtvksKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKklkevllQVEDER 1015
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1653960520 1276 GEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKVLELQRKLDNTTAAVQELGRENQSLQIK 1340
Cdd:pfam01576 1016 RHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
840-1342 |
2.04e-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: 49.33 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 840 ELQKVKMEKEALMTELSTVKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKTCKELKHQLQVQ---------MENTLK 910
Cdd:pfam05483 86 EAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENnatrhlcnlLKETCA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 911 EQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQ-----QLQGNINELKQSSEQKKKQIEALQGELKIA 985
Cdd:pfam05483 166 RSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARlemhfKLKEDHEKIQHLEEEYKKEINDKEKQVSLL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 986 VLQKTELENKLQQQL---TQAAQELAAEKEKISVLQNNYEKSQETFKQLQSDFYGRESELLATRQDLKSVEEKLSLAQED 1062
Cdd:pfam05483 246 LIQITEKENKMKDLTfllEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1063 LIS----NRNQIGNQNK-------LIQELKTAKATLEQDSAKKEQQLQERCKALQDIQKEKSLKEKELvNEKSKLAEIEE 1131
Cdd:pfam05483 326 ICQlteeKEAQMEELNKakaahsfVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL-EEMTKFKNNKE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1132 IKCRQEKEITKLNEELKSHKLESIKEITNLKDAKQLLIQQKLELQGKADSLKAAVEQEKRNQQILKDQVKKEEEELKKEF 1211
Cdd:pfam05483 405 VELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEK 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1212 IEKEaKLHSEIKEKEVGMKKHEENEAKLTMQITALNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQDE 1291
Cdd:pfam05483 485 LKNI-ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDE 563
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1653960520 1292 RRALLER-----------CLKGEGEIEKLQTKVLELQRKLDNTTAAVQELGRENQSLQIKHT 1342
Cdd:pfam05483 564 VKCKLDKseenarsieyeVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS 625
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
526-994 |
2.10e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 526 QNLEALLQKSKENISLLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVtqltEKLKNQSESHKQAQENLHDQVQEQ 605
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEL----EELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 606 KAHLRAAQdrvlsLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNK 685
Cdd:COG4717 129 PLYQELEA-----LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 686 ITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLEL 765
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 766 RATELSKQLEMEKEIVSSTRLDLQKKSEALESIkqkltkQEEEKKILKQDFETLSQETKIQHEELNNRIQTTVTELQKV- 844
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEEL------EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAe 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 845 KMEKEALMTELSTVKDKLSKVSDSlkNSKSEFEKenqkgKAAILDLEKTCKELKHQLQVQMENTLKEQKELKKSLEKE-- 922
Cdd:COG4717 358 ELEEELQLEELEQEIAALLAEAGV--EDEEELRA-----ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEel 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1653960520 923 KEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQL--QGNINELKQSSEQKKKQIEALQGELKIAVLQKTELEN 994
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAELRELAEEWAALKLALELLEE 504
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
362-474 |
2.13e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 49.31 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 362 RIHVELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEK-EQHGLQLQSEINQLHSKLlETERQLGEAHGRLKEQ 440
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAElRDELAELEEELEALKARW-EAEKELIEEIQELKEE 479
|
90 100 110
....*....|....*....|....*....|....
gi 1653960520 441 RQLSSEKLMDKEQQVADLQLKLSRLEEQLKEKVT 474
Cdd:COG0542 480 LEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
88-876 |
2.45e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.96 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 88 LRQEVQDLQASLKEEKwyseelkkelekyqglqqqeakpdgLVTDSSAELQSLEQQLEEaqtenfnikqmkdlfeqkaaQ 167
Cdd:pfam15921 108 LRQSVIDLQTKLQEMQ-------------------------MERDAMADIRRRESQSQE--------------------D 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 168 LATEIADIKSKYDEERSLREaaeqkvtrltEELNKEATVIQDLKTELLQRPGIedvavlkkeLVQVQTLMDNMtleRERE 247
Cdd:pfam15921 143 LRNQLQNTVHELEAAKCLKE----------DMLEDSNTQIEQLRKMMLSHEGV---------LQEIRSILVDF---EEAS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 248 SEKLKDECKKLQSQYASSEATISQLRSELakgPQEVAVYVQELQKLKSSVNELTQKNQTLTENLLKKEQDYTKLEEKHNE 327
Cdd:pfam15921 201 GKKIYEHDSMSTMHFRSLGSAISKILREL---DTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 328 -------ESVSKKNIQATLHQKDLDCQQLQSR---------LSASETSLHRIHVELSekgEATQKLKEELSEVETKYQHL 391
Cdd:pfam15921 278 veitgltEKASSARSQANSIQSQLEIIQEQARnqnsmymrqLSDLESTVSQLRSELR---EAKRMYEDKIEELEKQLVLA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 392 KAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQLG---EAHGRLKEQRQLSSEKLMDKEQQVADLQLKLSRLEEQ 468
Cdd:pfam15921 355 NSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSlekEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEAL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 469 LKekvTNSTELQHQLDKTKQQ---HQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLqkSKENISLLEKE 545
Cdd:pfam15921 435 LK---AMKSECQGQMERQMAAiqgKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTV--SDLTASLQEKE 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 546 REDLYAKIQAGEGETAVLNQLQEKNHTLQE-----QVTQLTEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDRVLSLE 620
Cdd:pfam15921 510 RAIEATNAEITKLRSRVDLKLQELQHLKNEgdhlrNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQ 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 621 TSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEaaktAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDK 700
Cdd:pfam15921 590 VEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE----ARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTS 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 701 QehcSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLELRATELSKQLEMEKEI 780
Cdd:pfam15921 666 R---NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQ 742
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 781 VSStrldLQKKSEALEsikQKLTKQEEEKKILKQDFETLSQEtkiqheelnnrIQTTVTELQKVKMEKEALMTELSTVKD 860
Cdd:pfam15921 743 IDA----LQSKIQFLE---EAMTNANKEKHFLKEEKNKLSQE-----------LSTVATEKNKMAGELEVLRSQERRLKE 804
|
810
....*....|....*.
gi 1653960520 861 KLSKVSDSLKNSKSEF 876
Cdd:pfam15921 805 KVANMEVALDKASLQF 820
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
741-1119 |
3.17e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 741 EVKASKEQALQDLQQQRQLNTDLELRATELSKQLEmekeivsstRLdlqkksealesikqkltKQEEEKKILKQDFETLS 820
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLE---------RL-----------------RREREKAERYQALLKEK 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 821 QETKIQheELNNRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKTCKELKHQ 900
Cdd:TIGR02169 221 REYEGY--ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 901 LQVQMENTLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQG 980
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 981 ELKIAVlqktelenklqqqltqaaQELAAEKEKISVLQNNYEKSQETFKQLQSDFYGRESELLATRQDLKSVEEKLSLAQ 1060
Cdd:TIGR02169 379 EFAETR------------------DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1653960520 1061 EDLISNRNQIgnqNKLIQELKTAKATLEqdsaKKEQQLQERCKALQDIQKEKSLKEKEL 1119
Cdd:TIGR02169 441 EEKEDKALEI---KKQEWKLEQLAADLS----KYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
397-596 |
3.44e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 397 QLQQQREEKEQHGLQLQSEINQLHSKLLETERQL---GEAHG--RLKEQRQLSSEKLMDKEQQVADLQLKLSRLEEQLke 471
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALeefRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARL-- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 472 kvtNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKEnisLLEKEREDLYA 551
Cdd:COG3206 243 ---AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA---QLQQEAQRILA 316
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1653960520 552 KIQagegetAVLNQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQE 596
Cdd:COG3206 317 SLE------AELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
366-989 |
3.51e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 366 ELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEKEQhglQLQSEINQLHSK-LLETERQLGEAHGRLKEQRQLS 444
Cdd:TIGR00618 247 QKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINR---ARKAAPLAAHIKaVTQIEQQAQRIHTELQSKMRSR 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 445 SEKLMDKEQQVADlqlklsRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQK 524
Cdd:TIGR00618 324 AKLLMKRAAHVKQ------QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 525 IQNLEALLQKSKENISLLEKEREDLYAKIQAGEGETavlnQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQENLHDQVQE 604
Cdd:TIGR00618 398 LCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ----ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQ 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 605 QKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTAQRADLQNHlDTAQNALQDKQQELN 684
Cdd:TIGR00618 474 QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTY-AQLETSEEDVYHQLT 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 685 KITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEgqiKKLEADSLEVKASKEQALQDLQQQRQLNTDLE 764
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ---DLTEKLSEAEDMLACEQHALLRKLQPEQDLQD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 765 LRATELSKQLEMEKEIVSSTRLDL---------------QKKSEALESIKQKLTKQEEEKKILKQDFETLSQETKIQHEE 829
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQLtltqervrehalsirVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 830 LNnRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDS--------LKNSKSEFEKENQKGKAAILDLEKTcKELKHQL 901
Cdd:TIGR00618 710 ET-HIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElmhqartvLKARTEAHFNNNEEVTAALQTGAEL-SHLAAEI 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 902 QVQMENTLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNIN-ELKQSSEQKKKQIEALQG 980
Cdd:TIGR00618 788 QFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEIThQLLKYEECSKQLAQLTQE 867
|
....*....
gi 1653960520 981 ELKIAVLQK 989
Cdd:TIGR00618 868 QAKIIQLSD 876
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
530-738 |
4.05e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 530 ALLQKSKENISLLEKEREDLYAKIQAGEGEtavLNQLQEKNHTLQEQVTQLTEKLKNQSEshkqaqenlhdQVQEQKAHL 609
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKE---LAALKKEEKALLKQLAALERRIAALAR-----------RIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 610 RAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQI-----KAKTELLLSAEAAKTA------------QRADLQNHLDTA 672
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLRALyrlgrQPPLALLLSPEDFLDAvrrlqylkylapARREQAEELRAD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1653960520 673 QNALQDKQQELNKITTQLDQVTAKLQDKQEhcsQLESHLKEYKEKYLSLEQKTEELEGQIKKLEAD 738
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERA---ALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| FYVE1_Vac1p_like |
cd15761 |
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ... |
1349-1406 |
4.26e-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: 43.03 E-value: 4.26e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1653960520 1349 WAEDNEVQNCMACGKGFSVTVRRHHCRQCGNIFCAE-C--------SAKNalTPSSKKPVRVCDACF 1406
Cdd:cd15761 4 WKKPSGKSRCSECGKTLNKKNGIVNCRKCGELFCNEhCrnriklnnSAEY--DPKNGKWCRCCEKCF 68
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
258-822 |
4.48e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.30 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 258 LQSQYASSEATISQLRSELAKGPQEVAVYVQELQK-LKSSVNELTQKNQTLTENLLKKEQDYTKLEEKH----NEESVSK 332
Cdd:pfam12128 263 LHFGYKSDETLIASRQEERQETSAELNQLLRTLDDqWKEKRDELNGELSAADAAVAKDRSELEALEDQHgaflDADIETA 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 333 KNIQATLHQKDLDCQQLQSRLSASETSLHRIHVELSE-KGEATQKLKEELSEVETKYQHLK-AEFKQLQQQREEKEQHGL 410
Cdd:pfam12128 343 AADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRrRSKIKEQNNRDIAGIKDKLAKIReARDRQLAVAEDDLQALES 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 411 QLQSEINQLHSKLLETERQLGEAHGRLK---EQRQLSSEKLMDKEQQvadlQLKLSRLEEQLKEKVTNSTELQHQLDKTK 487
Cdd:pfam12128 423 ELREQLEAGKLEFNEEEYRLKSRLGELKlrlNQATATPELLLQLENF----DERIERAREEQEAANAEVERLQSELRQAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 488 QQHQEQQALQQSTTAKLREAQNDLEQVLRQIgdkDQKIQNLEALLQKS----KENIS-LLEKE---REDLYAKIQAGE-- 557
Cdd:pfam12128 499 KRRDQASEALRQASRRLEERQSALDELELQL---FPQAGTLLHFLRKEapdwEQSIGkVISPEllhRTDLDPEVWDGSvg 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 558 ------GETAVLNQLQ-----EKNHTLQEQVTQLTEKLKNQSESHKQA-------------------------------- 594
Cdd:pfam12128 576 gelnlyGVKLDLKRIDvpewaASEEELRERLDKAEEALQSAREKQAAAeeqlvqangelekasreetfartalknarldl 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 595 ------QENLHDQVQEQ-KAHLRAAQDRVLSLETSVNELNSQLNESKEK-------------------VSQLDIQIKAKT 648
Cdd:pfam12128 656 rrlfdeKQSEKDKKNKAlAERKDSANERLNSLEAQLKQLDKKHQAWLEEqkeqkreartekqaywqvvEGALDAQLALLK 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 649 ELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLS-------- 720
Cdd:pfam12128 736 AAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQrrprlatq 815
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 721 ---LEQKTEELEGQIKKLEADSlevkaskEQALQDLQQQRQLNTDLELRATELSKQLEMEKEIVSSTRLDlQKKSEALES 797
Cdd:pfam12128 816 lsnIERAISELQQQLARLIADT-------KLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKED-ANSEQAQGS 887
|
650 660
....*....|....*....|....*
gi 1653960520 798 IKQKLTKQEEEKKILKQDFETLSQE 822
Cdd:pfam12128 888 IGERLAQLEDLKLKRDYLSESVKKY 912
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
91-843 |
4.79e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 91 EVQDLQASLKEEKWYSEELKKELE--KYQGLQQQEAKPDGLVTDSSAELQSLEQQLEEAQTENFNIKQMKDLFEQKAAQL 168
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELElkMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTEL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 169 ATEIADIKSKYD--EERSLREAAEQKVTRLTEELNkeatviqDLKTELLQRPGIEDVAVLKKELVQVQTLMDNMTLERER 246
Cdd:TIGR00606 346 LVEQGRLQLQADrhQEHIRARDSLIQSLATRLELD-------GFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 247 ESEKLKDE-CKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQKNQTLTenllKKEQDYTKLEEKH 325
Cdd:TIGR00606 419 SKERLKQEqADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELR----KAERELSKAEKNS 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 326 NEESVSKKNIQATLHQKDLD-----CQQLQSRLSASETSLHRIHVELSEKGEATQKLKEELSEVETKYQHLKAEF---KQ 397
Cdd:TIGR00606 495 LTETLKKEVKSLQNEKADLDrklrkLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFpnkKQ 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 398 LQQQREEKEQHGLQLQSEINQLHSKLLETER---QLGEAHGRLKEQRQLSSEKLMDKeQQVADLQLKLSRLEEQLKEKVT 474
Cdd:TIGR00606 575 LEDWLHSKSKEINQTRDRLAKLNKELASLEQnknHINNELESKEEQLSSYEDKLFDV-CGSQDEESDLERLKEEIEKSSK 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 475 NSTELQHQLDKTKQQHQEQQALQQS----------TTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEK 544
Cdd:TIGR00606 654 QRAMLAGATAVYSQFITQLTDENQSccpvcqrvfqTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 545 EREDLYAKIQAGegetavLNQLQEKNHTLQEQVTQLTEKLKNQSEshkqaqenlhdQVQEQKAHLRAAQDrVLSLETSVN 624
Cdd:TIGR00606 734 GRQSIIDLKEKE------IPELRNKLQKVNRDIQRLKNDIEEQET-----------LLGTIMPEEESAKV-CLTDVTIME 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 625 ELNSQLNESKEKVSQLdiqikaktelllsaeaAKTAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHC 704
Cdd:TIGR00606 796 RFQMELKDVERKIAQQ----------------AAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 705 SQLESHLKEYKEKYLSLEQKTEELEGQIKKLEadslevKASKEQALQDLQQQRQLNTDLELrATELSKQLEMEKEIVSST 784
Cdd:TIGR00606 860 QHLKSKTNELKSEKLQIGTNLQRRQQFEEQLV------ELSTEVQSLIREIKDAKEQDSPL-ETFLEKDQQEKEELISSK 932
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1653960520 785 RLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETKIQHEELNNRIQTTVTELQK 843
Cdd:TIGR00606 933 ETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEK 991
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
592-745 |
6.63e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 592 KQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTAQraDLQNHLDT 671
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE--ALQKEIES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1653960520 672 AQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKylsLEQKTEELEGQIKKLEADSLEVKAS 745
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAAK 171
|
|
| PTZ00303 |
PTZ00303 |
phosphatidylinositol kinase; Provisional |
1325-1410 |
7.29e-05 |
|
phosphatidylinositol kinase; Provisional
Pssm-ID: 140324 [Multi-domain] Cd Length: 1374 Bit Score: 47.39 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1325 AAVQELGRENQSLQIKHTQAL-NRKWAEDNEVQN-CMACGKGF-----SVTVRRHHCRQCGNIFCAECSAKNA------- 1390
Cdd:PTZ00303 428 ATVGGVAEENELNTFGLTKLLhNPSWQKDDESSDsCPSCGRAFislsrPLGTRAHHCRSCGIRLCVFCITKRAhysfakl 507
|
90 100
....*....|....*....|...
gi 1653960520 1391 LTPSSKKPVR---VCDACFNDLQ 1410
Cdd:PTZ00303 508 AKPGSSDEAEerlVCDTCYKEYE 530
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
532-1174 |
7.90e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 532 LQKSKENISLLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLT---EKLKNQSESHKQAQENLhdQVQEQKAH 608
Cdd:TIGR00618 217 YHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRariEELRAQEAVLEETQERI--NRARKAAP 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 609 LRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAktellLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNKITT 688
Cdd:TIGR00618 295 LAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAA-----HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 689 QLDQVTAKLQdkqeHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQQrqlntdlelrat 768
Cdd:TIGR00618 370 ISCQQHTLTQ----HIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ------------ 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 769 ELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETKIQHEELNNRIQTTVTELQKVKMEK 848
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHP 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 849 EALMTELSTVKDKLSKVsDSLKNSKSEFEKENQKGKAAILDLEKTCKELKHQLQVQMENTLKEQKELKKSLEKEKEASHQ 928
Cdd:TIGR00618 514 NPARQDIDNPGPLTRRM-QRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNI 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 929 LKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKIAVLQKTELENKLQQQLTQAAQEla 1008
Cdd:TIGR00618 593 TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVL-- 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1009 aEKEKISVLQNNYEKSQETFKQLQSDFYGRESELLATRQDLKSVEEKLSLAQEdlisnrnQIGNQNKLIQELKTAKATLE 1088
Cdd:TIGR00618 671 -PKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE-------IENASSSLGSDLAAREDALN 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1089 QDSAKKEQQLQERCKALQDIQKEKSLKEKELVNEKSKLAEIE---EIKCRQEKEITKLNEELKSHKLESIKEITNLKDAK 1165
Cdd:TIGR00618 743 QSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAaeiQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQ 822
|
....*....
gi 1653960520 1166 QLLIQQKLE 1174
Cdd:TIGR00618 823 CETLVQEEE 831
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
243-472 |
8.84e-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: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 243 ERERESEKLKDECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQKNQTLTENLLKKEQDytkLE 322
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE---LE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 323 EKHNEESVSKKNIQATLHQKDLDCQQLQSRLSASETSLHRIHVELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQR 402
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 403 EEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKEqrqlsseklmdKEQQVADLQLKLSRLEEQLKEK 472
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAE-----------LQQEAEELEALIARLEAEAAAA 239
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
619-872 |
9.22e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 619 LETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQ 698
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 699 DkqehcsqLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSL--EVKASKEQALQDLQQQRQLNTDLELRATELSKQLEM 776
Cdd:PHA02562 252 D-------PSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 777 EKEIVSSTRlDLQKKSEAL----ESIKQKLTKQEEEKKILKQDFETLSQETKIQHEElnnrIQTTVTELQKVKMEKealm 852
Cdd:PHA02562 325 LEEIMDEFN-EQSKKLLELknkiSTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEE----LAKLQDELDKIVKTK---- 395
|
250 260
....*....|....*....|
gi 1653960520 853 TELSTVKDKLSKVSDSLKNS 872
Cdd:PHA02562 396 SELVKEKYHRGIVTDLLKDS 415
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
939-1185 |
9.61e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 9.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 939 QLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKIAvlqktelenklqqqltqaAQELAAEKEKISVLQ 1018
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL------------------QAEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1019 NNYEKSQETFKQLQSDFY--GRESELLATRQDLKSVEEKLslaqeDLISNRNQI-GNQNKLIQELKTAKATLEQDSAKKE 1095
Cdd:COG3883 79 AEIEERREELGERARALYrsGGSVSYLDVLLGSESFSDFL-----DRLSALSKIaDADADLLEELKADKAELEAKKAELE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1096 QQLQERCKALQDIQKEKSLKEKELVNEKSKLAEIEEIKCRQEKEITKLNEELKSHKLESIKEITNLKDAKQLLIQQKLEL 1175
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
250
....*....|
gi 1653960520 1176 QGKADSLKAA 1185
Cdd:COG3883 234 AAAAAAAAAA 243
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
90-487 |
1.22e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 90 QEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKPDGLVTDSSAELQSLEQQLEEAQTENFNIKQMKDLFEQKAAQL- 168
Cdd:PRK03918 276 EELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLe 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 169 -----ATEIADIKSKYDEERSLR---------------EAAEQKVTRLTEELNKEATVIQDLKTELLQRPgiEDVAVLKK 228
Cdd:PRK03918 356 eleerHELYEEAKAKKEELERLKkrltgltpeklekelEELEKAKEEIEEEISKITARIGELKKEIKELK--KAIEELKK 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 229 ELVQVQTLMDNMTLE-RERESEKLKDECKKLQSQYASSEATISQLRSELAK------GPQEVAVYVQELQKLKSSVNELT 301
Cdd:PRK03918 434 AKGKCPVCGRELTEEhRKELLEEYTAELKRIEKELKEIEEKERKLRKELRElekvlkKESELIKLKELAEQLKELEEKLK 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 302 QKNqtlTENLLKKEQDYTKLEEKHNEESVSKKNIQATLHQKDL---DCQQLQSRLSASETSLHRIHVELSEKG-EATQKL 377
Cdd:PRK03918 514 KYN---LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGfESVEEL 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 378 KEELSEVETKYQHLkAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQLSSE--------KLM 449
Cdd:PRK03918 591 EERLKELEPFYNEY-LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeelreEYL 669
|
410 420 430
....*....|....*....|....*....|....*...
gi 1653960520 450 DKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTK 487
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
784-1111 |
1.23e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 784 TRLDLQKKSEALESIKQkltkQEEEKKILKQDFE-TLSQETKIQH-----EELNNRIQTTVTELQKVKMEKEALMTELST 857
Cdd:PRK11281 37 TEADVQAQLDALNKQKL----LEAEDKLVQQDLEqTLALLDKIDRqkeetEQLKQQLAQAPAKLRQAQAELEALKDDNDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 858 VK-------------DKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKTCKELKH---QLQvQMENTLKEQKELKKSLEK 921
Cdd:PRK11281 113 ETretlstlslrqleSRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYAnsqRLQ-QIRNLLKGGKVGGKALRP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 922 EKEASHQLKLEL----NSMQEQLIQAQNTL---------------KQNEKEEQQLQGNINE--LKQSSEQKKKQIEA--- 977
Cdd:PRK11281 192 SQRVLLQAEQALlnaqNDLQRKSLEGNTQLqdllqkqrdyltariQRLEHQLQLLQEAINSkrLTLSEKTVQEAQSQdea 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 978 --------LQGELKI------AVLQKTELENKLQQQLTQAAQEL-------AAEKEKISVLQNNYEKSQETFKQLQSDFY 1036
Cdd:PRK11281 272 ariqanplVAQELEInlqlsqRLLKATEKLNTLTQQNLRVKNWLdrltqseRNIKEQISVLKGSLLLSRILYQQQQALPS 351
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1653960520 1037 GRESELLATR-QDLKsveeklsLAQEDLISNRNQIGNQNKLIQELKTAKATLEQDSAKK--EQQLQERCKALQDIQKE 1111
Cdd:PRK11281 352 ADLIEGLADRiADLR-------LEQFEINQQRDALFQPDAYIDKLEAGHKSEVTDEVRDalLQLLDERRELLDQLNKQ 422
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
74-341 |
1.47e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 74 GESN---LALKRDDVTLLRQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKPDGlVTDSSAELQSLEQQLEEAQTE 150
Cdd:COG4913 605 GFDNrakLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAELEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 151 NFNIKQMkdlfEQKAAQLATEIADIKSKYDEERSLREAAEQKVTRLTEELnKEATVIQDLKTELLQRPGIEDVAVLKKEL 230
Cdd:COG4913 684 SDDLAAL----EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL-DELQDRLEAAEDLARLELRALLEERFAAA 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 231 VQ---VQTLMDNMTLERERESEKLKDECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLKssvneltqknqtl 307
Cdd:COG4913 759 LGdavERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLE------------- 825
|
250 260 270
....*....|....*....|....*....|....
gi 1653960520 308 TENLLKKEQDYTKLEEKHNEESVSkkNIQATLHQ 341
Cdd:COG4913 826 EDGLPEYEERFKELLNENSIEFVA--DLLSKLRR 857
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
75-307 |
1.49e-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: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 75 ESNLALKRDD----VTLLRQEVQDLQASLkeekwysEELKKELEKYQgLQQQEAKPDGLVTDSSAELQSLEQQLEEAQTE 150
Cdd:COG3206 163 EQNLELRREEarkaLEFLEEQLPELRKEL-------EEAEAALEEFR-QKNGLVDLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 151 NFNIKQMKDLFEQKAAQLATEIADIKSK--YDEERSLREAAEQKVTRLTEELNKEATVIQDLKTELlqrpgiedvAVLKK 228
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI---------AALRA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 229 ELVQvqtlmdnmtlERERESEKLKDECKKLQSQYASSEATISQLRSELAKGP---QEVAVYVQELQKLKSSVNELTQKNQ 305
Cdd:COG3206 306 QLQQ----------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPeleAELRRLEREVEVARELYESLLQRLE 375
|
..
gi 1653960520 306 TL 307
Cdd:COG3206 376 EA 377
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
386-661 |
1.84e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 386 TKYQHLKAEFKQLQQQREEKeqhgLQLQSEINQLHSKLLETERQLGEAHGRLKE-QRQLssEKLmdKEQQVADLQLKLSR 464
Cdd:PRK11281 49 NKQKLLEAEDKLVQQDLEQT----LALLDKIDRQKEETEQLKQQLAQAPAKLRQaQAEL--EAL--KDDNDEETRETLST 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 465 LeeqlkekvtNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEK 544
Cdd:PRK11281 121 L---------SLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 545 EREDLYakiqagEGETAVLNQLQEKNHTLQEQVTQLTEKLKNQseshkqaqenlHDQVQEQKAHLraaQDRVLSLETSVN 624
Cdd:PRK11281 192 SQRVLL------QAEQALLNAQNDLQRKSLEGNTQLQDLLQKQ-----------RDYLTARIQRL---EHQLQLLQEAIN 251
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1653960520 625 ELNsqLNESKEKVSQLDIQ---IKAKTELLLSAEAAKTAQ 661
Cdd:PRK11281 252 SKR--LTLSEKTVQEAQSQdeaARIQANPLVAQELEINLQ 289
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
375-563 |
1.90e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 375 QKLKEELSEVETKYQHLKAEFK--QLQQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQ-----LSSEK 447
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDalpelLQSPV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 448 LMDKEQQVADLQLKLSRLEE----------QLKEKVTN-STELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLR 516
Cdd:COG3206 265 IQQLRAQLAELEAELAELSArytpnhpdviALRAQIAAlRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLA 344
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1653960520 517 QIGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGEGETAVL 563
Cdd:COG3206 345 ELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVI 391
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
893-1118 |
2.02e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 893 TCKELKHQLqvqmeNTLKEQKelkkSLEKEKEASHQlklELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSseqkK 972
Cdd:PRK11281 37 TEADVQAQL-----DALNKQK----LLEAEDKLVQQ---DLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQA----Q 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 973 KQIEALQGELKIAVLQK------TELE---NKLQQQLTQAAQELAAEKEKISVLQ-----------NNYEKSQETFKQLQ 1032
Cdd:PRK11281 101 AELEALKDDNDEETRETlstlslRQLEsrlAQTLDQLQNAQNDLAEYNSQLVSLQtqperaqaalyANSQRLQQIRNLLK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1033 SDFYGRESeLLATRQDLKSVEEKLSLAQEDLisNRNQIGNQNKLiQELKTAKATLeqdSAKKEQQLQERCKALQDIQKEK 1112
Cdd:PRK11281 181 GGKVGGKA-LRPSQRVLLQAEQALLNAQNDL--QRKSLEGNTQL-QDLLQKQRDY---LTARIQRLEHQLQLLQEAINSK 253
|
....*.
gi 1653960520 1113 SLKEKE 1118
Cdd:PRK11281 254 RLTLSE 259
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
88-702 |
2.03e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 88 LRQEVQDLQASLKEEKwYSEELKKELEKYQGLQ-QQEAKPDGLVTDSSAELQSLEQQLEEAQtenfnikQMKDLFEQKAA 166
Cdd:PRK04863 518 LRMRLSELEQRLRQQQ-RAERLLAEFCKRLGKNlDDEDELEQLQEELEARLESLSESVSEAR-------ERRMALRQQLE 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 167 QLATEIADIKSKYDEERslreAAEQKVTRLTEELNKEATVIQDLkTELLQrpgieDVAVLKKELVQVQTlmdnmtlERER 246
Cdd:PRK04863 590 QLQARIQRLAARAPAWL----AAQDALARLREQSGEEFEDSQDV-TEYMQ-----QLLERERELTVERD-------ELAA 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 247 ESEKLKDECKKLQSQYASSEATISQLRSEL----------------------AKGPQEVAVYVQELqklkSSVNELTQKN 304
Cdd:PRK04863 653 RKQALDEEIERLSQPGGSEDPRLNALAERFggvllseiyddvsledapyfsaLYGPARHAIVVPDL----SDAAEQLAGL 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 305 QTLTENLLKKEQDYTKLEEkhneeSVSKkniqATLHQKDLdCQQL---QSRLS-----------ASETSLHRIHVELSEK 370
Cdd:PRK04863 729 EDCPEDLYLIEGDPDSFDD-----SVFS----VEELEKAV-VVKIadrQWRYSrfpevplfgraAREKRIEQLRAEREEL 798
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 371 GEATQKLKEELSEVETKYQHLK----------------AEFKQLQQQREEKEQHGLQLQSEINQLHSKLleteRQLGEAH 434
Cdd:PRK04863 799 AERYATLSFDVQKLQRLHQAFSrfigshlavafeadpeAELRQLNRRRVELERALADHESQEQQQRSQL----EQAKEGL 874
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 435 GRLkeQRQLSSEKLMDKEqqvaDLQLKLSRLEEQLKEkvtnstelqhqldktkqqhqeqqalqqsttakLREAQNDleqv 514
Cdd:PRK04863 875 SAL--NRLLPRLNLLADE----TLADRVEEIREQLDE--------------------------------AEEAKRF---- 912
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 515 LRQIGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGEGETAVLNQL-QEKNH-------TLQEQVTQLTEKLKN 586
Cdd:PRK04863 913 VQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVvQRRAHfsyedaaEMLAKNSDLNEKLRQ 992
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 587 QSESHKQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAktelllSAEAAKTAQRADLQ 666
Cdd:PRK04863 993 RLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADS------GAEERARARRDELH 1066
|
650 660 670
....*....|....*....|....*....|....*.
gi 1653960520 667 NHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQE 702
Cdd:PRK04863 1067 ARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLER 1102
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
892-1112 |
2.06e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 892 KTCKELKHQLQVQMENTLKEQKELKKsLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNE-----KEEQQLQGNINELKQ 966
Cdd:PHA02562 184 QTLDMKIDHIQQQIKTYNKNIEEQRK-KNGENIARKQNKYDELVEEAKTIKAEIEELTDEllnlvMDIEDPSAALNKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 967 SSEQKKKQIEALQGELKIavLQKTELENKLQQQLTQAAQELAAEKEKISVLQNNYEKSQETFKQLQSdfygRESELLATR 1046
Cdd:PHA02562 263 AAAKIKSKIEQFQKVIKM--YEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEE----IMDEFNEQS 336
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1653960520 1047 QDLKSVEEKLSLAQEDLISNRNQIGNQNKLIQELKTAKATLEQDSAKKEQQLQERCKALQDIQKEK 1112
Cdd:PHA02562 337 KKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
375-1031 |
2.35e-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: 45.73 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 375 QKLKEELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLletERQLGEAHGRLKEQRQLSSEKLMDKEQQ 454
Cdd:TIGR00618 197 ELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYL---TQKREAQEEQLKKQQLLKQLRARIEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 455 VADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQK 534
Cdd:TIGR00618 274 AQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 535 SKENISLLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQEN------------LHDQV 602
Cdd:TIGR00618 354 EIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTsafrdlqgqlahAKKQQ 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 603 QEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKtELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQE 682
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK-EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 683 LNKITTQLD-----------------QVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKAS 745
Cdd:TIGR00618 513 PNPARQDIDnpgpltrrmqrgeqtyaQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNI 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 746 KEQALQDLQQQRQLNTDLELratELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETKI 825
Cdd:TIGR00618 593 TVRLQDLTEKLSEAEDMLAC---EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRV 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 826 QHEELNNRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKTCKELKHqlqvqm 905
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ------ 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 906 enTLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLqgnINELKQSSEQKKKQIEALQGELKIA 985
Cdd:TIGR00618 744 --SLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRL---REEDTHLLKTLEAEIGQEIPSDEDI 818
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1653960520 986 VLQKTELENKLQQQLTQAAQELAAEKEKISVLQNNYEKSQETFKQL 1031
Cdd:TIGR00618 819 LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQL 864
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
689-949 |
2.50e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 689 QLDQVTAKLQDKQ----EHCSQLESHlkEYKEKYLSLEQKTEELegqIKKLEADSlevkaSKEQALQDLQQQRQLNTDLE 764
Cdd:PRK05771 17 YKDEVLEALHELGvvhiEDLKEELSN--ERLRKLRSLLTKLSEA---LDKLRSYL-----PKLNPLREEKKKVSVKSLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 765 LRATELSKQLEMEKEIVSstrldLQKKSEALESIKQKLTKQEEEKKILK---------QDFETLSQET-KIQHEELNNRI 834
Cdd:PRK05771 87 LIKDVEEELEKIEKEIKE-----LEEEISELENEIKELEQEIERLEPWGnfdldlsllLGFKYVSVFVgTVPEDKLEELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 835 QTTVTELQKVKMEKEALMTELS-TVKDKLSKVSDSLKnsKSEFEKENqkgkaaiLDLEKTCKELKHQLQVQMENTLKEQK 913
Cdd:PRK05771 162 LESDVENVEYISTDKGYVYVVVvVLKELSDEVEEELK--KLGFERLE-------LEEEGTPSELIREIKEELEEIEKERE 232
|
250 260 270
....*....|....*....|....*....|....*.
gi 1653960520 914 ELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQ 949
Cdd:PRK05771 233 SLLEELKELAKKYLEELLALYEYLEIELERAEALSK 268
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
248-747 |
2.57e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 248 SEKLKDECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQKNqtltENLLKKEQDYTKLEEKhne 327
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELE----KELESLEGSKRKLEEK--- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 328 esvsKKNIQATLHQKDLDCQQLQSRLSASEtslhrihvELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQR---EE 404
Cdd:PRK03918 261 ----IRELEERIEELKKEIEELEEKVKELK--------ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngiEE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 405 KEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQLSSEKLMDKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLD 484
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 485 KTKQQHQEQQALQQSTTA---KLREAQNDLEQVLRQIGDKDQK--IQNLEALLQKSKENISLLEKEREDLYAKIQAGEGE 559
Cdd:PRK03918 409 KITARIGELKKEIKELKKaieELKKAKGKCPVCGRELTEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 560 TAVLNQLQeKNHTLQEQVTQLTEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDRVLS-------LETSVNELNSQLNE 632
Cdd:PRK03918 489 LKKESELI-KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKelekleeLKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 633 SKEKVSQLDIQIKA---KTELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLES 709
Cdd:PRK03918 568 LEEELAELLKELEElgfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1653960520 710 HLKEYK-----EKYLSLEQKTEELEGQIKKLEADSLEVKASKE 747
Cdd:PRK03918 648 ELEELEkkyseEEYEELREEYLELSRELAGLRAELEELEKRRE 690
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
545-752 |
2.83e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 545 EREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLtEKLKNQSESHKQAQENLhDQVQEQKAHLRA--AQDRVLSLETS 622
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIELL-EPIRELAERYAAARERL-AELEYLRAALRLwfAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 623 VNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAA----KTAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQ 698
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQirgnGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1653960520 699 DKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQD 752
Cdd:COG4913 377 ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
379-815 |
3.06e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 379 EELSEVETKYQH---LKAEFKQLQQQREEKEqhglqlqSEINQLHSKLLETERQLGEAhgrlKEQRQLSSEKLMDKEQQV 455
Cdd:pfam10174 272 EEIKQMEVYKSHskfMKNKIDQLKQELSKKE-------SELLALQTKLETLTNQNSDC----KQHIEVLKESLTAKEQRA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 456 ADLQLKLSRLEEQLKEKvtnstelQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKS 535
Cdd:pfam10174 341 AILQTEVDALRLRLEEK-------ESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDK 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 536 KENISLLEKEREDLYAKIQAGEGETAVLNQ-LQEKNHT---LQEQVTQLTEKLKNQSESHKQAQENLHDQVQEQKAHLRA 611
Cdd:pfam10174 414 DKQLAGLKERVKSLQTDSSNTDTALTTLEEaLSEKERIierLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 612 AQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTE-------LLLSAEAAKTAQRA--DLQNHLDTAQNALQDKQQE 682
Cdd:pfam10174 494 KESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEecsklenQLKKAHNAEEAVRTnpEINDRIRLLEQEVARYKEE 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 683 LNKITTQLDQVTAKLQ-------DKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEvKASKEQALQDLQQ 755
Cdd:pfam10174 574 SGKAQAEVERLLGILReveneknDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLE-EARRREDNLADNS 652
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 756 QRQLNTDLELRATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQD 815
Cdd:pfam10174 653 QQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQE 712
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
370-473 |
3.08e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.46 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 370 KGEATQKLKEELSEVETKYQHLKAEFKQLQQQ-REEKE--QHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQLSSE 446
Cdd:COG0542 431 KKEQDEASFERLAELRDELAELEEELEALKARwEAEKEliEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLRE 510
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1653960520 447 --------------------KLMDKEQQvadlqlKLSRLEEQLKEKV 473
Cdd:COG0542 511 evteediaevvsrwtgipvgKLLEGERE------KLLNLEEELHERV 551
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
333-719 |
3.33e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 333 KNIQA--TLHQKDLdCQQLQSRLSAsetslhrihveLSEKGEATQKLKeelsevetKYQHLKAEF----KQLQQQREEKE 406
Cdd:PRK10929 33 EQAKAakTPAQAEI-VEALQSALNW-----------LEERKGSLERAK--------QYQQVIDNFpklsAELRQQLNNER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 407 QHGL---------QLQSEINQLHSKLLETERQLGEAHGRLKEqrqlSSEKLMDKEQQVADLQLKLSRLEEQLKEKVTNST 477
Cdd:PRK10929 93 DEPRsvppnmstdALEQEILQVSSQLLEKSRQAQQEQDRARE----ISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 478 EL-QHQLDKTKqqhqEQQALQQSTTAKLREAQ---NDLEQVLRQIGDKDQK-IQNLEALLQKSKENISLLEK-------E 545
Cdd:PRK10929 169 PLaQAQLTALQ----AESAALKALVDELELAQlsaNNRQELARLRSELAKKrSQQLDAYLQALRNQLNSQRQreaeralE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 546 REDLYAKiQAGEGETAVLNQLQeKNHTLQEQVTQLTEKLKNQSESHKQAQENLHdQVQEQKAHLRaAQDRVLSLETSVNE 625
Cdd:PRK10929 245 STELLAE-QSGDLPKSIVAQFK-INRELSQALNQQAQRMDLIASQQRQAASQTL-QVRQALNTLR-EQSQWLGVSNALGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 626 -LNSQLNESKE--KVSQLD---IQIKAKT---ELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQE-----LNKITTQLD 691
Cdd:PRK10929 321 aLRAQVARLPEmpKPQQLDtemAQLRVQRlryEDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRtqrelLNSLLSGGD 400
|
410 420 430
....*....|....*....|....*....|.
gi 1653960520 692 QVTAKLQDKQEHCSQLESHLKEYKE---KYL 719
Cdd:PRK10929 401 TLILELTKLKVANSQLEDALKEVNEathRYL 431
|
|
| FYVE_CARP1 |
cd15769 |
FYVE-like domain found in caspase regulator CARP1 and similar proteins; CARP1, also termed E3 ... |
1358-1405 |
3.62e-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: 39.59 E-value: 3.62e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1653960520 1358 CMACGKGFSVTVRRHHCRQCGNIFCAECSAknaltpsSKKPVRVCDAC 1405
Cdd:cd15769 4 CKACGLAFSVFRKKHVCCDCKKDFCSVCSV-------LQENLRRCSTC 44
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
566-946 |
4.25e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 45.05 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 566 LQEKNHTLQEQVTQLTEKlkNQSESHKQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIK 645
Cdd:pfam05911 485 LQDINDSLPEADSCLSSG--HPSTDASCDYITCKENSSVVEKEGSVSGDDKSSEETSKQSIQQDLSKAISKIIDFVEGLS 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 646 AKTELLLSAEAAKTAQRADLQNHLDTAQNALQDKQqELNKITTQLDQVTAKLQdkqEHCSQL--------ESHLKEYKEK 717
Cdd:pfam05911 563 KEALDDQDTSSDSSELSEVLQQFSATCNDVLSGKA-DLEDFVLELSHILDWIS---NHCFSLldvssmedEIKKHDCIDK 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 718 YLSLEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRqlNTDLELRATELSKQLEMEKEIVSstrLDLQKKSEALES 797
Cdd:pfam05911 639 VTLSENKVAQVDNGCSEIDNLSSDPEIPSDGPLVSGSNDL--KTEENKRLKEEFEQLKSEKENLE---VELASCTENLES 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 798 IKQKLTKQEEEKKILKQDFETLsqetkiqhEELNNRIQTtvtELQKVKMEKEALMTELSTVKDKLSKVSDSLKNSKSEFE 877
Cdd:pfam05911 714 TKSQLQESEQLIAELRSELASL--------KESNSLAET---QLKCMAESYEDLETRLTELEAELNELRQKFEALEVELE 782
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1653960520 878 KENQKGKaailDLEKTCKELKHQLQVqmentlKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNT 946
Cdd:pfam05911 783 EEKNCHE----ELEAKCLELQEQLER------NEKKESSNCDADQEDKKLQQEKEITAASEKLAECQET 841
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
502-738 |
4.35e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 502 AKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEK--------EREDLYAKIQAGEGEtavLNQLQEKNHTL 573
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanllADETLADRLEELREE---LDAAQEAQAFI 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 574 QEQVTQLT--EKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDRVLSLETSVN--------ELNSQLNESKEKVSQLDIQ 643
Cdd:COG3096 913 QQHGKALAqlEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQrrphfsyeDAVGLLGENSDLNEKLRAR 992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 644 I-KAKTELLLSAEAAKTAQ---------RADLQNHLDTAQNALQDKQQELNKITTQLDQVTA-----KLQDKQEHCSQLE 708
Cdd:COG3096 993 LeQAEEARREAREQLRQAQaqysqynqvLASLKSSRDAKQQTLQELEQELEELGVQADAEAEerariRRDELHEELSQNR 1072
|
250 260 270
....*....|....*....|....*....|
gi 1653960520 709 SHLKEYKEKYLSLEQKTEELEGQIKKLEAD 738
Cdd:COG3096 1073 SRRSQLEKQLTRCEAEMDSLQKRLRKAERD 1102
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
88-543 |
4.47e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.68 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 88 LRQEVQDLQ---ASLKEEKwysEELKKELEKYQGLQQQEAKPDGLVTDSSAELQSLEQQLEEAQTENFNIKQMKDLFEQK 164
Cdd:pfam05622 12 LAQRCHELDqqvSLLQEEK---NSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 165 AAQLATEIADIKSKYDEERSLREAA-----EQKVTRLT-EELNKEATVIQDLKTELlqrpgiEDVAVLKKelvQVQTLMD 238
Cdd:pfam05622 89 CEELEKEVLELQHRNEELTSLAEEAqalkdEMDILRESsDKVKKLEATVETYKKKL------EDLGDLRR---QVKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 239 NMTLERERESEkLKDECKKLQSqyasseatisqLRSELakgpqevAVYVQELQKLKSSVNELTQKNQTLtenllkkEQDY 318
Cdd:pfam05622 160 RNAEYMQRTLQ-LEEELKKANA-----------LRGQL-------ETYKRQVQELHGKLSEESKKADKL-------EFEY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 319 TKLEEKHNEESVSKKNIQA---TLHQ--KDLDCQQLQSRlsasetSLHRIHVELSEKGEATQKLKEEL--SEVETKYQHL 391
Cdd:pfam05622 214 KKLEEKLEALQKEKERLIIerdTLREtnEELRCAQLQQA------ELSQADALLSPSSDPGDNLAAEImpAEIREKLIRL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 392 KAEFKQLQQQREEKEQhglqlqseinqlhSKLLETERQLGEAHGR---LKEQRQLSSEKLMDKEQQVADLQLKLSRLEEQ 468
Cdd:pfam05622 288 QHENKMLRLGQEGSYR-------------ERLTELQQLLEDANRRkneLETQNRLANQRILELQQQVEELQKALQEQGSK 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1653960520 469 LKEKVTNSTELQHQLDKTKQQHQEQQalqqsttaKLREAQNDLEQVLRQigDKDQKIQNLEALLQKSKENISLLE 543
Cdd:pfam05622 355 AEDSSLLKQKLEEHLEKLHEAQSELQ--------KKKEQIEELEPKQDS--NLAQKIDELQEALRKKDEDMKAME 419
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
513-696 |
4.50e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.95 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 513 QVLRQIGDKDqkiqnLEALLQKSKENISLLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEKLKNQSESHK 592
Cdd:pfam00529 46 DVLFQLDPTD-----YQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 593 QAQENLHDQVQEQKAHLRAAQdrvlSLETSVNELNSQLNESKEKVSQLDIQIKAKTelllsaeAAKTAQRADLQNHLDTA 672
Cdd:pfam00529 121 QAQIDLARRRVLAPIGGISRE----SLVTAGALVAQAQANLLATVAQLDQIYVQIT-------QSAAENQAEVRSELSGA 189
|
170 180
....*....|....*....|....
gi 1653960520 673 QNALQDKQQELNKITTQLDQVTAK 696
Cdd:pfam00529 190 QLQIAEAEAELKLAKLDLERTEIR 213
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
584-702 |
4.69e-04 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 44.33 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 584 LKNQSESHKQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLdiqikaktelllSAEAAKTAQra 663
Cdd:TIGR04320 252 PPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANA------------QAQALQTAQ-- 317
|
90 100 110
....*....|....*....|....*....|....*....
gi 1653960520 664 dlqNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQE 702
Cdd:TIGR04320 318 ---NNLATAQAALANAEARLAKAKEALANLNADLAKKQA 353
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
163-404 |
5.15e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 163 QKAAQLATEIADIKSKYDEERSlREAAEQKVTRLTEELNKEATVIQDLKTEL---LQRPGIEDVAVLKKELVQVQTlmdn 239
Cdd:COG3206 148 ELAAAVANALAEAYLEQNLELR-REEARKALEFLEEQLPELRKELEEAEAALeefRQKNGLVDLSEEAKLLLQQLS---- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 240 mTLEREREseklkdeckKLQSQYASSEATISQLRSELAKGPQEVAVYVQ--ELQKLKSSVNELTQKNQTLTENLLKKEQD 317
Cdd:COG3206 223 -ELESQLA---------EARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 318 YTKLEEKHNE-ESVSKKNIQATLHQKDLDCQQLQSRLSASETSLhrihVELSEKGEATQKLKEELSEVETKYQHLKAEFK 396
Cdd:COG3206 293 VIALRAQIAAlRAQLQQEAQRILASLEAELEALQAREASLQAQL----AQLEARLAELPELEAELRRLEREVEVARELYE 368
|
....*...
gi 1653960520 397 QLQQQREE 404
Cdd:COG3206 369 SLLQRLEE 376
|
|
| FYVE_CARP2 |
cd15770 |
FYVE-like domain found in caspase regulator CARP2 and similar proteins; CARP2, also termed E3 ... |
1356-1394 |
5.34e-04 |
|
FYVE-like domain found in caspase regulator CARP2 and similar proteins; CARP2, also termed E3 ubiquitin-protein ligase rififylin, or caspases-8 and -10-associated RING finger protein 2, or FYVE-RING finger protein Sakura (Fring), or RING finger and FYVE-like domain-containing protein 1, or RING finger protein 189, or RING finger protein 34-like, is a novel caspase regulator containing a FYVE-type zinc finger domain. It regulates the p53 signaling pathway through degrading 14-3-3 sigma and stabilizing MDM2. CARP2 does not localize to membranes in the cell and is involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, CARP2 has an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus it belongs to a family of unique FYVE-type domains called FYVE-like domains. In addition to the N-terminal FYVE-like domain, CARP2 harbors a C-terminal RING domain.
Pssm-ID: 277309 Cd Length: 49 Bit Score: 39.06 E-value: 5.34e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1653960520 1356 QNCMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALTPS 1394
Cdd:cd15770 2 ISCKACGIRFASCARKHPCMDCKKNYCTACSSQAENGPS 40
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
132-323 |
7.10e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 132 DSSAELQSLEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEERSLREAAEQKVTRLTEELNKEATVIQDLK 211
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 212 TEL------LQRPGIEDVAVLK------KELVQVQTLMDNMTLERERESEKLKDECKKLQSQYASSEATISQLRSELAKG 279
Cdd:COG4942 104 EELaellraLYRLGRQPPLALLlspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1653960520 280 PQEVAVYVQELQKLKSSVNELTQKNQTLTENLLKKEQDYTKLEE 323
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
45-616 |
7.50e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 45 QCMKSLGSADELFKHY-----EAVHDAGNDSGH-----GGESNLALKRDDVTLLRQEVQDLQ--ASLKEEKWYSEELKKE 112
Cdd:COG4913 201 QSFKPIGDLDDFVREYmleepDTFEAADALVEHfddleRAHEALEDAREQIELLEPIRELAEryAAARERLAELEYLRAA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 113 LEKYQGLQQQEAKpDGLVTDSSAELQSLEQQLEEAQTENFNIKQMKDLFEQKAAQ--------LATEIADIKSKYDEERS 184
Cdd:COG4913 281 LRLWFAQRRLELL-EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 185 LREAAEQKVTRLTEELNKEATVIQDLKTELLQRpgiedVAVLKKELVQVQTLMDnmtlERERESEKLKDECKKLQSQYAS 264
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRAEAAAL-----LEALEEELEALEEALA----EAEAALRDLRRELRELEAEIAS 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 265 SEATIS-------QLRSELAK--GPQEVAV-YVQELQKLKSSVN------ELTQKNQTLTenLLKKEQDY---------T 319
Cdd:COG4913 431 LERRKSniparllALRDALAEalGLDEAELpFVGELIEVRPEEErwrgaiERVLGGFALT--LLVPPEHYaaalrwvnrL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 320 KLEEKHNEESVSKKniqatlhqkdldcQQLQSRLSASETSLhrIHVELSEKGEATQKLKEELSE------VET-----KY 388
Cdd:COG4913 509 HLRGRLVYERVRTG-------------LPDPERPRLDPDSL--AGKLDFKPHPFRAWLEAELGRrfdyvcVDSpeelrRH 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 389 Q---------HLKAEFKQLQQQREEKEQH--GLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQlsseklmdKEQQVAD 457
Cdd:COG4913 574 PraitragqvKGNGTRHEKDDRRRIRSRYvlGFDNRAKLAALEAELAELEEELAEAEERLEALEA--------ELDALQE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 458 LQLKLSRLEEQLKEKVtNSTELQHQLDKTKQQHqeqqalqqsttAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKE 537
Cdd:COG4913 646 RREALQRLAEYSWDEI-DVASAEREIAELEAEL-----------ERLDASSDDLAALEEQLEELEAELEELEEELDELKG 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 538 NISLLEKEREDLYAKIQAGEGETAVLNQLQEknhtlQEQVTQLTEKLKN--QSESHKQAQENLHDQVQEQKAHLRAAQDR 615
Cdd:COG4913 714 EIGRLEKELEQAEEELDELQDRLEAAEDLAR-----LELRALLEERFAAalGDAVERELRENLEERIDALRARLNRAEEE 788
|
.
gi 1653960520 616 V 616
Cdd:COG4913 789 L 789
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
537-702 |
8.47e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 537 ENISLLEKEREDLYAKIqagegetAVLNQL----QEKNHTLQEQVTQLTEKLkNQSESHKQAQENLHDQVQEQKAhlraa 612
Cdd:PRK09039 46 REISGKDSALDRLNSQI-------AELADLlsleRQGNQDLQDSVANLRASL-SAAEAERSRLQALLAELAGAGA----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 613 qdrvlSLETSVNELNSQLNESKekvsQLDIQIKAKTELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNKITTQLDq 692
Cdd:PRK09039 113 -----AAEGRAGELAQELDSEK----QVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLN- 182
|
170
....*....|
gi 1653960520 693 vTAKLQDKQE 702
Cdd:PRK09039 183 -VALAQRVQE 191
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1074-1297 |
8.62e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1074 NKLIQELKTAKATLEQDSAKKEQQlQERCKALQDIQKEKSLKEKELVNEKSKLAEIEEIKCRQEKEITKLNEELKSHK-- 1151
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREQA-RETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRer 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1152 -LESIKEITNLKDAKQL-------LIQQKLELQGKADSLKAAVEQEKRNQQILKDQVK------KEEEELKKEFIEKEAK 1217
Cdd:PRK02224 288 lEELEEERDDLLAEAGLddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAEslredaDDLEERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1218 LHSEIKEKEVGMKKHEENEAKLTMQITALNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVQNNQD---ERRA 1294
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARErveEAEA 447
|
...
gi 1653960520 1295 LLE 1297
Cdd:PRK02224 448 LLE 450
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
882-994 |
8.87e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 882 KGKAAILDLEKTCKELKHQLQVQMENTLKEQ--------KELKKSLEKEkeaSHQLKLELNSMQEQLIQAQNTLKQNEKE 953
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEAlleakeeiHKLRNEFEKE---LRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1653960520 954 EQQLQGNINELKQSSEQKKKQIEALQGELKIAVL-QKTELEN 994
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEeQLQELER 146
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
840-1069 |
1.00e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 840 ELQKVKMEKEALMTELSTVKDKLSKvsdsLKNSKSEFEKENQKGKAAILDLEKTCKELKHQLQV---QMENTLKEQKELK 916
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA----LKKEEKALLKQLAALERRIAALARRIRALEQELAAleaELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 917 KSLEKEKEashQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKIAVLQKTELENKL 996
Cdd:COG4942 97 AELEAQKE---ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1653960520 997 QQQLTQaaqeLAAEKEKISVLQNNYEKSQETFKQLQSDFYGRESELLATRQDLKSVEEKLSLAQEDLISNRNQ 1069
Cdd:COG4942 174 AELEAL----LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
87-646 |
1.30e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 87 LLRQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKPDGLVTDSSAELQSLEQQLEEAQTENFNIKQ-MKDL--FEQ 163
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSaLNELssLED 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 164 KAAQLATEIADIKSKydeeRSLREAAEQKVTRLTEELNKeatVIQDlkTELLQRPGIEDVAVLKKELVQVQTLMDNMTLE 243
Cdd:PRK01156 250 MKNRYESEIKTAESD----LSMELEKNNYYKELEERHMK---IIND--PVYKNRNYINDYFKYKNDIENKKQILSNIDAE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 244 RERESEKLKdECKKLQSQYasSEATISQLRSElakgpqevavyvqELQKLKSSVNELTQKNQTLTENLlkkEQDYTKLEE 323
Cdd:PRK01156 321 INKYHAIIK-KLSVLQKDY--NDYIKKKSRYD-------------DLNNQILELEGYEMDYNSYLKSI---ESLKKKIEE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 324 KHNEESVSKKNIQATLHQKDLDCQQLQSRLSASETSLHRIHVELSEKGEATQKLKEELSEVETKYQHLKAEFKQL---QQ 400
Cdd:PRK01156 382 YSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPvcgTT 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 401 QREEKEQHGLQLQSE-INQLHSKLLETERQLGEAHGRLKEQRQLSS--------------EKLMDKEQQVADLQLKLSRL 465
Cdd:PRK01156 462 LGEEKSNHIINHYNEkKSRLEEKIREIEIEVKDIDEKIVDLKKRKEyleseeinksineyNKIESARADLEDIKIKINEL 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 466 E------EQLKEKVtNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQ-NLEALLQKSKEN 538
Cdd:PRK01156 542 KdkhdkyEEIKNRY-KSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEiGFPDDKSYIDKS 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 539 ISLLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQE------NLHDQVQEQKAHLRAA 612
Cdd:PRK01156 621 IREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDiednlkKSRKALDDAKANRARL 700
|
570 580 590
....*....|....*....|....*....|....
gi 1653960520 613 QDRVLSLETSVNELNSQLNESKEKVSQLDIQIKA 646
Cdd:PRK01156 701 ESTIEILRTRINELSDRINDINETLESMKKIKKA 734
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
61-397 |
1.36e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 61 EAVHDAGNDSGhGGESNLALKRDDVTLLRQEVQDLQASLKEEKWYSEELKKELEKYQ----GLQQQEAKPDGLVTDSSAE 136
Cdd:PRK02224 398 ERFGDAPVDLG-NAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecGQPVEGSPHVETIEEDRER 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 137 LQSLEQQLEEAQTENFNIKQMKDLFEQkAAQLATEIADIKSKYDEERSL----REAAEQKVTRLtEELNKEAtviQDLKT 212
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELiaerRETIEEKRERA-EELRERA---AELEA 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 213 EllqrpgiedvAVLKKELVQvqtlmdnmtlERERESEKLKDECKKLQSQYASSEATISQLRsELAKGPQEVAVYVQELQK 292
Cdd:PRK02224 552 E----------AEEKREAAA----------EAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIER 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 293 LKSSVNELTQKNQTLTENLLKKEQDYTKLEEKHNEESVSK------------KNIQATLHQKDLDCQQLQSRLSASETSL 360
Cdd:PRK02224 611 LREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEaredkeraeeylEQVEEKLDELREERDDLQAEIGAVENEL 690
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1653960520 361 HRI------HVELSEKGEATQKLKEELSEVETKYQHLKAEFKQ 397
Cdd:PRK02224 691 EELeelrerREALENRVEALEALYDEAEELESMYGDLRAELRQ 733
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
766-1157 |
1.56e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.11 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 766 RATELSKQLEMEKEIVSSTRLDLqkkseaLESIKQKLTKQEEEKKILkqdfetlsqetkiqHEELNNRIQTTVTELQKVK 845
Cdd:PTZ00108 996 RKEYLLGKLERELARLSNKVRFI------KHVINGELVITNAKKKDL--------------VKELKKLGYVRFKDIIKKK 1055
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 846 MEKealmtelSTVKDKLSKVSDSLKNSKS-EFEKENQKGKAAILDLEKT--CKELKHQLQVQMENTLKEQKELKKS---- 918
Cdd:PTZ00108 1056 SEK-------ITAEEEEGAEEDDEADDEDdEEELGAAVSYDYLLSMPIWslTKEKVEKLNAELEKKEKELEKLKNTtpkd 1128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 919 -----LEKEKEA--SHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKIAVLQKTE 991
Cdd:PTZ00108 1129 mwledLDKFEEAleEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRK 1208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 992 LENKLQQQLTQAAQELAAEKEKISVLQNNYEKSQETFKQLQSDFYGRESEllATRQDLKSVEEKLSLAQEDLISNRNQIG 1071
Cdd:PTZ00108 1209 LDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDND--EFSSDDLSKEGKPKNAPKRVSAVQYSPP 1286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1072 NQNKLIQELKTAKATLEQDSAKKEQQLqercKALQDIQKEKSLKEKELVNEKSKLAEiEEIKCRQEKEiTKLNEELKSHK 1151
Cdd:PTZ00108 1287 PPSKRPDGESNGGSKPSSPTKKKVKKR----LEGSLAALKKKKKSEKKTARKKKSKT-RVKQASASQS-SRLLRRPRKKK 1360
|
....*.
gi 1653960520 1152 LESIKE 1157
Cdd:PTZ00108 1361 SDSSSE 1366
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
463-737 |
1.92e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 463 SRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLRE---AQNDLEQVLRQIGDKDQKIQNLEALLQKSKENI 539
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAElneAESDLEQDYQAASDHLNLVQTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 540 SLLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEKLKN-------------QSESHKQA------------ 594
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADyqqaldvqqtraiQYQQAVQAlerakqlcglpd 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 595 --QENLHDQVQEQKAHLRAAQDRVLSLETSVN---ELNSQLNESKEKVSQLDIQIKAKT------ELLLSAEAAK--TAQ 661
Cdd:PRK04863 435 ltADNAEDWLEEFQAKEQEATEELLSLEQKLSvaqAAHSQFEQAYQLVRKIAGEVSRSEawdvarELLRRLREQRhlAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 662 RADLQNHLDTAQNALQdKQQELNKITTQLDQVTAK-------LQDKQEHCSQLESHLKEYK----EKYLSLEQKTEELEG 730
Cdd:PRK04863 515 LQQLRMRLSELEQRLR-QQQRAERLLAEFCKRLGKnlddedeLEQLQEELEARLESLSESVsearERRMALRQQLEQLQA 593
|
....*..
gi 1653960520 731 QIKKLEA 737
Cdd:PRK04863 594 RIQRLAA 600
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
244-636 |
2.09e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.58 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 244 RERESEKLKDECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQEL-QKLKSSVNELTQKN-QTLTENLLKKEQDYTKL 321
Cdd:PLN02939 40 RGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELpQKSTSSDDDHNRASmQRDEAIAAIDNEQQTNS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 322 EEKHNEESVSKKNIQATLHQKDLDCQQL-QSRLSAsetsLHRIHVELSEKgeatQKLKEELSEVETKYQHLKAEFKQLQQ 400
Cdd:PLN02939 120 KDGEQLSDFQLEDLVGMIQNAEKNILLLnQARLQA----LEDLEKILTEK----EALQGKINILEMRLSETDARIKLAAQ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 401 QREEKEQHGLQLQSEINQLhskLLETERQLGEAHGRLKEQRQLSSEKLMDKeqqvADLQLklsrleeqLKEKVTNSTELQ 480
Cdd:PLN02939 192 EKIHVEILEEQLEKLRNEL---LIRGATEGLCVHSLSKELDVLKEENMLLK----DDIQF--------LKAELIEVAETE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 481 HQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVL-RQIGDKDQKIQNLEALLQKSK---ENISLLEKEREDLYAKIQAG 556
Cdd:PLN02939 257 ERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSpLQYDCWWEKVENLQDLLDRATnqvEKAALVLDQNQDLRDKVDKL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 557 EGETAVLNQLQEKNhtlqEQVTQLTEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDrvlsletsvnELNSQLNESKEK 636
Cdd:PLN02939 337 EASLKEANVSKFSS----YKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQD----------TLSKLKEESKKR 402
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
136-639 |
2.09e-03 |
|
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: 42.80 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 136 ELQSLEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEERSLREAAEQKVTRLTEELNKEATVIQDLKTELL 215
Cdd:pfam15921 343 KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 216 QRpgiedvavlkkelvqvqtlmdNMTLER-ERESEKLKDECkklQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLK 294
Cdd:pfam15921 423 DR---------------------NMEVQRlEALLKAMKSEC---QGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 295 SSVNELTQKNQTLTENLLKKEQDYTKLEEKHNEESVSKKNIQATLHQKDLDCQQLQ------SRLSASETSLHRIHVELS 368
Cdd:pfam15921 479 KVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQhlknegDHLRNVQTECEALKLQMA 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 369 EKGEATQKLKEELSEV-ETKYQH------LKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQR 441
Cdd:pfam15921 559 EKDKVIEILRQQIENMtQLVGQHgrtagaMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLV 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 442 QLSSEKLmdkeQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAK----LREAQNDLEQVLRQ 517
Cdd:pfam15921 639 NAGSERL----RAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKlkmqLKSAQSELEQTRNT 714
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 518 IGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAgeGETAVLNQLQEKnHTLQEQVTQLTEKLKN-QSESHKQAQE 596
Cdd:pfam15921 715 LKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQF--LEEAMTNANKEK-HFLKEEKNKLSQELSTvATEKNKMAGE 791
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1653960520 597 nlhdqVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQ 639
Cdd:pfam15921 792 -----LEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQR 829
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
135-568 |
2.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 135 AELQSLEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEERSLREAAE-----QKVTRLTEELNKEATVIQD 209
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 210 LKTELLQ-RPGIEDVAVLKKELVQVQT----LMDNMTLERERESEKLKDECKKLQSQYASSEATISQLRSELAKGPQEVA 284
Cdd:COG4717 151 LEERLEElRELEEELEELEAELAELQEeleeLLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 285 VYVQEL--QKLKSSVNELTQKNQTLTENLLKKEQDYTKLEEKHNEESVSKKNIQATLhqkdLDCQQLQSRLSASETSLHR 362
Cdd:COG4717 231 QLENELeaAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLA----LLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 363 IHVELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQ 442
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 443 LssEKLMDKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTkqqhqEQQALQQSTTAKLREAQNDLEQVLRQIGDKD 522
Cdd:COG4717 387 L--RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE-----ELEEELEELEEELEELEEELEELREELAELE 459
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1653960520 523 QKIQNLEallqkSKENISLLEKEREDLYAKIQAGEGETAVLNQLQE 568
Cdd:COG4717 460 AELEQLE-----EDGELAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
108-733 |
2.41e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 108 ELKKELEKYQGLQQQEAKPDGLVTDSSAELQSLEQQLEEAQTENfnikqmkdlfeqkaaQLATEIADIKSKYDEERSLRE 187
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQT---------------QQSHAYLTQKREAQEEQLKKQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 188 AAEQKVTRLTEELNKEATVIQDLKTELLQRPGIEDVAVLKKELVQVQTLMDNMTLERERESEKLKDECKKLQSQYASSEA 267
Cdd:TIGR00618 260 QLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSS 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 268 TISQLRSELAKGPQEVAVYVQELQKLksSVNELTQKNQTLTENLLKKEQDYTKLEEKHN---EESVSKKNIQATLHQKDL 344
Cdd:TIGR00618 340 IEEQRRLLQTLHSQEIHIRDAHEVAT--SIREISCQQHTLTQHIHTLQQQKTTLTQKLQslcKELDILQREQATIDTRTS 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 345 DCQQLQSRLSASETSLHRIHVELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEKEQHGLQlQSEINQLHSKLL 424
Cdd:TIGR00618 418 AFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ-ETRKKAVVLARL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 425 ----ETERQLGEAHGRLKEQRQLSSE------KLMDKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQ 494
Cdd:TIGR00618 497 lelqEEPCPLCGSCIHPNPARQDIDNpgpltrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILT 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 495 ALQQSTTAKLREAQNDLEQVLRQIGdkdqkiQNLEALLQKSKENISLLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQ 574
Cdd:TIGR00618 577 QCDNRSKEDIPNLQNITVRLQDLTE------KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 575 EQVTQLTEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSA 654
Cdd:TIGR00618 651 LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSL 730
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1653960520 655 EAAKTAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIK 733
Cdd:TIGR00618 731 GSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIG 809
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
372-565 |
2.43e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 372 EATQKLKEELSEVEtKYQHLKAEFKQLQQQREEKEQHGLQLQSeinqlhsklleTERQLGEAHGRLkeQRQLSSEKLMDK 451
Cdd:PRK04863 493 EAWDVARELLRRLR-EQRHLAEQLQQLRMRLSELEQRLRQQQR-----------AERLLAEFCKRL--GKNLDDEDELEQ 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 452 EQqvADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQalqqSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEAL 531
Cdd:PRK04863 559 LQ--EELEARLESLSESVSEARERRMALRQQLEQLQARIQRLA----ARAPAWLAAQDALARLREQSGEEFEDSQDVTEY 632
|
170 180 190
....*....|....*....|....*....|....
gi 1653960520 532 LQKSKENISLLEKEREDLYAKIQAGEGETAVLNQ 565
Cdd:PRK04863 633 MQQLLERERELTVERDELAARKQALDEEIERLSQ 666
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
840-983 |
2.43e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 840 ELQKVKMEKEALMTELSTVKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKtckelkhQLQvQMENTLKEQKELkksL 919
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEK-------RLL-QKEENLDRKLEL---L 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1653960520 920 EKEKEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELkqSSEQKKKQI-EALQGELK 983
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL--TAEEAKEILlEKVEEEAR 168
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
542-1333 |
2.47e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 542 LEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQENLHD------QVQEQKAHLRAAQDR 615
Cdd:TIGR00606 191 LRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPlknrlkEIEHNLSKIMKLDNE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 616 VLSLETSVNE---LNSQLNESKEKVSQ-LDIQIKAKTELLLSAEAAKTAQRADLQNHLDTAQNALQDKQQELNKITTQLD 691
Cdd:TIGR00606 271 IKALKSRKKQmekDNSELELKMEKVFQgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQG 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 692 QVTAKLQDKQEHC---------SQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQLNTD 762
Cdd:TIGR00606 351 RLQLQADRHQEHIrardsliqsLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 763 LELRATELSKQLEMEKEIVSSTRLDLQKKSEALESIK----------QKLTKQEEEKKILKQDFET---LSQETKIQHEE 829
Cdd:TIGR00606 431 IRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEgssdrileldQELRKAERELSKAEKNSLTetlKKEVKSLQNEK 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 830 LN--NRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDSLKNSKSEfeKENQKGKAAILDLEKTCKELKHQLQVQMEN 907
Cdd:TIGR00606 511 ADldRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRH--SDELTSLLGYFPNKKQLEDWLHSKSKEINQ 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 908 TLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQnEKEEQQLQGNINELKQSSEQKKKQIEALQGELKIAVL 987
Cdd:TIGR00606 589 TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD-VCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQ 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 988 QKTELENKLQQQLTQAAQELAAEKEK---ISVLQNNYEKSQETFKQLQSDFY--------------GRESELLATRQDLK 1050
Cdd:TIGR00606 668 FITQLTDENQSCCPVCQRVFQTEAELqefISDLQSKLRLAPDKLKSTESELKkkekrrdemlglapGRQSIIDLKEKEIP 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1051 SVEEKLSLAQEDLISNRNQIGNQNKLIQ----ELKTAKA-------------TLEQDSAKKEQQLQER-----CKALQDI 1108
Cdd:TIGR00606 748 ELRNKLQKVNRDIQRLKNDIEEQETLLGtimpEEESAKVcltdvtimerfqmELKDVERKIAQQAAKLqgsdlDRTVQQV 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1109 QKEKSLKEKELVNEKSKLAEIEEIKCRQEKEITKLNE---ELKSHKLESIKEITNLKDAKQLLIQQKLELQGKADSLKAA 1185
Cdd:TIGR00606 828 NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1186 VEQEKRNQQILKDqvkkeeeelkkefiekeaklhsEIKEKEVGMKKHEENEAKLTMQITALNENLGTVKKEWQSSQRRVS 1265
Cdd:TIGR00606 908 KEQDSPLETFLEK----------------------DQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1653960520 1266 E-LEKQTDDLRGEIAVLEATVQNNQDERRALLE--RCLKGEGEIEKLQTKVLELQRKLDNTTAAVQELGRE 1333
Cdd:TIGR00606 966 DgKDDYLKQKETELNTVNAQLEECEKHQEKINEdmRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEE 1036
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
410-1116 |
2.54e-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: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 410 LQLQSEINQLHSKLLEterqLGEAHGRLKEQRQLSSEKLMDKEQQVADLQLKLSRLEEQLKEKVTnstELQHQLDKTKQQ 489
Cdd:pfam12128 244 TKLQQEFNTLESAELR----LSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRD---ELNGELSAADAA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 490 HQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSkenISLLEKEREDLYAKIQAGEGETAV-LNQLQE 568
Cdd:pfam12128 317 VAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEER---LKALTGKHQDVTAKYNRRRSKIKEqNNRDIA 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 569 KNHTLQEQVTQLTEKLKNQSESHKQAQEN-LHDQVQEQKAHLRAAQDRvlsLETSVNELNSQLNeSKEKVSQLDIQIKAK 647
Cdd:pfam12128 394 GIKDKLAKIREARDRQLAVAEDDLQALESeLREQLEAGKLEFNEEEYR---LKSRLGELKLRLN-QATATPELLLQLENF 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 648 TELLLSAEAAKTAQRADLQnhldtaqnalqDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKylsLEQKTEE 727
Cdd:pfam12128 470 DERIERAREEQEAANAEVE-----------RLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQ---LFPQAGT 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 728 LegqikkLEADSLEVKASKEQALQDLQQQRQLNTDLELRATELSKQLEMEkeiVSSTRLDLQKkSEALESIKQkltkqEE 807
Cdd:pfam12128 536 L------LHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELN---LYGVKLDLKR-IDVPEWAAS-----EE 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 808 EKKILKQDFETLSQETKIQHEELNNRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDslknsksefEKENQKGKaai 887
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD---------EKQSEKDK--- 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 888 ldLEKTCKELKHQLQVQMENTLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNekeeqQLQGNINELKQS 967
Cdd:pfam12128 669 --KNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDA-----QLALLKAAIAAR 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 968 SEQKKKQIEALQGELKIAvLQKTELENKLQQQLTQAAQELAAEKEKISVLQNNYEK----SQETFKQ----LQSDFYGRE 1039
Cdd:pfam12128 742 RSGAKAELKALETWYKRD-LASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRyfdwYQETWLQrrprLATQLSNIE 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1040 SELLATRQDLKSVEEKLSLAQEDLISNRNQIGNQNKLIQEL---------KTAKATLEQDSAKKEQQLQERCKALQDIQ- 1109
Cdd:pfam12128 821 RAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENlrglrcemsKLATLKEDANSEQAQGSIGERLAQLEDLKl 900
|
....*..
gi 1653960520 1110 KEKSLKE 1116
Cdd:pfam12128 901 KRDYLSE 907
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
85-979 |
2.69e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.51 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 85 VTLLRQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKPDGLVTDSSAELQSLEQQLEEAQTENFNIKQMKDLFEQk 164
Cdd:PTZ00440 452 INELKKSINQLKTLISIMKSFYDLIISEKDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEDYYIT- 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 165 aaqlateIADIKSKYDEERSLREAAEQKVTRLTEELNKEATVIQDLKTELLQRPG----IEDVAVLKKELVQVQTLMDNM 240
Cdd:PTZ00440 531 -------IEGLKNEIEGLIELIKYYLQSIETLIKDEKLKRSMKNDIKNKIKYIEEnvdhIKDIISLNDEIDNIIQQIEEL 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 241 TLERERESEKLKDECKKLQsqyasseATISQLRSELAKGPQEVAVYVQE--LQKLKSSVNELTQKNQtLTENLLKKEQDY 318
Cdd:PTZ00440 604 INEALFNKEKFINEKNDLQ-------EKVKYILNKFYKGDLQELLDELShfLDDHKYLYHEAKSKED-LQTLLNTSKNEY 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 319 TKLEEKHNEesvskkNIQATLHQKDldcQQLQSRLSASETSLHRIHVELSekgeatQKLKEELSEVETKYQHLKAEFKQL 398
Cdd:PTZ00440 676 EKLEFMKSD------NIDNIIKNLK---KELQNLLSLKENIIKKQLNNIE------QDISNSLNQYTIKYNDLKSSIEEY 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 399 QQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAHGrLKEQRQLSSEKLMDKEQQVADlQLKLSRLEEQLKEKVTNSTE 478
Cdd:PTZ00440 741 KEEEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKN-TYEEFLQYKDTILNKENKISN-DINILKENKKNNQDLLNSYN 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 479 LQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEKeredLYAKIQAGEG 558
Cdd:PTZ00440 819 ILIQKLEAHTEKNDEELKQLLQKFPTEDENLNLKELEKEFNENNQIVDNIIKDIENMNKNINIIKT----LNIAINRSNS 894
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 559 ETAVLNQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDrvlslETSVNELNSQLNESKEKVS 638
Cdd:PTZ00440 895 NKQLVEHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKLNLLNNLNKEKEKIEKQLS-----DTKINNLKMQIEKTLEYYD 969
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 639 QLDIQIKAKTELLLSAEAAKTAQRADLQ---NHLDTAQNALQDK------QQELNKITTQLDQVTAKLQDKQEHCSQLES 709
Cdd:PTZ00440 970 KSKENINGNDGTHLEKLDKEKDEWEHFKseiDKLNVNYNILNKKiddlikKQHDDIIELIDKLIKEKGKEIEEKVDQYIS 1049
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 710 HLKEYKEKYLSLE-------QKTEELEGQIKKLEAdslEVKASKEQALQDLQQQRQLNTDLELRATELSKQLEMEKEIVS 782
Cdd:PTZ00440 1050 LLEKMKTKLSSFHfnidikkYKNPKIKEEIKLLEE---KVEALLKKIDENKNKLIEIKNKSHEHVVNADKEKNKQTEHYN 1126
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 783 STRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETKIQHEELNNRIQTTVTELQKVKMEKEALMTELSTVKDKL 862
Cdd:PTZ00440 1127 KKKKSLEKIYKQMEKTLKELENMNLEDITLNEVNEIEIEYERILIDHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKNM 1206
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 863 SK-------------VSDSLKNSKSEFEK-----ENQKGKAAILDLEKTCKELKHQLQVQMENTLKEQKELKKSLEKEKE 924
Cdd:PTZ00440 1207 SKerndhlttfeynaYYDKATASYENIEEltteaKGLKGEANRSTNVDELKEIKLQVFSYLQQVIKENNKMENALHEIKN 1286
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1653960520 925 ASHQLKLE---------LNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQ 979
Cdd:PTZ00440 1287 MYEFLISIdsekilkeiLNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAKEHKNKIYGSLE 1350
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
253-485 |
2.77e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 253 DECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQKNQTLTENLLKKEQDYTKLEEKHNEESVSK 332
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 333 KNIQATLhQKDLDCQQLQSRLSASETSLHRihvelsekgeatqklkEELSEVETKYQHLKaefkQLQQQREEKEQHGLQL 412
Cdd:COG4942 100 EAQKEEL-AELLRALYRLGRQPPLALLLSP----------------EDFLDAVRRLQYLK----YLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1653960520 413 QSEINQLHSKLLETERQLGEAHGRLKEQRQLSSEKLMDKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDK 485
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
904-1112 |
2.89e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 904 QMENTLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELK 983
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 984 IAVLQKTELEnklQQQLTQAAQELAAEKEKISVLQNNYEKSQETFKQLQSDFYGRESELLATRQDLKSVEEKLSLAQEDL 1063
Cdd:COG3883 97 RSGGSVSYLD---VLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1653960520 1064 ISNRNQignQNKLIQELKTAKATLEQDSAKKEQQLQERCKALQDIQKEK 1112
Cdd:COG3883 174 EAQQAE---QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
75-588 |
3.23e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 75 ESNLALKRDDVTLLRQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKPDGLVTDSSAELQSLEQQLEEAQTENFNI 154
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 155 -KQMKDLFE-QKAAQLATEIADIKSKYDEERSLREAAEQKVTRLTEELNKEATVIQDLKTELLQRPGIE-----DVAVLK 227
Cdd:PRK03918 279 eEKVKELKElKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLkelekRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 228 ---KELVQVQTLMDNMTLERERES----EKLKDECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLKSSVNEL 300
Cdd:PRK03918 359 erhELYEEAKAKKEELERLKKRLTgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 301 TQKNQTLTE----NLLKK--------EQDYTKLEEKHNEESVSKKNIQATLHQ--KDLDCQQLQSRLSASETSLHRIHVE 366
Cdd:PRK03918 439 PVCGRELTEehrkELLEEytaelkriEKELKEIEEKERKLRKELRELEKVLKKesELIKLKELAEQLKELEEKLKKYNLE 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 367 -LSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEKEqhglQLQSEINQLHSKLLETERQLG--------EAHGRL 437
Cdd:PRK03918 519 eLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA----ELEKKLDELEEELAELLKELEelgfesveELEERL 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 438 KEQRQLSSE--KLMDKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQqsTTAKLREAQNDLEQVL 515
Cdd:PRK03918 595 KELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEELREEYLELS 672
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1653960520 516 RQIGDKDQKIQNLEALLQKSKENISLLEKEREdlyaKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEKLKNQS 588
Cdd:PRK03918 673 RELAGLRAELEELEKRREEIKKTLEKLKEELE----EREKAKKELEKLEKALERVEELREKVKKYKALLKERA 741
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
360-518 |
3.32e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 360 LHRIHVELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAHGrLKE 439
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-NKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1653960520 440 QRQLSSEklmdkeqqVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQI 518
Cdd:COG1579 91 YEALQKE--------IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
300-640 |
3.39e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 300 LTQKNQTLTENLLKKEQDYTKLEEKHNEESVSKKNIQATLHQKDLDCQQLQSRLSASETSLHRIHVELSEKGEATQKLKE 379
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 380 ELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQLSSEKLMDKEQQVADLQ 459
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 460 LKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENI 539
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 540 SLLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDRVLSL 619
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
330 340
....*....|....*....|.
gi 1653960520 620 ETSVNELNSQLNESKEKVSQL 640
Cdd:COG4372 349 GLLDNDVLELLSKGAEAGVAD 369
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
375-609 |
3.53e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.60 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 375 QKLKEELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHS-KL-------LETERQLGEAHGRLKEQRQLSSE 446
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAaALqpgeeeeLEEERRRLSNAEKLREALQEALE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 447 KLMDKEQQVADLqlkLSRLEEQLKEKVTNSTELQHQLDKTkqqhqeqqalqQSTTAKLREAQNDLEQVLRQI-------G 519
Cdd:COG0497 234 ALSGGEGGALDL---LGQALRALERLAEYDPSLAELAERL-----------ESALIELEEAASELRRYLDSLefdperlE 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 520 DKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEKLknqSESHKQAQENLH 599
Cdd:COG0497 300 EVEERLALLRRLARKYGVTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKL---SAARKKAAKKLE 376
|
250
....*....|
gi 1653960520 600 DQVQEQKAHL 609
Cdd:COG0497 377 KAVTAELADL 386
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
136-392 |
3.95e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 136 ELQSLEQQLEEAQTEnfnIKQMKDLFEQKAAQLATEIADIKSKYDEERSLREAAEQKVTRLTEELnkEATVIQDLKTEll 215
Cdd:PHA02562 182 QIQTLDMKIDHIQQQ---IKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDEL--LNLVMDIEDPS-- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 216 qrpgiEDVAVLKKELVQVQTLMDnmTLERERESEKLKDECKKLQSQYASSEATISQLR---SELAKGPQEVAVYVQELQK 292
Cdd:PHA02562 255 -----AALNKLNTAAAKIKSKIE--QFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKdklKELQHSLEKLDTAIDELEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 293 LKSSVNELTQKNQTLTENLLKKEQDYTKLEEKhneesvsKKNIQATLhqkdldcQQLQSRLSASETSLHRIHVELSEKGE 372
Cdd:PHA02562 328 IMDEFNEQSKKLLELKNKISTNKQSLITLVDK-------AKKVKAAI-------EELQAEFVDNAEELAKLQDELDKIVK 393
|
250 260
....*....|....*....|
gi 1653960520 373 ATQKLKEELSEVETKYQHLK 392
Cdd:PHA02562 394 TKSELVKEKYHRGIVTDLLK 413
|
|
| PHD2_KMT2A |
cd15590 |
PHD finger 2 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, ... |
1358-1405 |
4.21e-03 |
|
PHD finger 2 found in histone-lysine N-methyltransferase 2A (KMT2A); KMT2A (also termed ALL-1, CXXC-type zinc finger protein 7, myeloid/lymphoid or mixed-lineage leukemia protein 1 (MLL1), trithorax-like protein (Htrx), or zinc finger protein HRX) is a histone methyltransferase that belongs to the MLL subfamily of H3K4-specific histone lysine methyltransferases (KMT2). It regulates chromatin-mediated transcription through the catalysis of methylation of histone 3 lysine 4 (H3K4), and is frequently rearranged in acute leukemia. KMT2A functions as the catalytic subunit in the MLL1 complex, which also contains WDR5, RbBP5, ASH2L and DPY30 as integral core subunits required for the efficient methylation activity of the complex. The MLL1 complex is highly active and specific for H3K4 methylation. KMT2A contains a CxxC (x for any residue) zinc finger domain, three plant homeodomain (PHD) fingers, a Bromodomain domain, an extended PHD (ePHD) finger, Cys2HisCys5HisCys2His, two FY (phenylalanine tyrosine)-rich domains, and a SET (Suppressor of variegation, Enhancer of zeste, Trithorax) domain. This model corresponds to the second PHD finger.
Pssm-ID: 277065 Cd Length: 50 Bit Score: 36.54 E-value: 4.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1653960520 1358 CMACGKGFSVTVRRHHCRQCGNIFCAECSAKNALT-PSSKKPVRVCDAC 1405
Cdd:cd15590 2 CHVCGRQHQATKQLLECNKCRNSYHPECLGPNYPTkPTKKKRVWICTKC 50
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
107-303 |
4.23e-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: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 107 EELKKELEKYQGLQQQEAKPDGLVTDSSAELQSLEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYDEERSL- 185
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 186 --REAAEQKVTRLT-----------EELNKEATVIQDLKTELLQRpgIEDVAVLKKELVQVQTLMDNMTLERERESEKLK 252
Cdd:COG4942 107 aeLLRALYRLGRQPplalllspedfLDAVRRLQYLKYLAPARREQ--AEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1653960520 253 DECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQK 303
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
247-549 |
4.47e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 247 ESEKLKDECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQKNQTLTENLLKKEQDYTKLEEKHN 326
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 327 EESVSKKNIQATLHQKDLDCQQLQSRLSASETSLHRIHVELSEKGEATQKLKEELSEVETkyQHLKAEFKQLQQQREEKE 406
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEAEQALDELLKEANRNA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 407 QHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQLSSEKLMDKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKT 486
Cdd:COG4372 197 EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEE 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1653960520 487 KQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEKEREDL 549
Cdd:COG4372 277 ELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
924-1175 |
4.64e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 924 EASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKIAvlqKTELENKLQQQLTQA 1003
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQA---QAELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1004 AQELaaekEKISVlqnnyeksqetfKQLqsdfygrESELLATRQDLKSVEEKLSLAQEDLISNRNQ-------IGNQNKL 1076
Cdd:PRK11281 115 RETL----STLSL------------RQL-------ESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQperaqaaLYANSQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1077 IQE----LKTAKATLEQDSAKKEQQLQERCKAL--QDIQKEKSLKEKELVNE--KSKLAEIEEIKCRQEKEITKLNEELK 1148
Cdd:PRK11281 172 LQQirnlLKGGKVGGKALRPSQRVLLQAEQALLnaQNDLQRKSLEGNTQLQDllQKQRDYLTARIQRLEHQLQLLQEAIN 251
|
250 260 270
....*....|....*....|....*....|....*
gi 1653960520 1149 SHKL----ESIKEITNLKDAKQL----LIQQKLEL 1175
Cdd:PRK11281 252 SKRLtlseKTVQEAQSQDEAARIqanpLVAQELEI 286
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
75-539 |
4.73e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 75 ESNLALKRDDVTLLRQEVQDLQASLKEEKWYSEELKKELEKYQGLQQQEAKpdglvtdsSAELQSLEQQLEEAQTEnfnI 154
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL--------EAELAELPERLEELEER---L 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 155 KQMKDLFEQKAAQLATEIADIKSKYDEERSLREAAEQKVTRLTEELNKEATVIQDLKTELlqrpgiedvAVLKKELVQVQ 234
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL---------EEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 235 TLMDNMTLERERESEKLKDECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLKSSVNELTQKNQTltenllKK 314
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKA------SL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 315 EQDYTKLEEKHNEESVSKKNIQATLHQKDLDCQQLQSRLSASETSLHRIHVELSEKGEATQKLKEELSEvetkyQHLKAE 394
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE-----QEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 395 FKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAHGRLKEQRQLSSEKLMdkEQQVADLQLKLSRLEEQLKEKVT 474
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEELEELRE 453
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1653960520 475 NSTELQHQLDKTKQQHqeqqalqqsTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENI 539
Cdd:COG4717 454 ELAELEAELEQLEEDG---------ELAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
675-1111 |
5.42e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 675 ALQDKQQELNKITTQLDQVT-AKLQDKQEHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEAdsLEVKASKEQALQDL 753
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE--LREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 754 QQQRQLNTDLELRATELSKQLEmekeivsstrlDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETKIQHEElnnR 833
Cdd:COG4717 128 LPLYQELEALEAELAELPERLE-----------ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---E 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 834 IQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDSLKNSKSEFEKENQKGK-----------AAILDLEKTCKELKHQ-- 900
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaAALLALLGLGGSLLSLil 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 901 ------------LQVQMENTLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKqss 968
Cdd:COG4717 274 tiagvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ--- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 969 eQKKKQIEALQGELKIAVLQKtELENKLQQQLTQAAQELAAEKEKISVLQNNYEKSQETFKQLQSDFYGRESELLATrqD 1048
Cdd:COG4717 351 -ELLREAEELEEELQLEELEQ-EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL--D 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1653960520 1049 LKSVEEKLSLAQEDLISNRNQIGNQNKLIQELKTAKATLEQDS--AKKEQQLQERCKALQDIQKE 1111
Cdd:COG4717 427 EEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEE 491
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
379-1106 |
5.49e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 379 EELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETERQLGEAH---GRLKEQRQLSSEKLMDKEQQV 455
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEemrARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 456 ADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKS 535
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 536 KENISLLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDR 615
Cdd:pfam01576 165 TSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 616 VLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTaqradlqnhldTAQNALQDKQQELNKITTQLDQVTA 695
Cdd:pfam01576 245 LQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARN-----------KAEKQRRDLGEELEALKTELEDTLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 696 KLQDKQEHCSQLESHLKEYKEkylSLEQKTEELEGQIkkleadslevkasKEQALQDLQQQRQLNTDLElRATELSKQLE 775
Cdd:pfam01576 314 TTAAQQELRSKREQEVTELKK---ALEEETRSHEAQL-------------QEMRQKHTQALEELTEQLE-QAKRNKANLE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 776 MEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETKIQHEELNNRIQTTVTELQKVKMEKEALMTEL 855
Cdd:pfam01576 377 KAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKN 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 856 STVKDKLSKVSDSLKNSKSEFEKENQKgKAAILDLEKTCKELKHQLQVQMENTLKEQKELKKSLEKEKEASHQLKLELNS 935
Cdd:pfam01576 457 IKLSKDVSSLESQLQDTQELLQEETRQ-KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 936 MQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELK---IAVLQKTELENKLQQQLTQAAQELAAEKE 1012
Cdd:pfam01576 536 DAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDdllVDLDHQRQLVSNLEKKQKKFDQMLAEEKA 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1013 KISVLQNNYEKSQETFKQLQSDFYGRESEL---LATRQDLKSVEEKLSLAQEDLISNRNQIGnqnKLIQELKTAKATLEQ 1089
Cdd:pfam01576 616 ISARYAEERDRAEAEAREKETRALSLARALeeaLEAKEELERTNKQLRAEMEDLVSSKDDVG---KNVHELERSKRALEQ 692
|
730
....*....|....*..
gi 1653960520 1090 DSAKKEQQLQERCKALQ 1106
Cdd:pfam01576 693 QVEEMKTQLEELEDELQ 709
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
417-595 |
5.55e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 417 NQLHSKLLETERQLGEAHGRLKEQRQLSSEKLMDKEQQVADLQLKLSRLEEQLKEKVTNSTELQHQLDKTKQQHQEQQAL 496
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 497 QQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGEGE----TAVLNQLQEKNHT 572
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEiaerEEELKELEEQLES 161
|
170 180
....*....|....*....|...
gi 1653960520 573 LQEQVTQLTEKLKNQSESHKQAQ 595
Cdd:COG4372 162 LQEELAALEQELQALSEAEAEQA 184
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
502-888 |
5.90e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 502 AKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEKERE--DLYAKIQAGEGE----TAVLNQLQEKNHTLQE 575
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAElaelPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 576 QVTQLTEKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAE 655
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 656 AAKTAQRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQ-----DKQEHCSQLESHLKEYKEKYLSLEQKTEELEG 730
Cdd:COG4717 241 LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLgllalLFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 731 QIKKLEADSLEVKASKEQALQDLQQQRQLNtDLELRATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKK 810
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQ-ELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQE 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 811 ILKQ-----------DFETLSQETKIQHEELNNRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDSLKNSKSEFEKE 879
Cdd:COG4717 400 LKEEleeleeqleelLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELE 479
|
....*....
gi 1653960520 880 NQKGKAAIL 888
Cdd:COG4717 480 ELKAELREL 488
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
787-1310 |
6.49e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 787 DLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETKIQHEELN----------------NRIQTTVTELQKVKMEKEA 850
Cdd:PRK01156 191 KLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlksalnelssledmkNRYESEIKTAESDLSMELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 851 LMTELSTVKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKTCKELKHQLQVQMENTLKEQkelkkslekEKEASHQLK 930
Cdd:PRK01156 271 KNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLS---------VLQKDYNDY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 931 LELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKKKQIEALQGE----LKIAVLQKTELE---NKLQQQLTQA 1003
Cdd:PRK01156 342 IKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFiseiLKIQEIDPDAIKkelNEINVKLQDI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1004 AQELAAEKEKISVLQNNYEKSQETFKQLQSD----FYGRESELLATRQDLKSVEEKLSLAQEDLISNRNQIGNQNKLIQE 1079
Cdd:PRK01156 422 SSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVD 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1080 LKTAKATLEQDSAKK----EQQLQERCKALQDIQ-KEKSLKEKEL----VNEKSKLAEIEEIKCRQEKEITKLN------ 1144
Cdd:PRK01156 502 LKKRKEYLESEEINKsineYNKIESARADLEDIKiKINELKDKHDkyeeIKNRYKSLKLEDLDSKRTSWLNALAvislid 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1145 -EELKSHKLESIKEITNLKDAKQLLIQQKLELQGKADSLKAAVEQEKRNQQILKDQVKKEEEELKKEFIEKEaklhsEIK 1223
Cdd:PRK01156 582 iETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKID-----NYK 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 1224 EKEVGMKKHEENEAKLTMQITALNENLGTVKKEWQSSQRRVSELEKQTDDLRGEIAVLEATVqnnqDERRALLERCLKGE 1303
Cdd:PRK01156 657 KQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI----NDINETLESMKKIK 732
|
....*..
gi 1653960520 1304 GEIEKLQ 1310
Cdd:PRK01156 733 KAIGDLK 739
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
828-993 |
6.67e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.13 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 828 EELNNRIQTTVTELQKVKMEKEALMTELSTVKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKTCKELKHQLQvQMEN 907
Cdd:pfam09787 50 EELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELR-YLEE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 908 TLKEQKELKKSLEKEKEAshqlklELNSMQEQLIQAQntlkQNEKEEQQLQGNINELKQSSEQKKKQIEALQGELKIAVL 987
Cdd:pfam09787 129 ELRRSKATLQSRIKDREA------EIEKLRNQLTSKS----QSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVL 198
|
....*.
gi 1653960520 988 QKTELE 993
Cdd:pfam09787 199 QLERME 204
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
427-649 |
7.16e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 427 ERQLGEAHGRLKEQRqlssEKLMDKEQQVADLQLKLSRLEeQLKEKVTNSTELQHQLDktkqqhqeqqalqqstTAKLRE 506
Cdd:COG4913 220 EPDTFEAADALVEHF----DDLERAHEALEDAREQIELLE-PIRELAERYAAARERLA----------------ELEYLR 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 507 AQNDLEQVLRQIGDKDQKIQNLEALLQKSKENISLLEKEREDLYAKIQAGEGE-----TAVLNQLQEKNHTLQEQVTQLT 581
Cdd:COG4913 279 AALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgngGDRLEQLEREIERLERELEERE 358
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1653960520 582 EKLKNQSESHKQAQENLHDQVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTE 649
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
135-245 |
7.21e-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: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 135 AELQSLEQQLEEAQTENFNIKQMKDLFEQ-KAAQLATEIADIKSKYDEERSLREAAEQKVTRlteelnkeatvIQDLKTE 213
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFeRLAELRDELAELEEELEALKARWEAEKELIEE-----------IQELKEE 479
|
90 100 110
....*....|....*....|....*....|...
gi 1653960520 214 LLQRPGieDVAVLKKELVQVQT-LMDNMTLERE 245
Cdd:COG0542 480 LEQRYG--KIPELEKELAELEEeLAELAPLLRE 510
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
895-985 |
7.72e-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: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 895 KELKHQL-QVQMEntlkeqkelKKSLEKEKEASHQLKL-ELNSMQEQLIQAQNTLKQNEKEEQQLQGNINELKQSSEQKK 972
Cdd:COG0542 414 DELERRLeQLEIE---------KEALKKEQDEASFERLaELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRY 484
|
90
....*....|...
gi 1653960520 973 KQIEALQGELKIA 985
Cdd:COG0542 485 GKIPELEKELAEL 497
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
689-869 |
8.96e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 689 QLDQVTAKLQDKQ----EHCSQLESHLKEYKEKYLSLEQKTEELEGQIKKLEADsLEVKASKEQALQDLQQQRQLNtdlE 764
Cdd:PRK00409 517 KLNELIASLEELEreleQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE-AEKEAQQAIKEAKKEADEIIK---E 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 765 LRATELSKQLEMEKEIVSSTRLDLQKKSEALESIKQKLTKQEEEKKI--------LKQDFETLSQETKIQHEELNNRIQT 836
Cdd:PRK00409 593 LRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVgdevkylsLGQKGEVLSIPDDKEAIVQAGIMKM 672
|
170 180 190
....*....|....*....|....*....|....*
gi 1653960520 837 TV--TELQKVKMEKEALMTELSTVKDKLSKVSDSL 869
Cdd:PRK00409 673 KVplSDLEKIQKPKKKKKKKPKTVKPKPRTVSLEL 707
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
117-471 |
9.15e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.42 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 117 QGLQQQEAKPDGLVTDSSAELQSLEQQLEEAQTENFNIKQMK---DLFEQKAAQLATEIADIKskyDEERSLRE-----A 188
Cdd:PRK10929 30 QELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQYQqviDNFPKLSAELRQQLNNER---DEPRSVPPnmstdA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 189 AEQKV----TRLTEE---LNKEATVIQDLKTELLQRPGIEDVAvlKKELVQV----QTLMDNMTLERERESEKLKDECKK 257
Cdd:PRK10929 107 LEQEIlqvsSQLLEKsrqAQQEQDRAREISDSLSQLPQQQTEA--RRQLNEIerrlQTLGTPNTPLAQAQLTALQAESAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 258 LQSQY---------ASSEATISQLRSELAKgpQEVAVYVQELQKLKSSVNELTQKNQTL----TENLLKKEQDytkLEEK 324
Cdd:PRK10929 185 LKALVdelelaqlsANNRQELARLRSELAK--KRSQQLDAYLQALRNQLNSQRQREAERalesTELLAEQSGD---LPKS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 325 HNEESVSKKNIQATLHQ--KDLDCQQLQSRLSASET-----SLHRIHVE---LSEK---GEATQKLKEELSEVeTKYQHL 391
Cdd:PRK10929 260 IVAQFKINRELSQALNQqaQRMDLIASQQRQAASQTlqvrqALNTLREQsqwLGVSnalGEALRAQVARLPEM-PKPQQL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 392 KAEFKQLQQQR------EEKEQHGLQLQSEINQlhsKLLETERQLGEAhgRLKEQRQLSSEKLMDKEQQVADL-QLKL-- 462
Cdd:PRK10929 339 DTEMAQLRVQRlryedlLNKQPQLRQIRQADGQ---PLTAEQNRILDA--QLRTQRELLNSLLSGGDTLILELtKLKVan 413
|
....*....
gi 1653960520 463 SRLEEQLKE 471
Cdd:PRK10929 414 SQLEDALKE 422
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
349-469 |
9.52e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653960520 349 LQSRLSASETSLHRIHVELSEkgeatqkLKEELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLHSKLLETER 428
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAE-------LADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG 116
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1653960520 429 QLGEAHGRLKEQRQLSSEKLmdkeQQVADLQLKLSRLEEQL 469
Cdd:PRK09039 117 RAGELAQELDSEKQVSARAL----AQVELLNQQIAALRRQL 153
|
|
| |
