|
Name |
Accession |
Description |
Interval |
E-value |
| FYVE_FYCO1 |
cd15726 |
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ... |
970-1027 |
6.99e-37 |
|
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: 132.68 E-value: 6.99e-37
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1894925314 970 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1027
Cdd:cd15726 1 WQDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKACF 58
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
43-850 |
1.30e-27 |
|
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: 121.70 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 43 EVREKQLR---ERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCL 119
Cdd:TIGR02168 221 ELRELELAllvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 120 QGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIPSDAAQE 199
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 200 MQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQ-LKEDARASLERLVK-EMAPLQEELSGKGQEADQLWRRLQELL 277
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 278 AHTSSweeeLAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLER-- 355
Cdd:TIGR02168 461 EALEE----LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGye 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 356 ----LAGPPGPELPVAGEKNEALVPVNSSLQEAWGK------PEEEQRGLQEAQLDDTKVQEGSQE--EELRQANRELEK 423
Cdd:TIGR02168 537 aaieAALGGRLQAVVVENLNAAKKAIAFLKQNELGRvtflplDSIKGTEIQGNDREILKNIEGFLGvaKDLVKFDPKLRK 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 424 ELQNVVGRNQLLEGKLQALQadyqalQQRESAIQGSLASLEAEQASIRHL----GDQMEASLLA-------VRKAKEAMK 492
Cdd:TIGR02168 617 ALSYLLGGVLVVDDLDNALE------LAKKLRPGYRIVTLDGDLVRPGGVitggSAKTNSSILErrreieeLEEKIEELE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 493 AQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptDNEARELAAQLA 572
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL------SKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 573 LSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLkeqnealnrahvQELLQCSERE 652
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL------------RERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 653 GALQEERADEAQQREEELRALQEELSqakcsseeaqLEHAELQEQLhrantdtAELGIQVCALTVEKERVEEALAcavqE 732
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLA----------AEIEELEELI-------EELESELEALLNERASLEEALA----L 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 733 LQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIM 812
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQ----------LELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961
|
810 820 830
....*....|....*....|....*....|....*...
gi 1894925314 813 DYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLK 850
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELK 999
|
|
| FYVE |
pfam01363 |
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ... |
969-1032 |
3.65e-25 |
|
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: 99.76 E-value: 3.65e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925314 969 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVL---SKHGGKKERCCRACFQKLSE 1032
Cdd:pfam01363 2 VWVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISllpELGSNKPVRVCDACYDTLQK 68
|
|
| FYVE |
smart00064 |
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ... |
969-1031 |
1.99e-24 |
|
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: 97.50 E-value: 1.99e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925314 969 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGG--KKERCCRACFQKLS 1031
Cdd:smart00064 3 HWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGieRPVRVCDDCYENLN 67
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
202-944 |
1.09e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 108.99 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 202 ELGEKLQALERERTKVEEVnRQQSAQLEQLVKELQLKEdarasLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTS 281
Cdd:TIGR02168 197 ELERQLKSLERQAEKAERY-KELKAELRELELALLVLR-----LEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 282 SWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPG 361
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 362 PELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQ------EAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQ-L 434
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRskvaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 435 LEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLRE 514
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 515 EVEQCQQLA----------EARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELA---------AQLALSQ 575
Cdd:TIGR02168 511 LLKNQSGLSgilgvlseliSVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTflpldsikgTEIQGND 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 576 AQLEVHQGEVQRLQAQVVDLQAKMRAALDD-------QDKVQSQLSMAEAvLREHKTLV---------------QQLKEQ 633
Cdd:TIGR02168 591 REILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKK-LRPGYRIVtldgdlvrpggvitgGSAKTN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 634 NEALNRAhvQELLQCsEREGALQEERADEAQQR----EEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELG 709
Cdd:TIGR02168 670 SSILERR--REIEEL-EEKIEELEEKIAELEKAlaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 710 IQVCALTVEKERVE---EALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAE 786
Cdd:TIGR02168 747 ERIAQLSKELTELEaeiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 787 QRAQSLQEAAHQELNTLKFQ---LSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCT 863
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQieeLSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 864 SNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVtnrERNDQKMLADLDDLNRTKKYLEERLIE 943
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA---EALENKIEDDEEEARRRLKRLENKIKE 983
|
.
gi 1894925314 944 L 944
Cdd:TIGR02168 984 L 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
389-899 |
3.30e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.78 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 389 EEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQA 468
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 469 SIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLT 548
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 549 AEKgqqgvgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQ 628
Cdd:COG1196 407 EAE---------EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 629 QLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQ-AKCSSEEAQLEHAELQEQLHRANTDTAE 707
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVlIGVEAAYEAALEAALAAALQNIVVEDDE 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 708 LGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQ 787
Cdd:COG1196 558 VAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALR 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 788 RAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEEcKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHL 867
Cdd:COG1196 638 RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL-LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
490 500 510
....*....|....*....|....*....|..
gi 1894925314 868 AECQAAMLRKDKEGAALREDLERTQKELEKAT 899
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-763 |
8.24e-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: 96.28 E-value: 8.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 26 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERgrtaaedNVRLTCLVAELQKQWEVT 105
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE-------LYALANEISRLEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 106 QATQNTVKELQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDT 185
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 186 KGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLE---------QLVKELQLKEDARASLERLVKEMAPLQ 256
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelkelqaELEELEEELEELQEELERLEEALEELR 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 257 EELSGKGQEADQLWRRLQEL---LAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQF-------LETQLAQVS 326
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVdegyeaaIEAALGGRL 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 327 QH--VSDLEEQKKQLIQDKDHLSQQVGML---------------ERLAGPPG------------PELPVAGEKNEALVPV 377
Cdd:TIGR02168 548 QAvvVENLNAAKKAIAFLKQNELGRVTFLpldsikgteiqgndrEILKNIEGflgvakdlvkfdPKLRKALSYLLGGVLV 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 378 NSSLQEAWGKPEEEQRGLQEAQLDDTKV-----------------QEGSQE--------EELRQANRELEKELQNVVGRN 432
Cdd:TIGR02168 628 VDDLDNALELAKKLRPGYRIVTLDGDLVrpggvitggsaktnssiLERRREieeleekiEELEEKIAELEKALAELRKEL 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 433 QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQL 512
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 513 REEVEQCQQLAEARHRELRALESQCQQQTqlIEVLTAEKGQQGVgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAQV 592
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLN--EEAANLRERLESL----ERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 593 VDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRaHVQELlqcserEGALQEERADEAQQREEELRA 672
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES-KRSEL------RRELEELREKLAQLELRLEGL 934
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 673 LQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEaasrEREGLERQVA 752
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKE----RYDFLTAQKE 1010
|
810
....*....|.
gi 1894925314 753 GLQQEKESLQE 763
Cdd:TIGR02168 1011 DLTEAKETLEE 1021
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
200-902 |
2.46e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.15 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 200 MQELGEKLQALERERTKVEEVnRQQSAQLEQLVKELQLKEDARaslerlvkemapLQEELSGKGQEADQLWRRLQELLAH 279
Cdd:COG1196 195 LGELERQLEPLERQAEKAERY-RELKEELKELEAELLLLKLRE------------LEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 280 TSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQvgmlerlagp 359
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE---------- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 360 pgpelpvAGEKNEALVPVNSSLQEAwgkpeEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQnvvgRNQLLEGKL 439
Cdd:COG1196 332 -------LEELEEELEELEEELEEA-----EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE----ELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 440 QALQADYQALQQRESAIQGSLASLEAEQASIrhlgdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 519
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEEL-------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 520 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKM 599
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 600 RAALDDQDKVQSQlsmAEAVLREHKtlvqQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQ 679
Cdd:COG1196 549 QNIVVEDDEVAAA---AIEYLKAAK----AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 680 AkcssEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALAcAVQELQDAKEAASREREGLERQVAGLQQEKE 759
Cdd:COG1196 622 L----LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG-SRRELLAALLEAEAELEELAERLAEEELELE 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 760 SLQEKLKAAKAAagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEEckslrgqlEEQGRQL 839
Cdd:COG1196 697 EALLAEEEEERE------LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE--------LPEPPDL 762
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1894925314 840 QAAEEAVEKLKATQADMGeklscTSNHLAECQAAMLRKDKEG-AALREDLERTQKELEKATTKI 902
Cdd:COG1196 763 EELERELERLEREIEALG-----PVNLLAIEEYEELEERYDFlSEQREDLEEARETLEEAIEEI 821
|
|
| FYVE_like_SF |
cd00065 |
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ... |
978-1027 |
6.06e-18 |
|
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: 78.73 E-value: 6.06e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1894925314 978 HCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKH--GGKKERCCRACF 1027
Cdd:cd00065 1 RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSfgSGKPVRVCDSCY 52
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
47-661 |
1.38e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.84 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 47 KQLRERMQQLDREnqELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCLQGLELGA 126
Cdd:COG1196 216 RELKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 127 AEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASfpgwlamAQQKADTASDtkgrqepipsDAAQEMQELGEK 206
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE-------LEEELEELEE----------ELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 207 LQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEE 286
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 287 LAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQqvgMLERLAGPPGPELPV 366
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE---AEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 367 AGEKNEALVPVNSSLQEAWGK------PEEEQRGLQEAQLDDTKVQEGSQEEELRQ---------ANRELEKELQNVVGR 431
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAayeaalEAALAAALQNIVVEDDEVAAAAIEYLKAAkagratflpLDKIRARAALAAALA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 432 NQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQ 511
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 512 LREEVEQCQQLAEARHRELRALESQCQQQTQLIEvltaekgqqgvgpptdnEARELAAQLALSQAQLEVHQGEVQRLQAQ 591
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEER-----------------ELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925314 592 VVDLQAKMRAALDDQDKVQSQLSMAEAVLREHktlVQQLKEQNEAL---NRAHVQELLQCSEREGALQEERAD 661
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERE---LERLEREIEALgpvNLLAIEEYEELEERYDFLSEQRED 806
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
620-966 |
1.73e-17 |
|
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: 88.58 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 620 LREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLH 699
Cdd:TIGR02168 205 LERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 700 RANTDTAELGIQVCALTVEKERVEEALacavQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQ 779
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERL----ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 780 AQLAQAEQRAQSLQEAAHQELNTLKfqlsaeimdyqSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEK 859
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLR-----------SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 860 LSC-----TSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLcQEVTNRERNDQKMLADLDDLNRTK 934
Cdd:TIGR02168 430 LEEaelkeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL-AQLQARLDSLERLQENLEGFSEGV 508
|
330 340 350
....*....|....*....|....*....|..
gi 1894925314 935 KYLEERLIELLRDKDALWQKsdaLEFQQKLSA 966
Cdd:TIGR02168 509 KALLKNQSGLSGILGVLSEL---ISVDEGYEA 537
|
|
| FYVE_PIKfyve_Fab1 |
cd15725 |
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ... |
970-1028 |
2.56e-17 |
|
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: 76.98 E-value: 2.56e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925314 970 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE--RCCRACFQ 1028
Cdd:cd15725 2 WMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGdlRVCTYCCK 62
|
|
| FYVE_EEA1 |
cd15730 |
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ... |
969-1027 |
3.99e-17 |
|
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: 76.67 E-value: 3.99e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1894925314 969 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1027
Cdd:cd15730 2 KWADDEEVQNCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDACF 60
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
84-761 |
2.47e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.60 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 84 AAEDN-VRLTCLVAELQKQWEV--TQATQ-NTVKELQTCLQGLELGAAEKE-EDYHTALRRLESMLQPLAQELEATRDSL 158
Cdd:COG1196 183 ATEENlERLEDILGELERQLEPleRQAEKaERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 159 DKKNQHLASfpgwLAMAQQKADTASDTKGrqepipsdaaQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQL- 237
Cdd:COG1196 263 AELEAELEE----LRLELEELELELEEAQ----------AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEl 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 238 ---KEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAelrrekkqqqeekelleqevrSLTRQ 314
Cdd:COG1196 329 eeeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE---------------------ELAEE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 315 LQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLsqqvgmlerlagppgpelpvageknealvpvnsslqeawgkpEEEQRG 394
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERL------------------------------------------EEELEE 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 395 LQEAQLddtkvQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLG 474
Cdd:COG1196 426 LEEALA-----ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 475 DQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALEsqcqqqtQLIEVLTAEKGQQ 554
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA-------AAIEYLKAAKAGR 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 555 GVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQN 634
Cdd:COG1196 574 ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 635 EALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKcSSEEAQLEHAELQEQLHRANTDTAELGIQVCA 714
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL-AEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1894925314 715 LTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESL 761
Cdd:COG1196 733 EREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
489-861 |
2.72e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.60 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 489 EAMKAQMAEKEAILQSKEGECQQLREEVEQcqqlAEaRHRELRALESQCQQQTQLIEVLTAEKgqqgvgpptdnEARELA 568
Cdd:COG1196 182 EATEENLERLEDILGELERQLEPLERQAEK----AE-RYRELKEELKELEAELLLLKLRELEA-----------ELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 569 AQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAvlrEHKTLVQQLKEQNEALNRAHVQEllqc 648
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA---ELARLEQDIARLEERRRELEERL---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 649 sEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAelgiqvcaltvEKERVEEALAC 728
Cdd:COG1196 319 -EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA-----------EAEEELEELAE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 729 AVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKfQLS 808
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE----------LEEALAELEEEEEEEEEALEEAAEEEA-ELE 455
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1894925314 809 AEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLS 861
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
621-940 |
3.75e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.22 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 621 REHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHR 700
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 701 ANTDTAELgiqvcaltvekERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSlpgLQA 780
Cdd:COG1196 293 LLAELARL-----------EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE---AEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 781 QLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKL 860
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELE-ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 861 SCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLcQEVTNRERNDQKMLADLDDLNRTKKYLEER 940
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL-AEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
|
| FYVE_LST2 |
cd15731 |
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ... |
969-1027 |
1.39e-15 |
|
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: 72.38 E-value: 1.39e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925314 969 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYC-CNNYVLSKHG-GKKERCCRACF 1027
Cdd:cd15731 4 LWVPDEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCsSNSVPLPRYGqMKPVRVCNHCF 64
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
199-941 |
4.72e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 80.88 E-value: 4.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 199 EMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGkgQEADQLWRRLQELLA 278
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE--EEQLRVKEKIGELEA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 279 HTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAG 358
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 359 PPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTkvqegSQEEELRQANRELEKELQNVVGRNQLLEGK 438
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN-----AAIAGIEAKINELEEEKEDKALEIKKQEWK 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 439 LQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGecqqlreeveQ 518
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHG----------T 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 519 CQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGV--------GPPTDNEARELAAQLALSQAqleVHQGEVQRLQA 590
Cdd:TIGR02169 527 VAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIellkrrkaGRATFLPLNKMRDERRDLSI---LSEDGVIGFAV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 591 QVVDLQAKMRAA----LDDQDKVQSqLSMAEAVLREHK--TLVQQLKEQNEALNRAHVQ-------------ELLQCSER 651
Cdd:TIGR02169 604 DLVEFDPKYEPAfkyvFGDTLVVED-IEAARRLMGKYRmvTLEGELFEKSGAMTGGSRAprggilfsrsepaELQRLRER 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 652 EGALQEERADEAQQREE---ELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALAC 728
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRienRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 729 AVQELQDAKEAASREREGLERQVAGLQQEK-ESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKfql 807
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ--- 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 808 sAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQaamlRKDKEGAALRED 887
Cdd:TIGR02169 840 -EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE----RKIEELEAQIEK 914
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1894925314 888 LERTQKELeKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERL 941
Cdd:TIGR02169 915 KRKRLSEL-KAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI 967
|
|
| FYVE_endofin |
cd15729 |
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ... |
970-1030 |
9.68e-15 |
|
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: 70.07 E-value: 9.68e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925314 970 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCN-NYVLSKHGGKKERCCRACFQKL 1030
Cdd:cd15729 7 WVPDSEAPNCMQCEVKFTFTKRRHHCRACGKVLCSACCSlKARLEYLDNKEARVCVPCYQTL 68
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
396-951 |
1.47e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.95 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 396 QEAQLDDTKVQEGSQEEELRQANREL---EKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRH 472
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELqelEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 473 LGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHR------------------------ 528
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESrleeleeqletlrskvaqlelqia 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 529 ----ELRALESQCQQQTQLIEVLTAEKGQQGvGPPTDNEARELAAQLALS-------QAQLEVHQGEVQRLQAQVVDLQA 597
Cdd:TIGR02168 397 slnnEIERLEARLERLEDRRERLQQEIEELL-KKLEEAELKELQAELEELeeeleelQEELERLEEALEELREELEEAEQ 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 598 KMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAH-----VQELLQCSER-----EGALQE---------- 657
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSgilgvLSELISVDEGyeaaiEAALGGrlqavvvenl 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 658 ---ERADEAQQREEELRALQEELSQAK------------------------CSSEEAQLEHA------------ELQEQL 698
Cdd:TIGR02168 556 naaKKAIAFLKQNELGRVTFLPLDSIKgteiqgndreilkniegflgvakdLVKFDPKLRKAlsyllggvlvvdDLDNAL 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 699 HRANTDTAELGI-------------------QVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKE 759
Cdd:TIGR02168 636 ELAKKLRPGYRIvtldgdlvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 760 SLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGE---ECKSLRGQLEEQ- 835
Cdd:TIGR02168 716 QLRKELEELSRQ---ISALRKDLARLEAEVEQLEERIAQLSKELT-ELEAEIEELEERLEEAEEelaEAEAEIEELEAQi 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 836 ----------GRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATT---KI 902
Cdd:TIGR02168 792 eqlkeelkalREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEElieEL 871
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1894925314 903 QEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDAL 951
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
|
| FYVE_RUFY1_like |
cd15721 |
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ... |
970-1027 |
3.84e-14 |
|
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: 68.18 E-value: 3.84e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1894925314 970 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1027
Cdd:cd15721 1 WADDKEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
|
|
| FYVE_MTMR3 |
cd15732 |
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ... |
969-1027 |
4.09e-14 |
|
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: 68.00 E-value: 4.09e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925314 969 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNN--YVLSKHGGKKERCCRACF 1027
Cdd:cd15732 1 RWVPDHLAASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQklPVPSQQLFEPSRVCKSCF 61
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
390-824 |
6.22e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.88 E-value: 6.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 390 EEQRGLQEAQLDDTKVQEGSQE-EELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGS-LASLEAEQ 467
Cdd:COG4913 268 RERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 468 ASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQ-TQLIEV 546
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRElRELEAE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 547 LTAEKGQQGVGPPTDNEAR-ELAAQLALSQAQL-------EVHQGEV--------------------QRLQAQVVDL--Q 596
Cdd:COG4913 428 IASLERRKSNIPARLLALRdALAEALGLDEAELpfvgeliEVRPEEErwrgaiervlggfaltllvpPEHYAAALRWvnR 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 597 AKMRAALDDQdKVQSQLSMAEAVLREHKTLVQQLK-EQNEAlnRAHVQELLQ------CSEREGALQEER---------- 659
Cdd:COG4913 508 LHLRGRLVYE-RVRTGLPDPERPRLDPDSLAGKLDfKPHPF--RAWLEAELGrrfdyvCVDSPEELRRHPraitragqvk 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 660 ------------------------ADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANT---------DTA 706
Cdd:COG4913 585 gngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVA 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 707 ELGIQVCALTVEKERVE------EALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQA 780
Cdd:COG4913 665 SAEREIAELEAELERLDassddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1894925314 781 QLAQA---EQRAQSLQEAAHQElntLKFQLSAEIMDYQSRLKNAGEE 824
Cdd:COG4913 745 LELRAlleERFAAALGDAVERE---LRENLEERIDALRARLNRAEEE 788
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
193-923 |
9.33e-14 |
|
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: 76.55 E-value: 9.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 193 PSDAAQEMQELgEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKED--------ARASLERLVKEMAPLQEELSGKGQ 264
Cdd:TIGR00618 162 SKEKKELLMNL-FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLctpcmpdtYHERKQVLEKELKHLREALQQTQQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 265 EADQLwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLetQLAQVSQHVSDLEEQKKQLIQDkd 344
Cdd:TIGR00618 241 SHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTE-- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 345 hLSQQVGMLERLAGPPGPELpvageKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLD--DTKVQEGSQEEELRQANRELE 422
Cdd:TIGR00618 316 -LQSKMRSRAKLLMKRAAHV-----KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSirEISCQQHTLTQHIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 423 KELQNVVGRNQLLEgKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASL---LAVRKAKEAMKAQMAEKE 499
Cdd:TIGR00618 390 TLTQKLQSLCKELD-ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAItctAQCEKLEKIHLQESAQSL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 500 AILQSKEGECQQLREEVEQCQQLAEARHRELRalESQCQQQTQLIEvLTAEKGQQGVGPPTDNEARELAAQLALSQAQLE 579
Cdd:TIGR00618 469 KEREQQLQTKEQIHLQETRKKAVVLARLLELQ--EEPCPLCGSCIH-PNPARQDIDNPGPLTRRMQRGEQTYAQLETSEE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 580 VHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEER 659
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 660 ADeaQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRAntdtaelgiqvcALTVEKERVEEALACAVQELQDAKEA 739
Cdd:TIGR00618 626 DL--QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAL------------SIRVLPKELLASRQLALQKMQSEKEQ 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 740 ASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQ-RAQSLQEAAHQELNTLKFQLSAEIMDYQSRL 818
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDaLNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 819 --KNAGEECKSLRGQLEEQGRQLqaaEEAVEKLKATQADMGEKLsctsnhlaecQAAMLRKDKEGAALREDLERTQKELE 896
Cdd:TIGR00618 772 aaLQTGAELSHLAAEIQFFNRLR---EEDTHLLKTLEAEIGQEI----------PSDEDILNLQCETLVQEEEQFLSRLE 838
|
730 740
....*....|....*....|....*..
gi 1894925314 897 KATTKIQEYYNKLCQEVTNRERNDQKM 923
Cdd:TIGR00618 839 EKSATLGEITHQLLKYEECSKQLAQLT 865
|
|
| FYVE_MTMR4 |
cd15733 |
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ... |
970-1027 |
1.31e-13 |
|
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: 66.69 E-value: 1.31e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925314 970 WLGDTEANHCLDCKREFsWMV-RRHHCRICGRIFCYYCCNnyvlSKHGGKKE------RCCRACF 1027
Cdd:cd15733 1 WVPDHAASHCFGCDCEF-WLAkRKHHCRNCGNVFCADCSN----YKLPIPDEqlydpvRVCNSCY 60
|
|
| FYVE_ZF21 |
cd15727 |
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ... |
967-1012 |
1.36e-13 |
|
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: 66.63 E-value: 1.36e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1894925314 967 EERWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVL 1012
Cdd:cd15727 1 EPPWVPDKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVP 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-550 |
3.28e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 27 EALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQ 106
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 107 ATQNTVKELQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFpgwLAMAQQKADTASDTK 186
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL---AAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 187 GRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEA 266
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 267 DQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTrqlqfLETQLAQVSQH-VSDLEEQKKQLIQDkdh 345
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA-----LEAALAAALQNiVVEDDEVAAAAIEY--- 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 346 lsqqvgmLERLAGPPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKEL 425
Cdd:COG1196 566 -------LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 426 QnvVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQmaEKEAILQSK 505
Cdd:COG1196 639 A--VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE--ERELAEAEE 714
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1894925314 506 EGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAE 550
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
|
| FYVE_scVPS27p_like |
cd15760 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
975-1027 |
6.97e-13 |
|
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: 64.63 E-value: 6.97e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925314 975 EANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYV-LSKHGGKKERC--CRACF 1027
Cdd:cd15760 4 PDSRCDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIpLPHLGPLGVPQrvCDRCF 59
|
|
| FYVE_RUFY1 |
cd15758 |
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ... |
970-1026 |
1.61e-12 |
|
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: 63.93 E-value: 1.61e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925314 970 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRAC 1026
Cdd:cd15758 6 WLKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSC 62
|
|
| FYVE_Hrs |
cd15720 |
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ... |
974-1030 |
1.71e-12 |
|
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: 63.56 E-value: 1.71e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1894925314 974 TEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNY-VLSKHGGKKE-RCCRACFQKL 1030
Cdd:cd15720 3 KDGDECHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSsTIPKFGIEKEvRVCDPCYEKL 61
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-903 |
2.29e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.02 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 28 ALEGFDEMRLELDQLEVREKQLRERMQQLdrenqelraavsqQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQA 107
Cdd:TIGR02169 175 ALEELEEVEENIERLDLIIDEKRQQLERL-------------RREREKAERYQALLKEKREYEGYELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 108 TQNTVKELQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKnqhLASFPGWLAMAQQKADtasdtkg 187
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK---IGELEAEIASLERSIA------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 188 rqepipsDAAQEMQELGEKLQALERERTKVEEvnrqqsaQLEQLVKELqlkedaraslERLVKEMAPLQEELSGKGQEAD 267
Cdd:TIGR02169 312 -------EKERELEDAEERLAKLEAEIDKLLA-------EIEELEREI----------EEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 268 QLWRRLQELLAHTSSWEeelaelrREKKQQQEEKELLEQEVRSLTRQ-------LQFLETQLAQVSQHVSDLEEQKKQLI 340
Cdd:TIGR02169 368 DLRAELEEVDKEFAETR-------DELKDYREKLEKLKREINELKREldrlqeeLQRLSEELADLNAAIAGIEAKINELE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 341 QDKDHLSQQVGMLERlagppgpELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQE--AQLDDTKVQEGSQEEELRQAN 418
Cdd:TIGR02169 441 EEKEDKALEIKKQEW-------KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRelAEAEAQARASEERVRGGRAVE 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 419 RELEKELQNVVGrnqlLEGKLQALQADYQAlqQRESAIQGSLASLEAE-----QASIRHLGDQM--EASLLAVRKakeaM 491
Cdd:TIGR02169 514 EVLKASIQGVHG----TVAQLGSVGERYAT--AIEVAAGNRLNNVVVEddavaKEAIELLKRRKagRATFLPLNK----M 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 492 KAQMAEKEAIlqSKEGECQQLREEVEQCQQLAEA------------RHRELRALESQCQQQTQLIEVL----------TA 549
Cdd:TIGR02169 584 RDERRDLSIL--SEDGVIGFAVDLVEFDPKYEPAfkyvfgdtlvveDIEAARRLMGKYRMVTLEGELFeksgamtggsRA 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 550 EKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEavlREHKTLVQQ 629
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE---QEEEKLKER 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 630 LKEQnealnRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELsqakcSSEEAQLEHAELQeqlhrantdtaELG 709
Cdd:TIGR02169 739 LEEL-----EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL-----NDLEARLSHSRIP-----------EIQ 797
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 710 IQVCALTVEKERVEEALACAVQELQD---AKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAE 786
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRltlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN----------LNGKKEELE 867
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 787 QRAQSLQeaahqelntlkfqlsAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNH 866
Cdd:TIGR02169 868 EELEELE---------------AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
890 900 910
....*....|....*....|....*....|....*..
gi 1894925314 867 LAECQAAmLRKDKEGAALREDLERTQKELEKATTKIQ 903
Cdd:TIGR02169 933 LSEIEDP-KGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
379-708 |
2.81e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.64 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 379 SSLQEAWGKPEEEQRGLQEAQLDDTKVQEgsQEEELRQANRELEKELQNVvgrnqllEGKLQALQADYQALQQRESAIQG 458
Cdd:TIGR02169 709 QELSDASRKIGEIEKEIEQLEQEEEKLKE--RLEELEEDLSSLEQEIENV-------KSELKELEARIEELEEDLHKLEE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 459 SLASLEAEQAsiRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQlaearhrELRALESQCQ 538
Cdd:TIGR02169 780 ALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE-------QRIDLKEQIK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 539 QQTQLIEVLTAEKgqqgvgpptdneaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEA 618
Cdd:TIGR02169 851 SIEKEIENLNGKK-------------EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 619 VLREHKTLVQQLKEQNEAL--NRAHVQELLQCSEREGALQEERadeaQQREEELRALQEELSQAKCSSEEAQLEHAELQE 696
Cdd:TIGR02169 918 RLSELKAKLEALEEELSEIedPKGEDEEIPEEELSLEDVQAEL----QRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE 993
|
330
....*....|..
gi 1894925314 697 QLHRANTDTAEL 708
Cdd:TIGR02169 994 KRAKLEEERKAI 1005
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
661-968 |
4.96e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 4.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 661 DEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEealacaVQELQDAKEAA 740
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE------LEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 741 SREREGLERQVAGLQQEKESLQEKLkaakaaagslpglqAQLAQAEQRAQSLQEAAHQELNTLKfqlsAEIMDYQSRLKN 820
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERL--------------EELEEELAELEEELEELEEELEELE----EELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 821 AGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATT 900
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1894925314 901 KIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEE 968
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
195-819 |
5.16e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 70.71 E-value: 5.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 195 DAAQEMQELgekLQALERERTKVEEVnRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQeelsgkgqeadqLWRRLQ 274
Cdd:COG4913 225 EAADALVEH---FDDLERAHEALEDA-REQIELLEPIRELAERYAAARERLAELEYLRAALR------------LWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 275 ELLAhtssWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVS-QHVSDLEEQKKQLIQDKDHLSQQVGML 353
Cdd:COG4913 289 RLEL----LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 354 ERLAGPPGPELPVAGEKNEALVPVNSSLQEAWgkpeEEQRGLQEAQLDDTKVqegsQEEELRQANRELEKELQNVVGRNQ 433
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAALLEAL----EEELEALEEALAEAEA----ALRDLRRELRELEAEIASLERRKS 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 434 LLEGKLQALQADY-QALQQRES--------------------AIQGSLASL------EAEQAS-----IRHLGDQMEASL 481
Cdd:COG4913 437 NIPARLLALRDALaEALGLDEAelpfvgelievrpeeerwrgAIERVLGGFaltllvPPEHYAaalrwVNRLHLRGRLVY 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 482 LAVRKAKEAMKAQMAEKEAI---LQSKEGECQQ-LREEVEQ-----CQQLAEARHRELRALESQCQ--QQTQLievltAE 550
Cdd:COG4913 517 ERVRTGLPDPERPRLDPDSLagkLDFKPHPFRAwLEAELGRrfdyvCVDSPEELRRHPRAITRAGQvkGNGTR-----HE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 551 KGQQGVGPPT-----DNEAR--ELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKmRAALDDQDKVQSQLSMAEAVLREh 623
Cdd:COG4913 592 KDDRRRIRSRyvlgfDNRAKlaALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVASAERE- 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 624 ktlVQQLKEQNEALNRAHvQELLQCSEREGALQEERaDEAQQREEELRALQEELSQAKcssEEAQLEHAELQEQLHRANT 703
Cdd:COG4913 670 ---IAELEAELERLDASS-DDLAALEEQLEELEAEL-EELEEELDELKGEIGRLEKEL---EQAEEELDELQDRLEAAED 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 704 DTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQE-KESLQEKLKAAKAAAGSLPGLQAQL 782
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALL 821
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1894925314 783 AQ--------AEQR-AQSLQEAAHQELNTLKFQLSAEIMDYQSRLK 819
Cdd:COG4913 822 DRleedglpeYEERfKELLNENSIEFVADLLSKLRRAIREIKERID 867
|
|
| FYVE_RABE_unchar |
cd15739 |
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ... |
967-1027 |
5.89e-12 |
|
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: 62.36 E-value: 5.89e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925314 967 EERWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1027
Cdd:cd15739 1 EVRWQHEDDVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCH 61
|
|
| FYVE_RUFY4 |
cd15745 |
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ... |
978-1027 |
6.91e-12 |
|
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: 61.36 E-value: 6.91e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1894925314 978 HCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKH--GGKKERCCRACF 1027
Cdd:cd15745 1 ACAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVLSVpdTCIYLRVCKTCY 52
|
|
| FYVE_PKHF |
cd15717 |
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ... |
970-1027 |
8.79e-12 |
|
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: 61.23 E-value: 8.79e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 970 WLGDTEANHCLDCKR-EFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE-RCCRACF 1027
Cdd:cd15717 2 WVPDSEAPVCMHCKKtKFTAINRRHHCRKCGAVVCGACSSKKFLLPHQSSKPlRVCDTCY 61
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
311-967 |
1.53e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.33 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 311 LTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLagppgpelpvagekneaLVPVNSSLQEawgKPEE 390
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL-----------------LEELNKKIKD---LGEE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 391 EQRGLQEaQLDDTKVQEGSQEEELRQANRELEKelqnvvgrnqlLEGKLQALQADYqalqqreSAIQGSLASLEAEQASI 470
Cdd:TIGR02169 288 EQLRVKE-KIGELEAEIASLERSIAEKERELED-----------AEERLAKLEAEI-------DKLLAEIEELEREIEEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 471 RHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAE 550
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 551 -KGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQ 629
Cdd:TIGR02169 429 iAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 630 LKEQNEALNR------AHVQELLQCSERE---------GALQ------EERADEAQQREEE----------LRALQEELS 678
Cdd:TIGR02169 509 GRAVEEVLKAsiqgvhGTVAQLGSVGERYataievaagNRLNnvvvedDAVAKEAIELLKRrkagratflpLNKMRDERR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 679 QAKCSSEEAQLEHA----ELQEQLHRA------------NTDTA-ELGIQVCALTVEKERVE-----------EALACAV 730
Cdd:TIGR02169 589 DLSILSEDGVIGFAvdlvEFDPKYEPAfkyvfgdtlvveDIEAArRLMGKYRMVTLEGELFEksgamtggsraPRGGILF 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 731 QELQDAKEAASRER-EGLERQVAGLQQEKESLQ----EKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHqelntlkf 805
Cdd:TIGR02169 669 SRSEPAELQRLRERlEGLKRELSSLQSELRRIEnrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE-------- 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 806 QLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADmgEKLSCTSNHLAECQAAMLRKDKEGAALR 885
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIE 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 886 EDLERTQKELEKATTKIQEYYNKL----------CQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDAL-WQK 954
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRidlkeqiksiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELeAQL 898
|
730
....*....|...
gi 1894925314 955 SDALEFQQKLSAE 967
Cdd:TIGR02169 899 RELERKIEELEAQ 911
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
657-969 |
1.63e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 657 EERADEAQQREEELRALQEELsqakcsseEAQLEHAELQ-EQLHRANTDTAELGI-QVCALTVEKERVEEALACAVQELQ 734
Cdd:COG1196 178 ERKLEATEENLERLEDILGEL--------ERQLEPLERQaEKAERYRELKEELKElEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 735 DAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDY 814
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE-ELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 815 QSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKE 894
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925314 895 LEKATTKIQEYYnklcQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEER 969
Cdd:COG1196 409 EEALLERLERLE----EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
409-762 |
1.80e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 69.22 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 409 SQEEELRQANRELEKE---LQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAE---QASIRHLGDQMEASLL 482
Cdd:PRK04863 290 ELRRELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIeryQADLEELEERLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 483 AVRKAKEamkaQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRE-------LRALESqCQQQTQL-----------I 544
Cdd:PRK04863 370 VVEEADE----QQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRaiqyqqaVQALER-AKQLCGLpdltadnaedwL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 545 EVLTAEKGQQgvgpptDNEARELAAQLALSQAQLEVHQ----------GEVQRLQAQVVdlqakMRAALDDQDKVQSQLS 614
Cdd:PRK04863 445 EEFQAKEQEA------TEELLSLEQKLSVAQAAHSQFEqayqlvrkiaGEVSRSEAWDV-----ARELLRRLREQRHLAE 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 615 MAEAVLREHKTLVQQLKEQNEAlnrahvQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAEL 694
Cdd:PRK04863 514 QLQQLRMRLSELEQRLRQQQRA------ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 695 QEQL--------------HRANTDTAELGIQVCALTVEKERVEEALacavQELQDAKEAASREREGLERQVAGLQQEKES 760
Cdd:PRK04863 588 LEQLqariqrlaarapawLAAQDALARLREQSGEEFEDSQDVTEYM----QQLLERERELTVERDELAARKQALDEEIER 663
|
..
gi 1894925314 761 LQ 762
Cdd:PRK04863 664 LS 665
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
131-680 |
2.02e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 131 EDYHTALRRLE---SMLQPL---AQELEATRDSLDKKNQHLASFPGWlaMAQQKADTAsdtkgrqepipsdaAQEMQELG 204
Cdd:COG4913 238 ERAHEALEDAReqiELLEPIrelAERYAAARERLAELEYLRAALRLW--FAQRRLELL--------------EAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 205 EKLQALERERTKVEEVNRQQSAQLEQLvkELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQEL----LAHT 280
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDEL--EAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALglplPASA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 281 SSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKK----QLIQDKDHLSQQVGMLERl 356
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGLDEA- 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 357 agppgpELPVAGEkneaLVPVNSSlQEAWgkpeeeqrglqeaqlddtkvqEGSQEEELRQANREL------EKELQNVVG 430
Cdd:COG4913 459 ------ELPFVGE----LIEVRPE-EERW---------------------RGAIERVLGGFALTLlvppehYAAALRWVN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 431 RNQLlEGKLQALQAD-YQALQQRESAIQGSLAS-LEAEQASIR-----HLGDQM-------EASLLAVRKA--KEAM--- 491
Cdd:COG4913 507 RLHL-RGRLVYERVRtGLPDPERPRLDPDSLAGkLDFKPHPFRawleaELGRRFdyvcvdsPEELRRHPRAitRAGQvkg 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 492 KAQMAEK----------------EAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQG 555
Cdd:COG4913 586 NGTRHEKddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 556 VgpptDNEARELAAQLAlsqaQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNE 635
Cdd:COG4913 666 A----EREIAELEAELE----RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1894925314 636 ALNRAHVQELLQCSE--REGALQEERADEAQQR-EEELRALQEELSQA 680
Cdd:COG4913 738 AAEDLARLELRALLEerFAAALGDAVERELRENlEERIDALRARLNRA 785
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
411-795 |
2.37e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.56 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 411 EEELRQANRELEKELQNVvGRNQLLEG----KLQALQAD------YQALQQRESAIQGSLASLEaeqasirhlgdqmeas 480
Cdd:TIGR02169 169 DRKKEKALEELEEVEENI-ERLDLIIDekrqQLERLRRErekaerYQALLKEKREYEGYELLKE---------------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 481 LLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQlievltaekgqqgvgppt 560
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK------------------ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 561 dNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAkmraaldDQDKVQSQLSMAEAVLREHKTLVQQLKEqnEALNRA 640
Cdd:TIGR02169 294 -EKIGELEAEIASLERSIAEKERELEDAEERLAKLEA-------EIDKLLAEIEELEREIEEERKRRDKLTE--EYAELK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 641 HVQELLQCSeregaLQEERADEAQQREEeLRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQvcaLTVEKE 720
Cdd:TIGR02169 364 EELEDLRAE-----LEEVDKEFAETRDE-LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA---IAGIEA 434
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925314 721 RVEEaLACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQEA 795
Cdd:TIGR02169 435 KINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKE---LSKLQRELAEAEAQARASEER 505
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
202-951 |
2.77e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.56 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 202 ELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQL-KEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAht 280
Cdd:TIGR02169 195 EKRQQLERLRREREKAERYQALLKEKREYEGYELLKeKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ-- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 281 ssweEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVgmlerlagpp 360
Cdd:TIGR02169 273 ----LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI---------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 361 gpelpvageknealvpvnsslqeawgkpEEEQRGLQEAQLDDTKVQEgsQEEELRQANRELEKELQNVVGRNQLLEGKLQ 440
Cdd:TIGR02169 339 ----------------------------EELEREIEEERKRRDKLTE--EYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 441 ALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQ 520
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 521 QLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARE-----------LAAQL----ALSQAQLEVHQGev 585
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEvlkasiqgvhgTVAQLgsvgERYATAIEVAAG-- 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 586 QRLQAQVVDLQA-----------------------KMRAALDDQDK--------------------------------VQ 610
Cdd:TIGR02169 547 NRLNNVVVEDDAvakeaiellkrrkagratflplnKMRDERRDLSIlsedgvigfavdlvefdpkyepafkyvfgdtlVV 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 611 SQLSMAEAVLREHK--TLVQQLKEQNEALNRAHVQ-------------ELLQCSEREGALQEERADEAQqreeELRALQE 675
Cdd:TIGR02169 627 EDIEAARRLMGKYRmvTLEGELFEKSGAMTGGSRAprggilfsrsepaELQRLRERLEGLKRELSSLQS----ELRRIEN 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 676 ELSQAKCSSEEAQLEHAELQEQLHRANTDTAELgiqvcaltveKERVEEaLACAVQELQDAKEAASREREGLERQVAGLQ 755
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKL----------KERLEE-LEEDLSSLEQEIENVKSELKELEARIEELE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 756 QEKESLQEKLKAakaaagslpgLQAQLAQaeQRAQSLQEAAhQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQ 835
Cdd:TIGR02169 772 EDLHKLEEALND----------LEARLSH--SRIPEIQAEL-SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 836 GRQLQAAEEAVEKLKATQADMGEKLsctsnhlaecqAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTN 915
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKK-----------EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
810 820 830
....*....|....*....|....*....|....*.
gi 1894925314 916 RERNDQKMLADLDDLNRTKKYLEERLIELLRDKDAL 951
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
|
| FYVE_RBNS5 |
cd15716 |
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ... |
970-1031 |
3.09e-11 |
|
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: 59.66 E-value: 3.09e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925314 970 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCcnnyvlSKHGGKKERCCRACFQKLS 1031
Cdd:cd15716 4 WVNDSDVPFCPDCGKKFNLARRRHHCRLCGSIMCNKC------SQFLPLHIRCCHHCKDLLE 59
|
|
| FYVE_ZFYV1 |
cd15734 |
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ... |
970-1027 |
3.75e-11 |
|
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: 59.65 E-value: 3.75e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 970 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE--RCCRACF 1027
Cdd:cd15734 2 WVPDSEIKECSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRGWDHpvRVCDPCA 61
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
419-983 |
4.86e-11 |
|
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: 67.45 E-value: 4.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 419 RELEKELQNVVGRNQLLEGKLQALQADYQ-----ALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKA 493
Cdd:pfam15921 227 RELDTEISYLKGRIFPVEDQLEALKSESQnkielLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 494 QMAEKEAI----LQSKEGECQQLREEVEQCQQLAEARHRELRalESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAA 569
Cdd:pfam15921 307 QARNQNSMymrqLSDLESTVSQLRSELREAKRMYEDKIEELE--KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 570 QLALSQAQLEVHQG----------------------------EVQRLQAQVVDLQAKMRAALDDQdkvQSQLSMAEAVLR 621
Cdd:pfam15921 385 DLHKREKELSLEKEqnkrlwdrdtgnsitidhlrrelddrnmEVQRLEALLKAMKSECQGQMERQ---MAAIQGKNESLE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 622 EHKTLVQQLKEQNEALnRAHVQEL------LQCSERE-----GALQE-ERADEAQQRE------------EELRALQEE- 676
Cdd:pfam15921 462 KVSSLTAQLESTKEML-RKVVEELtakkmtLESSERTvsdltASLQEkERAIEATNAEitklrsrvdlklQELQHLKNEg 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 677 --LSQAKCSSEEAQLEHAE-------LQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQ------DAKEAAS 741
Cdd:pfam15921 541 dhLRNVQTECEALKLQMAEkdkvieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQefkilkDKKDAKI 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 742 REregLERQVAGLQQEKESLqeklkaakAAAGSlPGLQAQLAQAEQRAQSLQEA--AHQELNTLkfqlSAEIMDYQSRLK 819
Cdd:pfam15921 621 RE---LEARVSDLELEKVKL--------VNAGS-ERLRAVKDIKQERDQLLNEVktSRNELNSL----SEDYEVLKRNFR 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 820 NAGEECKSLRGQLEeqgRQLQAAEEAVEKLKATQADMgeklSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKAT 899
Cdd:pfam15921 685 NKSEEMETTTNKLK---MQLKSAQSELEQTRNTLKSM----EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 900 TK-------IQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERL--IELLRDKDALwQKSDALEFQQKLSAEERW 970
Cdd:pfam15921 758 TNankekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVanMEVALDKASL-QFAECQDIIQRQEQESVR 836
|
650
....*....|...
gi 1894925314 971 LgdtEANHCLDCK 983
Cdd:pfam15921 837 L---KLQHTLDVK 846
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
19-896 |
1.38e-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: 65.91 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 19 DLNSPLNNEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQT---ERERGRTAAEDNVRltclv 95
Cdd:pfam15921 60 ELDSPRKIIAYPGKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTklqEMQMERDAMADIRR----- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 96 AELQKQWEVTQATQNTVKELQT--CLQGLELGAAEKE-EDYHTALRRLESMLQPLAQELEATRDSLDKK--------NQH 164
Cdd:pfam15921 135 RESQSQEDLRNQLQNTVHELEAakCLKEDMLEDSNTQiEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmsTMH 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 165 LASFPGWLAMAQQKADTA-SDTKGRQEPIPsdaaqemqelgEKLQALERE-RTKVEEVNRQQSAQLEQLVKELQLK---- 238
Cdd:pfam15921 215 FRSLGSAISKILRELDTEiSYLKGRIFPVE-----------DQLEALKSEsQNKIELLLQQHQDRIEQLISEHEVEitgl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 239 ----EDARASLERLVKEMAPLQEElsGKGQEADQLwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSltrQ 314
Cdd:pfam15921 284 tekaSSARSQANSIQSQLEIIQEQ--ARNQNSMYM-RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANS---E 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 315 LQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQqvgmlerlagppgpELPVAGEKNEALvpvnsslqeaWgkpeeeqrg 394
Cdd:pfam15921 358 LTEARTERDQFSQESGNLDDQLQKLLADLHKREK--------------ELSLEKEQNKRL----------W--------- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 395 lqeaqldDTKVQEGSQEEELRqanRELEKELQNVvgrnQLLEGKLQALQADYQA-LQQRESAIQGSLASLEaeqaSIRHL 473
Cdd:pfam15921 405 -------DRDTGNSITIDHLR---RELDDRNMEV----QRLEALLKAMKSECQGqMERQMAAIQGKNESLE----KVSSL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 474 GDQMEASLLAVRKAKEAMKAqmaeKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEkGQ 553
Cdd:pfam15921 467 TAQLESTKEMLRKVVEELTA----KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE-GD 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 554 QGVGPPTDNEARELaaQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTL------- 626
Cdd:pfam15921 542 HLRNVQTECEALKL--QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILkdkkdak 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 627 VQQLKEQNEALNRAHVQELLQCSEREGALQeeraDEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTA 706
Cdd:pfam15921 620 IRELEARVSDLELEKVKLVNAGSERLRAVK----DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTN 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 707 ELGIQVCALTVEKERVEEALacavQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAE 786
Cdd:pfam15921 696 KLKMQLKSAQSELEQTRNTL----KSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQF----------LEEAMTNAN 761
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 787 QRAQSLQEAahqelntlKFQLSAEimdyqsrLKNAGEECKSLRGQLEeqgrQLQAAEeavEKLKATQADMGEKLSCTSNH 866
Cdd:pfam15921 762 KEKHFLKEE--------KNKLSQE-------LSTVATEKNKMAGELE----VLRSQE---RRLKEKVANMEVALDKASLQ 819
|
890 900 910
....*....|....*....|....*....|
gi 1894925314 867 LAECQAAMLRKDKEGAALREDLERTQKELE 896
Cdd:pfam15921 820 FAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
667-976 |
1.38e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.24 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 667 EEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELgIQVCALTVEKERVEealacaVQELQDAKEAASREREG 746
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKEKREYE------GYELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 747 LERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQ-----AEQRAQSLQEAAHqELNTLKFQLSAEIMDYQSRLKNA 821
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIG-ELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 822 GEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTK 901
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 902 IqeyyNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALE-----FQQKLSAEERWLGDTEA 976
Cdd:TIGR02169 401 I----NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkleqLAADLSKYEQELYDLKE 476
|
|
| FYVE2_Vac1p_like |
cd15737 |
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ... |
969-1003 |
1.56e-10 |
|
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: 58.67 E-value: 1.56e-10
10 20 30
....*....|....*....|....*....|....*
gi 1894925314 969 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFC 1003
Cdd:cd15737 1 PWEDDSSVTHCPICLRSFGLLLRKHHCRLCGKVVC 35
|
|
| FYVE_RUFY2 |
cd15759 |
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ... |
970-1026 |
1.78e-10 |
|
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: 58.11 E-value: 1.78e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925314 970 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRAC 1026
Cdd:cd15759 4 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSC 60
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
584-846 |
2.02e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 584 EVQRLQAQVVDLQAKMRAALDDQDKVQsQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQEllqcSEREGALQEERADEA 663
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAALRLWF----AQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 664 qqrEEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDT-AELGIQVCALTVEKERVEEALACAVQELQDAKEAASR 742
Cdd:COG4913 301 ---RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 743 EREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQelntlkfqLSAEIMDYQSRLKNAG 822
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEA----------LEEALAEAEAALRDLRRELRE--------LEAEIASLERRKSNIP 439
|
250 260
....*....|....*....|....
gi 1894925314 823 EECKSLRGQLEEqgrQLQAAEEAV 846
Cdd:COG4913 440 ARLLALRDALAE---ALGLDEAEL 460
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
34-834 |
2.35e-10 |
|
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: 65.36 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 34 EMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQgEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQA----TQ 109
Cdd:COG3096 310 EMARELEELSARESDLEQDYQAASDHLNLVQTALRQQ-EKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEArleaAE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 110 NTVKELQTCL----QGLELgAAEKEEDYHTALRRLESmlqplAQELeatrdsLDKKNQHLASFPGWLAMAQQKADTASDT 185
Cdd:COG3096 389 EEVDSLKSQLadyqQALDV-QQTRAIQYQQAVQALEK-----ARAL------CGLPDLTPENAEDYLAAFRAKEQQATEE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 186 KGRQEPIPSDAAQEMQELGEKLQALERertKVEEVNRQQSAQLEQlvkelQLKEDARaSLERLVKEMAPLQEELSgkgqE 265
Cdd:COG3096 457 VLELEQKLSVADAARRQFEKAYELVCK---IAGEVERSQAWQTAR-----ELLRRYR-SQQALAQRLQQLRAQLA----E 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 266 ADQLWRRLQELlahtssweeelaelRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDH 345
Cdd:COG3096 524 LEQRLRQQQNA--------------ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 346 LSQQVGMLERLAgppgpelPVAGEKNEALvpvnSSLQEAWGKPEEEQRGLQEA--QLDDTKVQEGSQEEELRQANRELEK 423
Cdd:COG3096 590 LRARIKELAARA-------PAWLAAQDAL----ERLREQSGEALADSQEVTAAmqQLLEREREATVERDELAARKQALES 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 424 ELQNVVGRNQLLEGKLQALQADYQALQQRE-------------SAIQGSLAS------LEAEQASIRHLGDQMEASLL-- 482
Cdd:COG3096 659 QIERLSQPGGAEDPRLLALAERLGGVLLSEiyddvtledapyfSALYGPARHaivvpdLSAVKEQLAGLEDCPEDLYLie 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 483 --------AVRKAKEAMKAQMA--EKEAILQSKEGEC---------QQLREEVEQCQQLAEaRHRELRALESQCQQQTQL 543
Cdd:COG3096 739 gdpdsfddSVFDAEELEDAVVVklSDRQWRYSRFPEVplfgraareKRLEELRAERDELAE-QYAKASFDVQKLQRLHQA 817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 544 IEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLqakmRAALDDQDKVQSQLS-MAEAVLRE 622
Cdd:COG3096 818 FSQFVGGHLAVAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQL----KEQLQLLNKLLPQANlLADETLAD 893
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 623 hktLVQQLKEQNEALNRAhVQELLQCSEREGALqEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAEL----QEQL 698
Cdd:COG3096 894 ---RLEELREELDAAQEA-QAFIQQHGKALAQL-EPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALsevvQRRP 968
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 699 HRANTDTAELGIQVCALTvekERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGL 778
Cdd:COG3096 969 HFSYEDAVGLLGENSDLN---EKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL 1045
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925314 779 QAQL-AQAEQRAQSLQEAAHQELNTLKFQLS----------AEIMDYQSRLKNAGEECKSLRGQLEE 834
Cdd:COG3096 1046 GVQAdAEAEERARIRRDELHEELSQNRSRRSqlekqltrceAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| FYVE_PKHF2 |
cd15755 |
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ... |
970-1030 |
3.96e-10 |
|
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: 56.97 E-value: 3.96e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925314 970 WLGDTEANHCLDCKR-EFSWMVRRHHCRICGRIFCYYCC-NNYVLSKHGGKKERCCRACFQKL 1030
Cdd:cd15755 2 WVPDSEATVCMRCQKaKFTPVNRRHHCRKCGFVVCGPCSeKKFLLPSQSSKPVRVCDFCYDLL 64
|
|
| FYVE_ZFY26 |
cd15724 |
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ... |
970-1028 |
4.20e-10 |
|
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: 56.75 E-value: 4.20e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925314 970 WLGDTEANHCLDCKRE-FSWMVRRHHCRICGRIFCYYCCNNYVL-SKHGGKKERCCRACFQ 1028
Cdd:cd15724 1 WVPDEAVSVCMVCQVErFSMFNRRHHCRRCGRVVCSSCSTKKMLvEGYRENPVRVCDQCYE 61
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
115-807 |
4.46e-10 |
|
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: 64.22 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 115 LQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIPS 194
Cdd:TIGR00618 199 LTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 195 DA-AQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEElsgkgQEADQLWRRL 273
Cdd:TIGR00618 279 LEeTQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-----RRLLQTLHSQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 274 QELLAhtssweeelaelrrekkqqqeekelleqevRSLTRQLQFLETQLAQVS--QHVSDLEEQKKQLIQDKDHLSQQVG 351
Cdd:TIGR00618 354 EIHIR------------------------------DAHEVATSIREISCQQHTltQHIHTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 352 MLERLAGPPGPELpvageknEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKV-QEGSQEE----ELRQANRELEKELQ 426
Cdd:TIGR00618 404 ILQREQATIDTRT-------SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTaQCEKLEKihlqESAQSLKEREQQLQ 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 427 NVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGdqmeasllAVRKAKEAMKAQMAEKEAILQSKE 506
Cdd:TIGR00618 477 TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPG--------PLTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 507 GECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEkgQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQ 586
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNI--TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 587 RLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERAD----- 661
Cdd:TIGR00618 627 LQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQcqtll 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 662 -EAQQREEELRALQEELSQAKcSSEEAQLEhAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQ---ELQDAK 737
Cdd:TIGR00618 707 rELETHIEEYDREFNEIENAS-SSLGSDLA-AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQtgaELSHLA 784
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 738 EAASREREGLERQVAGLQQEKESLQEKLkaaKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQL 807
Cdd:TIGR00618 785 AEIQFFNRLREEDTHLLKTLEAEIGQEI---PSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-687 |
5.70e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 5.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 26 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEdnvRLTCLVAELQKQWEVT 105
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA---RLERLEDRRERLQQEI 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 106 QATQNTVKELQtcLQGLELGAAEKEEDYHTALRRLESmlqpLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDT 185
Cdd:TIGR02168 424 EELLKKLEEAE--LKELQAELEELEEELEELQEELER----LEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 186 KGRQEPIPSDAAQEMQE----------------------------LGEKLQAL------------------ERERTKVEE 219
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNqsglsgilgvlselisvdegyeaaieaaLGGRLQAVvvenlnaakkaiaflkqnELGRVTFLP 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 220 VNRQQSAQLEQLVKE-LQLKEDARASLERLVKEMAPLQEELSG---------KGQEADQLWRRLQ----------ELLAH 279
Cdd:TIGR02168 578 LDSIKGTEIQGNDREiLKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvvdDLDNALELAKKLRpgyrivtldgDLVRP 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 280 TSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERlagp 359
Cdd:TIGR02168 658 GGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK---- 733
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 360 pgpELPVAGEKNEALVPVNSSLQEAWGKPEEeqrglQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKL 439
Cdd:TIGR02168 734 ---DLARLEAEVEQLEERIAQLSKELTELEA-----EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 440 QALQADYQALQQRESAIQGSLASLEAEQASIrhlgdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 519
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAAT-------ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 520 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQqgvgppTDNEARELAAQLALSQAQLEVHQGEVQRLQAQV-VDLQAK 598
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSE------LRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLT 952
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 599 MRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAlnrahvqellqcseregALQEerADEAQQREEELRALQEELS 678
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA-----------------AIEE--YEELKERYDFLTAQKEDLT 1013
|
....*....
gi 1894925314 679 QAKCSSEEA 687
Cdd:TIGR02168 1014 EAKETLEEA 1022
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
454-897 |
7.05e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.82 E-value: 7.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 454 SAIQGSLAS-LEAEQASIRHLGDQMEASLLAVRKAKEAMKaqmaekeaILQSKEGECQQLREEVEQCQQLAEARHRELRA 532
Cdd:PRK04863 211 SAITRSLRDyLLPENSGVRKAFQDMEAALRENRMTLEAIR--------VTQSDRDLFKHLITESTNYVAADYMRHANERR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 533 LESQcqqqtqliEVLTAEKGQQGvgpptdneARElaaQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQ 612
Cdd:PRK04863 283 VHLE--------EALELRRELYT--------SRR---QLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 613 LSMAEAVLR---EHKTLVQQLKEQNEAlnRAHVQELLQCSEREGALQEERADEA-------QQREEEL--RALQEElsQA 680
Cdd:PRK04863 344 LRQQEKIERyqaDLEELEERLEEQNEV--VEEADEQQEENEARAEAAEEEVDELksqladyQQALDVQqtRAIQYQ--QA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 681 KCSSEEAQlehaelqEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLE--RQVAG----- 753
Cdd:PRK04863 420 VQALERAK-------QLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQlvRKIAGevsrs 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 754 -LQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEA----------------AHQELNTLKFQLSAEIMDYQS 816
Cdd:PRK04863 493 eAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAerllaefckrlgknldDEDELEQLQEELEARLESLSE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 817 RLKNAGEECKSLRGQLEEQGRQLQ----------AAEEAVEKLkatQADMGEKLScTSNHLAECQAAMLRKDKEGAALRE 886
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARIQrlaarapawlAAQDALARL---REQSGEEFE-DSQDVTEYMQQLLERERELTVERD 648
|
490
....*....|.
gi 1894925314 887 DLERTQKELEK 897
Cdd:PRK04863 649 ELAARKQALDE 659
|
|
| FYVE_FGD6 |
cd15743 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ... |
970-1027 |
8.29e-10 |
|
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: 55.91 E-value: 8.29e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1894925314 970 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNN-YVLSKHGGKKERCCRACF 1027
Cdd:cd15743 3 WIPDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNkAPLEYLKNKSARVCDECF 61
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
381-796 |
8.43e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 8.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 381 LQEAWGKPEEEQRGLQEAQLDDTKVQEGSQE-EELRQANRELEKELQN--VVGRNQLLEGKLQALQADYQALQQRESAIQ 457
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAElEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 458 GSLASLEAEQASIRHLGDQMEAsllAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQC 537
Cdd:COG4717 160 ELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 538 ---------QQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALS-------------QAQLEVHQGEVQRLQAQVVDL 595
Cdd:COG4717 237 eaaaleerlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgllallflllarEKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 596 QAKMRAALDDQDKVQSQLS--MAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcsEREGALQEERADEaqqrEEELRAL 673
Cdd:COG4717 317 EEEELEELLAALGLPPDLSpeELLELLDRIEELQELLREAEELEEELQLEELEQ--EIAALLAEAGVED----EEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 674 QEELSQAkcssEEAQLEHAELQEQLHRANTDTAELgiqvcALTVEKERVEEALacavQELQDAKEAASREREGLERQVAG 753
Cdd:COG4717 391 LEQAEEY----QELKEELEELEEQLEELLGELEEL-----LEALDEEELEEEL----EELEEELEELEEELEELREELAE 457
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1894925314 754 LQQEKESLQEKlkaakaaaGSLPGLQAQLAQAEQRAQSLQEAA 796
Cdd:COG4717 458 LEAELEQLEED--------GELAELLQELEELKAELRELAEEW 492
|
|
| FYVE_FGD1_2_4 |
cd15741 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ... |
969-1030 |
1.27e-09 |
|
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: 55.57 E-value: 1.27e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1894925314 969 RWLGDTEANHCLDCKREFSWMV-RRHHCRICGRIFCYYCCNNYV-LSKHGGKKERCCRACFQKL 1030
Cdd:cd15741 2 RWVRDNEVTMCMRCKEPFNALTrRRHHCRACGYVVCWKCSDYKAtLEYDGNKLNRVCKHCYVIL 65
|
|
| FYVE_ANFY1 |
cd15728 |
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ... |
967-1030 |
1.42e-09 |
|
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: 55.12 E-value: 1.42e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925314 967 EERWlgdTEANHCLDCKREFSWMVRRHHCRICGRIFCYYC-CNNYVLSKHG-GKKERCCRACFQKL 1030
Cdd:cd15728 1 EPPW---ADGDYCYECGVKFGITTRKHHCRHCGRLLCSKCsTKEVPIIKFDlNKPVRVCDVCFDVL 63
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
562-898 |
1.88e-09 |
|
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: 62.28 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 562 NEARELAAQLAlsqaQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRah 641
Cdd:COG3096 278 NERRELSERAL----ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIER-- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 642 vqellqcseregalqeeradeaqqREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVC----ALTV 717
Cdd:COG3096 352 ------------------------YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqALDV 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 718 EKER----------VEEALAC-------------------------------AVQELQDAKEAASREREGLE--RQVAG- 753
Cdd:COG3096 408 QQTRaiqyqqavqaLEKARALcglpdltpenaedylaafrakeqqateevleLEQKLSVADAARRQFEKAYElvCKIAGe 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 754 ------LQQEKESLqEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEA----------------AHQELNTLKFQLSAEI 811
Cdd:COG3096 488 versqaWQTARELL-RRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAerlleefcqrigqqldAAEELEELLAELEAQL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 812 MDYQSRLKNAGE---ECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAM---LRKDKEGAALR 885
Cdd:COG3096 567 EELEEQAAEAVEqrsELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMqqlLEREREATVER 646
|
410
....*....|...
gi 1894925314 886 EDLERTQKELEKA 898
Cdd:COG3096 647 DELAARKQALESQ 659
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
309-856 |
2.11e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 309 RSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQqvgMLERLAgppgpelpvagEKNEALVPVnsslqeawgkp 388
Cdd:PRK02224 202 KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADE---VLEEHE-----------ERREELETL----------- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 389 EEEQRGLQEAQLDDTKVQEGSQEE--ELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAE 466
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEvrDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 467 QASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEV 546
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 547 LTAEKGQQgVGPPTDNEA--RELAAQLALSQAQLEV--------------HQGEVQRLQAQVVDLQAKMRAALDDQDKVQ 610
Cdd:PRK02224 417 LREERDEL-REREAELEAtlRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 611 SQLSMAEAvLREHKTLVQQLKEQNEAlnrahVQELLqcseregALQEERADEAQQREEELRALQEEL-SQAKCSSEEAQL 689
Cdd:PRK02224 496 ERLERAED-LVEAEDRIERLEERRED-----LEELI-------AERRETIEEKRERAEELRERAAELeAEAEEKREAAAE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 690 EHAELQEQLHRAntdtAELGIQVCALTVEKERVEeALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAK 769
Cdd:PRK02224 563 AEEEAEEAREEV----AELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKR 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 770 AAAGSLPGLQAQLAQAE-QRAQSLQEAAHQELNTL---KFQLSAEIMDYQSRLKNAgEECKSLRGQLEEQGRQLQAAEEA 845
Cdd:PRK02224 638 ELEAEFDEARIEEAREDkERAEEYLEQVEEKLDELreeRDDLQAEIGAVENELEEL-EELRERREALENRVEALEALYDE 716
|
570
....*....|.
gi 1894925314 846 VEKLKATQADM 856
Cdd:PRK02224 717 AEELESMYGDL 727
|
|
| FYVE_WDFY3 |
cd15719 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ... |
970-1030 |
2.33e-09 |
|
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: 54.70 E-value: 2.33e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925314 970 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNN--YVLSKHGGKKERCCRACFQKL 1030
Cdd:cd15719 3 WVKDEGGDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFesEIRRLRISRPVRVCQACYNIL 65
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
363-976 |
3.42e-09 |
|
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: 61.62 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 363 ELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANrELEKELQNVVGRNQLLEGKLQAL 442
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKE-ALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 443 QADYQALQQRESAIQGSLASLEAEqasIRHLGdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQL 522
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKK---IKDLG---EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 523 AEARHRELRALESQCQQQTQLIEVLTAE-KGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRA 601
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 602 ALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALN---RAHVQELLQCSE-REGALQEERADEAQQR--EEELRALQE 675
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAleiKKQEWKLEQLAAdLSKYEQELYDLKEEYDrvEKELSKLQR 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 676 ELSQAkcsseEAQLEHAELQEQLHRANTDTAELGIQ-VCALTVEKERVEEALACAVQ-----ELQ----DAKEAASRERE 745
Cdd:TIGR02169 491 ELAEA-----EAQARASEERVRGGRAVEEVLKASIQgVHGTVAQLGSVGERYATAIEvaagnRLNnvvvEDDAVAKEAIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 746 GLERQVAGLQ--------QEKESLQEKLKAAKAAA--------------------------------------------- 772
Cdd:TIGR02169 566 LLKRRKAGRAtflplnkmRDERRDLSILSEDGVIGfavdlvefdpkyepafkyvfgdtlvvedieaarrlmgkyrmvtle 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 773 ------------GSLPGLQAQLAQAEQRAQSLQEAAH-QELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQL 839
Cdd:TIGR02169 646 gelfeksgamtgGSRAPRGGILFSRSEPAELQRLRERlEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 840 QAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEK--------ATTKIQEYYNKLCQ 911
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlshsRIPEIQAELSKLEE 805
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925314 912 EVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALwqKSDALEFQQKLSAEERWLGDTEA 976
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL--KEQIKSIEKEIENLNGKKEELEE 868
|
|
| FYVE_spVPS27p_like |
cd15735 |
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ... |
974-1027 |
4.21e-09 |
|
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: 53.69 E-value: 4.21e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925314 974 TEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE--RCCRACF 1027
Cdd:cd15735 4 VDSDVCMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPHFGINQpvRVCDGCY 59
|
|
| FYVE_ZFY19 |
cd15749 |
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ... |
979-1027 |
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: 53.28 E-value: 4.45e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1894925314 979 CLDCKREFSWMVRRHHCRICGRIFCYYCCN-NYVLSKHGGKKERCCRACF 1027
Cdd:cd15749 2 CFGCAAKFSLFKKECGCKNCGRSFCKGCLTfSAVVPRKGNQKQKVCKQCH 51
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
203-850 |
4.82e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 203 LGEKLQALERERTKVEEVnRQQSAQLEQLVKElqlKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELlahtss 282
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKF-IKRTENIEELIKE---KEKELEEVLREINEISSELPELREELEKLEKEVKELEEL------ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 283 weeelaelRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQliqdkdhlsqqvgmLERLAGPPGP 362
Cdd:PRK03918 237 --------KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE--------------LKELKEKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 363 ELPVAGEKNEALVPVNsSLQEAWGKPEEEQRGLQEaqlddtKVQEGSQEEELRQANRELEKELQNVVGRnqlLEGKLQAL 442
Cdd:PRK03918 295 YIKLSEFYEEYLDELR-EIEKRLSRLEEEINGIEE------RIKELEEKEERLEELKKKLKELEKRLEE---LEERHELY 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 443 QaDYQALQQRESAIQGSLASLEAEQAsirhlgdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEqcqql 522
Cdd:PRK03918 365 E-EAKAKKEELERLKKRLTGLTPEKL---------EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE----- 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 523 aearhrELRALESQCQQQTQLIevltaekgqqgvgppTDNEARELaaqlalsqaqLEVHQGEVQRLQAQVVDLQAKMRAA 602
Cdd:PRK03918 430 ------ELKKAKGKCPVCGREL---------------TEEHRKEL----------LEEYTAELKRIEKELKEIEEKERKL 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 603 LDDQDKVQSQLSMAEAVLREHKTLvQQLKEQNEALNRAHVQELlqcsEREGALQEERADEAQQREEELRALQEELSQAK- 681
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELA-EQLKELEEKLKKYNLEEL----EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEe 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 682 CSSEEAQLEHA--ELQEQLHRANTDTAELGIQvcALTVEKERVEEaLACAVQELQDAKEAASREREGLERqvagLQQEKE 759
Cdd:PRK03918 554 LKKKLAELEKKldELEEELAELLKELEELGFE--SVEELEERLKE-LEPFYNEYLELKDAEKELEREEKE----LKKLEE 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 760 SLQEKLKAAKAAAGSLPGLQAQLAQAEQRaqsLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQL 839
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKK---YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
650
....*....|.
gi 1894925314 840 QAAEEAVEKLK 850
Cdd:PRK03918 704 EEREKAKKELE 714
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
38-904 |
6.84e-09 |
|
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: 60.57 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 38 ELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTC-----------LVAELQKQWEVTQ 106
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAArkqeleeilheLESRLEEEEERSQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 107 ATQNTVKELQTCLQGLElGAAEKEEDYHTALR----RLESMLQPLAQELEATRDSLDKKN-------QHLASFPGWLAMA 175
Cdd:pfam01576 93 QLQNEKKKMQQHIQDLE-EQLDEEEAARQKLQlekvTTEAKIKKLEEDILLLEDQNSKLSkerklleERISEFTSNLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 176 QQKADTASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEevnrQQSAQLEQLVKELQLK-EDARASLERLVKEMAP 254
Cdd:pfam01576 172 EEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLE----GESTDLQEQIAELQAQiAELRAQLAKKEEELQA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 255 LQEELSGKGQEADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQ-FLETQLAQV---SQHVS 330
Cdd:pfam01576 248 ALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdTLDTTAAQQelrSKREQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 331 DLEEQKKQLIQDKDHLSQQVGMLERlagppgpelpvagEKNEALVPVNSSLqeawgkpeeEQRGLQEAQLDDTKVQEGSQ 410
Cdd:pfam01576 328 EVTELKKALEEETRSHEAQLQEMRQ-------------KHTQALEELTEQL---------EQAKRNKANLEKAKQALESE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 411 EEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEA 490
Cdd:pfam01576 386 NAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 491 MKAQMAEKEAILQ-------SKEGECQQLREEVEQCQQLAEARHRELRALESQCQQ-QTQLIEVLTAEKGQQGVGPPTDN 562
Cdd:pfam01576 466 LESQLQDTQELLQeetrqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTlQAQLSDMKKKLEEDAGTLEALEE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 563 EARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEavlREHKTLVQQLKEQNEALNRAhv 642
Cdd:pfam01576 546 GKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLE---KKQKKFDQMLAEEKAISARY-- 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 643 qellqCSEREGAlqeeradEAQQREEELRALQeeLSQAkcsSEEAQlehaELQEQLHRANTdtaELGIQVCALTVEKERV 722
Cdd:pfam01576 621 -----AEERDRA-------EAEAREKETRALS--LARA---LEEAL----EAKEELERTNK---QLRAEMEDLVSSKDDV 676
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 723 EEalacAVQELQDAKEAasreregLERQVAGLQQEKESLQEKLKAAKAAAGSLP-GLQAQLAQAEQRAQSLQEAAHQELN 801
Cdd:pfam01576 677 GK----NVHELERSKRA-------LEQQVEEMKTQLEELEDELQATEDAKLRLEvNMQALKAQFERDLQARDEQGEEKRR 745
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 802 TLKFQ---LSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAA----EEAVEKLKATQADMGEklsctsnHLAECQAAM 874
Cdd:pfam01576 746 QLVKQvreLEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAAnkgrEEAVKQLKKLQAQMKD-------LQRELEEAR 818
|
890 900 910
....*....|....*....|....*....|
gi 1894925314 875 LRKDKEGAALREDlERTQKELEKATTKIQE 904
Cdd:pfam01576 819 ASRDEILAQSKES-EKKLKNLEAELLQLQE 847
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
192-968 |
1.31e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 59.60 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 192 IPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLE--------RLVKEMAPLQEELSGKG 263
Cdd:pfam02463 157 EIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlkeklELEEEYLLYLDYLKLNE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 264 QEADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDK 343
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 344 DHLSQQVGMLERLagppgpelpvagEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEK 423
Cdd:pfam02463 317 KESEKEKKKAEKE------------LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 424 ELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIR----------HLGDQMEASLLAVRKAKEAMKA 493
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILeeeeesielkQGKLTEEKEELEKQELKLLKDE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 494 QMAEKEAILQSKEGECQQLREEVEQC--QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQL 571
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLsrQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 572 ALSQAQLEVHQGEVQRLQAQVvdLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLvqqlkEQNEALNRAHVQELLQCSER 651
Cdd:pfam02463 545 ISTAVIVEVSATADEVEERQK--LVRALTELPLGARKLRLLIPKLKLPLKSIAVL-----EIDPILNLAQLDKATLEADE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 652 EGALQEERADeaqQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQ 731
Cdd:pfam02463 618 DDKRAKVVEG---ILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEI 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 732 ELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEI 811
Cdd:pfam02463 695 LRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 812 MDYQSRLKNageECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLsctsnhLAECQAAMLRKDKEGAALREDLERT 891
Cdd:pfam02463 775 ELAEEREKT---EKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEE------QLLIEQEEKIKEEELEELALELKEE 845
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925314 892 QKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEE 968
Cdd:pfam02463 846 QKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEER 922
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
411-905 |
1.37e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 411 EEELRQANRELEKE----LQNVVGRNQLLEGKLQALQ---ADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEA--SL 481
Cdd:COG4717 48 LERLEKEADELFKPqgrkPELNLKELKELEEELKEAEekeEEYAELQEELEELEEELEELEAELEELREELEKLEKllQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 482 LAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEarhrELRALESQCQQQTQLIEVLTAEKGQQgvgppTD 561
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA----ELAELQEELEELLEQLSLATEEELQD-----LA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 562 NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAAlDDQDKVQSQLSMAEAVLRehkTLVQQLKEQNEALNRAH 641
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARLLLLIAAA---LLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 642 VQELLQcseregALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLhrantdtAELGIqvcALTVEKER 721
Cdd:COG4717 275 IAGVLF------LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL-------AALGL---PPDLSPEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 722 VEEALAcAVQELQDAKEAASREREglERQVAGLQQEKESLQEKLKAAKAaagslpglqAQLAQAEQRAQSLQEAAhQELN 801
Cdd:COG4717 339 LLELLD-RIEELQELLREAEELEE--ELQLEELEQEIAALLAEAGVEDE---------EELRAALEQAEEYQELK-EELE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 802 TLKFQLSAEIMDYQSRLKNAGEEckSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSctsnhlaecqaaMLRKDKEG 881
Cdd:COG4717 406 ELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELE------------QLEEDGEL 471
|
490 500
....*....|....*....|....
gi 1894925314 882 AALREDLERTQKELEKATTKIQEY 905
Cdd:COG4717 472 AELLQELEELKAELRELAEEWAAL 495
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
567-794 |
2.43e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 567 LAAQLALSQAQLEVHQGEVQRLQAQ--VVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNeALNRAHVQE 644
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL-GSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 645 LLQcSEREGALQEERADEAQQREEELRALQEELSQAKcsseeaqlehaELQEQLhrantdtaelgiqvcaltvekERVEE 724
Cdd:COG3206 259 LLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVI-----------ALRAQI---------------------AALRA 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 725 ALAcavQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKaakaaagSLPGLQAQLAQAEQRAQSLQE 794
Cdd:COG3206 306 QLQ---QEAQRILASLEAELEALQAREASLQAQLAQLEARLA-------ELPELEAELRRLEREVEVARE 365
|
|
| FYVE_PKHF1 |
cd15754 |
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ... |
970-1030 |
2.60e-08 |
|
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: 51.88 E-value: 2.60e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925314 970 WLGDTEANHCLDCKR-EFSWMVRRHHCRICGRIFCYYCCN-NYVLSKHGGKKERCCRACFQKL 1030
Cdd:cd15754 2 WIPDKATDICMRCTQtNFSLLTRRHHCRKCGFVVCHECSRqRFLIPRLSPKPVRVCSLCYRKL 64
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
390-756 |
2.69e-08 |
|
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: 58.81 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 390 EEQRGLQEAQLDDTKVQEGSQEE--ELRQANRELEKELQNVVGRNQLLEGKLQA----LQADYQALQQRESaiqgslasL 463
Cdd:COG3096 278 NERRELSERALELRRELFGARRQlaEEQYRLVEMARELEELSARESDLEQDYQAasdhLNLVQTALRQQEK--------I 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 464 EAEQASIRHLGDQMEASLLAVRKAKEamkaQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRE-------LRALEsQ 536
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAE----QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRaiqyqqaVQALE-K 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 537 CQQQTQLIEvLTAE-----------KGQQGvgpptDNEARELAAQLALSQAQLEVHQ----------GEVQRLQA----- 590
Cdd:COG3096 425 ARALCGLPD-LTPEnaedylaafraKEQQA-----TEEVLELEQKLSVADAARRQFEkayelvckiaGEVERSQAwqtar 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 591 QVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNR-------------AHVQELLQCSEREGALQE 657
Cdd:COG3096 499 ELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQqldaaeeleellaELEAQLEELEEQAAEAVE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 658 ERAdEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELgIQVCALTVEKERveealacavqELQDAK 737
Cdd:COG3096 579 QRS-ELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEV-TAAMQQLLERER----------EATVER 646
|
410
....*....|....*....
gi 1894925314 738 EAASREREGLERQVAGLQQ 756
Cdd:COG3096 647 DELAARKQALESQIERLSQ 665
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
396-904 |
3.28e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 396 QEAQLDDTKVQ-EGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLg 474
Cdd:PRK02224 185 QRGSLDQLKAQiEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDL- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 475 dqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVE---QCQQLAEARHRELRALESQCQQQTQLIEVLTAEK 551
Cdd:PRK02224 264 ---RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAH 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 552 GQQGVGPPTD------------NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLsmaEAV 619
Cdd:PRK02224 341 NEEAESLREDaddleeraeelrEEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL---EEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 620 LREHKTLVQQLKE-----QNEALNRAHVQELL---QCSEREGALQE-ERADEAQQREEELRALQEELsqakcssEEAQLE 690
Cdd:PRK02224 418 REERDELREREAEleatlRTARERVEEAEALLeagKCPECGQPVEGsPHVETIEEDRERVEELEAEL-------EDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 691 HAELQEQLHRAnTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKA 770
Cdd:PRK02224 491 VEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 771 AAGSLPGLQAQLAQAEQRAQSLqeaahqelntlkfqlsAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLK 850
Cdd:PRK02224 570 AREEVAELNSKLAELKERIESL----------------ERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR 633
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1894925314 851 ATQADMGEKLSctsnhlaecqaamlrkDKEGAALREDLERTQKELEKATTKIQE 904
Cdd:PRK02224 634 ERKRELEAEFD----------------EARIEEAREDKERAEEYLEQVEEKLDE 671
|
|
| FYVE_FGD5 |
cd15742 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ... |
979-1030 |
3.44e-08 |
|
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: 51.47 E-value: 3.44e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1894925314 979 CLDCKREFSWMVRRHHCRICGRIFCYYCC-NNYVLSKHGGKKERCCRACFQKL 1030
Cdd:cd15742 12 CMNCGSDFTLTLRRHHCHACGKIVCRNCSrNKYPLKYLKDRPAKVCDGCFAEL 64
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
520-764 |
3.50e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 520 QQLAEARHRELRALESQCQQQTQLIEVLTAEKgqqgvgpptdneaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKM 599
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEE-------------KALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 600 RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcSEREGALQEERADEAQQREEELRALQEELSQ 679
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 680 AKcssEEAQLEHAELQEQLHRANTDTAELGiqvcALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKE 759
Cdd:COG4942 165 LR---AELEAERAELEALLAELEEERAALE----ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
....*
gi 1894925314 760 SLQEK 764
Cdd:COG4942 238 AAAER 242
|
|
| FYVE_scVPS27p_Vac1p_like |
cd15736 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
979-1027 |
5.60e-08 |
|
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: 50.64 E-value: 5.60e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1894925314 979 CLDCKREFSWMVRRHHCRICGRIFC-YYCCNNYVLSKHG-----GKKERCCRACF 1027
Cdd:cd15736 2 CHTCSRTFNLNIRAHHCRKCGKLFCrRHLPNMIPLNLSAydprnGKWYRCCHSCF 56
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
311-964 |
9.54e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 9.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 311 LTRQLQFLETQLAQVSQH---VSDLEEQKKQLIQDKDHLsqqvgmlerlagppgpelpvaGEKNEALVPVNSSLQEAWGK 387
Cdd:PRK04863 319 LNEAESDLEQDYQAASDHlnlVQTALRQQEKIERYQADL---------------------EELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 388 PEEEQRGLQEAQL--DDTK-----VQEGSQEEELR-----QANRELEK----------ELQNVVGRNQLLEGKLQALQAD 445
Cdd:PRK04863 378 QEENEARAEAAEEevDELKsqladYQQALDVQQTRaiqyqQAVQALERakqlcglpdlTADNAEDWLEEFQAKEQEATEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 446 YQALQQRESAIQGSLASLEAEQASIRHLGDQMEASlLAVRKAKEAmkaqmaekeailqskegeCQQLREEVEQCQQLaEA 525
Cdd:PRK04863 458 LLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRS-EAWDVAREL------------------LRRLREQRHLAEQL-QQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 526 RHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLalsQAQLEVHQGEvqrlQAQVVDLQAKMRAALDD 605
Cdd:PRK04863 518 LRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEEL---EARLESLSES----VSEARERRMALRQQLEQ 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 606 QDKVQSQLSMAEAVLREHKTLVQQLKEQNEA--LNRAHVQELLQ-CSEREGALQEERaDEAQQREEELRALQEELSQAKC 682
Cdd:PRK04863 591 LQARIQRLAARAPAWLAAQDALARLREQSGEefEDSQDVTEYMQqLLERERELTVER-DELAARKQALDEEIERLSQPGG 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 683 SSEEAQLEHAE------LQE-----QLHRANTDTAELGIQVCALTV-EKERVEEALA----C------------------ 728
Cdd:PRK04863 670 SEDPRLNALAErfggvlLSEiyddvSLEDAPYFSALYGPARHAIVVpDLSDAAEQLAgledCpedlyliegdpdsfddsv 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 729 -AVQELQDA--KEAASRE-------------REGLERQVAGLQQEKESLQEKLkaakaaagslpglqAQLAQAEQRAQSL 792
Cdd:PRK04863 750 fSVEELEKAvvVKIADRQwrysrfpevplfgRAAREKRIEQLRAEREELAERY--------------ATLSFDVQKLQRL 815
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 793 QEAAHQELNT---LKFQL--SAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADM--------GEK 859
Cdd:PRK04863 816 HQAFSRFIGShlaVAFEAdpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLnlladetlADR 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 860 LSCTSNHLAECQAAMLRKDKEGAALR-------------EDLERTQKELEKATTKIQEYYNK---LCQEVTNRE----RN 919
Cdd:PRK04863 896 VEEIREQLDEAEEAKRFVQQHGNALAqlepivsvlqsdpEQFEQLKQDYQQAQQTQRDAKQQafaLTEVVQRRAhfsyED 975
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1894925314 920 DQKMLADLDDLN-RTKKYLEERLIELLRDKDALWQK----SDALEFQQKL 964
Cdd:PRK04863 976 AAEMLAKNSDLNeKLRQRLEQAEQERTRAREQLRQAqaqlAQYNQVLASL 1025
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
567-832 |
1.58e-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: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 567 LAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRahvqELL 646
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA----ELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 647 QCSEREGALQEERADEAQQREEELRALQEelsqakcSSEEAQLEHAELQEQLHRANTDTAELGiqvcALTVEKERVEEAL 726
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYR-------LGRQPPLALLLSPEDFLDAVRRLQYLK----YLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 727 ACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQEAAhQELNTLKFQ 806
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEA-EELEALIAR 231
|
250 260
....*....|....*....|....*.
gi 1894925314 807 LSAEIMDYQSRLKNAGEecKSLRGQL 832
Cdd:COG4942 232 LEAEAAAAAERTPAAGF--AALKGKL 255
|
|
| FYVE_MTMR_unchar |
cd15738 |
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ... |
970-1027 |
2.13e-07 |
|
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: 48.86 E-value: 2.13e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 970 WLGDTEANHClDCKREFSWMVRRHHCRICGRIFCYYCCNNYV-LSKH-GGKKERCCRACF 1027
Cdd:cd15738 3 WKSFRNVTEC-SCSTPFDHFSKKHHCWRCGNVFCTRCIDKQRaLPGHlSQRPVPVCRACY 61
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
406-632 |
3.01e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 406 QEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQ--ALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLA 483
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 484 VRKAKEAMKAQMAE--KEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEvltaekgqqgvgpptd 561
Cdd:COG3206 245 LRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ---------------- 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925314 562 neaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKE 632
Cdd:COG3206 309 ---QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
19-765 |
3.33e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 19 DLNSPLNNEALEGFDEMRLELDQLEVREkqlrerMQQLDRENQ-----ELRAAVSQQGEQLQTERERGRTAAEDNVRLTC 93
Cdd:PTZ00121 1019 DFNQNFNIEKIEELTEYGNNDDVLKEKD------IIDEDIDGNhegkaEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEA 1092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 94 LVAELQKQWEVTQATQNTVKELQTCLQglelgAAEKEEDYHTA--LRRLESmlqplAQELEATRDSLDKKNQHLASfpgw 171
Cdd:PTZ00121 1093 TEEAFGKAEEAKKTETGKAEEARKAEE-----AKKKAEDARKAeeARKAED-----ARKAEEARKAEDAKRVEIAR---- 1158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 172 lamAQQKADTASDTKGRQEPIPSDAAQEMQELGEKlqaleRERTKVEEVNRQQSAQLEQLVKELqlkEDARASLERLVKE 251
Cdd:PTZ00121 1159 ---KAEDARKAEEARKAEDAKKAEAARKAEEVRKA-----EELRKAEDARKAEAARKAEEERKA---EEARKAEDAKKAE 1227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 252 MAPLQEELSGKGQEAdqlwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSD 331
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEA----KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 332 LEEQKKQLIQDK--DHLSQQVGMLERLAGPPGPELPVAGEKNEAlvpvnsSLQEAWGKPEEEQRGLQEAQLDDTKVQEGS 409
Cdd:PTZ00121 1304 ADEAKKKAEEAKkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEA------AKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 410 QE--------EELRQANrELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQA----SIRHLGDQM 477
Cdd:PTZ00121 1378 KKadaakkkaEEKKKAD-EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAkkadEAKKKAEEA 1456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 478 EASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEV----EQCQQLAEARHR--ELRALES--------QCQQQTQL 543
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAkkkaDEAKKAAEAKKKadEAKKAEEakkadeakKAEEAKKA 1536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 544 IEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLR-- 621
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKae 1616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 622 EHKTLVQQLKEQNEAlnRAHVQELLQCSEREGALQEE----------RADEAQQREEELRALQEELSQA---KCSSEEAQ 688
Cdd:PTZ00121 1617 EAKIKAEELKKAEEE--KKKVEQLKKKEAEEKKKAEElkkaeeenkiKAAEEAKKAEEDKKKAEEAKKAeedEKKAAEAL 1694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 689 LEHAELQ---EQLHRANTDTAELGIQV-CALTVEKERVEEALACAVQELQDAKEAasREREGLERQVAGLQQEKESLQEK 764
Cdd:PTZ00121 1695 KKEAEEAkkaEELKKKEAEEKKKAEELkKAEEENKIKAEEAKKEAEEDKKKAEEA--KKDEEEKKKIAHLKKEEEKKAEE 1772
|
.
gi 1894925314 765 L 765
Cdd:PTZ00121 1773 I 1773
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
173-908 |
3.75e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 173 AMAQQKAD-TASDTKGRQEPIPSDAAQEMQELGEKLQALER--ERTKVEEVNRQQSAQLEQLVKELQlkEDARASLERLV 249
Cdd:PTZ00121 1083 AKEDNRADeATEEAFGKAEEAKKTETGKAEEARKAEEAKKKaeDARKAEEARKAEDARKAEEARKAE--DAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 250 KEMAplQEELSGKGQEAdqlwRRLQEllAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHV 329
Cdd:PTZ00121 1161 EDAR--KAEEARKAEDA----KKAEA--ARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 330 SDL---EEQKKQLIQDKDHLSQQVGMLERLAGPPGPELPVAGE---KNEALVPVNSSLQEAWGKPEEEQRGLQEAQlddT 403
Cdd:PTZ00121 1233 EEAkkdAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEearKADELKKAEEKKKADEAKKAEEKKKADEAK---K 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 404 KVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLA 483
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 484 VRKAKEAMK--------AQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQtqliEVLTAEKGQQG 555
Cdd:PTZ00121 1390 KKKADEAKKkaeedkkkADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE----EAKKAEEAKKK 1465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 556 VGPPTDNEARELAAQLALSQAQLEvHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLK---E 632
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAK-KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaeE 1544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 633 QNEALNRAHVQELLQCSEREGALQEERADE---------------AQQREEELRALQEELSQAKCSSEEAQLEHAELQEQ 697
Cdd:PTZ00121 1545 KKKADELKKAEELKKAEEKKKAEEAKKAEEdknmalrkaeeakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 698 LHRANTDTAELGIQVCALTVEKERVEEAL----ACAVQELQDAKEAASREREGLERQVAglQQEKESLQEKLKAAKAAAG 773
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKkaeeENKIKAAEEAKKAEEDKKKAEEAKKA--EEDEKKAAEALKKEAEEAK 1702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 774 SLPGLQAQLAQAEQRAQSLQEAahQELNTLKfqlsaeimdyqsrlknaGEECKslRGQLEEQGRQLQAAEEAVEKLKATQ 853
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKA--EEENKIK-----------------AEEAK--KEAEEDKKKAEEAKKDEEEKKKIAH 1761
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1894925314 854 ADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNK 908
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
660-899 |
4.18e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 660 ADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAelgiqvcaltvekerveeALACAVQELQDAKEA 739
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA------------------ALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 740 ASREREGLERQVAGLQQEKESLQEKLKA---AKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQS 816
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAEllrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 817 RLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELE 896
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
...
gi 1894925314 897 KAT 899
Cdd:COG4942 241 ERT 243
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
34-765 |
4.29e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 34 EMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQG--EQLQTERERGRTAAEDNVRLTCLVAELQKQWEV-TQATQN 110
Cdd:PRK04863 311 EMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEkiERYQADLEELEERLEEQNEVVEEADEQQEENEArAEAAEE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 111 TVKELQTCL----QGLELgAAEKEEDYHTALRRLESM-----LQPLAQE-LEATRDSLDKKNQHLASFpgwLAMAQQKAD 180
Cdd:PRK04863 391 EVDELKSQLadyqQALDV-QQTRAIQYQQAVQALERAkqlcgLPDLTADnAEDWLEEFQAKEQEATEE---LLSLEQKLS 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 181 TASDTKGRQEPI------------PSDAAQEMQEL----------GEKLQALERERTKVEEVNRQQsAQLEQLVKEL--- 235
Cdd:PRK04863 467 VAQAAHSQFEQAyqlvrkiagevsRSEAWDVARELlrrlreqrhlAEQLQQLRMRLSELEQRLRQQ-QRAERLLAEFckr 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 236 ------------QLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAelrrekkqqqeekel 303
Cdd:PRK04863 546 lgknlddedeleQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQD--------------- 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 304 leqevrSLTR-QLQFLETQL--AQVSQHVSDLEEQKKQLIQDKDHLSQQVGML----ERLAGPPGPELPVAGEKNEALVP 376
Cdd:PRK04863 611 ------ALARlREQSGEEFEdsQDVTEYMQQLLERERELTVERDELAARKQALdeeiERLSQPGGSEDPRLNALAERFGG 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 377 VnsSLQEAWgkpeeeqrglqeaqlDDTKVQEGSQEE----ELRQA--NRELEKELQNVVGRNQLLEgKLQALQADYQALQ 450
Cdd:PRK04863 685 V--LLSEIY---------------DDVSLEDAPYFSalygPARHAivVPDLSDAAEQLAGLEDCPE-DLYLIEGDPDSFD 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 451 QresaiqGSLASLEAEQASIRHLGD-QMEASL-----LAVRKAKEAmkaQMAEKEAILQSKEGECQQLREEVEQCQQLAE 524
Cdd:PRK04863 747 D------SVFSVEELEKAVVVKIADrQWRYSRfpevpLFGRAAREK---RIEQLRAEREELAERYATLSFDVQKLQRLHQ 817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 525 A------------------------------RHRELRALESQCQQQTQLIEvlTAEKGQQGVG-----------PPTDNE 563
Cdd:PRK04863 818 AfsrfigshlavafeadpeaelrqlnrrrveLERALADHESQEQQQRSQLE--QAKEGLSALNrllprlnlladETLADR 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 564 ARELAAQLA-LSQAQLEVHQGevQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEalNRAH- 641
Cdd:PRK04863 896 VEEIREQLDeAEEAKRFVQQH--GNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQ--RRAHf 971
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 642 -----VQELLQCSEREGALQEERADEAQQRE---EELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVC 713
Cdd:PRK04863 972 syedaAEMLAKNSDLNEKLRQRLEQAEQERTrarEQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPAD 1051
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1894925314 714 altvekERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKL 765
Cdd:PRK04863 1052 ------SGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKL 1097
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
34-698 |
5.32e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 34 EMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQgEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVK 113
Cdd:TIGR00618 202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQT-QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 114 ELQTCLQglELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLAsfpgwlAMAQQKADTASDTKgrqepip 193
Cdd:TIGR00618 281 ETQERIN--RARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA------AHVKQQSSIEEQRR------- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 194 sdAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEElSGKGQEADQLWRRL 273
Cdd:TIGR00618 346 --LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE-QATIDTRTSAFRDL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 274 QELLAHTSSWEEELAELRREKKQ----QQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQ 349
Cdd:TIGR00618 423 QGQLAHAKKQQELQQRYAELCAAaitcTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 350 VGMLERLAGPPGPELPVAGEKNEALVPV---------------------NSSLQEAWGKPEEEQRGLQEAQLDDTKVQEG 408
Cdd:TIGR00618 503 PCPLCGSCIHPNPARQDIDNPGPLTRRMqrgeqtyaqletseedvyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRS 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 409 SQE--------EELRQANRELEKELQNVVGRNQLLEGKLQALQADYQA---LQQRESAIQGSLASLEAEQASIrhLGDQM 477
Cdd:TIGR00618 583 KEDipnlqnitVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVrlhLQQCSQELALKLTALHALQLTL--TQERV 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 478 EASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLievltaekgqqgvg 557
Cdd:TIGR00618 661 REHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENA-------------- 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 558 pptdneareLAAQLALSQAQLEVHQGEVQRLQAQvvdlqakMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAL 637
Cdd:TIGR00618 727 ---------SSSLGSDLAAREDALNQSLKELMHQ-------ARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFF 790
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925314 638 NRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQL 698
Cdd:TIGR00618 791 NRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
379-968 |
5.39e-07 |
|
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: 54.46 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 379 SSLQEAWGKPEEEQRGL--QEAQLDDTKVQEGSQEEELRQanrELEKELQNVVGRNQLLEGKLQALQADYQALQQ-RESA 455
Cdd:pfam12128 311 SAADAAVAKDRSELEALedQHGAFLDADIETAAADQEQLP---SWQSELENLEERLKALTGKHQDVTAKYNRRRSkIKEQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 456 IQGSLASLEAEQASIRhlgdqmeasllavrkakEAMKAQMAEKEAILQskeGECQQLREEVEQcqQLAEARhrelrales 535
Cdd:pfam12128 388 NNRDIAGIKDKLAKIR-----------------EARDRQLAVAEDDLQ---ALESELREQLEA--GKLEFN--------- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 536 qcQQQTQLIEVLTAEKGQQGVGPPTDnearELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSM 615
Cdd:pfam12128 437 --EEEYRLKSRLGELKLRLNQATATP----ELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQ 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 616 AEAVLREHKTLVQQLKEQNEAlnRAHvqELLQCSEREGALQEERADEAQQREEELRA-LQEELSQAKCSSEEA------- 687
Cdd:pfam12128 511 ASRRLEERQSALDELELQLFP--QAG--TLLHFLRKEAPDWEQSIGKVISPELLHRTdLDPEVWDGSVGGELNlygvkld 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 688 --QLEH---AELQEQLhRANTDTAELGIQvcALTVEKERVEEALACAVQELQDAKEAASREREGLE-------RQVAGLQ 755
Cdd:pfam12128 587 lkRIDVpewAASEEEL-RERLDKAEEALQ--SAREKQAAAEEQLVQANGELEKASREETFARTALKnarldlrRLFDEKQ 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 756 QEKESLQEKLKaakaaagslpglqAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEImdyqsrlknageeckslRGQLEEQ 835
Cdd:pfam12128 664 SEKDKKNKALA-------------ERKDSANERLNSLEAQLKQLDKKHQ-AWLEEQ-----------------KEQKREA 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 836 GRQLQAAEEAVEKLKATQADM--GEKLSCTSNHLAECQAAMLRKDKEGAAL-------------REDLERTQKELEKATT 900
Cdd:pfam12128 713 RTEKQAYWQVVEGALDAQLALlkAAIAARRSGAKAELKALETWYKRDLASLgvdpdviaklkreIRTLERKIERIAVRRQ 792
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925314 901 KIQEYYNKLcQEVTNRERndQKMLADLDDLNRTKKYLEERLIELL----RDKDALWQKSDALEFQQKLSAEE 968
Cdd:pfam12128 793 EVLRYFDWY-QETWLQRR--PRLATQLSNIERAISELQQQLARLIadtkLRRAKLEMERKASEKQQVRLSEN 861
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
236-490 |
5.89e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 236 QLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELlahtssweeelaelrrekkqqqeekellEQEVRSLTRQL 315
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----------------------------ERRIAALARRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 316 QFLETQLAQVSQHVSDLEEQ----KKQLIQDKDHLSQQVGMLERLAGPPGPELPVAGEKNEALVPVNSSLQEAwgkpeEE 391
Cdd:COG4942 72 RALEQELAALEAELAELEKEiaelRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-----AP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 392 QRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIR 471
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*....
gi 1894925314 472 HLGDQMEASLLAVRKAKEA 490
Cdd:COG4942 227 ALIARLEAEAAAAAERTPA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
200-724 |
6.67e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 200 MQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAH 279
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 280 TSSWEEElaelrrekkqqqeekelleqevRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLiqdkDHLSQQVGMLERlagp 359
Cdd:COG4717 128 LPLYQEL----------------------EALEAELAELPERLEELEERLEELRELEEEL----EELEAELAELQE---- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 360 pgpelpvagEKNEALVPVNSSLQEAWGKPEEEQrglqeaqlddtkvqegsqeEELRQANRELEKELQNVVGRNQLLEGKL 439
Cdd:COG4717 178 ---------ELEELLEQLSLATEEELQDLAEEL-------------------EELQQRLAELEEELEEAQEELEELEEEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 440 QALQADYQALQQRES-AIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQ 518
Cdd:COG4717 230 EQLENELEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 519 CQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVgpptdnEARELAAQL--ALSQAQLEVHQGEVQRLQAQVvdlQ 596
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE------ELQELLREAeeLEEELQLEELEQEIAALLAEA---G 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 597 AKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcsEREGALQEERADEAQQRE---EELRAL 673
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEelrEELAEL 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1894925314 674 QEELSQAKCSSE--EAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEE 724
Cdd:COG4717 459 EAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
313-680 |
7.01e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.19 E-value: 7.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 313 RQLQFLETQLAQVSQHVSDLEEQKKQLIQD----KDHLS------QQVGMLERLAGPPGPELPVAGEKNEALVPVNSSLQ 382
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDyqaaSDHLNlvqtalRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 383 EAwgkpeEEQRGLQEAQLDDTKVQEGSQEEEL----------RQANRELEKElQNVVGRNQL----LEGKLQALQADYQA 448
Cdd:COG3096 379 EA-----EARLEAAEEEVDSLKSQLADYQQALdvqqtraiqyQQAVQALEKA-RALCGLPDLtpenAEDYLAAFRAKEQQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 449 LQQRESAIQGSLASLEAEQAsirhlgdQMEASLLAVRKAKEAMKAQMAEKEAIlqskegecQQLREEVEQCQQLA----- 523
Cdd:COG3096 453 ATEEVLELEQKLSVADAARR-------QFEKAYELVCKIAGEVERSQAWQTAR--------ELLRRYRSQQALAQrlqql 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 524 EARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptdneaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAAL 603
Cdd:COG3096 518 RAQLAELEQRLRQQQNAERLLEEFCQRIGQQ----------LDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 604 DDQDKVQSQLSMAEAVLREHKTLVQQLKEQ-NEAL-NRAHVQELLQCS-EREGALQEERaDEAQQREEELRALQEELSQA 680
Cdd:COG3096 588 EQLRARIKELAARAPAWLAAQDALERLREQsGEALaDSQEVTAAMQQLlEREREATVER-DELAARKQALESQIERLSQP 666
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
390-602 |
8.28e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 390 EEQRGLQEAQLDDTKVQEGSQEEELRQANREL---EKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAE 466
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIaalARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 467 QASIRHLG-----------DQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALES 535
Cdd:COG4942 113 LYRLGRQPplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925314 536 QCQQQTQLIevltaekgqqgvgpptdneaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAA 602
Cdd:COG4942 193 LKAERQKLL--------------------ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| FYVE1_Vac1p_like |
cd15761 |
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ... |
970-1038 |
8.60e-07 |
|
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: 47.65 E-value: 8.60e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925314 970 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYV-LSKHG------GKKERCCRACFqklSEGPGSPD 1038
Cdd:cd15761 4 WKKPSGKSRCSECGKTLNKKNGIVNCRKCGELFCNEHCRNRIkLNNSAeydpknGKWCRCCEKCF---TSRPGYND 76
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
739-977 |
8.96e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 739 AASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSlpgLQAQLAQAEQRAQSLQEAAhQELNTLKFQLSAEIMDYQSRL 818
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA---LLKQLAALERRIAALARRI-RALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 819 KNAGEECKSLRGQLEEQGRQLQAAEEAVE-KLKATQAD------MGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERT 891
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPlALLLSPEDfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 892 QKELEKATTKIQEYYNKLCQEVTNRERNdqkmladLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEERWL 971
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKL-------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
....*.
gi 1894925314 972 GDTEAN 977
Cdd:COG4942 246 AGFAAL 251
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
41-397 |
1.24e-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: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 41 QLEVREKQLRERMQQLDRENQELRAAVSQQgEQLQTERERGRTAAEDNVRltclvaELQKQWEVTQATQNTVKELQTclq 120
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRI-ENRLDELSQELSDASRKIG------EIEKEIEQLEQEEEKLKERLE--- 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 121 glelgaaekeedyhtalrRLESMLQPLAQELEATRDSLDKKNQHLasfpgwlamAQQKADTASDTKGRQEPIPSDAAQEM 200
Cdd:TIGR02169 741 ------------------ELEEDLSSLEQEIENVKSELKELEARI---------EELEEDLHKLEEALNDLEARLSHSRI 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 201 QELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEmapLQEELSGKGQEADQLWRRLQELLAHT 280
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID---LKEQIKSIEKEIENLNGKKEELEEEL 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 281 SSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLErlagPP 360
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE----EI 946
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925314 361 GPELPVAG----------EKNEALVPVN--------------SSLQEAWGKPEEEQRGLQE 397
Cdd:TIGR02169 947 PEEELSLEdvqaelqrveEEIRALEPVNmlaiqeyeevlkrlDELKEKRAKLEEERKAILE 1007
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
649-898 |
1.27e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 649 SEREGALQEERADEAQQREEELRALQEELSQaKCSSEEAQLEHAELQEQLHRANTDTAELgiqvcALTVEKERVEE--AL 726
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDLHERLNGLES-ELAELDEEIERYEEQREQARETRDEADE-----VLEEHEERREEleTL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 727 ACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAG----SLPGLQAQLAQAEQRAQSLQE------AA 796
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARREELEDRDEELRDrleecrVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 797 HQELNTLKFQLSAEIMDYQSRLKNAGEECKSL-------RGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAE 869
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELeseleeaREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
250 260
....*....|....*....|....*....
gi 1894925314 870 CQAAMLRKDKEGAALREDLERTQKELEKA 898
Cdd:PRK02224 417 LREERDELREREAELEATLRTARERVEEA 445
|
|
| FYVE_WDFY1_like |
cd15718 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ... |
974-1027 |
1.63e-06 |
|
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: 46.93 E-value: 1.63e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925314 974 TEANHCLDCKREFSW----M-------VRRHHCRICGRIFCYYCCNNY-VLSKHGGKKE-RCCRACF 1027
Cdd:cd15718 4 AESDNCQKCSRPFFWnfkqMwekktlgVRQHHCRKCGKAVCDKCSSNRsTIPVMGFEFPvRVCNECY 70
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
188-890 |
1.97e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.48 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 188 RQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLK-------EDARASLERLVKEMAPLQEELS 260
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAEtelcaeaEEMRARLAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 261 GKGQEADQLWRRLQ----ELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQK 336
Cdd:pfam01576 82 SRLEEEEERSQQLQnekkKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 337 KQLIQDKDHLSQQVGMLERLAGPPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQE------AQLDDTKVQEGSQ 410
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEqiaelqAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 411 EEELRQANRELEKElqnvVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQasiRHLGDQMEasllAVRKAKEA 490
Cdd:pfam01576 242 EEELQAALARLEEE----TAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQR---RDLGEELE----ALKTELED 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 491 MKAQMAEKEAILQSKEGECQQLREEVEQ-----CQQLAEARHRELRALESQCQQQTQLIEVLTA-EKGQQGVgpptDNEA 564
Cdd:pfam01576 311 TLDTTAAQQELRSKREQEVTELKKALEEetrshEAQLQEMRQKHTQALEELTEQLEQAKRNKANlEKAKQAL----ESEN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 565 RELAAQL-ALSQAQLEVHQGEvQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQ 643
Cdd:pfam01576 387 AELQAELrTLQQAKQDSEHKR-KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 644 ELLQCSEREGALQEER------ADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTV 717
Cdd:pfam01576 466 LESQLQDTQELLQEETrqklnlSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 718 EKERVEEALACAVQELQDAKEAASReregLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQ--AEQRAQSLQ-- 793
Cdd:pfam01576 546 GKKRLQRELEALTQQLEEKAAAYDK----LEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQmlAEEKAISARya 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 794 ------EAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEE-------QGRQLQAAEEAVEKLKATQADMGEKL 860
Cdd:pfam01576 622 eerdraEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDlvsskddVGKNVHELERSKRALEQQVEEMKTQL 701
|
730 740 750
....*....|....*....|....*....|
gi 1894925314 861 SCTSNHLAECQAAMLRKDKEGAALREDLER 890
Cdd:pfam01576 702 EELEDELQATEDAKLRLEVNMQALKAQFER 731
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
490-741 |
2.49e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 490 AMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQqgvgppTDNEARELAA 569
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA------LEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 570 QLALSQAQLEVHQGEVQRL--QAQVVDLQAKMRAALDDQDKVQSQ--LSMAEAVLREHKTLVQQLKEQNEALNRAHvqel 645
Cdd:COG4942 91 EIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVrrLQYLKYLAPARREQAEELRADLAELAALR---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 646 lqcseregALQEERADEAQQREEELRALQEELSQAKcsseeaqlehAELQEQLHRANTDTAELGIQVCALTVEKERVEEA 725
Cdd:COG4942 167 --------AELEAERAELEALLAELEEERAALEALK----------AERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250
....*....|....*.
gi 1894925314 726 LACAVQELQDAKEAAS 741
Cdd:COG4942 229 IARLEAEAAAAAERTP 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
438-687 |
2.96e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 438 KLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQskegecqQLREEVE 517
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 518 QCQQLAEARHRELRALESQCQ---QQTQLIEVLTAEkgqqgvgpptdnEARELAAQLALSQAQLEVHQGEVQRLQAQVVD 594
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYrlgRQPPLALLLSPE------------DFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 595 LQAKMRAALDDQDKVQSQLSMAEAvlrEHKTLVQQLKEQNEALNRAhvqellqcsEREGALQEERADEAQQREEELRALQ 674
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEE---ERAALEALKAERQKLLARL---------EKELAELAAELAELQQEAEELEALI 229
|
250
....*....|...
gi 1894925314 675 EELSQAKCSSEEA 687
Cdd:COG4942 230 ARLEAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
584-966 |
3.87e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 584 EVQRLQAQVVDLQAKM---RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAlnRAHVQELLQCsEREGALQEERA 660
Cdd:COG4717 72 ELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQL--LPLYQELEAL-EAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 661 DEAQQREEELRALQEELsqakcssEEAQLEHAELQEQLHRANTDTAELGIQvcALTVEKERVEEALAcAVQELQDAKEAA 740
Cdd:COG4717 149 EELEERLEELRELEEEL-------EELEAELAELQEELEELLEQLSLATEE--ELQDLAEELEELQQ-RLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 741 SREREGLERQVAGLQQEKESLQEK------------------LKAAKAAAGSLP-----------GLQAQLAQAEQRAQS 791
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEerlkearlllliaaallaLLGLGGSLLSLIltiagvlflvlGLLALLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 792 LQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNH--LAE 869
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAalLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 870 CQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVtnRERNDQKMLADLDDLNRTKKYLEERLIELLRDKD 949
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL--EALDEEELEEELEELEEELEELEEELEELREELA 456
|
410
....*....|....*..
gi 1894925314 950 ALWQKSDALEFQQKLSA 966
Cdd:COG4717 457 ELEAELEQLEEDGELAE 473
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
314-540 |
3.99e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 314 QLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERlagppgpelpvagekneALVPVNSSLQEAwgkpeEEQR 393
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-----------------RIAALARRIRAL-----EQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 394 GLQEAQLDDTKVQEGSQEEELRQANRELEKELQNV--VGRNQLLEG------------KLQALQADYQALQQRESAIQGS 459
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLRALyrLGRQPPLALllspedfldavrRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 460 LASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQ 539
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
.
gi 1894925314 540 Q 540
Cdd:COG4942 239 A 239
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
613-959 |
4.83e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 613 LSMAEAVLREHKTLVQQ---LKEQNEALNRAhvqellqcseregalQEERADEAQQREEELRALQEELSQAKCSSEEAQL 689
Cdd:TIGR04523 203 LSNLKKKIQKNKSLESQiseLKKQNNQLKDN---------------IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 690 EHAELQEQLHRANTDTAELGIQVCALTVE-----KERVEEALACAVQELQDAKEaasrEREGLERQVAGLQQEKESLQEK 764
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEisdlnNQKEQDWNKELKSELKNQEK----KLEEIQNQISQNNKIISQLNEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 765 LKAAKAAAGSLPG----LQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQ 840
Cdd:TIGR04523 344 ISQLKKELTNSESenseKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 841 AAEEAVEKLKATQADMGEKLSCTSNhlaecqaamlrKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRERND 920
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTN-----------QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
330 340 350
....*....|....*....|....*....|....*....
gi 1894925314 921 QKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALE 959
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
116-763 |
5.97e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 116 QTCLQGLELGAAEKEE-DYHTALRRLEsmlqplaQELEATRDSLDKKNqhlasfpgwlamaqQKADTASDTKGRQEPIPS 194
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEkDLHERLNGLE-------SELAELDEEIERYE--------------EQREQARETRDEADEVLE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 195 DAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLvkelqlkEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQ 274
Cdd:PRK02224 245 EHEERREELETLEAEIEDLRETIAETEREREELAEEV-------RDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 275 EllahtssweeelaelrrekkqqqeekelleqevrsLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQvgmle 354
Cdd:PRK02224 318 E-----------------------------------LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER----- 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 355 rlagppgpelpvAGEKnealvpvnsslqeawgkpeEEQRGLQEAQLDDTKVQEGSQEEELrqanRELEKELQNVVGRNQL 434
Cdd:PRK02224 358 ------------AEEL-------------------REEAAELESELEEAREAVEDRREEI----EELEEEIEELRERFGD 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 435 LEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHlgdqmeasllAVRKAKEAMKAqmaekeailqSKEGECQQLRE 514
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARE----------RVEEAEALLEA----------GKCPECGQPVE 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 515 EVEQCQQLAEARHR------ELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRL 588
Cdd:PRK02224 463 GSPHVETIEEDRERveeleaELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 589 QAQVVDLQAKMRAALDDQDKVQSQlsmAEAVLREHKTLVQQLKEQNEALNR-AHVQELL----QCSEREGALQEERADEA 663
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEE---AEEAREEVAELNSKLAELKERIESlERIRTLLaaiaDAEDEIERLREKREALA 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 664 Q---QREEELRALQEELSQAKCSSEEAQLEhaELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAA 740
Cdd:PRK02224 620 ElndERRERLAEKRERKRELEAEFDEARIE--EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELR 697
|
650 660
....*....|....*....|....*.
gi 1894925314 741 SReREGLERQVAGLQ---QEKESLQE 763
Cdd:PRK02224 698 ER-REALENRVEALEalyDEAEELES 722
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
51-943 |
8.87e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.43 E-value: 8.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 51 ERMQQLdreNQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCLQGLE--LGAAE 128
Cdd:TIGR00606 189 ETLRQV---RQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEhnLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 129 KEEDYHTALRRLESMLQPLAQELEATRDSL----DKKNQHLASFPGwlAMAQQKADTASDTKGRQEPIpsdaAQEMQELG 204
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDLYHNHQ--RTVREKERELVDCQRELEKL----NKERRLLN 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 205 EKLQALERERTKVE---EVNRQQSAQLEQLVKELQLKEDAR-----ASLERLVKEMAPLQEE-LSGKGQEADQLWRRLQE 275
Cdd:TIGR00606 340 QEKTELLVEQGRLQlqaDRHQEHIRARDSLIQSLATRLELDgfergPFSERQIKNFHTLVIErQEDEAKTAAQLCADLQS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 276 LLAHTsswEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSqqvgMLER 355
Cdd:TIGR00606 420 KERLK---QEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELS----KAEK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 356 LAGPPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVG---RN 432
Cdd:TIGR00606 493 NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGyfpNK 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 433 QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLA--------------------VRKAKEAMK 492
Cdd:TIGR00606 573 KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSyedklfdvcgsqdeesdlerLKEEIEKSS 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 493 AQMAEKEAILQSKEGECQQLREEVEQCQQLAE---ARHRELRALESQCQQQTQLIEvlTAEKGQQGVGPPTDNEARELAA 569
Cdd:TIGR00606 653 KQRAMLAGATAVYSQFITQLTDENQSCCPVCQrvfQTEAELQEFISDLQSKLRLAP--DKLKSTESELKKKEKRRDEMLG 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 570 QLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHK------TLVQQLKEQNEALNRAHVQ 643
Cdd:TIGR00606 731 LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvTIMERFQMELKDVERKIAQ 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 644 ELLQCSEREGALQ-EERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERV 722
Cdd:TIGR00606 811 QAAKLQGSDLDRTvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQL 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 723 EEaLACAVQELQDAKEAASREREGLERQVAGLQQEKESLQeklkaakaaagslpglqaqlaqaeQRAQSLQEAAHQELNT 802
Cdd:TIGR00606 891 VE-LSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELI------------------------SSKETSNKKAQDKVND 945
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 803 LKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAA-EEAVEKLKATQADMGE-KLSCTSNHLAEC----QAAMLR 876
Cdd:TIGR00606 946 IKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQlEECEKHQEKINEDMRLmRQDIDTQKIQERwlqdNLTLRK 1025
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1894925314 877 KDKEGAALREDLERTQKEL-EKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIE 943
Cdd:TIGR00606 1026 RENELKEVEEELKQHLKEMgQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
563-695 |
9.21e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 49.28 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 563 EARELAAQLALSQAQLEVHQGEVQRLQAQVvDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHV 642
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLARLEAEL-GAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARA 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1894925314 643 QELLQCSEREGALQEERADEAQQRE-EELRALQEELSQAkcsseEAQLEHAELQ 695
Cdd:COG1566 156 ALDAAQAQLEAAQAQLAQAQAGLREeEELAAAQAQVAQA-----EAALAQAELN 204
|
|
| FYVE_protrudin |
cd15723 |
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ... |
979-1030 |
1.15e-05 |
|
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: 44.03 E-value: 1.15e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925314 979 CLDCKREFS-WMVRRHHCRICGRIFCYYCCNNYVLSKHGG------KKE--RCCRACFQKL 1030
Cdd:cd15723 2 CTGCGASFSvLLKKRRSCNNCGNAFCSRCCSKKVPRSVMGatapaaQREtvFVCSGCNDKL 62
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
448-969 |
1.35e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 448 ALQQRESAIQGSLASLEAEQASIRH-LG-DQMEASLLAVRKAKEAMKAQMAEKEAILQSKEgECQQLREEVEQcqQLAEA 525
Cdd:PRK03918 129 AIYIRQGEIDAILESDESREKVVRQiLGlDDYENAYKNLGEVIKEIKRRIERLEKFIKRTE-NIEELIKEKEK--ELEEV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 526 RhRELRALESQCQQQTQLIEVLTAEKgqqgvgpptdNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQ---AKMRAA 602
Cdd:PRK03918 206 L-REINEISSELPELREELEKLEKEV----------KELEELKEEIEELEKELESLEGSKRKLEEKIRELEeriEELKKE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 603 LDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRahVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKC 682
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE--IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 683 SSEEAQLEHAELQE---QLHRANTDTAELGIQvcaltvEKERVEEALacavQELQDAKEAASREREGLERQVAGLQQEKE 759
Cdd:PRK03918 353 RLEELEERHELYEEakaKKEELERLKKRLTGL------TPEKLEKEL----EELEKAKEEIEEEISKITARIGELKKEIK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 760 SLQEKLKAAKAAAGSLPGLQAQLAqaEQRAQSLQEAAHQELNtlkfQLSAEIMDYQSRLKNAGEECKSLRGQLEEQgRQL 839
Cdd:PRK03918 423 ELKKAIEELKKAKGKCPVCGRELT--EEHRKELLEEYTAELK----RIEKELKEIEEKERKLRKELRELEKVLKKE-SEL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 840 QAAEEAVEKLKATQadmgEKLSCTSnhlaecqaamlrkdkegaalREDLERTQKELEKattkIQEYYNKLCQEVTNRERN 919
Cdd:PRK03918 496 IKLKELAEQLKELE----EKLKKYN--------------------LEELEKKAEEYEK----LKEKLIKLKGEIKSLKKE 547
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1894925314 920 dqkmLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEER 969
Cdd:PRK03918 548 ----LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
411-765 |
1.48e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.12 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 411 EEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEA 490
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 491 MKAqmaEKEAILQSKEGECQQLREEVEQCQQLAEA---RHRELRALESQCQQQT-QLIEVLTAEKGQQGVGPPTDNEARE 566
Cdd:pfam07888 113 LSE---EKDALLAQRAAHEARIRELEEDIKTLTQRvleRETELERMKERAKKAGaQRKEEEAERKQLQAKLQQTEEELRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 567 LAAQLALSQAQLEVHQGEVQRLQAQVVDLQ----------AKMRAALDDQDKVQSQLSM----AEAVLREHKTLVQQLKE 632
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTqklttahrkeAENEALLEELRSLQERLNAserkVEGLGEELSSMAAQRDR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 633 QNEALNRAHVQEL---LQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELG 709
Cdd:pfam07888 270 TQAELHQARLQAAqltLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELG 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925314 710 IQV-CALTVEKERVEEalacaVQELQDAKEAASREREGLERQVAGLQQEKESLQEKL 765
Cdd:pfam07888 350 REKdCNRVQLSESRRE-----LQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
481-961 |
2.27e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.81 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 481 LLAVRKAKEAMKAQMAEKEAILQSKEGecqqlREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgppt 560
Cdd:TIGR00618 148 LLPQGEFAQFLKAKSKEKKELLMNLFP-----LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDT------ 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 561 dneARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKmraaLDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRA 640
Cdd:TIGR00618 217 ---YHERKQVLEKELKHLREALQQTQQSHAYLTQKREA----QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 641 --------HVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQv 712
Cdd:TIGR00618 290 rkaaplaaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 713 caltvEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLaQAEQRAQSL 792
Cdd:TIGR00618 369 -----EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ-ELQQRYAEL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 793 QEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAEC-- 870
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdn 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 871 ----QAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNK---LCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIE 943
Cdd:TIGR00618 523 pgplTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQmqeIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK 602
|
490
....*....|....*...
gi 1894925314 944 LLRDKDALWQKSDALEFQ 961
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRK 620
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
26-479 |
2.48e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 26 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERgRTAAEDNVRLTCLVAE--LQKQWE 103
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE-RDDLLAEAGLDDADAEavEARREE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 104 VTQATQNTVKELQTCLQGLEL------GAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQ 177
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAhneeaeSLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 178 KADTASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLE--------QLVKE---LQLKEDARASLE 246
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgQPVEGsphVETIEEDRERVE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 247 RLVKEMAPLQEELSGKGQEADQLwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQ-- 324
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEkr 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 325 ------------VSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGpPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQ 392
Cdd:PRK02224 558 eaaaeaeeeaeeAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREALAELNDERRERLAEKRERK 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 393 RGLqEAQLDDTKVqegsqeEELRQANRELEKELQNVvgrnqllEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRH 472
Cdd:PRK02224 637 REL-EAEFDEARI------EEAREDKERAEEYLEQV-------EEKLDELREERDDLQAEIGAVENELEELEELRERREA 702
|
....*..
gi 1894925314 473 LGDQMEA 479
Cdd:PRK02224 703 LENRVEA 709
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
203-606 |
2.62e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.35 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 203 LGEKLQALERERTkveEVNRQQSAQLEQLVKELQLKEDARASLERLVKEM----APLQEELSGKGQEADQLWRRLQELLA 278
Cdd:pfam07888 32 LQNRLEECLQERA---ELLQAQEAANRQREKEKERYKRDREQWERQRRELesrvAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 279 HTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLErlag 358
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTE---- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 359 ppgpelpvageknEALVPVNSSLQEAwgKPEEEQRGLQEAQLDDTKVQegsqeeelrqanrelekeLQNVVGRNQLLEGK 438
Cdd:pfam07888 185 -------------EELRSLSKEFQEL--RNSLAQRDTQVLQLQDTITT------------------LTQKLTTAHRKEAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 439 LQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAekEAILQSKEGECQQLREEvEQ 518
Cdd:pfam07888 232 NEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLA--DASLALREGRARWAQER-ET 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 519 CQQLAEARH-------RELRALESQCQQQTQLIEVLTAEKGQQ-----GVGPPTDNEARELAAQLALSQAQLEVHQGEVQ 586
Cdd:pfam07888 309 LQQSAEADKdrieklsAELQRLEERLQEERMEREKLEVELGREkdcnrVQLSESRRELQELKASLRVAQKEKEQLQAEKQ 388
|
410 420
....*....|....*....|
gi 1894925314 587 RLQAQVVDLQAKMRAALDDQ 606
Cdd:pfam07888 389 ELLEYIRQLEQRLETVADAK 408
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-252 |
2.96e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 26 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVT 105
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 106 QAT-----------QNTVKELQTCLQGLELGAAEKEEDYHTALRRLESM---LQPLAQELEATRDSLDKKNQHLASFPGW 171
Cdd:TIGR02168 851 SEDieslaaeieelEELIEELESELEALLNERASLEEALALLRSELEELseeLRELESKRSELRRELEELREKLAQLELR 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 172 LAMAQQKADT--------ASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVN-------RQQSAQLEQLVKELQ 236
Cdd:TIGR02168 931 LEGLEVRIDNlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNlaaieeyEELKERYDFLTAQKE 1010
|
250
....*....|....*.
gi 1894925314 237 LKEDARASLERLVKEM 252
Cdd:TIGR02168 1011 DLTEAKETLEEAIEEI 1026
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
562-799 |
3.22e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 562 NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREH----------KTLVQQL- 630
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsVSYLDVLl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 631 --KEQNEALNRAHVQELLQcseregALQEERADEAQQREEELRALQEELSQAKcssEEAQLEHAELQEQLHRANTDTAEL 708
Cdd:COG3883 110 gsESFSDFLDRLSALSKIA------DADADLLEELKADKAELEAKKAELEAKL---AELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 709 GIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQR 788
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAG 260
|
250
....*....|.
gi 1894925314 789 AQSLQEAAHQE 799
Cdd:COG3883 261 SAGAAGAAAGA 271
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
379-911 |
3.93e-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: 48.18 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 379 SSLQEAWGKPEEEQRGLQEAQLDDTKV----QEGSQE--------------------------EELRQANRELEKELQNV 428
Cdd:pfam05483 106 NKLQENRKIIEAQRKAIQELQFENEKVslklEEEIQEnkdlikennatrhlcnllketcarsaEKTKKYEYEREETRQVY 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 429 VGRNQLLEGKLQALQadyQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEA-------I 501
Cdd:pfam05483 186 MDLNNNIEKMILAFE---ELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENkmkdltfL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 502 LQSKEGECQQLREEV----EQCQQLAEARHRELRALES-QCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQA 576
Cdd:pfam05483 263 LEESRDKANQLEEKTklqdENLKELIEKKDHLTKELEDiKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNK 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 577 QLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKE--QNEALNRAHVQELLqcSEREGA 654
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKfkNNKEVELEELKKIL--AEDEKL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 655 LQEERADEA----------------QQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVE 718
Cdd:pfam05483 421 LDEKKQFEKiaeelkgkeqelifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLE 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 719 KERVEEALACAVQELQDAKE---AASREREGLERQVAGLQQEKESLQEKLKAAKAA-AGSLPGLQAQLAQAEQRAQSLQE 794
Cdd:pfam05483 501 NKELTQEASDMTLELKKHQEdiiNCKKQEERMLKQIENLEEKEMNLRDELESVREEfIQKGDEVKCKLDKSEENARSIEY 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 795 AAHQELNTLKF------QLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKL-SCTSNHL 867
Cdd:pfam05483 581 EVLKKEKQMKIlenkcnNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFeEIIDNYQ 660
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1894925314 868 AECQAAMLRKDKegaaLREDLERTQKELEKAtTKIQEYYNKLCQ 911
Cdd:pfam05483 661 KEIEDKKISEEK----LLEEVEKAKAIADEA-VKLQKEIDKRCQ 699
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
36-533 |
5.53e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 36 RLELDQLEVREKQLRERMQQLDrENQELRAAVSQQGEQLQTERERgRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKEL 115
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAE-LEELREELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 116 QTCLQGLElgaaEKEEDYHTALRRLESmlqpLAQELEATRDSLDKKNQHLaSFPGWLAMaqqkadtasdtkgrqepipSD 195
Cdd:COG4717 145 PERLEELE----ERLEELRELEEELEE----LEAELAELQEELEELLEQL-SLATEEEL-------------------QD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 196 AAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARaslerlvkemaplqeelsgKGQEADQLWRRLQE 275
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE-------------------RLKEARLLLLIAAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 276 LLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLsqqvgmler 355
Cdd:COG4717 258 LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL--------- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 356 lagppGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLddtkvqEGSQEEELRQANRELEKELQNVVGRNQLL 435
Cdd:COG4717 329 -----GLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL------EQEIAALLAEAGVEDEEELRAALEQAEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 436 EGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHlgDQMEASLLAVRKAKEAMKAQMAEKEAILQ--SKEGECQQLR 513
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEELEEEL--EELEEELEELEEELEELREELAELEAELEqlEEDGELAELL 475
|
490 500
....*....|....*....|
gi 1894925314 514 EEVEQCQQLAEARHRELRAL 533
Cdd:COG4717 476 QELEELKAELRELAEEWAAL 495
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
577-941 |
6.14e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 577 QLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTL-------VQQLKEQNEALNRAHVQELLQCS 649
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKikelekqLNQLKSEISDLNNQKEQDWNKEL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 650 EREGALQEERADEAQ----QREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEA 725
Cdd:TIGR04523 313 KSELKNQEKKLEEIQnqisQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 726 LACAVQELQDAKEaasrEREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQ------E 799
Cdd:TIGR04523 393 INDLESKIQNQEK----LNQQKDEQIKKLQQEKELLEKEIER----------LKETIIKNNSEIKDLTNQDSVkeliikN 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 800 LNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDK 879
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925314 880 EGAALREDLER-----TQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERL 941
Cdd:TIGR04523 539 KISDLEDELNKddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
409-959 |
6.53e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 409 SQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQ---QRESAIQGSLASLEAEQASIRHLGDQMEASLLAVR 485
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 486 KAKEAMKAQMAEkeaiLQSKEGECQQLREEVEqcqqlaeaRHRELRALESQCQQQTQLIEVLTAEKGQQGvgpptdNEAR 565
Cdd:PRK03918 266 ERIEELKKEIEE----LEEKVKELKELKEKAE--------EYIKLSEFYEEYLDELREIEKRLSRLEEEI------NGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 566 ELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAalddqdkvqsqLSMAEAVLREHKTLVQQLKEQN-EALNRahvqE 644
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHEL-----------YEEAKAKKEELERLKKRLTGLTpEKLEK----E 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 645 LLQCSEREGALQEE------RADEAQQREEELRALQEELSQAK-----CSSEEAQLEHAELQE----QLHRANTDTAELG 709
Cdd:PRK03918 393 LEELEKAKEEIEEEiskitaRIGELKKEIKELKKAIEELKKAKgkcpvCGRELTEEHRKELLEeytaELKRIEKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 710 IQVCALTVEKERVEEALAcAVQELQDAKEAASREREgLERQVAGLQQEKesLQEKLKAAKAAAGSLPGLQAQLAQAEQRA 789
Cdd:PRK03918 473 EKERKLRKELRELEKVLK-KESELIKLKELAEQLKE-LEEKLKKYNLEE--LEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 790 QSLQEaahqelntlkfqLSAEIMDYQSRLKNAGEECKSLRGQLEEQGrqLQAAEEAVEKLKATQADMGEKLScTSNHLAE 869
Cdd:PRK03918 549 EKLEE------------LKKKLAELEKKLDELEEELAELLKELEELG--FESVEELEERLKELEPFYNEYLE-LKDAEKE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 870 CQAAMLRKDKEGAAL---REDLERTQKELEKATTKI--------QEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLE 938
Cdd:PRK03918 614 LEREEKELKKLEEELdkaFEELAETEKRLEELRKELeelekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIK 693
|
570 580
....*....|....*....|.
gi 1894925314 939 ERLIELLRDKDALWQKSDALE 959
Cdd:PRK03918 694 KTLEKLKEELEEREKAKKELE 714
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
411-791 |
6.70e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 6.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 411 EEELRQanrELeKELQNVVGRNQLleGKLQALQADYQALQQResaiQGSLASLEAEQASI-------RHLGDQMEASLLA 483
Cdd:PRK10929 25 EKQITQ---EL-EQAKAAKTPAQA--EIVEALQSALNWLEER----KGSLERAKQYQQVIdnfpklsAELRQQLNNERDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 484 VRKAKEAMKAQMAEKEaILQSKegecQQLREEVEQCQQLAEaRHRELRALESQC-QQQTQLIEVLT-AEKGQQGVGPPTD 561
Cdd:PRK10929 95 PRSVPPNMSTDALEQE-ILQVS----SQLLEKSRQAQQEQD-RAREISDSLSQLpQQQTEARRQLNeIERRLQTLGTPNT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 562 nearelaaqlALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEavlREHKTLVQQLKEQNEALNRAH 641
Cdd:PRK10929 169 ----------PLAQAQLTALQAESAALKALVDELELAQLSANNRQELARLRSELAK---KRSQQLDAYLQALRNQLNSQR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 642 VQELLQCSEREGALQEERADEAQQREEELRaLQEELSQAkcSSEEAQlEHAELQEQLHRANTDTaelgIQV-CALTVEKE 720
Cdd:PRK10929 236 QREAERALESTELLAEQSGDLPKSIVAQFK-INRELSQA--LNQQAQ-RMDLIASQQRQAASQT----LQVrQALNTLRE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 721 RVE---------EALACAVQELQDAKEAASREREGLERQVAGLQQEK--ESLQEKLKAAKAAAGSLPGLQAQLAQAEQRA 789
Cdd:PRK10929 308 QSQwlgvsnalgEALRAQVARLPEMPKPQQLDTEMAQLRVQRLRYEDllNKQPQLRQIRQADGQPLTAEQNRILDAQLRT 387
|
..
gi 1894925314 790 QS 791
Cdd:PRK10929 388 QR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
40-278 |
7.77e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 40 DQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQterergrtaaednvrltclvaELQKQWEVTQATQNTVKELQTCL 119
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK---------------------QLAALERRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 120 QGLELGAAEKEEDYHTALRRLESMLQPLAQEL-EATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIpSDAAQ 198
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA-EELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 199 EMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLErlvKEMAPLQEELSGKGQEADQLWRRLQELLA 278
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEA 234
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
413-548 |
1.01e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.96 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 413 ELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQ--------------ASIRHLGDQME 478
Cdd:pfam15905 160 ELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKieekseteklleyiTELSCVSEQVE 239
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1894925314 479 ASLLAVRKAKEAMKAQMAE----KEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLT 548
Cdd:pfam15905 240 KYKLDIAQLEELLKEKNDEieslKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELK 313
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
195-530 |
1.25e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.48 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 195 DAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLkedarasLERLVKEMAPLQEElsgkgqeadQLWRRLQ 274
Cdd:COG3096 833 DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQL-------LNKLLPQANLLADE---------TLADRLE 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 275 ELLAHTSSweeelaelrreKKQQQEEKELLEQEVRSLTRQLQFLET---QLAQVSQHVSDLEEQKKQLIQDKDHLSQQVG 351
Cdd:COG3096 897 ELREELDA-----------AQEAQAFIQQHGKALAQLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVVQ 965
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 352 MLERLagppgpelpvAGEKNEALVPVNSSLQEAWgkpeeeqrglqEAQLDDTKVQEGSQEEELRQANRELEKELQnvvgR 431
Cdd:COG3096 966 RRPHF----------SYEDAVGLLGENSDLNEKL-----------RARLEQAEEARREAREQLRQAQAQYSQYNQ----V 1020
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 432 NQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHlgDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGEC-- 509
Cdd:COG3096 1021 LASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRR--DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLrk 1098
|
330 340 350
....*....|....*....|....*....|.
gi 1894925314 510 -----QQLREEVEQ-----CQQLAEARHREL 530
Cdd:COG3096 1099 aerdyKQEREQVVQakagwCAVLRLARDNDV 1129
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
440-896 |
1.27e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 46.39 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 440 QALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 519
Cdd:COG3899 770 RALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREA 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 520 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKM 599
Cdd:COG3899 850 LELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAA 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 600 RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQ 679
Cdd:COG3899 930 ALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAA 1009
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 680 AkCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKE 759
Cdd:COG3899 1010 A-AAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAAL 1088
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 760 SLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQL 839
Cdd:COG3899 1089 AAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAA 1168
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925314 840 QAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELE 896
Cdd:COG3899 1169 LALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLL 1225
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
410-900 |
1.51e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.33 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 410 QEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAiQGSLASLEAEQ--ASIRHLGD---QMEASLLAV 484
Cdd:PRK10246 231 EEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKA-QPQLAALSLAQpaRQLRPHWEriqEQSAALAHT 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 485 RKAKEAMKAQMAEKEA----ILQSKEGECQQLREEVEQCQQ-LAEAR-----HREL---RALESQC----QQQTQLIEVL 547
Cdd:PRK10246 310 RQQIEEVNTRLQSTMAlrarIRHHAAKQSAELQAQQQSLNTwLAEHDrfrqwNNELagwRAQFSQQtsdrEQLRQWQQQL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 548 TAEKGQQGVGPPT--DNEARELAAQLALSQAQLEVHQgEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKt 625
Cdd:PRK10246 390 THAEQKLNALPAItlTLTADEVAAALAQHAEQRPLRQ-RLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMR- 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 626 lvQQLKEQNEALNRahVQELLQCSEREGALQEERAD------------------EAQQREE------ELRALQEELSQAK 681
Cdd:PRK10246 468 --QRYKEKTQQLAD--VKTICEQEARIKDLEAQRAQlqagqpcplcgstshpavEAYQALEpgvnqsRLDALEKEVKKLG 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 682 CSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAK----EAASRERE------------ 745
Cdd:PRK10246 544 EEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQpwldAQEEHERQlrllsqrhelqg 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 746 ---GLERQVAGLQQEKESLQEKLKAAKAAAG-SLPGLQAQ---LAQAEQRAQSLQeAAHQELNTLKFQLSA--------- 809
Cdd:PRK10246 624 qiaAHNQQIIQYQQQIEQRQQQLLTALAGYAlTLPQEDEEaswLATRQQEAQSWQ-QRQNELTALQNRIQQltplletlp 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 810 --EIMDYQS------RLKNAGEECKSLRGQLEEQGRQlqaaeEAVEKLKATQADMGEKLSCTSNHLAECQA--AMLRKDK 879
Cdd:PRK10246 703 qsDDLPHSEetvaldNWRQVHEQCLSLHSQLQTLQQQ-----DVLEAQRLQKAQAQFDTALQASVFDDQQAflAALLDEE 777
|
570 580
....*....|....*....|.
gi 1894925314 880 EGAALREDLERTQKELEKATT 900
Cdd:PRK10246 778 TLTQLEQLKQNLENQRQQAQT 798
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
498-763 |
1.85e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 498 KEAILQSKEGECQQLREEVEQCQQLA------------------EARHRELRA----LESQCQQQTQLIEVLTAE-KGQQ 554
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAAnrqrekekerykrdreqwERQRRELESrvaeLKEELRQSREKHEELEEKyKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 555 GVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQN 634
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 635 EALNRAHVQELLQCSEREGALQE---------ERADEAQQRE-------EELRALQEELSQAKCSSEEAQLEHAEL---- 694
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQlqdtittltQKLTTAHRKEaeneallEELRSLQERLNASERKVEGLGEELSSMaaqr 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925314 695 ---QEQLHRANTDTAELGIQVCALTVEkerVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQE 763
Cdd:pfam07888 268 drtQAELHQARLQAAQLTLQLADASLA---LREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
390-700 |
1.87e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.88 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 390 EEQRGLQEAQlddtkvqEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGS-LASLEAEQA 468
Cdd:pfam17380 313 ERRRKLEEAE-------KARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISrMRELERLQM 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 469 SIRHLGDQMEASLLAVRKakeaMKAQMAEKEAILQSKEGECQQLREEVEqcqqlaEARHRELRALESQCQQQTQLIEVLT 548
Cdd:pfam17380 386 ERQQKNERVRQELEAARK----VKILEEERQRKIQQQKVEMEQIRAEQE------EARQREVRRLEEERAREMERVRLEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 549 AEKgQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQsqlsMAEAVLREHKTLVQ 628
Cdd:pfam17380 456 QER-QQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK----LLEKEMEERQKAIY 530
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925314 629 QLKEQNEAlnrahvqellqcseregalQEERadEAQQREEELRALQEELSQAkcSSEEAQLEHAELQEQLHR 700
Cdd:pfam17380 531 EEERRREA-------------------EEER--RKQQEMEERRRIQEQMRKA--TEERSRLEAMEREREMMR 579
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
714-959 |
1.95e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 714 ALTVEKERVEeALAcAVQELQDAKEAASREREGLERQVAGLQQEKEslQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQ 793
Cdd:COG4913 243 ALEDAREQIE-LLE-PIRELAERYAAARERLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 794 EAAHQELNTLKFQLSAEimDYQsRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAA 873
Cdd:COG4913 319 DALREELDELEAQIRGN--GGD-RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 874 MLRKDKEGAALREDLERTQKELEKATTKIQeyynklcQEVTNRERN----DQKMLADLDDLNRTKKYLEERL---IELL- 945
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELE-------AEIASLERRksniPARLLALRDALAEALGLDEAELpfvGELIe 468
|
250
....*....|....*
gi 1894925314 946 -RDKDALWQksDALE 959
Cdd:COG4913 469 vRPEEERWR--GAIE 481
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
409-965 |
2.22e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 409 SQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQ---MEASLLAVR 485
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQiseLKKQNNQLK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 486 KAKEAMKAQMAEKEAILQSKEGECQQLREE-------VEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKgQQGVGP 558
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEqnkikkqLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK-EQDWNK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 559 PTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLsmaeavlREHKTLVQQLKEQNEALN 638
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL-------EEKQNEIEKLKKENQSYK 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 639 RAHVQELLQCSEREGALQEERaDEAQQREEELRALQEELsqakcssEEAQLEHAELQEQLHRANTDTAELgiqvcaltve 718
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQE-KLNQQKDEQIKKLQQEK-------ELLEKEIERLKETIIKNNSEIKDL---------- 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 719 kERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQE---- 794
Cdd:TIGR04523 446 -TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE---LKKLNEEKKELEEKVKDLTKkiss 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 795 --AAHQELNTLKFQLSAEIMDYQSRLKNAGEECKS--LRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAEC 870
Cdd:TIGR04523 522 lkEKIEKLESEKKEKESKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 871 QAAMLRKDKEGAALREDLERTQKELEKATT---KIQEYYNKLCQEVTNRE---RNDQKMLADLDDLNRTKKYLEERLIEL 944
Cdd:TIGR04523 602 IKEIEEKEKKISSLEKELEKAKKENEKLSSiikNIKSKKNKLKQEVKQIKetiKEIRNKWPEIIKKIKESKTKIDDIIEL 681
|
570 580
....*....|....*....|.
gi 1894925314 945 LRDkdalWQKSDALEFQQKLS 965
Cdd:TIGR04523 682 MKD----WLKELSLHYKKYIT 698
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
396-678 |
2.48e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 396 QEAQLDDTKVQEGSQEEELRQANRELE--KELQNVVGRNQL-------LEGKLQALQADYQALQQRESAIQGSLASLEAe 466
Cdd:PRK11281 78 QKEETEQLKQQLAQAPAKLRQAQAELEalKDDNDEETRETLstlslrqLESRLAQTLDQLQNAQNDLAEYNSQLVSLQT- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 467 qASIRhlgdqmeasllaVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVeqcQQLAEArhrELRALESQCQQQTQLIEV 546
Cdd:PRK11281 157 -QPER------------AQAALYANSQRLQQIRNLLKGGKVGGKALRPSQ---RVLLQA---EQALLNAQNDLQRKSLEG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 547 LTaekgqqgvgpptdnearelaaQL-ALSQAQLEVHQGEVQRLQAQVVDLQakmrAALDDQDKVQSQLSMAEAVLREHKT 625
Cdd:PRK11281 218 NT---------------------QLqDLLQKQRDYLTARIQRLEHQLQLLQ----EAINSKRLTLSEKTVQEAQSQDEAA 272
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925314 626 LVQQ--LKEQNEALNRAHVQELLQCSEREGAL--QEERA----DEAQQREeelRALQEELS 678
Cdd:PRK11281 273 RIQAnpLVAQELEINLQLSQRLLKATEKLNTLtqQNLRVknwlDRLTQSE---RNIKEQIS 330
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
196-842 |
2.55e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.56 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 196 AAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQE--------ELSGKGQEAD 267
Cdd:PRK10246 214 TPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKaqpqlaalSLAQPARQLR 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 268 QLWRRLQEllaHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEE------------- 334
Cdd:PRK10246 294 PHWERIQE---QSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRfrqwnnelagwra 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 335 QKKQLIQDKDHLSQQVGML-----ERLAGPPGPELPVAGEKNEALVPVNsslqeawgkpeeEQRGLQEaQLDDTKVQEGS 409
Cdd:PRK10246 371 QFSQQTSDREQLRQWQQQLthaeqKLNALPAITLTLTADEVAAALAQHA------------EQRPLRQ-RLVALHGQIVP 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 410 QEEELRQANRELEKELQNVVGRNQLLEGKLQALQ------ADYQALQQRESAI---QGSLASLEAEQ-----ASIRHLGD 475
Cdd:PRK10246 438 QQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKektqqlADVKTICEQEARIkdlEAQRAQLQAGQpcplcGSTSHPAV 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 476 QMEASL-----LAVRKAKEAMKAQMAEKEAILQskeGECQQLREEVEQCQQLAEARHRELRALESQCQQqtqLIEVLTAE 550
Cdd:PRK10246 518 EAYQALepgvnQSRLDALEKEVKKLGEEGAALR---GQLDALTKQLQRDESEAQSLRQEEQALTQQWQA---VCASLNIT 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 551 KGQQGVGPPTDNEARELAAQLALS------QAQLEVHQGEVQRLQAQVVDLQAKMRAALD-------DQDKVQSQLSMAE 617
Cdd:PRK10246 592 LQPQDDIQPWLDAQEEHERQLRLLsqrhelQGQIAAHNQQIIQYQQQIEQRQQQLLTALAgyaltlpQEDEEASWLATRQ 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 618 AvlrEHKTLVQQLKEQNEALNR-AHVQELLQCSEREGALQEERADEAQqreEELRALQEElsqakCSSEEAQLEHAELQE 696
Cdd:PRK10246 672 Q---EAQSWQQRQNELTALQNRiQQLTPLLETLPQSDDLPHSEETVAL---DNWRQVHEQ-----CLSLHSQLQTLQQQD 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 697 QLHRANTDTAElgiqvcaltvekERVEEALACAVQELQDAKEAASREREGLERqvagLQQEKESLQEKLKAAKAaagslp 776
Cdd:PRK10246 741 VLEAQRLQKAQ------------AQFDTALQASVFDDQQAFLAALLDEETLTQ----LEQLKQNLENQRQQAQT------ 798
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1894925314 777 gLQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGEECKSLRGQL--EEQGRQLQAA 842
Cdd:PRK10246 799 -LVTQTAQALAQHQQHRPDGLDLTVTVE-QIQQELAQLAQQLRENTTRQGEIRQQLkqDADNRQQQQA 864
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
440-704 |
3.15e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 440 QALQADYQALQQRESaiqgslasLEAEQASIRHLGDQMEASLlavrKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 519
Cdd:PRK11281 39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 520 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptdNEARELAAQLALSQAQLEVHQGE----VQRLQ---AQV 592
Cdd:PRK11281 107 KDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQ-------NDLAEYNSQLVSLQTQPERAQAAlyanSQRLQqirNLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 593 VDLQAKMRAALDDQ-DKVQSQLSMAEAVLRehktLVQQLKEQNEALnrahvQELLQcseregALQEERADEAQQREEELR 671
Cdd:PRK11281 180 KGGKVGGKALRPSQrVLLQAEQALLNAQND----LQRKSLEGNTQL-----QDLLQ------KQRDYLTARIQRLEHQLQ 244
|
250 260 270
....*....|....*....|....*....|...
gi 1894925314 672 ALQEELSQAKCSSEEAQLEHAELQEQLHRANTD 704
Cdd:PRK11281 245 LLQEAINSKRLTLSEKTVQEAQSQDEAARIQAN 277
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
486-941 |
3.26e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.10 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 486 KAKEAMKAQMAEKEAILQSKEGECQQLREEVEQ----CQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptd 561
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRKIIEAqrkaIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLC------- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 562 NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQdKVQSQLSMAEA--VLREHKTLVQQLKE--QNEAL 637
Cdd:pfam05483 158 NLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL-RVQAENARLEMhfKLKEDHEKIQHLEEeyKKEIN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 638 NRAHVQELL--QCSEREGALQ------EERADEAQQREEELRALQEELSQA--KCSSEEAQLEHAELQEQLHRANTDTAE 707
Cdd:pfam05483 237 DKEKQVSLLliQITEKENKMKdltfllEESRDKANQLEEKTKLQDENLKELieKKDHLTKELEDIKMSLQRSMSTQKALE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 708 LGIQV-----CALTVEKErveealaCAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLP-GLQAQ 781
Cdd:pfam05483 317 EDLQIatktiCQLTEEKE-------AQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITmELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 782 LAQAEQRAQsLQEAAHQELNTLKFQLSAE--IMDYQSRLKNAGEEcksLRGQLEEQGRQLQAAEEAVEKLKATQADMGEK 859
Cdd:pfam05483 390 SSELEEMTK-FKNNKEVELEELKKILAEDekLLDEKKQFEKIAEE---LKGKEQELIFLLQAREKEIHDLEIQLTAIKTS 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 860 LSCTSNHLAECQAAMLR---KDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKY 936
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKeklKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN 545
|
....*
gi 1894925314 937 LEERL 941
Cdd:pfam05483 546 LRDEL 550
|
|
| FYVE_RUFY3 |
cd15744 |
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ... |
979-1027 |
3.43e-04 |
|
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: 39.71 E-value: 3.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1894925314 979 CLDCKREFSWMVR-RHHCRICGRIFCYYCCNNYV-LSKHGGKKERCCRACF 1027
Cdd:cd15744 2 CSLCQEDFASLALpKHNCYNCGGTFCDACSSNELpLPSSIYEPARVCDVCY 52
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
667-918 |
3.73e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 667 EEELRALQEELSQAKCSSEEAQLEHAELQEQLhrantdtaelgiqvcALTVEKERVEEALACAVQELQDAKEAASREREG 746
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQDLEQTL---------------ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 747 LERQVAGLQQEKESLQEKLkaakaaagSLPGLQAQLAQAEQRAQSLQEAahqeLNTLKFQLSAeimdYQSRLKNAGEECK 826
Cdd:PRK11281 103 LEALKDDNDEETRETLSTL--------SLRQLESRLAQTLDQLQNAQND----LAEYNSQLVS----LQTQPERAQAALY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 827 SLRGQLEEQGRQLQAAEEAVEKLKATQADMGEklscTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYY 906
Cdd:PRK11281 167 ANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQ----AEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQ 242
|
250
....*....|..
gi 1894925314 907 NKLCQEVTNRER 918
Cdd:PRK11281 243 LQLLQEAINSKR 254
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
498-765 |
3.96e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 44.28 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 498 KEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVgpptdnEARELAAQLALSQAQ 577
Cdd:pfam15742 4 GEKLKYQQQEEVQQLRQNLQRLQILCTSAEKELRYERGKNLDLKQHNSLLQEENIKIKA------ELKQAQQKLLDSTKM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 578 LEVHQGEVQRLQAQVVDLQAKMraaLDDQDKVQSQLSMAEAVLREHKTLVQQLK---EQNEALNRAHVQELLQCSEREGA 654
Cdd:pfam15742 78 CSSLTAEWKHCQQKIRELELEV---LKQAQSIKSQNSLQEKLAQEKSRVADAEEkilELQQKLEHAHKVCLTDTCILEKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 655 LQEERADEAQQREEELRA-LQEELSQAKCSSEEAQlehaELQEQLhRANTDTAELGIQVCALTVEKERVEEALACAVQEL 733
Cdd:pfam15742 155 QLEERIKEASENEAKLKQqYQEEQQKRKLLDQNVN----ELQQQV-RSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENE 229
|
250 260 270
....*....|....*....|....*....|..
gi 1894925314 734 QDAKEAASREREGLERQVAGLQQEKESLQEKL 765
Cdd:pfam15742 230 KRKSDEHLKSNQELSEKLSSLQQEKEALQEEL 261
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
656-856 |
4.05e-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: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 656 QEERADEAQQReeeLRALQEELSQAKcsseeAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALAcavqELQD 735
Cdd:COG3206 166 LELRREEARKA---LEFLEEQLPELR-----KELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLA----EARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 736 AKEAASREREGLERQVAGLQQEKESLQEklkaakaaAGSLPGLQAQLAQAEQRAQSLQE----------AAHQELNTLKF 805
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQ--------SPVIQQLRAQLAELEAELAELSArytpnhpdviALRAQIAALRA 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1894925314 806 QLSAEIMDYQSRLKNageECKSLRGQLEEQGRQLQAAEEAVEKLKATQADM 856
Cdd:COG3206 306 QLQQEAQRILASLEA---ELEALQAREASLQAQLAQLEARLAELPELEAEL 353
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
41-605 |
4.81e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 41 QLEVREKQLRERMQQLDRENQELRAAVSQQGE-QLQTERERGRTAAEDNVRL-----TCLVAELQKQWEVTQATQNTVKE 114
Cdd:TIGR00618 308 QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSiEEQRRLLQTLHSQEIHIRDahevaTSIREISCQQHTLTQHIHTLQQQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 115 LQTCLQGLELGAAEKEEdyhtaLRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIPS 194
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDI-----LQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 195 DAAQEMQELGEKLQALER-----ERTKVEEVNRQQSAQLEQLVKELQLKEDARAS-----LERLVKEMAPLQEELSGKGQ 264
Cdd:TIGR00618 463 ESAQSLKEREQQLQTKEQihlqeTRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLET 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 265 EADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQH-VSDLEEQKKQLIQDK 343
Cdd:TIGR00618 543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAeDMLACEQHALLRKLQ 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 344 DHLSQQVGMLERLAGPPGPELPVAGEKNEALVPVNSSLQEAWGKPEE------EQRGLQEAQLDDTKVQEGSQEEELRQA 417
Cdd:TIGR00618 623 PEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVlpkellASRQLALQKMQSEKEQLTYWKEMLAQC 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 418 NRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASirhlgdqmeasllaVRKAKEAMKAQMAE 497
Cdd:TIGR00618 703 QTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART--------------VLKARTEAHFNNNE 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 498 KEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQT---QLIEVLTAEKGQQGVgPPTDNEARELAAQLALS 574
Cdd:TIGR00618 769 EVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIpsdEDILNLQCETLVQEE-EQFLSRLEEKSATLGEI 847
|
570 580 590
....*....|....*....|....*....|.
gi 1894925314 575 QAQLEvHQGEVQRLQAQVVDLQAKMRAALDD 605
Cdd:TIGR00618 848 THQLL-KYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
36-605 |
4.89e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 36 RLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERgrtaaednvrltclVAELQKQWEvtQATQNTVKEL 115
Cdd:COG4913 280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREE--------------LDELEAQIR--GNGGDRLEQL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 116 QTCLQGLELGAAEKE---EDYHTALRRLESMLQPLAQELEATRDSLDkknQHLASFPGWLAMAQQKADTASDTKgrqepi 192
Cdd:COG4913 344 EREIERLERELEERErrrARLEALLAALGLPLPASAEEFAALRAEAA---ALLEALEEELEALEEALAEAEAAL------ 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 193 pSDAAQEMQELGEKLQALERERTKVEEvnRQQSAqLEQLVKELQLKEDaraslerlvkEMAPLQEELSGKGQEADqlWRR 272
Cdd:COG4913 415 -RDLRRELRELEAEIASLERRKSNIPA--RLLAL-RDALAEALGLDEA----------ELPFVGELIEVRPEEER--WRG 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 273 LQELLAHTSSweeelaelrrekkqqqeekelleqevRSLtrqlqfL--ETQLAQVSQHVSDLeeqkkqliqdkdHLSQQV 350
Cdd:COG4913 479 AIERVLGGFA--------------------------LTL------LvpPEHYAAALRWVNRL------------HLRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 351 gMLERLAGPPGPELPVAGEKNE--ALVPVNSSLQEAWGKPEEEQRGL-----QEAQLDDTK---VQEG--SQEEELRQAN 418
Cdd:COG4913 515 -VYERVRTGLPDPERPRLDPDSlaGKLDFKPHPFRAWLEAELGRRFDyvcvdSPEELRRHPraiTRAGqvKGNGTRHEKD 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 419 RELEKELQNVVGRN-----QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLgDQMEASLLAVRKAKEAMKA 493
Cdd:COG4913 594 DRRRIRSRYVLGFDnraklAALEAELAELEEELAEAEERLEALEAELDALQERREALQRL-AEYSWDEIDVASAEREIAE 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 494 QMAEKEAILQSKeGECQQLREEVEQCQQLAEARHRELRALESQC----QQQTQLIEVLTAEKGQQGVGPPTDNEARELAA 569
Cdd:COG4913 673 LEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIgrleKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
570 580 590
....*....|....*....|....*....|....*..
gi 1894925314 570 QLALSQAQLEVHQGEVQR-LQAQVVDLQAKMRAALDD 605
Cdd:COG4913 752 EERFAAALGDAVERELREnLEERIDALRARLNRAEEE 788
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
393-614 |
4.91e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 393 RGLQEaQLDDTKVQEGSQEEELRQANReLEKELQNVVGRNqllegkLQALQADYQALQQRESAIQGSLASLEAEQASIRH 472
Cdd:PHA02562 177 RELNQ-QIQTLDMKIDHIQQQIKTYNK-NIEEQRKKNGEN------IARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 473 LGDQMEASLLAVRKAKEAMKAQMA--EKEAILQSKEGEC----QQLREEVEQC----QQLAEARHRELRALESQCQQQTQ 542
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEqfQKVIKMYEKGGVCptctQQISEGPDRItkikDKLKELQHSLEKLDTAIDELEEI 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925314 543 LIEVLTAEKGQQGVgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLS 614
Cdd:PHA02562 329 MDEFNEQSKKLLEL----KNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKS 396
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
50-251 |
5.60e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 50 RERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEdnvRLTCLVAELQKQWEV--TQATQNTVKELQTCLQGLELGAA 127
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQE---RREALQRLAEYSWDEidVASAEREIAELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 128 EkeedyhtaLRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDtkgRQEPIPSDAAQEMQELGEKL 207
Cdd:COG4913 686 D--------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD---RLEAAEDLARLELRALLEER 754
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1894925314 208 QALERERTKVEEVNRQQSAQLEQLVKELqlkEDARASLERLVKE 251
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARL---NRAEEELERAMRA 795
|
|
| FYVE_FGD3 |
cd15740 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ... |
973-1027 |
5.82e-04 |
|
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: 39.21 E-value: 5.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925314 973 DTEANHCLDCKREFSWMV-RRHHCRICGRIFCYYCCNnyvLSKHGGKKERCCRACF 1027
Cdd:cd15740 2 EKEKQTCKGCNESFNSITkRRHHCKQCGAVICGKCSE---FKDLASRHNRVCRDCF 54
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
595-765 |
7.20e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 43.26 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 595 LQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcseregalqeeradeaqqrEEELRALQ 674
Cdd:pfam15905 168 LEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE-------------------TEKLLEYI 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 675 EELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERqvaGL 754
Cdd:pfam15905 229 TELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQ---TL 305
|
170
....*....|.
gi 1894925314 755 QQEKESLQEKL 765
Cdd:pfam15905 306 NAELEELKEKL 316
|
|
| GOLD_2 |
pfam13897 |
Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is ... |
1219-1264 |
7.34e-04 |
|
Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is always found combined with lipid- or membrane-association domains.
Pssm-ID: 464028 Cd Length: 133 Bit Score: 40.93 E-value: 7.34e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1894925314 1219 LIPTTRCNSHKENIQGQLKVRTPGIYMLIFDNTFSRFVSKKVFYHL 1264
Cdd:pfam13897 85 IVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKTLYYRV 130
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
742-925 |
8.90e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 742 REREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEA-AHQELNTLKFQLSAEIMDYQSRLKN 820
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 821 AGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKlscTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATT 900
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180
....*....|....*....|....*
gi 1894925314 901 KIQEYYNKLCQEVTNRERNDQKMLA 925
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLL 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
176-622 |
1.04e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 176 QQKADTASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLV------ 249
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllply 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 250 KEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAE----LRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQV 325
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAElaelQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 326 SQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPGPELPVAGeknEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKV 405
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLI---AAALLALLGLGGSLLSLILTIAGVLFLVLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 406 QEGSQEEELRQANRELEkELQNVVGRNQLLEGKLQALQADYQalqqresaiqgslASLEAEQASIRHLGDQMEASLLAVR 485
Cdd:COG4717 289 LFLLLAREKASLGKEAE-ELQALPALEELEEEELEELLAALG-------------LPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 486 KAKEAMK-----AQMAEKEAILQSKEGEC-QQLREEVEQCQQLAEARhRELRALESQCQQQTQLIEVLTAekgqqgvgpp 559
Cdd:COG4717 355 EAEELEEelqleELEQEIAALLAEAGVEDeEELRAALEQAEEYQELK-EELEELEEQLEELLGELEELLE---------- 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925314 560 tDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQ--DKVQSQLSMAEAVLRE 622
Cdd:COG4717 424 -ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRE 487
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
46-848 |
1.05e-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: 43.63 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 46 EKQLRERMQQLDRENQElRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEvtQATQNTVKELQTCLQGLELG 125
Cdd:pfam01576 270 EAQISELQEDLESERAA-RNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKRE--QEVTELKKALEEETRSHEAQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 126 AAEKEEDYHTALRRLESMLQPLA---QELEATRDSLDKKNQHLasfpgwlamaQQKADTASDTKGRQEPIPSDAAQEMQE 202
Cdd:pfam01576 347 LQEMRQKHTQALEELTEQLEQAKrnkANLEKAKQALESENAEL----------QAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 203 LGEKLQALERERTKVEEVNRQQSAQLEQLVKELqlkEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSS 282
Cdd:pfam01576 417 LQARLSESERQRAELAEKLSKLQSELESVSSLL---NEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQ 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 283 WEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQvgMLERLAGPPGP 362
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ--LEEKAAAYDKL 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 363 ELP---VAGEKNEALVPVNSSLQEAwGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELqnvvgRNQLLEGKL 439
Cdd:pfam01576 572 EKTknrLQQELDDLLVDLDHQRQLV-SNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKET-----RALSLARAL 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 440 QALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGecQQLREEVeqc 519
Cdd:pfam01576 646 EEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATED--AKLRLEV--- 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 520 qqlaearhrELRALESQCQQQTQLIEVLTAEKGQQGVgpptdNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKM 599
Cdd:pfam01576 721 ---------NMQALKAQFERDLQARDEQGEEKRRQLV-----KQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQI 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 600 RAALDDQDKVQSQLSMAEAVLREHKTLVQQLkeqnealnRAHVQELLQCSeregalqEERADEAQQREEELRALQEELSQ 679
Cdd:pfam01576 787 DAANKGREEAVKQLKKLQAQMKDLQRELEEA--------RASRDEILAQS-------KESEKKLKNLEAELLQLQEDLAA 851
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 680 AKCSSEEAQLEHAELQEQLHRANTDTAelgiqvcALTVEKERVEEALACAVQELQDAKEAAsrerEGLERQVAGLQQEKE 759
Cdd:pfam01576 852 SERARRQAQQERDELADEIASGASGKS-------ALQDEKRRLEARIAQLEEELEEEQSNT----ELLNDRLRKSTLQVE 920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 760 SLQEKLKAAKAAAGSLPGLQAQLaqaEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEeckslrgQLEEQGRQL 839
Cdd:pfam01576 921 QLTTELAAERSTSQKSESARQQL---ERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEE-------QLEQESRER 990
|
....*....
gi 1894925314 840 QAAEEAVEK 848
Cdd:pfam01576 991 QAANKLVRR 999
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
566-736 |
1.12e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.74 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 566 ELAAQLALSQAQLEVhQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLK--------EQNEAL 637
Cdd:cd22656 98 ELIDDLADATDDEEL-EEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEkalkdlltDEGGAI 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 638 NRAHVQELLQcseregALQEERADEAQQREEELRALQEELsqakcSSEEAQLEHAE-LQEQLHRANTDTAELgiqvcalt 716
Cdd:cd22656 177 ARKEIKDLQK------ELEKLNEEYAAKLKAKIDELKALI-----ADDEAKLAAALrLIADLTAADTDLDNL-------- 237
|
170 180
....*....|....*....|
gi 1894925314 717 veKERVEEALAcAVQELQDA 736
Cdd:cd22656 238 --LALIGPAIP-ALEKLQGA 254
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
565-805 |
1.24e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 565 RELAAQLalsqaqLEVH-QGEVQRLqaqvvdLQAKM-RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQnealnrahv 642
Cdd:COG0497 119 RELGELL------VDIHgQHEHQSL------LDPDAqRELLDAFAGLEELLEEYREAYRAWRALKKELEEL--------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 643 qellqcseregalqEERADEAQQREEELRALQEELSQAKCSS-EEAQLE-------HAE-LQEQLHRA------NTDTAE 707
Cdd:COG0497 178 --------------RADEAERARELDLLRFQLEELEAAALQPgEEEELEeerrrlsNAEkLREALQEAlealsgGEGGAL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 708 LGIQVCALTVEK------------ERVEEALAcavqELQDAKEAASREREGLE------------------------RQV 751
Cdd:COG0497 244 DLLGQALRALERlaeydpslaelaERLESALI----ELEEAASELRRYLDSLEfdperleeveerlallrrlarkygVTV 319
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1894925314 752 AGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQR---------------AQSLQEAAHQELNTLKF 805
Cdd:COG0497 320 EELLAYAEELRAELAELENSDERLEELEAELAEAEAElleaaeklsaarkkaAKKLEKAVTAELADLGM 388
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
733-931 |
1.32e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 733 LQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAG--SLPG------------------LQAQLAQAEQRAQSL 792
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEeaklllqqlselesqlaeARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 793 QEAAHQELNTLKFQL-SAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLsctsnhLAECQ 871
Cdd:COG3206 246 RAQLGSGPDALPELLqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI------LASLE 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 872 AAMLRKDKEGAALREDLERTQKELEKATTKIQEyYNKLCQEVTNRERNDQKMLADLDDLN 931
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLEREVEVARELYESLLQRLEEAR 378
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
779-912 |
1.37e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 779 QAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGE-ECKSLRGQLEEQGRQLQAAEEAVEKLKatqadmg 857
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEkELRERRNELQKLEKRLLQKEENLDRKL------- 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1894925314 858 EKLSctsnhlaecqaamlRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQE 912
Cdd:PRK12704 103 ELLE--------------KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
232-949 |
1.47e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 232 VKELQLKEDARASLERLVKEMApLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSL 311
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEA-LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 312 TRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPGP----ELPVAGEKNEALVPVNSSLQEAWGK 387
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKlqeeELKLLAKEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 388 PEEEQRGLQE--AQLDDTKVQEGSQEEELRQANRELEK---ELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLAS 462
Cdd:pfam02463 312 DEEKLKESEKekKKAEKELKKEKEEIEELEKELKELEIkreAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 463 LEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEarhRELRALESQCQQQTQ 542
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEEL---EKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 543 LIEVLTAEKgqQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQ----------------AKMRAALDDQ 606
Cdd:pfam02463 469 KSEDLLKET--QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggriisahgrlgdlgvAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 607 DKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEE 686
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 687 AQLEHAELQEQLHRANTDTAELGIQVcalTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLK 766
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGV---SLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 767 AAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNageecKSLRGQLEEQGRQLQAAEEAV 846
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL-----KKEEKEEEKSELSLKEKELAE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 847 EKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLAD 926
Cdd:pfam02463 779 EREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELER 858
|
730 740
....*....|....*....|...
gi 1894925314 927 LDDLNRTKKYLEERLIELLRDKD 949
Cdd:pfam02463 859 LEEEITKEELLQELLLKEEELEE 881
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
589-751 |
1.85e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 589 QAQVVDLQAkmraaLDDQ-DKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQRE 667
Cdd:COG1579 6 LRALLDLQE-----LDSElDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 668 --------EELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEA 739
Cdd:COG1579 81 qlgnvrnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
170
....*....|..
gi 1894925314 740 ASREREGLERQV 751
Cdd:COG1579 161 LEAEREELAAKI 172
|
|
| FYVE_CARP |
cd15750 |
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ... |
978-1026 |
1.93e-03 |
|
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: 37.34 E-value: 1.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1894925314 978 HCLDCKREFSWMVRRHHCRICGRIFCYYCcnnyvLSKHGGKKeRCCRAC 1026
Cdd:cd15750 2 PCESCGAKFSVFKRKRTCADCKRYFCSNC-----LSKEERGR-RRCRRC 44
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
310-470 |
2.36e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 310 SLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMlerlagppgpelpvaGEKNEALVPVNSSLQEAwgkpe 389
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS---------------GPDALPELLQSPVIQQL----- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 390 EEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVvgrNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQAS 469
Cdd:COG3206 269 RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL---QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345
|
.
gi 1894925314 470 I 470
Cdd:COG3206 346 L 346
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
73-726 |
2.39e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 73 QLQTERERgrtAAEDNVRLTCLVAELQKQWEVTQATQNT----VKELQTCLQGLELGAAEKEED---------YHTALRR 139
Cdd:pfam10174 120 RLQSEHER---QAKELFLLRKTLEEMELRIETQKQTLGArdesIKKLLEMLQSKGLPKKSGEEDwertrriaeAEMQLGH 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 140 LESMLQPLAQELEATRDSLDKKNQhlasfpgwlamaqqkadtasdtkGRQEPIPSDAAQEMQELGE-KLQALERERTKVE 218
Cdd:pfam10174 197 LEVLLDQKEKENIHLREELHRRNQ-----------------------LQPDPAKTKALQTVIEMKDtKISSLERNIRDLE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 219 -EVNRQQSAQL---EQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAELRREK 294
Cdd:pfam10174 254 dEVQMLKTNGLlhtEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 295 KQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERlagppgpELPVAGEKNEAL 374
Cdd:pfam10174 334 TAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKER-------KINVLQKKIENL 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 375 VPVNSSLQEAWGKPEEEQRGLQ--------------EAQLDDTKVQEGSQEEELRQaNRELEKELQNVVGRNQLLEGKLQ 440
Cdd:pfam10174 407 QEQLRDKDKQLAGLKERVKSLQtdssntdtalttleEALSEKERIIERLKEQRERE-DRERLEELESLKKENKDLKEKVS 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 441 ALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLL-----AVRKAKEAMKAQMAEKEAI--------LQSKEG 507
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEqkkeeCSKLENQLKKAHNAEEAVRtnpeindrIRLLEQ 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 508 ECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTdnearelaaqlalSQAQLEVHQGEVQR 587
Cdd:pfam10174 566 EVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNK-------------KVANIKHGQQEMKK 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 588 LQAQVVDLQakmRAALDDQDKVQSQLSMAEAVLREHKTLvQQLKEQNEALnrAHVQELLQcsEREGALQEERADEAQQRE 667
Cdd:pfam10174 633 KGAQLLEEA---RRREDNLADNSQQLQLEELMGALEKTR-QELDATKARL--SSTQQSLA--EKDGHLTNLRAERRKQLE 704
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1894925314 668 EELRALQEELsQAKCSSEEAQLEHAELQEQLHRANTDtaelgiQVCALTVEKERVEEAL 726
Cdd:pfam10174 705 EILEMKQEAL-LAAISEKDANIALLELSSSKKKKTQE------EVMALKREKDRLVHQL 756
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
719-860 |
2.92e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 719 KERVEEALACAVQELQDAKEAASREREGLERQVAGLQQE---KESLQEKLKaakaaaGSLPGLQAQLAQAEQRAQSLQea 795
Cdd:PRK09039 51 KDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASlsaAEAERSRLQ------ALLAELAGAGAAAEGRAGELA-- 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925314 796 ahQELNTLKfQLSAEIMdyqSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKL 860
Cdd:PRK09039 123 --QELDSEK-QVSARAL---AQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
33-267 |
3.21e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 33 DEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQAT-QNT 111
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 112 VKELQTCLQGLELGAAEKEEDYHTALRRLEsMLQPLAQELEATRDSLDKKNQHLasfpgwlamAQQKADTASDTKgrqep 191
Cdd:COG4942 110 LRALYRLGRQPPLALLLSPEDFLDAVRRLQ-YLKYLAPARREQAEELRADLAEL---------AALRAELEAERA----- 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925314 192 ipsDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEAD 267
Cdd:COG4942 175 ---ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
388-545 |
3.77e-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: 40.29 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 388 PEEEQRGLQEAQLDDTKVQEgsqeeeLRQANRELEKELQNvvgrnqlLEGKLQALQADYQALQQRESAIQGSLASLEAEQ 467
Cdd:COG1579 2 MPEDLRALLDLQELDSELDR------LEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 468 ASIRHLGDQMEASLLAVRKAKE---------AMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQ 538
Cdd:COG1579 69 EEVEARIKKYEEQLGNVRNNKEyealqkeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
....*..
gi 1894925314 539 QQTQLIE 545
Cdd:COG1579 149 EELAELE 155
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
386-954 |
3.77e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 386 GKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEG--KLQALQADYQALQQRESAIQGSLASL 463
Cdd:pfam10174 173 PKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDpaKTKALQTVIEMKDTKISSLERNIRDL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 464 EAEQASIRHLGD-----------QMEAsllaVRKAKEAMKAQMAEKEAILQSKEGE-----------------CQQ---- 511
Cdd:pfam10174 253 EDEVQMLKTNGLlhtedreeeikQMEV----YKSHSKFMKNKIDQLKQELSKKESEllalqtkletltnqnsdCKQhiev 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 512 LREEVEQCQQLAEARHRELRAL-------ESQCQQQTQLIEVLTAEKGQQGvgpptdNEARELAAQLALSQAQLEVHQGE 584
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEVDALrlrleekESFLNKKTKQLQDLTEEKSTLA------GEIRDLKDMLDVKERKINVLQKK 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 585 VQRLQAQVVD-------LQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELlqcseregalqE 657
Cdd:pfam10174 403 IENLQEQLRDkdkqlagLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEEL-----------E 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 658 ERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVcaltveKERVEEALACAVQeLQDAK 737
Cdd:pfam10174 472 SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAV------EQKKEECSKLENQ-LKKAH 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 738 EAASREREGLE--RQVAGLQQEKESLQEKlkaAKAAAGSLPGLQAQLAQAEQRA----------QSLQEAAHQELNTLKF 805
Cdd:pfam10174 545 NAEEAVRTNPEinDRIRLLEQEVARYKEE---SGKAQAEVERLLGILREVENEKndkdkkiaelESLTLRQMKEQNKKVA 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 806 QLSAeiMDYQSRLKNAGEECKSLRGQLEE----QGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAEcqaamlrKDKEG 881
Cdd:pfam10174 622 NIKH--GQQEMKKKGAQLLEEARRREDNLadnsQQLQLEELMGALEKTRQELDATKARLSSTQQSLAE-------KDGHL 692
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925314 882 AALRedLERtQKELEKATTKIQEyynKLCQEVTNRERNdqkmLADLDDLNRTKKYLEERLIELLRDKDALWQK 954
Cdd:pfam10174 693 TNLR--AER-RKQLEEILEMKQE---ALLAAISEKDAN----IALLELSSSKKKKTQEEVMALKREKDRLVHQ 755
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
778-964 |
3.91e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 778 LQAQLAQAEQRAQ--SLQEAAHQELNTLKFQLsAEIMDYQSRLKnageeckSLRGQLEEQGRQLQAAEEAVEKLKATQAD 855
Cdd:PRK11281 41 VQAQLDALNKQKLleAEDKLVQQDLEQTLALL-DKIDRQKEETE-------QLKQQLAQAPAKLRQAQAELEALKDDNDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 856 MGE-------------KLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRE--RND 920
Cdd:PRK11281 113 ETRetlstlslrqlesRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKalRPS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1894925314 921 QKM-----LADLD---DLNRTKKYLEERLIELLRDK-DALWQKSDALEFQQKL 964
Cdd:PRK11281 193 QRVllqaeQALLNaqnDLQRKSLEGNTQLQDLLQKQrDYLTARIQRLEHQLQL 245
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
316-639 |
4.29e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 316 QFLET---QLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPGPELPVAGEK--------------------NE 372
Cdd:PRK11281 63 QDLEQtlaLLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTlslrqlesrlaqtldqlqnaQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 373 ALVPVNSSLQEAWGKPEEEQRGLQEAQ---------LDDTKVQEGSQEEELRQanrELEKELQNVVGRN----QLLEG-- 437
Cdd:PRK11281 143 DLAEYNSQLVSLQTQPERAQAALYANSqrlqqirnlLKGGKVGGKALRPSQRV---LLQAEQALLNAQNdlqrKSLEGnt 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 438 KLQAL---QADYQALQQresaiqgslASLEAEQASIRHLGDQ--MEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQL 512
Cdd:PRK11281 220 QLQDLlqkQRDYLTARI---------QRLEHQLQLLQEAINSkrLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 513 REE-VEQCQQLAEARHRELRA---LESQCQQQTQLIEVLTAEKG---------QQGVGPPTDNEARELAAQLA-LSQAQL 578
Cdd:PRK11281 291 SQRlLKATEKLNTLTQQNLRVknwLDRLTQSERNIKEQISVLKGslllsrilyQQQQALPSADLIEGLADRIAdLRLEQF 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925314 579 EVHQ--GEVQRLQAQVVDLQAKMRAALDDQdkvqsqlsmaeavlrEHKTLVQQLKEQNEALNR 639
Cdd:PRK11281 371 EINQqrDALFQPDAYIDKLEAGHKSEVTDE---------------VRDALLQLLDERRELLDQ 418
|
|
| FYVE_WDFY1 |
cd15756 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ... |
969-1032 |
4.50e-03 |
|
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: 37.36 E-value: 4.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925314 969 RWLgdtEANHCLDCKREFSWMV-----------RRHHCRICGRIFCYYCCNNYVLSKHGG--KKERCCRACFQKLSE 1032
Cdd:cd15756 2 QWL---ESDSCQKCEQPFFWNIkqmwdtktlglRQHHCRKCGQAVCGKCSSKRSSYPIMGfeFQVRVCDSCFETIKD 75
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
570-796 |
4.83e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 570 QLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAvlrEHKTLVQQLKEQNEALNRAhvQELLqcs 649
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA---EIDKLQAEIAEAEAEIEER--REEL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 650 eregalqEERADEAQQREEELRALQEELSQakcSSEEAQLEHAELQEQLHRANTDTAElgiQVCALTVEKERVEEALACA 729
Cdd:COG3883 89 -------GERARALYRSGGSVSYLDVLLGS---ESFSDFLDRLSALSKIADADADLLE---ELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925314 730 VQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAA 796
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
629-969 |
5.06e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 629 QLKEQNEALNrahvqELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQlhrantdtAEL 708
Cdd:pfam17380 263 QTMTENEFLN-----QLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQ--------AEM 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 709 GIQVcALTVEKERVeealacavqelqdakeAASREREGLERQVAGLQQEKESL-QEKLKAAKAAAGSLPGLQAQLAQAEQ 787
Cdd:pfam17380 330 DRQA-AIYAEQERM----------------AMERERELERIRQEERKRELERIrQEEIAMEISRMRELERLQMERQQKNE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 788 RAQSLQEAAHqelntlKFQLSAEimDYQSRLKNAGEECKSLRGQLEE-QGRQLQAAEEA----VEKLKATQADMGEKLSC 862
Cdd:pfam17380 393 RVRQELEAAR------KVKILEE--ERQRKIQQQKVEMEQIRAEQEEaRQREVRRLEEErareMERVRLEEQERQQQVER 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 863 TSNHLAECQAAMLRKDKEgaalredlERTQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEE--R 940
Cdd:pfam17380 465 LRQQEEERKRKKLELEKE--------KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEErrR 536
|
330 340
....*....|....*....|....*....
gi 1894925314 941 LIELLRDKDALWQKSDALEFQQKLSAEER 969
Cdd:pfam17380 537 EAEEERRKQQEMEERRRIQEQMRKATEER 565
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
627-969 |
5.13e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 627 VQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEElsqaKCSSEEAQLEHAELQEQLHRANTDTA 706
Cdd:PTZ00121 1199 ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEE----RNNEEIRKFEEARMAHFARRQAAIKA 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 707 ELGIQVCAL--TVEKERVEEAL-ACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLA 783
Cdd:PTZ00121 1275 EEARKADELkkAEEKKKADEAKkAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA 1354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 784 QAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKL-----KATQADMGE 858
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdeakkKAEEKKKAD 1434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 859 KLSCTSNHLAecQAAMLRKDKEGAALREDLERTQKELEKA-TTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYL 937
Cdd:PTZ00121 1435 EAKKKAEEAK--KADEAKKKAEEAKKAEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512
|
330 340 350
....*....|....*....|....*....|...
gi 1894925314 938 EE-RLIELLRDKDALWQKSDALEFQQKLSAEER 969
Cdd:PTZ00121 1513 DEaKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
500-849 |
5.32e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.32 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 500 AILQSKEGECQQLREEVE------QCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQ---GVGPPTDNEARELAAQ 570
Cdd:PRK10246 160 AFLNAKPKERAELLEELTgteiygQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSltaSLQVLTDEEKQLLTAQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 571 LALSQA-QLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAE--AVLR-------EHKTLVQQLKEQNEALN-R 639
Cdd:PRK10246 240 QQQQQSlNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQpaRQLRphweriqEQSAALAHTRQQIEEVNtR 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 640 AHVQELLQCSEREGALQEERADEAQQRE--------EELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAEL-GI 710
Cdd:PRK10246 320 LQSTMALRARIRHHAAKQSAELQAQQQSlntwlaehDRFRQWNNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLnAL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 711 QVCALTVEKERVEEALAcavqelQDAKEAASRER-EGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQ----- 784
Cdd:PRK10246 400 PAITLTLTADEVAAALA------QHAEQRPLRQRlVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQrykek 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 785 ----AEQRAQSLQEAAHQELNTLKFQLSA---------------------EIMDYQSRL-------KNAGEECKSLRGQL 832
Cdd:PRK10246 474 tqqlADVKTICEQEARIKDLEAQRAQLQAgqpcplcgstshpaveayqalEPGVNQSRLdalekevKKLGEEGAALRGQL 553
|
410
....*....|....*..
gi 1894925314 833 EEQGRQLQAAEEAVEKL 849
Cdd:PRK10246 554 DALTKQLQRDESEAQSL 570
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
596-861 |
5.82e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 596 QAKMRAALDDQDKVQSQLsmaeAVLREHKTLVQQLKEQNEALNRAhvQELLQCSERegalQEERADEAQQR----EEELR 671
Cdd:PRK11281 28 RAASNGDLPTEADVQAQL----DALNKQKLLEAEDKLVQQDLEQT--LALLDKIDR----QKEETEQLKQQlaqaPAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 672 ALQEELSQAKCSSEE-----------AQLEH--AELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDake 738
Cdd:PRK11281 98 QAQAELEALKDDNDEetretlstlslRQLESrlAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 739 aasreregLERQVAGLQQEKE----SLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDY 814
Cdd:PRK11281 175 --------IRNLLKGGKVGGKalrpSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLL 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925314 815 QS-----RLKnageeckslrgQLEEQGRQLQAAEEAVE----KLKATQADMGEKLS 861
Cdd:PRK11281 247 QEainskRLT-----------LSEKTVQEAQSQDEAARiqanPLVAQELEINLQLS 291
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
501-708 |
5.82e-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: 40.51 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 501 ILQSKEGECQQLRE---------------EVEQCQQLAEARHRELRALESQCQQ-QTQLIEVltaEKGQQgvgpptdNEA 564
Cdd:pfam09787 19 ILQSKEKLIASLKEgsgvegldsstaltlELEELRQERDLLREEIQKLRGQIQQlRTELQEL---EAQQQ-------EEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 565 RELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLsmaEAVLREHKTLVQQLKEQ--NEALNRAHV 642
Cdd:pfam09787 89 ESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATL---QSRIKDREAEIEKLRNQltSKSQSSSSQ 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925314 643 QELlqcseregalqeeradeaqqrEEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAEL 708
Cdd:pfam09787 166 SEL---------------------ENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKEL 210
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
759-969 |
7.30e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 759 ESLQEKLKAAKAAAGSLPGL---QAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRgqleeq 835
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELnlkELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE------ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 836 grQLQAAEEAVEKLKATQADMgeklsctsNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVtn 915
Cdd:COG4717 123 --KLLQLLPLYQELEALEAEL--------AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT-- 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1894925314 916 rERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEER 969
Cdd:COG4717 191 -EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
310-545 |
8.88e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 310 SLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKD--HLSQQVGMLErlagppgpelpvageknEALVPVNSSLQEAwgk 387
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLL-----------------QQLSELESQLAEA--- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 388 peEEQRGLQEAQLDDTKVQEGSQEEELRQANREleKELQNVVGRNQLLEGKLQALQADYQ----ALQQRESAIQGSLASL 463
Cdd:COG3206 232 --RAELAEAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTpnhpDVIALRAQIAALRAQL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925314 464 EAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAE---ARHRELRALESQCQQQ 540
Cdd:COG3206 308 QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYEsllQRLEEARLAEALTVGN 387
|
....*
gi 1894925314 541 TQLIE 545
Cdd:COG3206 388 VRVID 392
|
|
| |
